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Conserved domains on  [gi|1370483048|ref|XP_024309093|]
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cytosolic 10-formyltetrahydrofolate dehydrogenase isoform X1 [Homo sapiens]

Protein Classification

bifunctional UDP-glucuronic acid decarboxylase/UDP-4-amino-4-deoxy-L-arabinose formyltransferase( domain architecture ID 10171313)

bifunctional UDP-glucuronic acid decarboxylase/UDP-4-amino-4-deoxy-L-arabinose formyltransferase is specific to the lipid A-Ara4N pathway; it catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid and formylates UDP-Ara4N

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 417-902 0e+00

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


:

Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 1009.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLM 496
Cdd:cd07140     1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 497 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYP 576
Cdd:cd07140    81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 577 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 656
Cdd:cd07140   161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 657 HIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:cd07140   241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 737 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 816
Cdd:cd07140   321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 817 DGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:cd07140   401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480


                  ....*.
gi 1370483048 897 TVTFEY 902
Cdd:cd07140   481 TVTIEY 486
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 1-203 1.06e-153

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


:

Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 449.59  E-value: 1.06e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647     1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08647    81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370483048 161 STLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGI 203
Cdd:cd08647   161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
FDH_Hydrolase_C cd08703
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...
 206-306 3.64e-51

The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.


:

Pssm-ID: 187731 [Multi-domain]  Cd Length: 100  Bit Score: 174.46  E-value: 3.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 206 KETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDK 285
Cdd:cd08703     1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGK 79

                          90       100
                  ....*....|....*....|.
gi 1370483048 286 MLLVKNIQLEDGKMILASNFF 306
Cdd:cd08703    80 MVNVKRLQFEDGKMIPASKYG 100
 
Name Accession Description Interval E-value
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 417-902 0e+00

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 1009.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLM 496
Cdd:cd07140     1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 497 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYP 576
Cdd:cd07140    81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 577 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 656
Cdd:cd07140   161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 657 HIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:cd07140   241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 737 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 816
Cdd:cd07140   321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 817 DGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:cd07140   401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480


                  ....*.
gi 1370483048 897 TVTFEY 902
Cdd:cd07140   481 TVTIEY 486
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 430-898 0e+00

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 621.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 430 FVDAEGaKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEAL 509
Cdd:pfam00171   1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 510 DAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARpnrnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLA 589
Cdd:pfam00171  78 ENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGR----LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 590 AGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKK 669
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 670 VSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQ 749
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 750 NHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANA 829
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIAND 389

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 830 TEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDV-AAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 421-902 0e+00

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 604.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 421 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQ 500
Cdd:COG1012     5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 501 EELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRnLTLTRKEPVGVCGIIIPWNYPLMML 580
Cdd:COG1012    83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPS--DAPGT-RAYVRREPLGVVGAITPWNFPLALA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:COG1012   159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 661 SCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:COG1012   239 AAA-ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR-PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgD 819
Cdd:COG1012   318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD--D 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 820 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:COG1012   396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTV 475


                  ....
gi 1370483048 899 TFEY 902
Cdd:COG1012   476 TIRL 479
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 414-898 2.82e-175

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 517.07  E-value: 2.82e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 414 NKRTVRMPH----QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLM 489
Cdd:PLN02766    9 GASGVKVPEikftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIM 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 490 YRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRNLTLtrKEPVGVCGI 569
Cdd:PLN02766   89 MKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM--SRQLQGYTL--KEPIGVVGH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 570 IIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFT 649
Cdd:PLN02766  165 IIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 650 GSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVE 729
Cdd:PLN02766  245 GSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVE 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 730 EVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPV 809
Cdd:PLN02766  325 KAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPV 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 810 MIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAAL 889
Cdd:PLN02766  405 MSLMKFK--TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDAL 482


                  ....*....
gi 1370483048 890 NEYLRVKTV 898
Cdd:PLN02766  483 DKYLQVKSV 491
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 425-896 8.25e-161

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 478.54  E-value: 8.25e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 505 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:TIGR01804  79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL----GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 664
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 744
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 745 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGdl 820
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE-- 391

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483048 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 1-203 1.06e-153

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 449.59  E-value: 1.06e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647     1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08647    81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370483048 161 STLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGI 203
Cdd:cd08647   161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-309 4.77e-77

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 253.49  E-value: 4.77e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:COG0223     1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQPESLKD-----PEFLEELR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:COG0223    76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:COG0223   156 GPDDTAGSLHDK-LAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAF 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 235 TEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPGVVTKAG----LILFGndDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:COG0223   235 TTLDGKRLKIWKARV-----------LEEAGGGAPGTILAVDkdglLVACG--DGALRLLELQPAGKKRMSAADFLRGY 300
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-180 2.56e-66

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 219.47  E-value: 2.56e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVI--GQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGA 78
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  79 ELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDD 158
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|..
gi 1370483048 159 TVSTLYNRFLFPEGiKGMVQAV 180
Cdd:pfam00551 161 TAETLYNRVADLEH-KALPRVL 181
FDH_Hydrolase_C cd08703
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...
 206-306 3.64e-51

The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.


Pssm-ID: 187731 [Multi-domain]  Cd Length: 100  Bit Score: 174.46  E-value: 3.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 206 KETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDK 285
Cdd:cd08703     1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGK 79

                          90       100
                  ....*....|....*....|.
gi 1370483048 286 MLLVKNIQLEDGKMILASNFF 306
Cdd:cd08703    80 MVNVKRLQFEDGKMIPASKYG 100
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 1-310 1.26e-49

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 177.98  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDG------KADPLGLEAEKDGVPVFKYsrwraKGQALPDVVAKYQ 74
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQP-----EKQRQLEELPLVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:TIGR00460  76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:TIGR00460 156 EEEDNSGTLSDK-LSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAW 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 235 TEACEQKLTFFnstlntsglvpEGDALPIPG-AHRPGVV---TKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAA 310
Cdd:TIGR00460 235 LTFEGKNIKIH-----------KAKVIDLSTyKAKPGEIvyhNKKGILVACGKDGILLLLSLQPPGKKVMRAEDFYNGSR 303
PRK06988 PRK06988
formyltransferase;
46-305 1.34e-26

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 111.32  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  46 AEKDGVPVFKYSrwrakGQALPDVVAKYQALGAELnVLPFCSQF-IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLI 124
Cdd:PRK06988   51 AAEHGIPVITPA-----DPNDPELRAAVAAAAPDF-IFSFYYRHmIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 125 HGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNrflfpegiKGMVQAVRLIAE-------GKAPRLPQPEEG 197
Cdd:PRK06988  125 NGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD--------KVTVAAEQTLWRvlpallaGEAPHLPNDLAQ 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 198 ATYEGIQKKETAKINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTLNTSGlvPEGDALPIPGAHrpgVVTKAG 276
Cdd:PRK06988  197 GSYFGGRKPEDGRIDWSKPAAQVYNLIRAvAPPYPGAFTDLGGTRFVVARARLAAPG--AAAARDLPPGLH---VSDNAL 271

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370483048 277 LILFGNDDKMLL--VKNIQLEDGKMILASNF 305
Cdd:PRK06988  272 FGVCGDGRAVSIleLRRQQDGGETVVTPAQF 302
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
205-309 6.99e-18

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 79.63  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 205 KKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPG--VVTKAGLILFGN 282
Cdd:pfam02911   3 KKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKASV-----------LDQESGAAPGtiVTVDKGGLLVAC 71

                          90       100
                  ....*....|....*....|....*..
gi 1370483048 283 DDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:pfam02911  72 GDGALLILELQLEGKKPMSAEDFLNGF 98
 
Name Accession Description Interval E-value
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 417-902 0e+00

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 1009.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLM 496
Cdd:cd07140     1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 497 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYP 576
Cdd:cd07140    81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 577 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 656
Cdd:cd07140   161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 657 HIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:cd07140   241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 737 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 816
Cdd:cd07140   321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 817 DGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:cd07140   401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480


                  ....*.
gi 1370483048 897 TVTFEY 902
Cdd:cd07140   481 TVTIEY 486
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 420-900 0e+00

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 778.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 420 MPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQH 499
Cdd:cd07091     2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 500 QEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMM 579
Cdd:cd07091    82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPID----GNFLAYTRREPIGVCGQIIPWNFPLLM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 580 LSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIM 659
Cdd:cd07091   158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 660 KSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNP 739
Cdd:cd07091   238 EAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 740 LDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgD 819
Cdd:cd07091   318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK--T 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 820 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07091   396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475


                  .
gi 1370483048 900 F 900
Cdd:cd07091   476 I 476
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 430-898 0e+00

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 621.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 430 FVDAEGaKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEAL 509
Cdd:pfam00171   1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 510 DAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARpnrnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLA 589
Cdd:pfam00171  78 ENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGR----LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 590 AGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKK 669
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 670 VSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQ 749
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 750 NHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANA 829
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIAND 389

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 830 TEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDV-AAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 422-899 0e+00

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 620.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGR-WGKISARDRGRLMYRLADLMEQHQ 500
Cdd:cd07141     7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpWRTMDASERGRLLNKLADLIERDR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 501 EELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMML 580
Cdd:cd07141    87 AYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMD----GDFFTYTRHEPVGVCGQIIPWNFPLLMA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07141   163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQ 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 661 SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:cd07141   243 AAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPF 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 820
Cdd:cd07141   323 DPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFK--TI 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07141   401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 421-902 0e+00

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 604.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 421 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQ 500
Cdd:COG1012     5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 501 EELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRnLTLTRKEPVGVCGIIIPWNYPLMML 580
Cdd:COG1012    83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPS--DAPGT-RAYVRREPLGVVGAITPWNFPLALA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:COG1012   159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 661 SCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:COG1012   239 AAA-ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR-PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgD 819
Cdd:COG1012   318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD--D 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 820 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:COG1012   396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTV 475


                  ....
gi 1370483048 899 TFEY 902
Cdd:COG1012   476 TIRL 479
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
 477-900 0e+00

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 566.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarPNRNL 556
Cdd:cd07078    14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEVIPSP---DPGEL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 636
Cdd:cd07078    90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 637 LSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVE 716
Cdd:cd07078   170 LASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 717 DSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR-PGFFFEPTVFTDVE 795
Cdd:cd07078   249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVPPTVLTDVD 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 796 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK-TDVAAPFGG 874
Cdd:cd07078   329 PDMPIAQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPFGG 406

                         410       420
                  ....*....|....*....|....*.
gi 1370483048 875 FKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07078   407 VKQSGIGREGGPYGLEEYTEPKTVTI 432
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
 415-898 0e+00

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 547.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 415 KRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgRWGKISARDRGRLMYRLAD 494
Cdd:cd07144     1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 495 LMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWN 574
Cdd:cd07144    80 LVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTS----PNKLAYTLHEPYGVCGQIIPWN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 575 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEV 654
Cdd:cd07144   156 YPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 655 GKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRK- 733
Cdd:cd07144   236 GRLVMKAAA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQn 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 734 MKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGN---QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVM 810
Cdd:cd07144   315 YKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEkapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVV 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 811 IISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALN 890
Cdd:cd07144   395 VISKFK--TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLE 472


                  ....*...
gi 1370483048 891 EYLRVKTV 898
Cdd:cd07144   473 TYTQTKAV 480
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
 441-900 0e+00

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 544.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALK 520
Cdd:cd07114     1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIR-ETR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSIQTFRYFAGWCDKIQGSTIPINqaRPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07114    80 AQVRYLAEWYRYYAGLADKIEGAVIPVD--KGDY-LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKSPL 680
Cdd:cd07114   157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARA-AAENLAPVTLELGGKSPN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07114   236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 761 YCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLAS 836
Cdd:cd07114   316 YVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE-EAI-ALANDSEYGLAA 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483048 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07114   394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 425-898 0e+00

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 540.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:cd07119     1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 505 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinqaRPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07119    81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYD----VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 664
Cdd:cd07119   156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 744
Cdd:cd07119   235 GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 745 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDl 820
Cdd:cd07119   315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE- 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483048 821 DAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07119   394 EAI-RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
 437-898 0e+00

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 537.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 437 KTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYT 516
Cdd:cd07112     2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 517 LALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVI 596
Cdd:cd07112    82 DALAVDVPSAANTFRWYAEAIDKVYGEVAPT----GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 597 KPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGG 676
Cdd:cd07112   158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 677 KSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 755
Cdd:cd07112   238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 756 VKLMEYCQHGVKEGATLVCGGNQV--PRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFG 833
Cdd:cd07112   318 DKVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE-EAV-ALANDSVYG 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 834 LASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07112   396 LAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
 421-898 0e+00

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 535.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 421 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQ 500
Cdd:cd07142     3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 501 EELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLTLtrKEPVGVCGIIIPWNYPLMML 580
Cdd:cd07142    83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADG--PHHVYTL--HEPIGVVGQIIPWNFPLLMF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07142   159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 661 SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:cd07142   239 LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 820
Cdd:cd07142   319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK--TV 396

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483048 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07142   397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
 417-898 0e+00

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 532.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 417 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGrWG-KISARDRGRLMYRLADL 495
Cdd:cd07143     2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETD-WGlKVSGSKRGRCLSKLADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 496 MEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARpnrnLTLTRKEPVGVCGIIIPWNY 575
Cdd:cd07143    81 MERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKK----LTYTRHEPIGVCGQIIPWNF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 576 PLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVG 655
Cdd:cd07143   157 PLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 656 KHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMK 735
Cdd:cd07143   237 RKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 736 VGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRF 815
Cdd:cd07143   317 VGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKF 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 816 ADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRV 895
Cdd:cd07143   397 KTE--EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQI 474


                  ...
gi 1370483048 896 KTV 898
Cdd:cd07143   475 KAV 477
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
 441-898 3.91e-180

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 527.39  E-value: 3.91e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK 520
Cdd:cd07115     1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSIQTFRYFAGWCDKIQGSTIPInqaRPnRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07115    79 LDVPRAADTFRYYAGWADKIEGEVIPV---RG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07115   155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSAN 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07115   234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 761 YCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFT 840
Cdd:cd07115   314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAGVWT 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483048 841 RDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07115   392 RDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
 442-900 9.72e-177

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 518.53  E-value: 9.72e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07103     2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 522 HVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07103    79 EVDYAASFLEWFAEEARRIYGRTIP--SPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 602 TPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 681
Cdd:cd07103   156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 761
Cdd:cd07103   235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 762 CQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTR 841
Cdd:cd07103   315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFD--TEDEVIARANDTPYGLAAYVFTR 392

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 842 DINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07103   393 DLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 414-898 2.82e-175

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 517.07  E-value: 2.82e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 414 NKRTVRMPH----QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLM 489
Cdd:PLN02766    9 GASGVKVPEikftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIM 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 490 YRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRNLTLtrKEPVGVCGI 569
Cdd:PLN02766   89 MKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM--SRQLQGYTL--KEPIGVVGH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 570 IIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFT 649
Cdd:PLN02766  165 IIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 650 GSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVE 729
Cdd:PLN02766  245 GSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVE 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 730 EVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPV 809
Cdd:PLN02766  325 KAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPV 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 810 MIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAAL 889
Cdd:PLN02766  405 MSLMKFK--TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDAL 482


                  ....*....
gi 1370483048 890 NEYLRVKTV 898
Cdd:PLN02766  483 DKYLQVKSV 491
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
 441-899 4.26e-171

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 504.41  E-value: 4.26e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK 520
Cdd:cd07093     1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSIQTFRYFAGWCDKIQGSTIPinqaRPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07093    79 RDIPRAAANFRFFADYILQLDGESYP----QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07093   155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPN 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07093   234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 761 YCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGdlDAVLSRANATEFGLAS 836
Cdd:cd07093   314 YVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAA 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483048 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07093   392 YVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
 441-898 6.78e-168

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 496.06  E-value: 6.78e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:cd07090     1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07090    78 VDIDSSADCLEYYAGLAPTLSGEHVPL----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07090   154 FTPLTALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07090   232 IIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 761 YCQHGVKEGATLVCGGNQVP-----RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 835
Cdd:cd07090   312 YIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFD--TEEEVIRRANDTTYGLA 389

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483048 836 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07090   390 AGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 423-898 1.03e-166

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 496.25  E-value: 1.03e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:PLN02466   59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLTLtrKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:PLN02466  139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADG--PHHVQTL--HEPIGVAGQIIPWNFPLLMFAW 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PLN02466  215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 663 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 742
Cdd:PLN02466  295 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 743 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDA 822
Cdd:PLN02466  375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK--DLDE 452

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483048 823 VLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PLN02466  453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 425-896 8.25e-161

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 478.54  E-value: 8.25e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 505 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:TIGR01804  79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL----GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 664
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 744
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 745 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGdl 820
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE-- 391

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483048 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 419-898 2.09e-157

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 470.52  E-value: 2.09e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 419 RMP-HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLME 497
Cdd:PRK13252    3 RQPlQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 498 QHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQArpnrNLTLTRKEPVGVCGIIIPWNYPL 577
Cdd:PRK13252   81 ERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGG----SFVYTRREPLGVCAGIGAWNYPI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 578 MMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKH 657
Cdd:PRK13252  157 QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 658 IMKSCAISnVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 737
Cdd:PRK13252  236 VMAAAAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 738 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR----PGFFFEPTVFTDVEDHMFIAKEESFGPVMIIS 813
Cdd:PRK13252  315 DPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVL 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 814 RFADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYL 893
Cdd:PRK13252  395 TFDDE--DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYT 472


                  ....*
gi 1370483048 894 RVKTV 898
Cdd:PRK13252  473 QIKSV 477
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
 424-900 5.44e-155

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 463.51  E-value: 5.44e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07138     1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGwcdkiQGSTIPINQARPNrnlTLTRKEPVGVCGIIIPWNYPLMMLSWK 583
Cdd:cd07138    79 AQAITLEMGAPITLARAAQVGLGIGHLRAAAD-----ALKDFEFEERRGN---SLVVREPIGVCGLITPWNWPLNQIVLK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScA 663
Cdd:cd07138   151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA-A 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 664 ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 743
Cdd:cd07138   230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 744 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR---PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDl 820
Cdd:cd07138   310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED- 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 821 DAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07138   389 EAI-AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
 472-900 1.40e-154

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 461.81  E-value: 1.40e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 472 FENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIpiNQAR 551
Cdd:cd07118    32 FDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEIEGAADLWRYAASLARTLHGDSY--NNLG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 552 PNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGS 631
Cdd:cd07118   109 DDM-LGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 632 LVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAG 711
Cdd:cd07118   188 TVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGS 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 712 RLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP-RPGFFFEPTV 790
Cdd:cd07118   267 RLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLAsAAGLFYQPTI 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 791 FTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAA 870
Cdd:cd07118   347 FTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPEL 424

                         410       420       430
                  ....*....|....*....|....*....|
gi 1370483048 871 PFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07118   425 PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
FMT_core_FDH_N cd08647
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...
 1-203 1.06e-153

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.


Pssm-ID: 187716 [Multi-domain]  Cd Length: 203  Bit Score: 449.59  E-value: 1.06e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647     1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08647    81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370483048 161 STLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGI 203
Cdd:cd08647   161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
 442-900 1.54e-151

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 454.00  E-value: 1.54e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEnGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKT 521
Cdd:cd07109     2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE-SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 522 HVGMSIQTFRYFAGWCDKIQGSTIPINQArpnrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07109    80 DVEAAARYFEYYGGAADKLHGETIPLGPG----YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 602 TPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 681
Cdd:cd07109   156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDrDTDHGPQNHHAHLVKLMEY 761
Cdd:cd07109   235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGF 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 762 CQHGVKEGATLVCGGNQV---PRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGV 838
Cdd:cd07109   314 VARARARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGV 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483048 839 FTRDINKALYVSDKLQAGTVFVNTYNKT-DVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07109   392 WTRDGDRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 477-900 2.28e-151

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 450.14  E-value: 2.28e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPINqarPNRNL 556
Cdd:cd06534    10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPSP---DPGGE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 636
Cdd:cd06534    86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 637 LSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVE 716
Cdd:cd06534   166 LLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 717 DSIHDEFVRRVVeevrkmkvgnpldrdtdhgpqnhhahlvklmeycqhgvkegatlvcggnqvprpgfffepTVFTDVED 796
Cdd:cd06534   245 ESIYDEFVEKLV------------------------------------------------------------TVLVDVDP 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 797 HMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK-TDVAAPFGGF 875
Cdd:cd06534   265 DMPIAQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGV 342

                         410       420
                  ....*....|....*....|....*
gi 1370483048 876 KQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd06534   343 KNSGIGREGGPYGLEEYTRTKTVVI 367
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
420-900 8.55e-150

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 450.13  E-value: 8.55e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 420 MPHQLFIGGEFVDAEGAkTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQH 499
Cdd:PRK13473    1 MQTKLLINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP--EWSQTTPKERAEALLKLADAIEEN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 500 QEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQG-----------STIpinqarpnrnltltRKEPVGVCG 568
Cdd:PRK13473   78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGkaageyleghtSMI--------------RRDPVGVVA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 569 IIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGF 648
Cdd:PRK13473  144 SIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSL 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 649 TGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 728
Cdd:PRK13473  223 TGSIATGKHVLSAAA-DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLA 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 729 EEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEG-ATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFG 807
Cdd:PRK13473  302 AAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFG 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 808 PVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEA 887
Cdd:PRK13473  382 PVVSVTPFD--DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLY 459

                         490
                  ....*....|...
gi 1370483048 888 ALNEYLRVKTVTF 900
Cdd:PRK13473  460 GLEDYTVVRHVMV 472
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
 424-900 3.81e-149

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 448.56  E-value: 3.81e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07139     1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWcdkiqGSTIPINQARP--NRNLTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07139    81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAAL-----ARDFPFEERRPgsGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07139   156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 662 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:cd07139   235 CG-ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP--GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGD 819
Cdd:cd07139   314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 820 lDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYnKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07139   394 -DAV-RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470


                  .
gi 1370483048 900 F 900
Cdd:cd07139   471 L 471
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
 425-898 6.69e-149

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415 [Multi-domain]  Cd Length: 473  Bit Score: 447.85  E-value: 6.69e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVdaEGAKTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07097     4 YIDGEWV--AGGDGEENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 504 ATIEALDAGAvyTLAL-KTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLTlTRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:cd07097    80 ARLLTREEGK--TLPEaRGEVTRAGQIFRYYAGEALRLSGETLP--STRPGVEVE-TTREPLGVVGLITPWNFPIAIPAW 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSc 662
Cdd:cd07097   155 KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 663 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 742
Cdd:cd07097   234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 743 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP--GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 820
Cdd:cd07097   314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVR--DY 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 821 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-TYNKTDVAAPFGGFKQSGFG-KDLGEAALNEYLRVKTV 898
Cdd:cd07097   392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
 442-900 7.15e-148

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 444.46  E-value: 7.15e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgkISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 521
Cdd:cd07092     2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRR--TTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 522 HVGMSIQTFRYFAGWCDKIQGSTIpiNQARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07092    80 ELPGAVDNFRFFAGAARTLEGPAA--GEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 602 TPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKSPLI 681
Cdd:cd07092   157 TPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADTLKRVHLELGGKAPVI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 761
Cdd:cd07092   235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 762 CQhGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTR 841
Cdd:cd07092   315 VE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSVWTR 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 842 DINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07092   392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
 425-898 6.52e-145

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 437.47  E-value: 6.52e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:cd07088     1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 505 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLTLtRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07088    79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIP--SDRPNENIFI-FKVPIGVVAGILPWNFPFFLIARKL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 664
Cdd:cd07088   155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 665 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 744
Cdd:cd07088   234 ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 745 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP-RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAV 823
Cdd:cd07088   314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFS--SLDEA 391

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 824 LSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07088   392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 422-902 7.35e-145

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 437.93  E-value: 7.35e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQE 501
Cdd:cd07559     1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK--TWGKTSVAERANILNKIADRIEENLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarpnRNLTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07559    79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE----DTLSYHFHEPLGVVGQIIPWNFPLLMAA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07559   155 WKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 662 cAISNVKKVSLELGGKSPLIIFAD-----CDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:cd07559   234 -AAENLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 737 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMII 812
Cdd:cd07559   313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 813 SRFADgdLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 892
Cdd:cd07559   393 ITFKD--EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470

                         490
                  ....*....|
gi 1370483048 893 LRVKTVTFEY 902
Cdd:cd07559   471 QQTKNILVSY 480
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
 442-900 2.73e-142

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 430.13  E-value: 2.73e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 521
Cdd:cd07089     2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 522 HVGMSIQTFRYFAGWCDKIQGS-TIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07089    81 QVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07089   161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKSAN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07089   240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 761 YCQHGVKEGATLVCGGNQVPR--PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFaDGDLDAVlsR-ANATEFGLASG 837
Cdd:cd07089   320 YIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPY-DDDDEAV--RiANDSDYGLSGG 396

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483048 838 VFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07089   397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
 424-894 3.81e-142

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 430.66  E-value: 3.81e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07111    24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQgstipinQARPNRnltltrkEPVGVCGIIIPWNYPLMMLSWK 583
Cdd:cd07111   102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-------TELAGW-------KPVGVVGQIVPWNFPLLMLAWK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 663
Cdd:cd07111   168 ICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 664 ISnVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 743
Cdd:cd07111   247 GT-GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKA 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 744 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAV 823
Cdd:cd07111   326 IDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFR--TAKEA 403

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483048 824 LSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLR 894
Cdd:cd07111   404 VALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
 423-898 1.88e-141

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 429.50  E-value: 1.88e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:PLN02278   26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRWYDLIIANKED 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:PLN02278  104 LAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPF--PDRRL-LVLKQPVGVVGAITPWNFPLAMITR 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PLN02278  180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 663 AiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 742
Cdd:PLN02278  260 A-ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 743 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDA 822
Cdd:PLN02278  339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKT-EEEA 417

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483048 823 VLSrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PLN02278  418 IAI-ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 441-899 1.00e-138

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 420.99  E-value: 1.00e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALk 520
Cdd:cd07110     1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSIQTFRYFAGWCDKIQgstipinqARPNRNLTL--------TRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGN 592
Cdd:cd07110    78 WDVDDVAGCFEYYADLAEQLD--------AKAERAVPLpsedfkarVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGC 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 593 TVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSL 672
Cdd:cd07110   150 TVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 673 ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHH 752
Cdd:cd07110   229 ELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 753 AHLVKLMEYCQHGVKEGATLVCGGN--QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVLSrANAT 830
Cdd:cd07110   309 AQYEKVLSFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED-EAIAL-ANDS 386

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 831 EFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07110   387 EYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
 475-899 9.32e-138

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 418.69  E-value: 9.32e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 475 GRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAvytlALKTH----VGMSIQTFRYFAGWCDKIQGSTIPinqA 550
Cdd:cd07108    33 PEWAATPARERGKLLARIADALEARSEELARLLALETGN----ALRTQarpeAAVLADLFRYFGGLAGELKGETLP---F 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 551 RPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSG 630
Cdd:cd07108   106 GPDV-LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEI-LAQVLPAGVLNVITGYG 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 631 SLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQ---MGMSsvFFNKGENC 707
Cdd:cd07108   184 EECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-DRLIPVSLELGGKSPMIVFPDADLDDAVDgaiAGMR--FTRQGQSC 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 708 IAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKE-GATLVCGGNQVP----RP 782
Cdd:cd07108   261 TAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPLPGegplAD 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 783 GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNT 862
Cdd:cd07108   341 GFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWK--DEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ 418

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1370483048 863 YNKTDVAAPFGGFKQSGFGKDLG-EAALNEYLRVKTVT 899
Cdd:cd07108   419 GGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVN 456
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
 424-902 2.59e-137

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 418.00  E-value: 2.59e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEnGRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07113     2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 504 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPN--RNLTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07113    81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQgeRYTAFTRREPVGVVAGIVPWNFSVMIAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07113   161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 662 cAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:cd07113   240 -AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPT--VFTDVEDHMFiaKEESFGPVMIISRFADGd 819
Cdd:cd07113   319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADSRLM--REETFGPVVSFVPYEDE- 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 820 lDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07113   396 -EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474


                  ...
gi 1370483048 900 FEY 902
Cdd:cd07113   475 IRY 477
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
 422-898 3.71e-134

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 409.92  E-value: 3.71e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQE 501
Cdd:cd07117     1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 502 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarpnRNLTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07117    79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE----DTLSIVLREPIGVVGQIIPWNFPFLMAA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:cd07117   155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 662 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:cd07117   234 AA-KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAd 817
Cdd:cd07117   313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK- 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 818 gDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKT 897
Cdd:cd07117   392 -TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKN 470


                  .
gi 1370483048 898 V 898
Cdd:cd07117   471 I 471
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 425-902 5.93e-134

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 409.43  E-value: 5.93e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAEGAKTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:cd07131     2 YIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 504 ATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWK 583
Cdd:cd07131    80 ARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVP--SELPNKDA-MTRRQPIGVVALITPWNFPVAIPSWK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 584 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 663
Cdd:cd07131   156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 664 ISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 743
Cdd:cd07131   236 RPN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEE 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 744 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR----PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGD 819
Cdd:cd07131   315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV--SS 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 820 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtyNKT---DVAAPFGGFKQSGFG-KDLGEAALNEYLRV 895
Cdd:cd07131   393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTigaEVHLPFGGVKKSGNGhREAGTTALDAFTEW 470


                  ....*..
gi 1370483048 896 KTVTFEY 902
Cdd:cd07131   471 KAVYVDY 477
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
 441-899 1.36e-133

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 407.53  E-value: 1.36e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALK 520
Cdd:cd07107     1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AML 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07107    78 GDVMVAAALLDYFAGLVTELKGETIPV----GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 601 VTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07107   154 QAPLSALRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA-EGIKHVTLELGGKNAL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 681 IIFADCDLNKAVQ---MGMSsvFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 757
Cdd:cd07107   232 IVFPDADPEAAADaavAGMN--FTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 758 LMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgdLDAVLSRANATEFG 833
Cdd:cd07107   310 VMHYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRD--EAEMVAQANGVEYG 387

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483048 834 LASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07107   388 LTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
 477-900 2.88e-133

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 406.53  E-value: 2.88e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGwcdkiqgSTIP--INQARPNR 554
Cdd:cd07106    35 WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGGAVAWLRYTAS-------LDLPdeVIEDDDTR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 555 NLTLTRKePVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLvG 634
Cdd:cd07106   107 RVELRRK-PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGEL-AQEVLPPGVLNVVSGGDEL-G 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 635 QRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAV-QMGMSSvFFNKGENCIAAGRL 713
Cdd:cd07106   184 PALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPDVDIDAVApKLFWGA-FINSGQVCAAIKRL 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 714 FVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTD 793
Cdd:cd07106   262 YVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDD 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 794 VEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFG 873
Cdd:cd07106   342 PPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFG 419

                         410       420
                  ....*....|....*....|....*..
gi 1370483048 874 GFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07106   420 GHKQSGIGVEFGIEGLKEYTQTQVINI 446
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
 423-898 3.31e-132

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 405.43  E-value: 3.31e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:PRK09847   21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:PRK09847  101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS----SHELAMIVREPVGVIAAIVPWNFPLLLTCW 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:PRK09847  177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 663 AISNVKKVSLELGGKSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:PRK09847  257 GDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGfFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdGDLD 821
Cdd:PRK09847  337 PATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFT-SEEQ 413

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370483048 822 AvLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PRK09847  414 A-LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
 440-900 5.16e-132

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 403.51  E-value: 5.16e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL 519
Cdd:cd07149     2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK--SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 520 KtHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 598
Cdd:cd07149    80 K-EVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 599 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHImksCAISNVKKVSLELGGKS 678
Cdd:cd07149   159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI---ARKAGLKKVTLELGSNA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 679 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 758
Cdd:cd07149   236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERI 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 759 MEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGV 838
Cdd:cd07149   316 EEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFD--TLDEAIAMANDSPYGLQAGV 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 839 FTRDINKALYVSDKLQAGTVFVN---TYnKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07149   391 FTNDLQKALKAARELEVGGVMINdssTF-RVD-HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
 443-899 3.86e-128

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 393.23  E-value: 3.86e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 443 NPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL-KT 521
Cdd:cd07150     5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWfET 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 522 HVGMSIqtFRYFAGWCDKIQGSTIPinQARPNRnLTLTRKEPVGVCGIIIPWNYPLMmLSWKTAA-CLAAGNTVVIKPAQ 600
Cdd:cd07150    83 TFTPEL--LRAAAGECRRVRGETLP--SDSPGT-VSMSVRRPLGVVAGITPFNYPLI-LATKKVAfALAAGNTVVLKPSE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 601 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 680
Cdd:cd07150   157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 681 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 760
Cdd:cd07150   236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 761 YCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAvLSRANATEFGLASGVFT 840
Cdd:cd07150   316 QVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKD-AEEA-LELANDTEYGLSAAILT 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 841 RDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07150   391 NDLQRAFKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
 477-899 3.52e-127

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 389.97  E-value: 3.52e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYtlaLKTH--VGMSIQTFRYFAGWCDKIQGSTIPinQARPNR 554
Cdd:cd07104    16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTR---PKAAfeVGAAIAILREAAGLPRRPEGEILP--SDVPGK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 555 nLTLTRKEPVGVCGIIIPWNYPLMmLSWKTAA-CLAAGNTVVIKPAQVTPLT-ALKFAELTLKAGIPKGVVNVLPGSGSL 632
Cdd:cd07104    91 -ESMVRRVPLGVVGVISPFNFPLI-LAMRSVApALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 633 VGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGR 712
Cdd:cd07104   169 IGDALVEHPRVRMISFTGSTAVGRHIGELAG-RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGR 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 713 LFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqvPRPGFFFEPTVFT 792
Cdd:cd07104   248 ILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG---TYEGLFYQPTVLS 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 793 DVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKtDVAA 870
Cdd:cd07104   325 DVTPDMPIFREEIFGPVAPVIPFDD-DEEAV-ELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdqTVND-EPHV 401

                         410       420
                  ....*....|....*....|....*....
gi 1370483048 871 PFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07104   402 PFGGVKASGGGRFGGPASLEEFTEWQWIT 430
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
 440-898 5.91e-127

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 390.56  E-value: 5.91e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAl 519
Cdd:cd07145     2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 520 KTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 598
Cdd:cd07145    79 RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 599 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKS 678
Cdd:cd07145   159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASK-AGGTGKKVALELGGSD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 679 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 758
Cdd:cd07145   238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 759 MEYCQHGVKEGATLVCGGNQVprPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLASGV 838
Cdd:cd07145   318 ENLVNDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDE-EAV-EIANSTEYGLQASV 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483048 839 FTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07145   394 FTNDINRALKVARELEAGGVVINdsTRFRWD-NLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454
PLN02467 PLN02467
betaine aldehyde dehydrogenase
 423-899 2.83e-125

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 387.94  E-value: 2.83e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGR---WGKISARDRGRLMYRLADLMEQH 499
Cdd:PLN02467    9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKgkdWARTTGAVRAKYLRAIAAKITER 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 500 QEELATIEALDAGAVYTLALKTHVGMSiQTFRYFAGWCDKIQGS-----TIPINQARPNrnltlTRKEPVGVCGIIIPWN 574
Cdd:PLN02467   89 KSELAKLETLDCGKPLDEAAWDMDDVA-GCFEYYADLAEALDAKqkapvSLPMETFKGY-----VLKEPLGVVGLITPWN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 575 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEV 654
Cdd:PLN02467  163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 655 GKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKM 734
Cdd:PLN02467  243 GRKIMTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 735 KVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGN--QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMII 812
Cdd:PLN02467  322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 813 SRFADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 892
Cdd:PLN02467  402 KTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENY 479


                  ....*..
gi 1370483048 893 LRVKTVT 899
Cdd:PLN02467  480 LSVKQVT 486
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
 441-899 1.05e-119

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 371.68  E-value: 1.05e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:cd07120     1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSIQTFRYFAGWCDKIQGSTIpinQARPNrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 600
Cdd:cd07120    79 FEISGAISELRYYAGLARTEAGRMI---EPEPG-SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 601 VTPLTALKFAELTLKA-GIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSP 679
Cdd:cd07120   155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTP 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 680 LIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLM 759
Cdd:cd07120   234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 760 EYCQHGVKEGATLVCGGNQVPR---PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLAS 836
Cdd:cd07120   314 RMVERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA-EAV-ALANDTDYGLAA 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483048 837 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07120   392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
 425-902 9.88e-117

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 364.58  E-value: 9.88e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAeGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:cd07086     2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEALG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 505 TIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07086    79 RLVSLEMGKILPEGL-GEVQEMIDICDYAVGLSRMLYGLTIP--SERPGHRL-MEQWNPLGVVGVITAFNFPVAVPGWNA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKA----GIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07086   155 AIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 661 SCAISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 740
Cdd:cd07086   234 TVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 741 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR--PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadG 818
Cdd:cd07086   313 DEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF--D 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 819 DLDAVLSRANATEFGLASGVFTRDINKAL-YVSDK-LQAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRV 895
Cdd:cd07086   391 SLEEAIAINNDVPQGLSSSIFTEDLREAFrWLGPKgSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRR 470


                  ....*..
gi 1370483048 896 KTVTFEY 902
Cdd:cd07086   471 STCTINY 477
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
422-896 1.76e-116

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 364.23  E-value: 1.76e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 422 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQE 501
Cdd:PRK11241   11 QQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 502 ELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLtLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:PRK11241   89 DLARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQ--ADKRL-IVIKQPIGVTAAITPWNFPAAMIT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:PRK11241  165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQ 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 662 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:PRK11241  245 CA-KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 742 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLD 821
Cdd:PRK11241  324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF--KDEA 401

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 822 AVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:PRK11241  402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
 477-898 2.99e-114

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 356.38  E-value: 2.99e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAgwcDKI----QGSTIPINQARp 552
Cdd:cd07100    15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYA---ENAeaflADEPIETDAGK- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 553 nrnlTLTRKEPVGVCGIIIPWNYPLmmlsWKT----AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPG 628
Cdd:cd07100    90 ----AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 629 SGSLVGQrLSDHPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCI 708
Cdd:cd07100   162 DSDQVEA-IIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 709 AAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEP 788
Cdd:cd07100   240 AAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPP 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 789 TVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAV-LsrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTD 867
Cdd:cd07100   320 TVLTDVTPGMPAYDEELFGPVAAVIKVKDEE-EAIaL--ANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSD 396

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1370483048 868 VAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07100   397 PRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
 440-900 2.52e-111

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 349.42  E-value: 2.52e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL 519
Cdd:cd07094     2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 520 KtHVGMSIQTFRYFAGWCDKIQGSTIP--INQARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIK 597
Cdd:cd07094    80 V-EVDRAIDTLRLAAEEAERIRGEEIPldATQGSDNR-LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 598 PAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMkscAISNVKKVSLELGGK 677
Cdd:cd07094   158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALR---ANAGGKRIALELGGN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 678 SPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 757
Cdd:cd07094   235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 758 LMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASG 837
Cdd:cd07094   315 VERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAG 389

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 838 VFTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07094   390 IFTRDLNVAFKAAEKLEVGGVMVNdsSAFRTD-WMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
 425-902 1.68e-110

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.


Pssm-ID: 143434 [Multi-domain]  Cd Length: 479  Bit Score: 348.29  E-value: 1.68e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:cd07116     4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE--AWGKTSVAERANILNKIADRMEANLEMLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 505 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07116    82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEID----ENTVAYHFHEPLGVVGQIIPWNFPLLMATWKL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 585 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAI 664
Cdd:cd07116   158 APALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY-AS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 665 SNVKKVSLELGGKSPLIIFADCD------LNKAVQmGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGN 738
Cdd:cd07116   236 ENIIPVTLELGGKSPNIFFADVMdaddafFDKALE-GFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 739 PLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDvEDHMFIAKEESFGPVMIISR 814
Cdd:cd07116   315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGgllgGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTT 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 815 FAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLR 894
Cdd:cd07116   394 FK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471


                  ....*...
gi 1370483048 895 VKTVTFEY 902
Cdd:cd07116   472 TKNLLVSY 479
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
 428-899 2.93e-107

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 339.28  E-value: 2.93e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 428 GEFVDAEGAKTSETINPTDGSVICQVSLAqvTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIE 507
Cdd:cd07151     1 GEWRDGTSERTIDVLNPYTGETLAEIPAA--SKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 508 ALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPIN-QARPNRnltlTRKEPVGVCGIIIPWNYPLMMLSWKTAA 586
Cdd:cd07151    79 IRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvPGKENR----VYREPLGVVGVISPWNFPLHLSMRSVAP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 587 CLAAGNTVVIKPAQVTPLTA-LKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiS 665
Cdd:cd07151   154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG-R 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 666 NVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTD 745
Cdd:cd07151   233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 746 HGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqvPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFaDGDLDAVlS 825
Cdd:cd07151   313 VGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKA-DDEEEAL-E 387

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 826 RANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07151   388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
 424-899 5.80e-106

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 337.27  E-value: 5.80e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGakTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:cd07124    35 LVIGGKEVRTEE--KIESRNPADPSeVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGStiPINQARPNRNLTltRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:cd07124   111 LAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGF--PVEMVPGEDNRY--VYRPLGVGAVISPWNFPLAILAG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:cd07124   186 MTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERA 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 663 A-----ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 737
Cdd:cd07124   266 AkvqpgQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVG 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 738 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNqVPRP---GFFFEPTVFTDVEDHMFIAKEESFGPVMIISR 814
Cdd:cd07124   346 DPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE-VLELaaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 815 FAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGtvfvNTY-NKTDVAA-----PFGGFKQSGFG-KDLGEA 887
Cdd:cd07124   424 AK--DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVG----NLYaNRKITGAlvgrqPFGGFKMSGTGsKAGGPD 497

                         490
                  ....*....|..
gi 1370483048 888 ALNEYLRVKTVT 899
Cdd:cd07124   498 YLLQFMQPKTVT 509
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
 477-899 2.24e-105

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 333.80  E-value: 2.24e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKI-QGSTIPINQARPNRN 555
Cdd:cd07099    34 WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEVLLALEAIDWAARNAPRVlAPRKVPTGLLMPNKK 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 556 LTLTRkEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQ 635
Cdd:cd07099   113 ATVEY-RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 636 RLSDHPdVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:cd07099   191 ALIDAG-VDKVAFTGSVATGRKVMAAAA-ERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYV 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 716 EDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVE 795
Cdd:cd07099   269 HESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVP 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 796 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKTDVAAPFG 873
Cdd:cd07099   349 HDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINdvLLTAGIPALPFG 426

                         410       420
                  ....*....|....*....|....*.
gi 1370483048 874 GFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07099   427 GVKDSGGGRRHGAEGLREFCRPKAIA 452
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
 489-902 1.68e-102

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 324.77  E-value: 1.68e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 489 MYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINqaRPNRNLtLTRKEPVGVCG 568
Cdd:PRK10090    1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSD--RPGENI-LLFKRALGVTT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 569 IIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGF 648
Cdd:PRK10090   77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 649 TGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 728
Cdd:PRK10090  157 TGSVSAGEKIMAAAA-KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 729 EEVRKMKVGNPLDRDT-DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFG 807
Cdd:PRK10090  236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 808 PVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEA 887
Cdd:PRK10090  316 PVLPVVAFD--TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKH 393

                         410
                  ....*....|....*
gi 1370483048 888 ALNEYLRVKTVTFEY 902
Cdd:PRK10090  394 GLHEYLQTQVVYLQS 408
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 423-899 2.20e-102

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 326.78  E-value: 2.20e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 423 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:cd07085     2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNlTLTRKEPVGVCGIIIPWNYPLMMLSW 582
Cdd:cd07085    80 LARLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLE--NVARGID-TYSYRQPLGVVAGITPFNFPAMIPLW 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVgQRLSDHPDVRKIGFTGSTEVGKHIMKSc 662
Cdd:cd07085   156 MFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYER- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 663 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 742
Cdd:cd07085   234 AAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 743 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRfADg 818
Cdd:cd07085   314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR-VD- 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 819 DLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynkTDVAAP-----FGGFKQSGFGkDL---GEAALN 890
Cdd:cd07085   392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLhfyGKDGVR 466


                  ....*....
gi 1370483048 891 EYLRVKTVT 899
Cdd:cd07085   467 FYTQTKTVT 475
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
 440-896 5.29e-102

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 324.97  E-value: 5.29e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAl 519
Cdd:cd07147     2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMR--ALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 520 KTHVGMSIQTFRYFAGWCDKIQGSTIPIN-QARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 598
Cdd:cd07147    79 RGEVARAIDTFRIAAEEATRIYGEVLPLDiSARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 599 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAisnVKKVSLELGGKS 678
Cdd:cd07147   159 ASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAG---KKKVVLELGGNA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 679 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 758
Cdd:cd07147   235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 759 MEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGV 838
Cdd:cd07147   315 EGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQAGV 389

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483048 839 FTRDINKALYVSDKLQAGTVFVNtynktDV------AAPFGGFKQSGFGKDLGEAALNEYLRVK 896
Cdd:cd07147   390 FTRDLEKALRAWDELEVGGVVIN-----DVptfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
 476-899 1.05e-99

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 318.87  E-value: 1.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 476 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK--THVGMsiqTFRYFAGWCDKI-----QGSTIPIn 548
Cdd:cd07101    33 AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEevLDVAI---VARYYARRAERLlkprrRRGAIPV- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 549 qarpnrnLTLTR--KEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL 626
Cdd:cd07101   109 -------LTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVV 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 627 PGSGSLVGQRLSDHPDVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGEN 706
Cdd:cd07101   182 TGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQL 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 707 CIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPG-FF 785
Cdd:cd07101   259 CVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGpYF 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 786 FEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN---- 861
Cdd:cd07101   339 YEPTVLTGVTEDMELFAEETFGPVVSIYRVADDD-EAI-ELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegya 416

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1370483048 862 -TYNKTDvaAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:cd07101   417 aAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
 477-900 1.04e-98

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 315.67  E-value: 1.04e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRnL 556
Cdd:cd07105    16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWA-GFNVDLAAGMLREAASLITQIIGGSIP--SDKPGT-L 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL---PGSGSLV 633
Cdd:cd07105    92 AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 634 GQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRL 713
Cdd:cd07105   172 VEALIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERI 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 714 FVEDSIHDEFVRRVVEEVRKMKVGnpldrDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP-GFFFEPTVFT 792
Cdd:cd07105   251 IVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPsGTSMPPTILD 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 793 DVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-AP 871
Cdd:cd07105   326 NVTPDMDIYSEESFGPVVSIIRVKD-EEEAV-RIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEPtLP 403

                         410       420
                  ....*....|....*....|....*....
gi 1370483048 872 FGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07105   404 HGGVKSSGYGRFNGKWGIDEFTETKWITI 432
D1pyr5carbox2 TIGR01237
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...
 424-899 1.61e-96

delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]


Pssm-ID: 200087 [Multi-domain]  Cd Length: 511  Bit Score: 312.57  E-value: 1.61e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGAKTSetINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:TIGR01237  35 LVINGERVETENKIVS--INPCDKSeVVGTVSKASQEHAEHALQAAAKAFEA--WKKTDPEERAAILFKAAAIVRRRRHE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTiPINQARPNRNLTLTrkEPVGVCGIIIPWNYPLMMLSW 582
Cdd:TIGR01237 111 FSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGK-PVNSREGETNQYVY--TPTGVTVVISPWNFPFAIMVG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 583 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 662
Cdd:TIGR01237 187 MTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 663 AI-----SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 737
Cdd:TIGR01237 267 AKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVG 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 738 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAd 817
Cdd:TIGR01237 347 PPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS- 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 818 gDLDAVLSRANATEFGLASGVFTRD---INKAlyvSDKLQAGTVFvntYNKTDVAA-----PFGGFKQSGFG-KDLGEAA 888
Cdd:TIGR01237 425 -DFDEALEIANNTEYGLTGGVISNNrdhINRA---KAEFEVGNLY---FNRNITGAivgyqPFGGFKMSGTDsKAGGPDY 497

                         490
                  ....*....|.
gi 1370483048 889 LNEYLRVKTVT 899
Cdd:TIGR01237 498 LALFMQAKTVT 508
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
 476-899 1.38e-95

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 310.27  E-value: 1.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 476 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK--THVGMsiqTFRYFAGWCDKI-----QGSTIPIn 548
Cdd:PRK09407   69 AWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEevLDVAL---TARYYARRAPKLlaprrRAGALPV- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 549 qarpnrnLTLTR--KEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL 626
Cdd:PRK09407  145 -------LTKTTelRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVV 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 627 PGSGSLVGQRLSDHPDVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGEN 706
Cdd:PRK09407  218 TGPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAG-RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQL 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 707 CIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqVPRP--G- 783
Cdd:PRK09407  295 CISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGG--KARPdlGp 372

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 784 FFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-- 861
Cdd:PRK09407  373 LFYEPTVLTGVTPDMELAREETFGPVVSVYPVA--DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeg 450

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1370483048 862 ---TYNKTDvaAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 899
Cdd:PRK09407  451 yaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
 477-888 2.75e-94

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 304.22  E-value: 2.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVytlALKTH--VGMSIQTFRYFAGWCDKIQGSTIPINQARpnr 554
Cdd:cd07152    29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSI---RPKAGfeVGAAIGELHEAAGLPTQPQGEILPSAPGR--- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 555 nLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTA-LKFAELTLKAGIPKGVVNVLPGsGSLV 633
Cdd:cd07152   103 -LSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GADA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 634 GQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRL 713
Cdd:cd07152   181 GEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRH 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 714 FVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTD 793
Cdd:cd07152   260 LVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YDGLFYRPTVLSG 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 794 VEDHMFIAKEESFGPVMIISRFADGDLDAVLsrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKtDVAAP 871
Cdd:cd07152   337 VKPGMPAFDEEIFGPVAPVTVFDSDEEAVAL--ANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINdqTVND-EPHNP 413

                         410
                  ....*....|....*..
gi 1370483048 872 FGGFKQSGFGKDLGEAA 888
Cdd:cd07152   414 FGGMGASGNGSRFGGPA 430
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
 425-881 6.36e-94

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 304.11  E-value: 6.36e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAEGaKTSETINPTDGSVICQVSLaqvTDVDKAVAAAKDAFENGRWGK--ISARDRGRLMYRLADLMEQHQEE 502
Cdd:cd07082     5 LINGEWKESSG-KTIEVYSPIDGEVIGSVPA---LSALEILEAAETAYDAGRGWWptMPLEERIDCLHKFADLLKENKEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:cd07082    81 VANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGkIAQVRREPLGVVLAIGPFNYPLNLTV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKs 661
Cdd:cd07082   160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 662 caISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 741
Cdd:cd07082   239 --QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 742 RDTDHGP---QNHHAHLVKLMEycqHGVKEGATLVCGGNQvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdg 818
Cdd:cd07082   317 NGVDITPlidPKSADFVEGLID---DAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN-- 389

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 819 DLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK--TDVaAPFGGFKQSGFG 881
Cdd:cd07082   390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgPDH-FPFLGRKDSGIG 453
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
 424-879 2.98e-93

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 303.78  E-value: 2.98e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGAKTSetINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:PRK03137   39 LIIGGERITTEDKIVS--INPANKSeVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHE 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKI-QGStiPINQaRPNRNLTLtRKEPVGVCGIIIPWNYPLMMLS 581
Cdd:PRK03137  115 FSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLaDGK--PVES-RPGEHNRY-FYIPLGVGVVISPWNFPFAIMA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 582 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 661
Cdd:PRK03137  190 GMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYER 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 662 CAISN-----VKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:PRK03137  270 AAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTV 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 737 GNPLDrDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 816
Cdd:PRK03137  350 GNPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483048 817 dgDLDAVLSRANATEFGLASGVFTRD---INKA--------LYVSDKLQAGTVFVNtynktdvaaPFGGFKQSG 879
Cdd:PRK03137  428 --DFDHALEIANNTEYGLTGAVISNNrehLEKArrefhvgnLYFNRGCTGAIVGYH---------PFGGFNMSG 490
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
 477-900 1.07e-91

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.


Pssm-ID: 143416 [Multi-domain]  Cd Length: 465  Bit Score: 298.06  E-value: 1.07e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavytlalKTHVGMS---IQTFryfagwCDKIQ-----GSTIPIN 548
Cdd:cd07098    34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTG-------KTMVDASlgeILVT------CEKIRwtlkhGEKALRP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 549 QARPNRNLTLTRK-----EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKA----GIP 619
Cdd:cd07098   101 ESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHD 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 620 KGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKsCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSV 699
Cdd:cd07098   181 PDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMA-AAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGT 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 700 FFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQV 779
Cdd:cd07098   259 FQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRY 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 780 PRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQA 855
Cdd:cd07098   339 PHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASD-DEEAV-EIANSTEYGLGASVFGKDIKRARRIASQLET 416

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1370483048 856 GTVFVNTYNKT--DVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07098   417 GMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
 440-899 8.74e-91

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 295.04  E-value: 8.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 440 ETINPTDGSVIcqvslAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavytLAL 519
Cdd:cd07146     2 EVRNPYTGEVV-----GTVPAGTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESG----LCL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 520 KT---HVGMSIQTFRYFAGWCDKIQGSTIPINQARP-NRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVV 595
Cdd:cd07146    73 KDtryEVGRAADVLRFAAAEALRDDGESFSCDLTANgKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 596 IKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHImksCAISNVKKVSLELG 675
Cdd:cd07146   153 LKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 676 GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 755
Cdd:cd07146   230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 756 VKLMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 835
Cdd:cd07146   310 IQIENRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGLS 384

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483048 836 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLG-EAALNEYLRVKTVT 899
Cdd:cd07146   385 SGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGGKEGvREAMKEMTNVKTYS 450
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
 442-900 1.23e-84

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 278.75  E-value: 1.23e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 442 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 521
Cdd:cd07102     1 ISPIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 522 HVGMsIQTFRYFAGWCDKIQGSTIPINQARPNRNLtltRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 601
Cdd:cd07102    79 IRGM-LERARYMISIAEEALADIRVPEKDGFERYI---RREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 602 TPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 681
Cdd:cd07102   155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAA-GRFIKVGLELGGKDPAY 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 682 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 761
Cdd:cd07102   233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 762 CQHGVKEGATLVCGGNQVPRP---GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAVLsRANATEFGLASGV 838
Cdd:cd07102   313 IADAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKS-DAEAIA-LMNDSEYGLTASV 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483048 839 FTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:cd07102   391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
 441-898 1.09e-82

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 273.92  E-value: 1.09e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:PRK09406    5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYR--TTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-K 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSIQTFRYFAGWCDKIQGSTiPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLmmlsWKT----AACLAAGNTVVI 596
Cdd:PRK09406   82 AEALKCAKGFRYYAEHAEALLADE-PADAAAVGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 597 KPAQVTPLTALKFAELTLKAGIPKGV-VNVLPGSGSlVGQRLSDhPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELG 675
Cdd:PRK09406  157 KHASNVPQTALYLADLFRRAGFPDGCfQTLLVGSGA-VEAILRD-PRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 676 GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 755
Cdd:PRK09406  234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 756 VKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 835
Cdd:PRK09406  314 DEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVA--DIDEAIEIANATTFGLG 391

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483048 836 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PRK09406  392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
 424-881 4.38e-78

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 263.29  E-value: 4.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGAktsETINPTDG-SVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEE 502
Cdd:cd07125    36 IINGEETETGEGA---PVIDPADHeRTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 503 LATIEALDAGAvyTLAlKTHVGMS--IQTFRYFAGWCDKIQGSTIPINQARPNRNLTLtrkEPVGVCGIIIPWNYPLMML 580
Cdd:cd07125   111 LIALAAAEAGK--TLA-DADAEVReaIDFCRYYAAQARELFSDPELPGPTGELNGLEL---HGRGVFVCISPWNFPLAIF 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 581 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07125   185 TGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINR 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 661 SCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGN 738
Cdd:cd07125   265 ALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGD 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 739 PLDRDTDHGP-------QNHHAHlvklmeyCQHGVKEgATLVCggnQVPRP---GFFFEPTVFTDVEDhmFIAKEESFGP 808
Cdd:cd07125   345 PWDLSTDVGPlidkpagKLLRAH-------TELMRGE-AWLIA---PAPLDdgnGYFVAPGIIEIVGI--FDLTTEVFGP 411

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 809 VMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGtvfvNTY-NKTDVAA-----PFGGFKQSGFG 881
Cdd:cd07125   412 ILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYiNRNITGAivgrqPFGGWGLSGTG 486
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
1-309 4.77e-77

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 253.49  E-value: 4.77e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:COG0223     1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQPESLKD-----PEFLEELR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:COG0223    76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:COG0223   156 GPDDTAGSLHDK-LAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAF 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 235 TEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPGVVTKAG----LILFGndDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:COG0223   235 TTLDGKRLKIWKARV-----------LEEAGGGAPGTILAVDkdglLVACG--DGALRLLELQPAGKKRMSAADFLRGY 300
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
 416-899 1.72e-73

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 250.19  E-value: 1.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 416 RTVRMPH-QLFIGGEFVDAEGAKTSetINPTD-GSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLA 493
Cdd:cd07083    12 KEEFGRAyPLVIGGEWVDTKERMVS--VSPFApSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 494 DLMEQHQEELATIEALDAGAVYTLALKThVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCgiIIPW 573
Cdd:cd07083    88 DLLRRRRRELIATLTYEVGKNWVEAIDD-VAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVV--ISPW 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 574 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTE 653
Cdd:cd07083   165 NFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 654 VGKHIMKSCA-----ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 728
Cdd:cd07083   245 TGKKIYEAAArlapgQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 729 EEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGP 808
Cdd:cd07083   325 KRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGP 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 809 VMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAA--PFGGFKQSGFG-KDLG 885
Cdd:cd07083   404 VLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGTNaKTGG 483

                         490
                  ....*....|....
gi 1370483048 886 EAALNEYLRVKTVT 899
Cdd:cd07083   484 PHYLRRFLEMKAVA 497
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
 435-902 3.62e-72

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 245.58  E-value: 3.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 435 GAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAV 514
Cdd:cd07130    10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 515 YTLAL----------KTHVGMSIQtfryfagwcdkIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:cd07130    88 LPEGLgevqemidicDFAVGLSRQ-----------LYGLTIP--SERPGHRM-MEQWNPLGVVGVITAFNFPVAVWGWNA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 585 AACLAAGNTVVIKPAQVTPLTALK----FAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMK 660
Cdd:cd07130   154 AIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 661 SCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQmgmsSVFF----NKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 736
Cdd:cd07130   233 AVA-ARFGRSLLELGGNNAIIVMEDADLDLAVR----AVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRI 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 737 GNPLDRDTDHGPQnHHAHLVKLMEYC-QHGVKEGATLVCGGNQVPRPGFFFEPTVFTdVEDHMFIAKEESFGPVMIISRF 815
Cdd:cd07130   308 GDPLDDGTLVGPL-HTKAAVDNYLAAiEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKF 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 816 AdgDLDAVLSRANATEFGLASGVFTRDINKAL-----YVSDklqAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAAL 889
Cdd:cd07130   386 D--TLEEAIAWNNEVPQGLSSSIFTTDLRNAFrwlgpKGSD---CGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAW 460

                         490
                  ....*....|...
gi 1370483048 890 NEYLRVKTVTFEY 902
Cdd:cd07130   461 KQYMRRSTCTINY 473
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 1-180 2.56e-66

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 219.47  E-value: 2.56e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVI--GQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGA 78
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  79 ELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDD 158
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160

                         170       180
                  ....*....|....*....|..
gi 1370483048 159 TVSTLYNRFLFPEGiKGMVQAV 180
Cdd:pfam00551 161 TAETLYNRVADLEH-KALPRVL 181
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
 441-898 7.70e-66

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 228.21  E-value: 7.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 441 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 520
Cdd:PRK13968   11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 521 THVGMSiqtfryfAGWCDKIQGSTIPINQARPN---RNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIK 597
Cdd:PRK13968   88 AEVAKS-------ANLCDWYAEHGPAMLKAEPTlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 598 PAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDhPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELGGK 677
Cdd:PRK13968  161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAI-GAQAGAALKKCVLELGGS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 678 SPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 757
Cdd:PRK13968  239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 758 LMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISrfADGDLDAVLSRANATEFGLASG 837
Cdd:PRK13968  319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAIT--VAKDAEHALELANDSEFGLSAT 396

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483048 838 VFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PRK13968  397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
 440-881 1.77e-62

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 218.44  E-value: 1.77e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 440 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEN-GRWgkISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLA 518
Cdd:cd07148     2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 519 lKTHVGMSIQTFRYFAGWCDKIQGSTIPIN--QARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVI 596
Cdd:cd07148    80 -KVEVTRAIDGVELAADELGQLGGREIPMGltPASAGR-IAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 597 KPAQVTPLTALKFAELTLKAGIPKGVVNVLPgSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNvkKVSLELGG 676
Cdd:cd07148   158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RCALEHGG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 677 KSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLV 756
Cdd:cd07148   235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 757 KLMEYCQHGVKEGATLVCGGNQVPRPgfFFEPTVFTDVEDHMFIAKEESFGPVMIIsrFADGDLDAVLSRANATEFGLAS 836
Cdd:cd07148   315 RVEEWVNEAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCV--YSYDDLDEAIAQANSLPVAFQA 390

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1370483048 837 GVFTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFG 881
Cdd:cd07148   391 AVFTKDLDVALKAVRRLDATAVMVNdhTAFRVD-WMPFAGRRQSGYG 436
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
 560-886 7.85e-60

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 210.55  E-value: 7.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVnVLPGsGSLVGQRLSD 639
Cdd:cd07134    97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-DAEVAQALLE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 640 HPdVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSI 719
Cdd:cd07134   175 LP-FDHIFFTGSPAVGKIVMAAAA-KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESV 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 720 HDEFVRRVVEEVRKMKVGNPLDRDTDHGP----QNHHAHLVKLMEycqHGVKEGATLVCGGnQVPRPGFFFEPTVFTDVE 795
Cdd:cd07134   253 KDAFVEHLKAEIEKFYGKDAARKASPDLArivnDRHFDRLKGLLD---DAVAKGAKVEFGG-QFDAAQRYIAPTVLTNVT 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 796 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynktDVAA----- 870
Cdd:cd07134   329 PDMKIMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-----DVVLhflnp 401

                         330
                  ....*....|....*...
gi 1370483048 871 --PFGGFKQSGFGKDLGE 886
Cdd:cd07134   402 nlPFGGVNNSGIGSYHGV 419
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
 560-898 9.78e-59

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.


Pssm-ID: 143406 [Multi-domain]  Cd Length: 426  Bit Score: 206.99  E-value: 9.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSlVGQRLSD 639
Cdd:cd07087    97 IPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-VATALLA 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 640 HP-DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDS 718
Cdd:cd07087   175 EPfD--HIFFTGSPAVGKIVMEAAA-KHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 719 IHDEFVRRVVEEVRKMkVGNPLDRDTDHGPQNHHAHLVKLMEYcqhgvKEGATLVCGGnQVPRPGFFFEPTVFTDVEDHM 798
Cdd:cd07087   252 IKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASL-----LDDGKVVIGG-QVDKEERYIAPTILDDVSPDS 324

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 799 FIAKEESFGPVM-IISRfadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynktDV-------AA 870
Cdd:cd07087   325 PLMQEEIFGPILpILTY---DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN-----DVllhaaipNL 396

                         330       340
                  ....*....|....*....|....*...
gi 1370483048 871 PFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07087   397 PFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 477-879 2.62e-58

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 205.97  E-value: 2.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGA--------VYTLALKthVGMSIQTFRYFAGwcDKiqgsTIPIN 548
Cdd:cd07095    16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKplweaqteVAAMAGK--IDISIKAYHERTG--ER----ATPMA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 549 QARpnrnlTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPG 628
Cdd:cd07095    88 QGR-----AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 629 SGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCI 708
Cdd:cd07095   163 GRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCT 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 709 AAGRLFVEDS-IHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFE 787
Cdd:cd07095   242 CARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLS 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 788 PTVF--TDVEDHmfiAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDinKALY--VSDKLQAGTVFVN-T 862
Cdd:cd07095   322 PGIIdvTDAADV---PDEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDD--EALFerFLARIRAGIVNWNrP 394

                         410
                  ....*....|....*..
gi 1370483048 863 YNKTDVAAPFGGFKQSG 879
Cdd:cd07095   395 TTGASSTAPFGGVGLSG 411
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
425-881 4.39e-54

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 203.89  E-value: 4.39e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  425 FIGGEFVDAEGAKTsETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:PRK11904   551 WQAGPIINGEGEAR-PVVSPADRRrVVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEANRAEL 627

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  504 ATIEALDAGavytlalKT-HVGMS-----IQTFRYFAgwcdkiqgstipiNQARpnRNLTLTRKEP-------------- 563
Cdd:PRK11904   628 IALCVREAG-------KTlQDAIAevreaVDFCRYYA-------------AQAR--RLFGAPEKLPgptgesnelrlhgr 685

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  564 -VGVCgiIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPD 642
Cdd:PRK11904   686 gVFVC--ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPR 763

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  643 VRKIGFTGSTEVGKHI-----MKSCAIsnvkkVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:PRK11904   764 IAGVAFTGSTETARIInrtlaARDGPI-----VPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFV 838

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  716 EDSIHDefvrRVVE----EVRKMKVGNPLDRDTDHGP---QNHHAhlvKLMEYCQHgVKEGATLVCggnQVPRP-----G 783
Cdd:PRK11904   839 QEDIAD----RVIEmlkgAMAELKVGDPRLLSTDVGPvidAEAKA---NLDAHIER-MKREARLLA---QLPLPagtenG 907

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  784 FFFEPTVFtdvE-DHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVnt 862
Cdd:PRK11904   908 HFVAPTAF---EiDSISQLEREVFGPILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYV-- 982

                          490       500
                   ....*....|....*....|....
gi 1370483048  863 yNKTDVAA-----PFGGFKQSGFG 881
Cdd:PRK11904   983 -NRNQIGAvvgvqPFGGQGLSGTG 1005
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
 477-885 1.12e-53

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273518 [Multi-domain]  Cd Length: 500  Bit Score: 195.13  E-value: 1.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAgwcdkiqgstipiNQARpnRNL 556
Cdd:TIGR01238  90 WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAI-AEVREAVDFCRYYA-------------KQVR--DVL 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 636
Cdd:TIGR01238 154 GEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 637 LSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLF 714
Cdd:TIGR01238 234 LTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLC 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 715 VEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGP-------QNHHAHLVKlMEYCQHGVKEgatLVCGGNQVPRPGFFFE 787
Cdd:TIGR01238 314 VQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPvidaeakQNLLAHIEH-MSQTQKKIAQ---LTLDDSRACQHGTFVA 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 788 PTVFTdvEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTD 867
Cdd:TIGR01238 390 PTLFE--LDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYV---NRNQ 464

                         410       420
                  ....*....|....*....|...
gi 1370483048 868 VAA-----PFGGFKQSGFGKDLG 885
Cdd:TIGR01238 465 VGAvvgvqPFGGQGLSGTGPKAG 487
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
 477-881 5.95e-52

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 198.17  E-value: 5.95e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAgwcdkiqgstipiNQARpnRNL 556
Cdd:PRK11905   606 WSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAI-AEVREAVDFLRYYA-------------AQAR--RLL 669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  557 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 636
Cdd:PRK11905   670 NGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAA 749

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  637 LSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLF 714
Cdd:PRK11905   750 LVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLC 829

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  715 VEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLvcggNQVPRP-----GFFFEPT 789
Cdd:PRK11905   830 LQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLPaetekGTFVAPT 905

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  790 VFtDVEDhmfIA--KEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTD 867
Cdd:PRK11905   906 LI-EIDS---ISdlEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYV---NRNI 978

                          410
                   ....*....|....*....
gi 1370483048  868 VAA-----PFGGFKQSGFG 881
Cdd:PRK11905   979 IGAvvgvqPFGGEGLSGTG 997
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
476-881 9.23e-52

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 197.47  E-value: 9.23e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  476 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAG------------AVytlalkthvgmsiqTF-RYFAgwcdkiqg 542
Cdd:COG4230    608 AWSATPVEERAAILERAADLLEAHRAELMALLVREAGktlpdaiaevreAV--------------DFcRYYA-------- 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  543 stipiNQARpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGV 622
Cdd:COG4230    666 -----AQAR-RLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADV 739

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  623 VNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLI---------IFADCdlnka 691
Cdd:COG4230    740 LQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLiaETGGQNAMIvdssalpeqVVDDV----- 814

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  692 vqmgMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGP------QNhhahlvKLMEYCQHG 765
Cdd:COG4230    815 ----LASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPvidaeaRA------NLEAHIERM 884

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  766 VKEGATLVcggnQVPRP-----GFFFEPTVF--TDVEDhmfiAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGV 838
Cdd:COG4230    885 RAEGRLVH----QLPLPeecanGTFVAPTLIeiDSISD----LEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGV 956

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1370483048  839 FTRdINK-ALYVSDKLQAGTVFVntyNKTDVAA-----PFGGFKQSGFG 881
Cdd:COG4230    957 HSR-IDEtIDRVAARARVGNVYV---NRNIIGAvvgvqPFGGEGLSGTG 1001
FDH_Hydrolase_C cd08703
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...
 206-306 3.64e-51

The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.


Pssm-ID: 187731 [Multi-domain]  Cd Length: 100  Bit Score: 174.46  E-value: 3.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 206 KETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDK 285
Cdd:cd08703     1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGK 79

                          90       100
                  ....*....|....*....|.
gi 1370483048 286 MLLVKNIQLEDGKMILASNFF 306
Cdd:cd08703    80 MVNVKRLQFEDGKMIPASKYG 100
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 3-182 2.53e-50

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.


Pssm-ID: 187712 [Multi-domain]  Cd Length: 173  Bit Score: 174.78  E-value: 2.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   3 IAVIGQSLFGQEVYCHLR-KEGHEVVGVFTVPDKDGKADPLGLEAEKDGVpvfkysrWRAKGQALPDVVAKYQALGAELN 81
Cdd:cd08369     1 IVILGSGNIGQRVLKALLsKEGHEIVGVVTHPDSPRGTAQLSLELVGGKV-------YLDSNINTPELLELLKEFAPDLI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  82 VLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVS 161
Cdd:cd08369    74 VSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAG 153

                         170       180
                  ....*....|....*....|.
gi 1370483048 162 TLYNRfLFPEGIKGMVQAVRL 182
Cdd:cd08369   154 TLYQR-LIELGPKLLKEALQK 173
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
 481-881 2.68e-50

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.


Pssm-ID: 143451 [Multi-domain]  Cd Length: 434  Bit Score: 183.46  E-value: 2.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 481 SARDRGRLMYRLADLMEQHQEELAtiEALDA-----GAVYTLALKthVGMSIQTFRY----FAGWCdkiqgstipinqaR 551
Cdd:cd07133    18 SLEERRDRLDRLKALLLDNQDALA--EAISAdfghrSRHETLLAE--ILPSIAGIKHarkhLKKWM-------------K 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 552 PNR---NLTLT------RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGV 622
Cdd:cd07133    81 PSRrhvGLLFLpakaevEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 623 VNVLPGsGSLVGQRLS----DHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSS 698
Cdd:cd07133   160 VAVVTG-GADVAAAFSslpfDH-----LLFTGSTAVGRHVMRAAA-ENLTPVTLELGGKSPAIIAPDADLAKAAERIAFG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 699 VFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKM---KVGNPldrdtDHGPQNHHAHLVKLMEYCQHGVKEGATLV-C 774
Cdd:cd07133   233 KLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeL 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 775 GGNQVPRPGF-FFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKL 853
Cdd:cd07133   308 NPAGEDFAATrKLPPTLVLNVTDDMRVMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRT 385

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1370483048 854 QAGTVFVNtynktDVA-------APFGGFKQSGFG 881
Cdd:cd07133   386 HSGGVTIN-----DTLlhvaqddLPFGGVGASGMG 415
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
 425-881 1.12e-49

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 183.42  E-value: 1.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFVDAEGAKTSETINPTDGSVicQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:PLN00412   19 YADGEWRTSSSGKSVAITNPSTRKT--QYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 505 tiEALdagaVYTLA-----LKTHVGMSIQTFRYFA-------GWCDKIQGSTIPINQarpnRN-LTLTRKEPVGVCGIII 571
Cdd:PLN00412   97 --ECL----VKEIAkpakdAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNE----RNkYCLTSKIPLGVVLAIP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 572 PWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGS 651
Cdd:PLN00412  167 PFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 652 tEVGKHIMKSCAISNVKkvsLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEV 731
Cdd:PLN00412  247 -DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKV 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 732 RKMKVGNPLDrDTDHGP------QNHHAHLVKlmeycqHGVKEGATLVcggNQVPRPGFFFEPTVFTDVEDHMFIAKEES 805
Cdd:PLN00412  323 AKLTVGPPED-DCDITPvvsessANFIEGLVM------DAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEP 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370483048 806 FGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTY-NKTDVAAPFGGFKQSGFG 881
Cdd:PLN00412  393 FGPVLPVIRI--NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIG 467
fmt TIGR00460
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...
 1-310 1.26e-49

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273088 [Multi-domain]  Cd Length: 313  Bit Score: 177.98  E-value: 1.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDG------KADPLGLEAEKDGVPVFKYsrwraKGQALPDVVAKYQ 74
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQP-----EKQRQLEELPLVR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:TIGR00460  76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAW 234
Cdd:TIGR00460 156 EEEDNSGTLSDK-LSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAW 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 235 TEACEQKLTFFnstlntsglvpEGDALPIPG-AHRPGVV---TKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAA 310
Cdd:TIGR00460 235 LTFEGKNIKIH-----------KAKVIDLSTyKAKPGEIvyhNKKGILVACGKDGILLLLSLQPPGKKVMRAEDFYNGSR 303
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
 560-898 3.58e-49

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.


Pssm-ID: 143453 [Multi-domain]  Cd Length: 436  Bit Score: 180.49  E-value: 3.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPG----SGSLVGQ 635
Cdd:cd07135   105 RKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGgvpeTTALLEQ 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 636 RLSdhpdvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:cd07135   184 KFD------KIFYTGSGRVGRIIAEAAA-KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 716 EDSIHDEFVRRVVEEVRKMkVGNPLDRDTDHG---PQNHHAHLVKLMEycqhgvKEGATLVCGG--NQVPRpgfFFEPTV 790
Cdd:cd07135   257 DPSVYDEFVEELKKVLDEF-YPGGANASPDYTrivNPRHFNRLKSLLD------TTKGKVVIGGemDEATR---FIPPTI 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 791 FTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-TYNKTDV- 868
Cdd:cd07135   327 VSDVSWDDSLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVd 404

                         330       340       350
                  ....*....|....*....|....*....|
gi 1370483048 869 AAPFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07135   405 NAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 560-898 4.08e-49

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 181.77  E-value: 4.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGsGSLVGQRLSD 639
Cdd:PTZ00381  106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLK 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 640 HP-DVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDS 718
Cdd:PTZ00381  184 EPfDH--IFFTGSPRVGKLVMQAAA-ENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 719 IHDEFVRRVVEEVRKMKVGNPLdRDTDHGPQNHHAHLVKLME-YCQHGVKegatLVCGGnQVPRPGFFFEPTVFTDVEDH 797
Cdd:PTZ00381  261 IKDKFIEALKEAIKEFFGEDPK-KSEDYSRIVNEFHTKRLAElIKDHGGK----VVYGG-EVDIENKYVAPTIIVNPDLD 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 798 MFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKTDVAAPFGGF 875
Cdd:PTZ00381  335 SPLMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGV 412

                         330       340
                  ....*....|....*....|...
gi 1370483048 876 KQSGFGKDLGEAALNEYLRVKTV 898
Cdd:PTZ00381  413 GNSGMGAYHGKYGFDTFSHPKPV 435
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
 419-902 5.24e-49

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 183.79  E-value: 5.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 419 RMPHqlFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQ 498
Cdd:PLN02419  113 RVPN--LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRK 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 499 HQEELATIEALDAGAVytlaLKTHVGMSIQTFRYFAGWCDKiqgSTIPINQARPNRNL---TLTRKEPVGVCGIIIPWNY 575
Cdd:PLN02419  189 NMDKLAMNITTEQGKT----LKDSHGDIFRGLEVVEHACGM---ATLQMGEYLPNVSNgvdTYSIREPLGVCAGICPFNF 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 576 PLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQrLSDHPDVRKIGFTGSTEVG 655
Cdd:PLN02419  262 PAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAG 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 656 KHIMKSCAISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGR-LFVEDSihDEFVRRVVEEVRKM 734
Cdd:PLN02419  341 MHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVERAKAL 417

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 735 KVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGF----FFEPTVFTDVEDHMFIAKEESFGPVM 810
Cdd:PLN02419  418 KVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVL 497

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 811 IISRfaDGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTynKTDVAAPFGGF--KQSGFGKDL---G 885
Cdd:PLN02419  498 VCMQ--ANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgNKASFAGDLnfyG 573

                         490
                  ....*....|....*..
gi 1370483048 886 EAALNEYLRVKTVTFEY 902
Cdd:PLN02419  574 KAGVDFFTQIKLVTQKQ 590
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
 560-881 7.27e-48

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 176.93  E-value: 7.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 560 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPG----SGSLVGQ 635
Cdd:cd07136    97 YYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGgveeNQELLDQ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 636 RLsDHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:cd07136   176 KF-DY-----IFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 716 EDSIHDEFVRRVVEEVRKMKVGNPLDRDtDHGPQNHHAHLVKLMEYCQHGvkegaTLVCGGNqVPRPGFFFEPTVFTDVE 795
Cdd:cd07136   249 HESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNG-----KIVFGGN-TDRETLYIEPTILDNVT 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 796 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAG------TV--FVNTYnktd 867
Cdd:cd07136   322 WDDPVMQEEIFGPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggcindTImhLANPY---- 395

                         330
                  ....*....|....
gi 1370483048 868 vaAPFGGFKQSGFG 881
Cdd:cd07136   396 --LPFGGVGNSGMG 407
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 1-200 3.15e-45

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187715 [Multi-domain]  Cd Length: 204  Bit Score: 161.46  E-value: 3.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:cd08646     1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPrgrGKkltPSPVKELALELGLPVLQPEKLKD-----EEFLEELK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:cd08646    76 ALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPI 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370483048 155 LPDDTVSTLYNRfLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATY 200
Cdd:cd08646   156 DPDDTAGELLDK-LAELGADLLLEVLDDIEAGKLNPVPQDESEATY 200
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
 424-879 4.45e-45

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 169.75  E-value: 4.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 424 LFIGGEFVDAEGAkTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEEL 503
Cdd:PRK09457    3 LWINGDWIAGQGE-AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP--AWARLSFEERQAIVERFAALLEENKEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 504 ATIEALDAGA--------VYTLALKthVGMSIQTFRYFAGwcdkiqgstipiNQARPNRNLTLT-RKEPVGVCGIIIPWN 574
Cdd:PRK09457   80 AEVIARETGKplweaateVTAMINK--IAISIQAYHERTG------------EKRSEMADGAAVlRHRPHGVVAVFGPYN 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 575 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEV 654
Cdd:PRK09457  146 FPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANT 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 655 GKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIH-DEFVRRVVEEVRK 733
Cdd:PRK09457  225 GYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 734 MKVGNPlDRDTD--HGPQNHHAHLVKLMEYCQHGVKEGA------TLVCGGNQVPRPGfFFEPTVFTDVEDhmfiakEES 805
Cdd:PRK09457  305 LTVGRW-DAEPQpfMGAVISEQAAQGLVAAQAQLLALGGksllemTQLQAGTGLLTPG-IIDVTGVAELPD------EEY 376

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483048 806 FGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVfvnTYNK----TDVAAPFGGFKQSG 879
Cdd:PRK09457  377 FGPLLQVVRYD--DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NWNKpltgASSAAPFGGVGASG 449
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
 425-902 1.96e-43

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 165.39  E-value: 1.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 425 FIGGEFvdAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELA 504
Cdd:PLN02315   24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYLG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 505 TIEALDAGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 584
Cdd:PLN02315  100 RLVSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIP--SERPN-HMMMEVWNPLGIVGVITAFNFPCAVLGWNA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 585 AACLAAGNTVVIKPAQVTPLTALK----FAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEVGkhIMK 660
Cdd:PLN02315  176 CIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG--LMV 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 661 SCAI-SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNP 739
Cdd:PLN02315  253 QQTVnARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDP 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 740 LDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVfTDVEDHMFIAKEESFGPVMIISRFAdgD 819
Cdd:PLN02315  333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFK--T 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 820 LDAVLSRANATEFGLASGVFTRD---INKAL--YVSDklqAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALNEYL 893
Cdd:PLN02315  410 LEEAIEINNSVPQGLSSSIFTRNpetIFKWIgpLGSD---CGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYM 486


                  ....*....
gi 1370483048 894 RVKTVTFEY 902
Cdd:PLN02315  487 RRSTCTINY 495
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 1-201 4.92e-43

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 154.93  E-value: 4.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKAdplgLEAEKDGVPVFKysrwrakGQALPDVVAKYQALGAEL 80
Cdd:cd08822     1 MKIAIAGQKWFGTAVLEALRARGIALLGVAAPEEGDRLA----AAARTAGSRGLP-------RAGVAVLPADAIPPGTDL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08822    70 IVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370483048 161 STLYNRFLFPEGIKGMVQAV-RLIAEGKAPRLPQPEEGATYE 201
Cdd:cd08822   150 AELWRRALAPMGVKLLTQVIdALLRGGNLPAQPQDERLATWE 191
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
 484-881 7.51e-41

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 163.22  E-value: 7.51e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  484 DRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGwcdkiqgstipinQARPN-RNLTltrKE 562
Cdd:PRK11809   705 ERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI-AEVREAVDFLRYYAG-------------QVRDDfDNDT---HR 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  563 PVG--VCgiIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDH 640
Cdd:PRK11809   768 PLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVAD 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  641 PDVRKIGFTGSTEVGKHIMKSCA---ISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 715
Cdd:PRK11809   846 ARVRGVMFTGSTEVARLLQRNLAgrlDPQGRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  716 EDSIHDEFVRRVVEEVRKMKVGNPlDR-DTDHGP-------QNHHAHlVKLMEYCQHGVkegatlvcggNQVPRP----- 782
Cdd:PRK11809   926 QDDVADRTLKMLRGAMAECRMGNP-DRlSTDIGPvidaeakANIERH-IQAMRAKGRPV----------FQAAREnsedw 993

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  783 --GFFFEPTVftdVE-DHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTR-DINKAlYVSDKLQAGTV 858
Cdd:PRK11809   994 qsGTFVPPTL---IElDSFDELKREVFGPVLHVVRYNRNQLDELIEQINASGYGLTLGVHTRiDETIA-QVTGSAHVGNL 1069

                          410       420
                   ....*....|....*....|....*...
gi 1370483048  859 FVntyNKTDVAA-----PFGGFKQSGFG 881
Cdd:PRK11809  1070 YV---NRNMVGAvvgvqPFGGEGLSGTG 1094
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
 591-879 3.37e-40

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.


Pssm-ID: 143441 [Multi-domain]  Cd Length: 522  Bit Score: 156.21  E-value: 3.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 591 GNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA--ISNVK 668
Cdd:cd07123   197 GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenLDRYR 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 669 ---KVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTD 745
Cdd:cd07123   277 typRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNF 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 746 HGPQNHHAHLVKLMEYCQHGVKE-GATLVCGGNQVPRPGFFFEPTVF--TDVEDHMFiaKEESFGPVMIISRFADGDLDA 822
Cdd:cd07123   357 MGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIetTDPKHKLM--TEEIFGPVLTVYVYPDSDFEE 434

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 823 VLSRAN-ATEFGLASGVFTRD---INKAlyvSDKLQ--AGTVFVNTYNKTDVAA--PFGGFKQSG 879
Cdd:cd07123   435 TLELVDtTSPYALTGAIFAQDrkaIREA---TDALRnaAGNFYINDKPTGAVVGqqPFGGARASG 496
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 551-882 1.70e-38

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 149.29  E-value: 1.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 551 RPNRNLT------LTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtlkagIPK---- 620
Cdd:cd07132    82 PVKKNLAtllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKyldk 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 621 ---GVVNV-LPGSGSLVGQRLsDHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGM 696
Cdd:cd07132   157 ecyPVVLGgVEETTELLKQRF-DY-----IFYTGSTSVGKIVMQAAA-KHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 697 SSVFFNKGENCIAAGRLFVEDSIHDEFV---RRVVEEVrkmkVGNPLDRDTDHGP---QNHHAHLVKLMeycqhgvkEGA 770
Cdd:cd07132   230 WGKFINAGQTCIAPDYVLCTPEVQEKFVealKKTLKEF----YGEDPKESPDYGRiinDRHFQRLKKLL--------SGG 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 771 TLVCGGNQVPRPGfFFEPTVFTDVEDHMFIAKEESFGPVMIIsrFADGDLDAVLSRANATEFGLASGVFTRD---INKAL 847
Cdd:cd07132   298 KVAIGGQTDEKER-YIAPTVLTDVKPSDPVMQEEIFGPILPI--VTVNNLDEAIEFINSREKPLALYVFSNNkkvINKIL 374

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1370483048 848 yvsDKLQAGTVFVNtynktDV-------AAPFGGFKQSGFGK 882
Cdd:cd07132   375 ---SNTSSGGVCVN-----DTimhytldSLPFGGVGNSGMGA 408
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 2-166 3.71e-31

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 120.45  E-value: 3.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   2 KIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADP----LGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQALG 77
Cdd:cd08651     1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSdyldLDSFARKNGIPYYKFTDIND-----EEIIEWIKEAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  78 AELNvlpFC---SQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEV 154
Cdd:cd08651    76 PDII---FVfgwSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPI 152

                         170
                  ....*....|..
gi 1370483048 155 LPDDTVSTLYNR 166
Cdd:cd08651   153 DKDDTANSLYDK 164
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
 562-898 4.86e-29

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.


Pssm-ID: 143455 [Multi-domain]  Cd Length: 432  Bit Score: 120.98  E-value: 4.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 562 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHP 641
Cdd:cd07137   100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALLEQKW 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 642 DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVF-FNKGENCIAAGRLFVEDSIH 720
Cdd:cd07137   179 D--KIFFTGSPRVGRIIMAAAA-KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFA 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 721 DEFVRRVVEEVRKMKVGNPldRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnQVPRPGFFFEPTVFTDVEDHMFI 800
Cdd:cd07137   256 PTLIDALKNTLEKFFGENP--KESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG-ERDEKNLYIEPTILLDPPLDSSI 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 801 AKEESFGPVM-IIS-RFADGDLDAVLSRANAtefgLASGVFTRdiNKALY--VSDKLQAGTVFVNtynktDVAA------ 870
Cdd:cd07137   333 MTEEIFGPLLpIITvKKIEESIEIINSRPKP----LAAYVFTK--NKELKrrIVAETSSGGVTFN-----DTVVqyaidt 401

                         330       340
                  ....*....|....*....|....*....
gi 1370483048 871 -PFGGFKQSGFGKDLGEAALNEYLRVKTV 898
Cdd:cd07137   402 lPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
 475-894 2.15e-27

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.


Pssm-ID: 143403 [Multi-domain]  Cd Length: 442  Bit Score: 116.57  E-value: 2.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 475 GRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKthVGMSIQTFRYFAGWCDKIQGSTIPINQARPNR 554
Cdd:cd07084    13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAEN--ICGDQVQLRARAFVIYSYRIPHEPGNHLGQGL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 555 NLTLTRKE-PVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVLPGSGSL 632
Cdd:cd07084    91 KQQSHGYRwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 633 vGQRLSDHPDVRKIGFTGSTEVGKHImkscaISNVK--KVSLELGGKSPLIIFADCDLNKAV------QMGMSSvffnkG 704
Cdd:cd07084   171 -MQALLLHPNPKMVLFTGSSRVAEKL-----ALDAKqaRIYLELAGFNWKVLGPDAQAVDYVawqcvqDMTACS-----G 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 705 ENCIAAGRLFV-EDSIHDEFVRRVVEEVRKMKVGNPL-----DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQ 778
Cdd:cd07084   240 QKCTAQSMLFVpENWSKTPLVEKLKALLARRKLEDLLlgpvqTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIYGAC 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 779 VPRPGFFFEPTVFTDVEDHMfiakEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQ-AGT 857
Cdd:cd07084   320 VASALFVPIDEILKTYELVT----EEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGR 395

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1370483048 858 VFVNTYNKTDVAAP---FGGFKQSGFGKDLGEA-ALNEYLR 894
Cdd:cd07084   396 TYAILRGRTGVAPNqnhGGGPAADPRGAGIGGPeAIKLVWR 436
PRK06988 PRK06988
formyltransferase;
46-305 1.34e-26

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 111.32  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  46 AEKDGVPVFKYSrwrakGQALPDVVAKYQALGAELnVLPFCSQF-IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLI 124
Cdd:PRK06988   51 AAEHGIPVITPA-----DPNDPELRAAVAAAAPDF-IFSFYYRHmIPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 125 HGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNrflfpegiKGMVQAVRLIAE-------GKAPRLPQPEEG 197
Cdd:PRK06988  125 NGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD--------KVTVAAEQTLWRvlpallaGEAPHLPNDLAQ 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 198 ATYEGIQKKETAKINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTLNTSGlvPEGDALPIPGAHrpgVVTKAG 276
Cdd:PRK06988  197 GSYFGGRKPEDGRIDWSKPAAQVYNLIRAvAPPYPGAFTDLGGTRFVVARARLAAPG--AAAARDLPPGLH---VSDNAL 271

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370483048 277 LILFGNDDKMLL--VKNIQLEDGKMILASNF 305
Cdd:PRK06988  272 FGVCGDGRAVSIleLRRQQDGGETVVTPAQF 302
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
 562-900 2.94e-26

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 113.60  E-value: 2.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 562 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHP 641
Cdd:PLN02174  111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQKW 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 642 DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVF-FNKGENCIAAGRLFVEDSIH 720
Cdd:PLN02174  190 D--KIFYTGSSKIGRVIMAAAA-KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 721 DEFVRRVVEEVRKMKVGNPLD-RDTDH-GPQNHHAHLVKLMEYcqhgvKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHM 798
Cdd:PLN02174  267 PKVIDAMKKELETFYGKNPMEsKDMSRiVNSTHFDRLSKLLDE-----KEVSDKIVYGGEKDRENLKIAPTILLDVPLDS 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 799 FIAKEESFGPVMIISRFADGD--LDAVLSRANAtefgLASGVFTRDINKALYVSDKLQAGTVFVNtynktDVAA------ 870
Cdd:PLN02174  342 LIMSEEIFGPLLPILTLNNLEesFDVIRSRPKP----LAAYLFTHNKKLKERFAATVSAGGIVVN-----DIAVhlalht 412

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1370483048 871 -PFGGFKQSGFGKDLGEAALNEYLRVKTVTF 900
Cdd:PLN02174  413 lPFGGVGESGMGAYHGKFSFDAFSHKKAVLY 443
PLN02203 PLN02203
aldehyde dehydrogenase
 562-882 1.93e-25

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 110.97  E-value: 1.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 562 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTAlKFaeltLKAGIPK----GVVNVLPGsGSLVGQRL 637
Cdd:PLN02203  107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-AF----LAANIPKyldsKAVKVIEG-GPAVGEQL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 638 SDHP-DvrKIGFTGSTEVGKHIMkSCAISNVKKVSLELGGKSPLIIfaDC-DLNKAVQMGMSSVFFNK-----GENCIAA 710
Cdd:PLN02203  181 LQHKwD--KIFFTGSPRVGRIIM-TAAAKHLTPVALELGGKCPCIV--DSlSSSRDTKVAVNRIVGGKwgscaGQACIAI 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 711 GRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHaHLVKLMEYCQHGVKEgATLVCGGNQVPRpGFFFEPTV 790
Cdd:PLN02203  256 DYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKK-HFQRLSNLLKDPRVA-ASIVHGGSIDEK-KLFIEPTI 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 791 FTDVEDHMFIAKEESFGPVM-IISRFADGDLDAVLsraNATEFGLASGVFTRDINKALYVSDKLQAGTVfvnTYNKTDV- 868
Cdd:PLN02203  333 LLNPPLDSDIMTEEIFGPLLpIITVKKIEDSIAFI---NSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAIIq 406

                         330
                  ....*....|....*...
gi 1370483048 869 ----AAPFGGFKQSGFGK 882
Cdd:PLN02203  407 yacdSLPFGGVGESGFGR 424
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 1-202 1.77e-21

ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.


Pssm-ID: 187713 [Multi-domain]  Cd Length: 203  Bit Score: 93.18  E-value: 1.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKA---DPLGLEAEKDGVPVFkysrwRAKGQALPDVVAKYQALG 77
Cdd:cd08644     1 MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNPGENiwfGSVAQLAREHGIPVF-----TPDDINHPEWVERLRALK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  78 AELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPD 157
Cdd:cd08644    76 PDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370483048 158 DTVSTLYNRFLFPEGIKgMVQAVRLIAEGKAPRLPQPEEGATYEG 202
Cdd:cd08644   156 DTAKSLFHKLCVAARRL-LARTLPALKAGKARERPQDETQASYFG 199
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 19-248 1.20e-20

bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 97.36  E-value: 1.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  19 LRKEGHEVVGVFTVPDKDGKADPLG----LEAEKdGVPVF-----KYSRWRAKGQAL-PDVVAK--YQALGAElnvlpfc 86
Cdd:PRK08125   19 LLAAGYEIAAVFTHTDNPGENHFFGsvarLAAEL-GIPVYapedvNHPLWVERIRELaPDVIFSfyYRNLLSD------- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  87 sqfipmEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNR 166
Cdd:PRK08125   91 ------EILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 167 FLFPEGiKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFF 245
Cdd:PRK08125  165 LCHAAR-QLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAvTDPWPGAFSYVGEQKFTVW 243


                  ...
gi 1370483048 246 NST 248
Cdd:PRK08125  244 SSR 246
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 25-187 3.98e-19

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 86.63  E-value: 3.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  25 EVVGVFTvpdkDgKADPLGLE-AEKDGVPVF-----KYSRWRAKGQALPDVVAKYQAlgaELNVL---------PFCSQF 89
Cdd:COG0299    30 EIVLVIS----N-RPDAYGLErARAAGIPTFvldhkDFPSREAFDAALLEALDAYGP---DLVVLagfmriltpEFVRAF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  90 ipmeiisaprHGSII-YHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFL 168
Cdd:COG0299   102 ----------PGRIInIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARIL 171

                         170
                  ....*....|....*....
gi 1370483048 169 fPEGIKGMVQAVRLIAEGK 187
Cdd:COG0299   172 -EQEHRLYPEAIRLLAEGR 189
Formyl_trans_C pfam02911
Formyl transferase, C-terminal domain;
205-309 6.99e-18

Formyl transferase, C-terminal domain;


Pssm-ID: 460744 [Multi-domain]  Cd Length: 99  Bit Score: 79.63  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 205 KKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPG--VVTKAGLILFGN 282
Cdd:pfam02911   3 KKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKASV-----------LDQESGAAPGtiVTVDKGGLLVAC 71

                          90       100
                  ....*....|....*....|....*..
gi 1370483048 283 DDKMLLVKNIQLEDGKMILASNFFKGA 309
Cdd:pfam02911  72 GDGALLILELQLEGKKPMSAEDFLNGF 98
PLN02285 PLN02285
methionyl-tRNA formyltransferase
 25-233 3.71e-17

methionyl-tRNA formyltransferase


Pssm-ID: 215159 [Multi-domain]  Cd Length: 334  Bit Score: 83.59  E-value: 3.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  25 EVVGVFTVPDKDGK------ADPLGLEAEKDGVP---VFKYSRWRAkgqalPDVVAKYQALGAELNVLPFCSQFIPMEII 95
Cdd:PLN02285   37 EVAAVVTQPPARRGrgrklmPSPVAQLALDRGFPpdlIFTPEKAGE-----EDFLSALRELQPDLCITAAYGNILPQKFL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  96 SAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRfLFPEGIKG 175
Cdd:PLN02285  112 DIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPL-LFELGTKL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 176 MVQAVRLIAEGKAPR--LPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGA 233
Cdd:PLN02285  191 LLRELPSVLDGSAKDkaTPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGWPGT 250
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
 477-826 9.93e-17

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.


Pssm-ID: 143447 [Multi-domain]  Cd Length: 454  Bit Score: 83.74  E-value: 9.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavYTLALKT-HVGMSIQTFRYFA------GWCDKIQGSTIPINQ 549
Cdd:cd07129    15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgELGRTTGQLRLFAdlvregSWLDARIDPADPDRQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 550 ARPNRNLTLtRKEPVGVCGIIIPWNYPLM--MLSWKTAACLAAGNTVVIK--PAQvtPLTALKFAELTLKA----GIPKG 621
Cdd:cd07129    93 PLPRPDLRR-MLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAH--PGTSELVARAIRAAlratGLPAG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 622 VVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNV-KKVSLELGGKSPLIIFADCDLNKAVQMGMS--- 697
Cdd:cd07129   170 VFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFILPGALAERGEAIAQGfvg 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 698 SVFFNKGENCIAAGRLFVEDSIH-DEFVRRVVEEVRKMKVGNPLdrdtDHGPQNHHahlvklmeycQHGVKE-----GAT 771
Cdd:cd07129   250 SLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTML----TPGIAEAY----------RQGVEAlaaapGVR 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483048 772 LVCGGNQvPRPGFFFEPTVF-TDVEDhmFIAK----EESFGPVMIISRFAD-GDLDAVLSR 826
Cdd:cd07129   316 VLAGGAA-AEGGNQAAPTLFkVDAAA--FLADpalqEEVFGPASLVVRYDDaAELLAVAEA 373
FMT_core_GART cd08645
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ...
 38-174 6.14e-16

Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.


Pssm-ID: 187714 [Multi-domain]  Cd Length: 183  Bit Score: 76.66  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  38 KADPLGLE-AEKDGVPVF-----KYSRWRAKGQALPDVVAKYQAlgaELNVL---------PFCSQFipmeiisaprHGS 102
Cdd:cd08645    36 NPDAYGLErAKKAGIPTFvinrkDFPSREEFDEALLELLKEYKV---DLIVLagfmrilspEFLEAF----------PGR 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 103 II-YHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRF------LFPEGIK 174
Cdd:cd08645   103 IInIHPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERIhalehrLYPEAIK 181
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 67-181 3.39e-15

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 73.79  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  67 PDVVAKYQALGAELNVLPFCSqFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGD-KKGGFSIFWADDGLDTGD 145
Cdd:cd08653    37 PEVVAALRALAPDVVSVYGCG-IIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDpDNVGVTVHLVDAGIDTGD 115

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1370483048 146 LLLQKECEVLPDDTVSTLYNRfLFPEGIKGMVQAVR 181
Cdd:cd08653   116 VLAQARPPLAAGDTLLSLYLR-LYRAGVELMVEAIA 150
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
480-817 2.41e-13

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 73.59  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 480 ISARDRGRLMYRLADLMEQHQEELATI-----------EALDA-GAVYTLALKTHVGMSIQTFRYFAGwCDKIQGSTIPI 547
Cdd:PRK11903   60 LTYAQRAALLAAIVKVLQANRDAYYDIatansgttrndSAVDIdGGIFTLGYYAKLGAALGDARLLRD-GEAVQLGKDPA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 548 NQARpnRNLTLTRkepvGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVL 626
Cdd:PRK11903  139 FQGQ--HVLVPTR----GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVV 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 627 PGSGSlvgqRLSDH---PDVrkIGFTGSTEVGKHIMKSCA-ISNVKKVSLElggkspliifADcDLNKAV---QMGMSSV 699
Cdd:PRK11903  213 CGSSA----GLLDHlqpFDV--VSFTGSAETAAVLRSHPAvVQRSVRVNVE----------AD-SLNSALlgpDAAPGSE 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 700 FFN-------------KGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHgV 766
Cdd:PRK11903  276 AFDlfvkevvremtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-L 354

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 767 KEGATLVCGGNQV------PRPGFFFEPTVF--TDVEDHMFIAKEESFGPVMIISRFAD 817
Cdd:PRK11903  355 RAQAEVLFDGGGFalvdadPAVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRD 413
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 18-163 3.67e-13

N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.


Pssm-ID: 187718 [Multi-domain]  Cd Length: 166  Bit Score: 68.05  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  18 HLRKEGHEVVGVFTvPDkdgkadplgleaekdgvPVFKysRWrAKGQALPdVVAKYQALGAELNVLPFCSQF-------I 90
Cdd:cd08649    17 QLLAAGHRIAAVVS-TD-----------------PAIR--AW-AAAEGIA-VLEPGEALEELLSDEPFDWLFsivnlriL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483048  91 PMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTL 163
Cdd:cd08649    75 PSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDTALSL 147
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 38-178 4.29e-13

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 68.55  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  38 KADPLGLE-AEKDGVPVFKYSR--WRAKGQALPDVVAKYQALGAELNVlpfCSQFipMEIISAP---RHGSIIY--HPSL 109
Cdd:TIGR00639  37 KPDAYGLErAAQAGIPTFVLSLkdFPSREAFDQAIIEELRAHEVDLVV---LAGF--MRILGPTflsRFAGRILniHPSL 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 110 LPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRF------LFPEGIKGMVQ 178
Cdd:TIGR00639 112 LPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRIhkqehrIYPLAIAWFAQ 186
Met_tRNA_FMT_C cd08704
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...
 207-302 1.25e-12

C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.


Pssm-ID: 187732 [Multi-domain]  Cd Length: 87  Bit Score: 64.09  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 207 ETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTlntsgLVPEGDALPIPGAhrpGVVTKAGLILFGNDDkM 286
Cdd:cd08704     1 EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGKRLKILKAE-----VLEESGEAAPGTI---LAVDKKGLLVACGDG-A 71

                          90
                  ....*....|....*.
gi 1370483048 287 LLVKNIQLEDGKMILA 302
Cdd:cd08704    72 LEILELQPEGKKRMSA 87
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 84-184 2.06e-11

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 63.62  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  84 PFCSQF---IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTV 160
Cdd:cd08823    75 VVVFTFpyrIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTY 154

                          90       100
                  ....*....|....*....|....
gi 1370483048 161 STLYNRfLFPEGIKGMVQAVRLIA 184
Cdd:cd08823   155 GLLCSR-LAMLAVGLLEELYQNLA 177
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
 492-739 3.18e-11

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 66.09  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 492 LADLMEQHQEELATIEALDAGA-VYTLALKTHVGMSIQ---------TFRYFAGWCDKIQGSTipinqaRPNRNLTLTRK 561
Cdd:cd07077    25 IANALYDTRQRLASEAVSERGAyIRSLIANWIAMMGCSesklyknidTERGITASVGHIQDVL------LPDNGETYVRA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 562 EPVGVCGIIIPWNYPLMMLSwKTAACLAAGNTVVIKPAQVTPLTALKFAELT---LKAGIPKGVVNVLPGSGSLVGQRLS 638
Cdd:cd07077    99 FPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFqaaDAAHGPKILVLYVPHPSDELAEELL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 639 DHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSlelGGKSPLIIFADCDLNKAVQMGMSSVFFNkGENCIAAGRLFVEDS 718
Cdd:cd07077   178 SHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFG---AGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDD 253

                         250       260
                  ....*....|....*....|.
gi 1370483048 719 IHDEFVRRVVEEVRKMKVGNP 739
Cdd:cd07077   254 VLDPLYEEFKLKLVVEGLKVP 274
FMT_core_HypX_N cd08650
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ...
 13-180 7.38e-11

HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain.


Pssm-ID: 187719 [Multi-domain]  Cd Length: 151  Bit Score: 61.09  E-value: 7.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  13 QEVYCHLRKEGHEVVGVFTVPDkdgkadplglEAEKDGVPVFKysrwrakgqalPDVVakyqalgaelnVLPFCSQFIPM 92
Cdd:cd08650    15 QRAFLELRERGHEVSVEYALSD----------DEMREAVALFA-----------PDLI-----------ICPFLKKRIPE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  93 EIISapRHGSIIYHPSLlPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEG 172
Cdd:cd08650    63 EIWS--NYPCLIVHPGI-VGDRGPSSLDWAILEGEKEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYRGEVTDAA 139


                  ....*...
gi 1370483048 173 IKGMVQAV 180
Cdd:cd08650   140 VKAVLEAV 147
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
 477-889 2.08e-10

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.


Pssm-ID: 143445  Cd Length: 549  Bit Score: 64.42  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 477 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK---THV---GMSIQTFRYFAgwCDKIQGSTIPINQA 550
Cdd:cd07127   100 WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQaggPHAqdrGLEAVAYAWRE--MSRIPPTAEWEKPQ 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 551 RPNRNLTLTRK---EPVGV-----CGIIIPWN-YPLMMlswktaACLAAGNTVVIKP--AQVTPLT-ALKFAELTL-KAG 617
Cdd:cd07127   178 GKHDPLAMEKTftvVPRGValvigCSTFPTWNgYPGLF------ASLATGNPVIVKPhpAAILPLAiTVQVAREVLaEAG 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 618 I-PKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisNVKKVSLELGGKSPLIIFADCDLNKAVQ-MG 695
Cdd:cd07127   252 FdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANA---RQAQVYTEKAGVNTVVVDSTDDLKAMLRnLA 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 696 MSSVFFNkGENCIAAGRLFV-EDSI--------HDEFVRRVVEEVRKMkVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGv 766
Cdd:cd07127   329 FSLSLYS-GQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLG- 405

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 767 kegatlvcggnQVPRPGFFFEPTVFTDVEDH--MFIA---------KEESFGPVMIISRFADGDLDAVLSRANATEFG-L 834
Cdd:cd07127   406 -----------EVLLASEAVAHPEFPDARVRtpLLLKldasdeaayAEERFGPIAFVVATDSTDHSIELARESVREHGaM 474

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483048 835 ASGVFTRD-------INKALYVSDKLQ---AGTVFVNTynktdvAAPFGGFKQSGfGKDLGEAAL 889
Cdd:cd07127   475 TVGVYSTDpevvervQEAALDAGVALSinlTGGVFVNQ------SAAFSDFHGTG-ANPAANAAL 532
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
 556-862 2.31e-10

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143400 [Multi-domain]  Cd Length: 439  Bit Score: 63.82  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 556 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGS 631
Cdd:cd07081    88 GTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSI 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 632 LVGQRLSDHPDVRKIGFTGstevGKHIMKScAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAG 711
Cdd:cd07081   168 ELAQRLMKFPGIGLLLATG----GPAVVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQ 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 712 RLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNH--HAHLVklmeycqhGVKEGATLVCGGNQVPRPG--FFFE 787
Cdd:cd07081   243 SVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGdvNRDIV--------GQDAYKIAAAAGLKVPQETriLIGE 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 788 PTVftdVEDHMFIAKEEsFGPVMIISR---FADGDLDAvLSRANATEFGLASGVFTRDIN---KALYVSDKLQAGTVFVN 861
Cdd:cd07081   315 VTS---LAEHEPFAHEK-LSPVLAMYRaanFADADAKA-LALKLEGGCGHTSAMYSDNIKaieNMNQFANAMKTSRFVKN 389


                  .
gi 1370483048 862 T 862
Cdd:cd07081   390 G 390
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
 563-863 4.03e-10

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.


Pssm-ID: 143444  Cd Length: 489  Bit Score: 63.28  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 563 PVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDhPD 642
Cdd:cd07126   142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-AN 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 643 VRKIGFTGSTEVGKHImkscAISNVKKVSLELGGKSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFV-EDSIH 720
Cdd:cd07126   221 PRMTLFTGSSKVAERL----ALELHGKVKLEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAhENWVQ 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 721 DEFVRRVVE--EVRKMK---VGNPLDRDTdhgpQNHHAHLVKLMEYcqhgvkEGATLVCGGNQVP-----------RPGF 784
Cdd:cd07126   297 AGILDKLKAlaEQRKLEdltIGPVLTWTT----ERILDHVDKLLAI------PGAKVLFGGKPLTnhsipsiygayEPTA 366

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 785 FFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINkalyVSDKLQAGTVFVNTY 863
Cdd:cd07126   367 VFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIR----FLQEVLANTVNGTTY 441
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 85-164 3.25e-09

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 57.07  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  85 FCSQF---IPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVS 161
Cdd:cd08820    74 ISVQYhwiLPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVI 153


                  ...
gi 1370483048 162 TLY 164
Cdd:cd08820   154 SLY 156
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
 574-842 3.55e-08

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.


Pssm-ID: 143446 [Multi-domain]  Cd Length: 513  Bit Score: 56.89  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 574 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVLPGS-GSLVGQRlsDHPDVrkIGFTGS 651
Cdd:cd07128   155 NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSvGDLLDHL--GEQDV--VAFTGS 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 652 TEVGKHIMkscAISNVKKVSLelggksPLIIFADcDLNKAV-----QMGMSSV-FFNK----------GENCIAAGRLFV 715
Cdd:cd07128   231 AATAAKLR---AHPNIVARSI------RFNAEAD-SLNAAIlgpdaTPGTPEFdLFVKevaremtvkaGQKCTAIRRAFV 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 716 EDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPqnhhahLVKLMEycQHGVKEG-------ATLVCGGNQVPRP------ 782
Cdd:cd07128   301 PEARVDAVIEALKARLAKVVVGDPRLEGVRMGP------LVSREQ--REDVRAAvatllaeAEVVFGGPDRFEVvgadae 372

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483048 783 -GFFFEPTVF--------TDVEDHmfiakeESFGPVMIIsrFADGDLDAVLSRANATEFGLASGVFTRD 842
Cdd:cd07128   373 kGAFFPPTLLlcddpdaaTAVHDV------EAFGPVATL--MPYDSLAEAIELAARGRGSLVASVVTND 433
ALDH_F20_ACDH cd07122
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ...
 562-725 6.38e-07

Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143440 [Multi-domain]  Cd Length: 436  Bit Score: 52.88  E-value: 6.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 562 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP---AQVTPLTALKF-AELTLKAGIPKGVVNVLPGSGSLVGQRL 637
Cdd:cd07122    94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIELTQEL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 638 SDHPDVRKIGFTGSTevgkhimkscaiSNVK------KVSLELG-GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAA 710
Cdd:cd07122   174 MKHPDVDLILATGGP------------GMVKaayssgKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASE 241

                         170
                  ....*....|....*
gi 1370483048 711 GRLFVEDSIHDEFVR 725
Cdd:cd07122   242 QSVIVDDEIYDEVRA 256
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
86-215 8.96e-07

dTDP-4-amino-4,6-dideoxyglucose formyltransferase;


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 51.06  E-value: 8.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  86 CSQFIPMEIISAPRhgSIIYHPSLLPRHRGASAINWTLIHGDKKGGfSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYN 165
Cdd:PRK07579   74 CKQRFPAKLVNGVR--CINIHPGFNPYNRGWFPQVFSIINGLKIGA-TIHEMDEQLDHGPIIAQREVEIESWDSSGSVYA 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370483048 166 RFLFPEgIKGMVQAVRLIAEGKAPRLpQPEEGATYEGIQK-KETAKINWDQ 215
Cdd:PRK07579  151 RVMDIE-RELVLEHFDAIRDGSYTAK-KPATEGNLNSKKDfKQLREIDLDE 199
ALDH_EutE cd07121
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ...
 556-730 9.02e-07

Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.


Pssm-ID: 143439 [Multi-domain]  Cd Length: 429  Bit Score: 52.24  E-value: 9.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 556 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVL--PGS 629
Cdd:cd07121    90 LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIAEAGGPDNLVVTVeePTI 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 630 GSLvgQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisnvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIA 709
Cdd:cd07121   170 ETT--NELMAHPDINLLVVTGGPAVVKAALSSG-----KKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIA 242

                         170       180
                  ....*....|....*....|.
gi 1370483048 710 AGRLFVEDSIHDEFVRRVVEE 730
Cdd:cd07121   243 EKEVIAVDSVADYLIAAMQRN 263
PRK15398 PRK15398
aldehyde dehydrogenase;
556-730 1.25e-06

aldehyde dehydrogenase;


Pssm-ID: 237956  Cd Length: 465  Bit Score: 51.83  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 556 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVL--PGS 629
Cdd:PRK15398  122 LTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVaePTI 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 630 GSLvgQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisnvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIA 709
Cdd:PRK15398  202 ETA--QRLMKHPGIALLVVTGGPAVVKAAMKSG-----KKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIA 274

                         170       180
                  ....*....|....*....|.
gi 1370483048 710 AGRLFVEDSIHDEFVRRVVEE 730
Cdd:PRK15398  275 EKEVIVVDSVADELMRLMEKN 295
Arna_FMT_C cd08702
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ...
 210-305 3.78e-06

C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.


Pssm-ID: 187730  Cd Length: 92  Bit Score: 46.08  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048 210 KINWDQPAEAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTlntsgLVPEGDALPIPGAhrpgVVTKAG---LILFGndDK 285
Cdd:cd08702     4 LIDWRMSAREIYNLVRAvTKPYPGAFTFVGGQKIKIWKAR-----PVDDAFYNGEPGK----VLSVDGdplIVACG--DG 72

                          90       100
                  ....*....|....*....|
gi 1370483048 286 MLLVKNIQLEDGKMILASNF 305
Cdd:cd08702    73 ALEILEAELDGGLPLAGEQL 92
PLN02331 PLN02331
phosphoribosylglycinamide formyltransferase
 46-171 3.29e-04

phosphoribosylglycinamide formyltransferase


Pssm-ID: 177965 [Multi-domain]  Cd Length: 207  Bit Score: 42.76  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  46 AEKDGVPVFKYSRWRAKGQALP--DVVAKYQALGAELNVLPFCSQFIPMEIISA-PRhgSII-YHPSLLPRH--RGASAI 119
Cdd:PLN02331   45 ARENGIPVLVYPKTKGEPDGLSpdELVDALRGAGVDFVLLAGYLKLIPVELVRAyPR--SILnIHPALLPAFggKGYYGI 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483048 120 NwtlIH------GDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPE 171
Cdd:PLN02331  123 K---VHkaviasGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLHEE 177
FMT_core_like_1 cd08821
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 84-225 8.63e-03

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187723 [Multi-domain]  Cd Length: 211  Bit Score: 38.45  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483048  84 PFCSQFIPMEIISapRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLpdDTVSTL 163
Cdd:cd08821    51 PHWSWIIPKEIFE--NFECVVFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYLKRDLSLK--GTAEEI 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483048 164 YNRflFPEGIKGMVqaVRLIAEGKAPrLPQPEEGATYEGiQKKETAKINWDQPAEAIHNWIR 225
Cdd:cd08821   127 YER--ASKISLKMI--PELVTKKPKP-IKQEGEPVTFKR-RTPEQSNISNEANLEKIYDFIR 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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