NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2108433413|gb|UCH90357|]
View 

MAG: NAD(P)-dependent glycerol-1-phosphate dehydrogenase [Thermoplasmata archaeon]

Protein Classification

dehydroquinate synthase/iron-containing alcohol dehydrogenase family protein( domain architecture ID 760)

dehydroquinate synthase (DHQS)/iron-containing alcohol dehydrogenase (FeADH) family protein

CATH:  3.40.50.1970
Gene Ontology:  GO:0046872|GO:0030554
PubMed:  9685163|35751426
SCOP:  3001905

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DHQ_Fe-ADH super family cl02872
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 1-343 0e+00

Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


The actual alignment was detected with superfamily member PRK00843:

Pssm-ID: 445950  Cd Length: 350  Bit Score: 504.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   1 MELPREVLVGHDTLDNVGGACKRLKMEGPALIIADSNTKKIAGEAVIESLQQHnYEVLVTTIEDATIEEVERVKVKIEDD 80
Cdd:PRK00843    8 IQLPRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDA-GDVEVVIVDEATMEEVEKVEEKAKDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  81 KINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRINA 160
Cdd:PRK00843   87 NAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYRLLA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 161 AGCGDLISNETAVLDWELAHKEKNEDISTYAKTLSKMTAFVIEKYAEIISAGGEEGAWHVIKALVASGVAMSIAGSSRPC 240
Cdd:PRK00843  167 AGCGDIISNYTAVKDWRLAHRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSSRPA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 241 SGAEHMFSHKLDAIAPKPALHGEQCAIGTIMMMKLHGGDWEALKKTLVTIGTPTTAQEIGIGSEFIIQSLMEAHTIRVDR 320
Cdd:PRK00843  247 SGSEHLFSHALDRLAPGPALHGEQCGVGTIIMMYLHGGDWRKIRDALKKIGAPTTAKELGIDDEYIIEALTIAHTIRPER 326

                         330       340
                  ....*....|....*....|....
gi 2108433413 321 YTILG-SGLTKGVATELAESTGVI 343
Cdd:PRK00843  327 YTILGdRGLTREAAEKAARITGVI 350
 
Name Accession Description Interval E-value
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 1-343 0e+00

NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed


Pssm-ID: 179139  Cd Length: 350  Bit Score: 504.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   1 MELPREVLVGHDTLDNVGGACKRLKMEGPALIIADSNTKKIAGEAVIESLQQHnYEVLVTTIEDATIEEVERVKVKIEDD 80
Cdd:PRK00843    8 IQLPRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDA-GDVEVVIVDEATMEEVEKVEEKAKDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  81 KINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRINA 160
Cdd:PRK00843   87 NAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYRLLA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 161 AGCGDLISNETAVLDWELAHKEKNEDISTYAKTLSKMTAFVIEKYAEIISAGGEEGAWHVIKALVASGVAMSIAGSSRPC 240
Cdd:PRK00843  167 AGCGDIISNYTAVKDWRLAHRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSSRPA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 241 SGAEHMFSHKLDAIAPKPALHGEQCAIGTIMMMKLHGGDWEALKKTLVTIGTPTTAQEIGIGSEFIIQSLMEAHTIRVDR 320
Cdd:PRK00843  247 SGSEHLFSHALDRLAPGPALHGEQCGVGTIIMMYLHGGDWRKIRDALKKIGAPTTAKELGIDDEYIIEALTIAHTIRPER 326

                         330       340
                  ....*....|....*....|....
gi 2108433413 321 YTILG-SGLTKGVATELAESTGVI 343
Cdd:PRK00843  327 YTILGdRGLTREAAEKAARITGVI 350
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 3-343 1.29e-167

Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.


Pssm-ID: 341452  Cd Length: 343  Bit Score: 470.11  E-value: 1.29e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   3 LPREVLVGHDTLDNVGGACKRLKMEGPALIIADSNTKKIAGEAVIESLQqhNYEVLVTTIEDATIE---EVERVKVKIED 79
Cdd:cd08173     1 LPRNVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLE--SSGVEVVIVDIATIEeaaEVEKVKKLIKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  80 DKINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRIN 159
Cdd:cd08173    79 SKADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKPYSIKAKAPIAIIADTEIISKAPKRLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 160 AAGCGDLISNETAVLDWELAHKEKNEDISTYAKTLSKMTAFVIEKYAEIISAGGEEGAWHVIKALVASGVAMSIAGSSRP 239
Cdd:cd08173   159 AAGCGDLISNITAVKDWRLAHRLKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVRTVVKALISSGVAMSIAGSSRP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 240 CSGAEHMFSHKLDAIAPKPALHGEQCAIGTIMMMKLHGGDWEALKKTLVTIGTPTTAQEIGIGSEFIIQSLMEAHTIRVD 319
Cdd:cd08173   239 ASGSEHLFSHALDKLAPGPALHGEQCGVGTIMMAYLHGGDWKEIREALKKIGAPTTAKELGLDKEIIIEALTIAHKIRPE 318

                         330       340
                  ....*....|....*....|....*
gi 2108433413 320 RYTILG-SGLTKGVATELAESTGVI 343
Cdd:cd08173   319 RYTILGdNGLTEEAAERLARITGVI 343
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 1-329 2.17e-107

Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440140 [Multi-domain]  Cd Length: 355  Bit Score: 317.88  E-value: 2.17e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   1 MELPREVLVGHDTLDNVGGACKRLKmeGPALIIADSNTKKIAGEAVIESLQQHNYEV-LVTTIEDATIEEVERVKVKIED 79
Cdd:COG0371     3 IILPRRYVQGEGALDELGEYLADLG--KRALIITGPTALKAAGDRLEESLEDAGIEVeVEVFGGECSEEEIERLAEEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  80 DKINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDD---RKKSYDGHTPFALIADTAIIAQAPK 156
Cdd:COG0371    81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDgafDGYSFLAKNPDLVLVDTDIIAKAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 157 RINAAGCGDLISNETAVLDWELAHKE-KNEDISTYAKTLSKMTAFVIEKYAE--IISAG----GEEGAWHVIKALVASGV 229
Cdd:COG0371   161 RLLAAGIGDALAKWYEARDWSLAHRDlAGEYYTEAAVALARLCAETLLEYGEaaIKAVEagvvTPALERVVEANLLLSGL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 230 AMSIaGSSRPCSGAEHMFSHKLDAI-APKPALHGEQCAIGTIMMMKLHGGD--WEALKKTLVTIGTPTTAQEIGIGSEFI 306
Cdd:COG0371   241 AMGI-GSSRPGSGAAHAIHNGLTALpETHHALHGEKVAFGTLVQLVLEGRPeeIEELLDFLRSVGLPTTLADLGLDDETE 319

                         330       340
                  ....*....|....*....|...
gi 2108433413 307 IQSLMEAHTIRVDRYTILGSGLT 329
Cdd:COG0371   320 EELLTVAEAARPERYTILNLPFE 342
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
9-266 2.54e-78

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 239.90  E-value: 2.54e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   9 VGHDTLDNVGGACKRLKMEGpALIIADSNTKKIAGEAVIESLQQHNYEVLV--TTIEDATIEEVERVKVKIEDDKINLVL 86
Cdd:pfam13685   2 IGPGALGRLGEYLAELGFRR-VALVADANTYAAAGRKVAESLKRAGIEVETrlEVAGNADMETAEKLVGALRERDADAVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  87 GVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRINAAGCGDL 166
Cdd:pfam13685  81 GVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVDGKKRSIPAAAPFGVIADTDVIAAAPRRLLASGVGDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 167 ISNETAVLDWELAHKEKnedistYAKTLSKMTAFVIEKYA-EIISAGGEEgawhVIKALVASGVAMSIAGSSRPCSGAEH 245
Cdd:pfam13685 161 LAKITAVADWELAHAEE------VAAPLALLSAAMVMNFAdRPLRDPGDI----EALAELLSALAMGGAGSSRPASGSEH 230

                         250       260
                  ....*....|....*....|.
gi 2108433413 246 MFSHKLDAIAPKPALHGEQCA 266
Cdd:pfam13685 231 LISHALDMIAPKQALHGEQVG 251
 
Name Accession Description Interval E-value
egsA PRK00843
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
 1-343 0e+00

NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed


Pssm-ID: 179139  Cd Length: 350  Bit Score: 504.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   1 MELPREVLVGHDTLDNVGGACKRLKMEGPALIIADSNTKKIAGEAVIESLQQHnYEVLVTTIEDATIEEVERVKVKIEDD 80
Cdd:PRK00843    8 IQLPRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAGDRVEENLEDA-GDVEVVIVDEATMEEVEKVEEKAKDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  81 KINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRINA 160
Cdd:PRK00843   87 NAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGKPVSVKAKPPLAVIADTEIIAKAPYRLLA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 161 AGCGDLISNETAVLDWELAHKEKNEDISTYAKTLSKMTAFVIEKYAEIISAGGEEGAWHVIKALVASGVAMSIAGSSRPC 240
Cdd:PRK00843  167 AGCGDIISNYTAVKDWRLAHRLRGEYYSEYAAALSLMTAKMLIENADIIKPGLEESARLVVKALISSGVAMSIAGSSRPA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 241 SGAEHMFSHKLDAIAPKPALHGEQCAIGTIMMMKLHGGDWEALKKTLVTIGTPTTAQEIGIGSEFIIQSLMEAHTIRVDR 320
Cdd:PRK00843  247 SGSEHLFSHALDRLAPGPALHGEQCGVGTIIMMYLHGGDWRKIRDALKKIGAPTTAKELGIDDEYIIEALTIAHTIRPER 326

                         330       340
                  ....*....|....*....|....
gi 2108433413 321 YTILG-SGLTKGVATELAESTGVI 343
Cdd:PRK00843  327 YTILGdRGLTREAAEKAARITGVI 350
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
 3-343 1.29e-167

Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.


Pssm-ID: 341452  Cd Length: 343  Bit Score: 470.11  E-value: 1.29e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   3 LPREVLVGHDTLDNVGGACKRLKMEGPALIIADSNTKKIAGEAVIESLQqhNYEVLVTTIEDATIE---EVERVKVKIED 79
Cdd:cd08173     1 LPRNVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAGKRVEDLLE--SSGVEVVIVDIATIEeaaEVEKVKKLIKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  80 DKINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRIN 159
Cdd:cd08173    79 SKADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKPYSIKAKAPIAIIADTEIISKAPKRLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 160 AAGCGDLISNETAVLDWELAHKEKNEDISTYAKTLSKMTAFVIEKYAEIISAGGEEGAWHVIKALVASGVAMSIAGSSRP 239
Cdd:cd08173   159 AAGCGDLISNITAVKDWRLAHRLKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVRTVVKALISSGVAMSIAGSSRP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 240 CSGAEHMFSHKLDAIAPKPALHGEQCAIGTIMMMKLHGGDWEALKKTLVTIGTPTTAQEIGIGSEFIIQSLMEAHTIRVD 319
Cdd:cd08173   239 ASGSEHLFSHALDKLAPGPALHGEQCGVGTIMMAYLHGGDWKEIREALKKIGAPTTAKELGLDKEIIIEALTIAHKIRPE 318

                         330       340
                  ....*....|....*....|....*
gi 2108433413 320 RYTILG-SGLTKGVATELAESTGVI 343
Cdd:cd08173   319 RYTILGdNGLTEEAAERLARITGVI 343
GldA COG0371
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ...
 1-329 2.17e-107

Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440140 [Multi-domain]  Cd Length: 355  Bit Score: 317.88  E-value: 2.17e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   1 MELPREVLVGHDTLDNVGGACKRLKmeGPALIIADSNTKKIAGEAVIESLQQHNYEV-LVTTIEDATIEEVERVKVKIED 79
Cdd:COG0371     3 IILPRRYVQGEGALDELGEYLADLG--KRALIITGPTALKAAGDRLEESLEDAGIEVeVEVFGGECSEEEIERLAEEAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  80 DKINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDD---RKKSYDGHTPFALIADTAIIAQAPK 156
Cdd:COG0371    81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDgafDGYSFLAKNPDLVLVDTDIIAKAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 157 RINAAGCGDLISNETAVLDWELAHKE-KNEDISTYAKTLSKMTAFVIEKYAE--IISAG----GEEGAWHVIKALVASGV 229
Cdd:COG0371   161 RLLAAGIGDALAKWYEARDWSLAHRDlAGEYYTEAAVALARLCAETLLEYGEaaIKAVEagvvTPALERVVEANLLLSGL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 230 AMSIaGSSRPCSGAEHMFSHKLDAI-APKPALHGEQCAIGTIMMMKLHGGD--WEALKKTLVTIGTPTTAQEIGIGSEFI 306
Cdd:COG0371   241 AMGI-GSSRPGSGAAHAIHNGLTALpETHHALHGEKVAFGTLVQLVLEGRPeeIEELLDFLRSVGLPTTLADLGLDDETE 319

                         330       340
                  ....*....|....*....|...
gi 2108433413 307 IQSLMEAHTIRVDRYTILGSGLT 329
Cdd:COG0371   320 EELLTVAEAARPERYTILNLPFE 342
G1PDH-like cd08174
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ...
 4-324 4.53e-96

Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.


Pssm-ID: 341453 [Multi-domain]  Cd Length: 332  Bit Score: 288.26  E-value: 4.53e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLKME-GPALIIADSNTKKIAGEAVIESLQQHNYEVLVTTIEDATIEEVerVKVKIEDDKI 82
Cdd:cd08174     1 PLILKIEEGALEHLGKYLADRNQGfGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEENTDNSAEEL--AEKAFSLPKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  83 NLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRINAAG 162
Cdd:cd08174    79 DAIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGKRKSLGAKMPYGVIVDLDVIKSAPRRLILAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 163 CGDLISNETAVLDWELAHKEKNEDISTYAKTLSKMTAFVI--EKYAEIISaggEEGAWHVIKALVASGVAMSIAGSSRPC 240
Cdd:cd08174   159 IGDLISNITALYDWKLAEEKGGEPVDDFAYLLSRTAADSLlnTPGKDIKD---DEFLKELAESLVLSGIAMEIAGSSRPA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 241 SGAEHMFSHKLDAIAPKPALHGEQCAIGTIMMMKLHGGDWEALKKTLVTIGTPTTAQEIGIGSEFIIQSLMEAHTIRVDR 320
Cdd:cd08174   236 SGSEHLISHALDKLFPGPALHGIQVGLGTYFMSFLQGQRYEEIRDVLKRTGFPLNPSDLGLTKEEFIEAVKLAPSTRPGR 315


                  ....
gi 2108433413 321 YTIL 324
Cdd:cd08174   316 YTIL 319
G1PDH_related cd08549
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ...
 4-325 8.39e-93

Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.


Pssm-ID: 341479 [Multi-domain]  Cd Length: 331  Bit Score: 279.83  E-value: 8.39e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLKMEGPaLIIADSNTKKIAGEAVIESLQQHnyeVLVTTIEDATIEEVERVKVKIEDdkin 83
Cdd:cd08549     1 PRYTIVGDGAINKIEEILKKLNLKRV-LIITGKNTKAKYCRFFYDQLKTV---CDIVYYDNIDNLEDELKKYTFYD---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  84 LVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRINAAGC 163
Cdd:cd08549    73 CVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIPGVKKTFMADAPIAIIADTEIIKKSPRRLLSAGI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 164 GDLISNETAVLDWELAHKEKNEDISTYAKTLSKMTAFVIEKYAEiISAGGEEGAWHVIKALVASGVAMSIAGSSRPCSGA 243
Cdd:cd08549   153 GDLVSNITAVLDWKLAHKEKGEKYSEFAAILSKTSAKELVSYVL-KASDLEEYHRVLVKALVGSGIAMAIAGSSRPASGS 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 244 EHMFSHKLDAIAPK----PALHGEQCAIGTIMMMKLHG-------GDWEALKKTLVTIGTPTTAQEIGIGSEFIIQSLME 312
Cdd:cd08549   232 EHLFSHALDKLKEEylniNVLHGEQVGVGTIIMSYLHEkenkklsGLHERIKMILKKVGAPTTAKQLGIDEDLIIEALTE 311

                         330
                  ....*....|...
gi 2108433413 313 AHTIRVDRYTILG 325
Cdd:cd08549   312 AHKIRPRRYTLLD 324
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
 5-324 2.68e-80

Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.


Pssm-ID: 341454  Cd Length: 340  Bit Score: 248.19  E-value: 2.68e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   5 REVLVGHDTLDNVGGACKRLKMEGPALIIADSNTKKIAGEAVIESLQQHNYEVLVTTI---EDATIEEVERVKVKIE-DD 80
Cdd:cd08175     2 KEIVIGEGALKKLPEYLKELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFpgeGDLIADEAAVGKVLLElEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  81 KINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRINA 160
Cdd:cd08175    82 DTDLIIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIVDGVKKTFPAHAPKAIFADLDVLANAPQRMIA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 161 AGCGDLISNETAVLDWELAHKEKNEDISTYAktlSKMTAFVIEKY---AEIISAGGEEGAWHVIKALVASGVAMSIAGSS 237
Cdd:cd08175   162 AGFGDLLGKYTALADWKLSHLLGGEYYCPEV---ADLVQEALEKCldnAEGIAARDPEAIEALMEALILSGLAMQLVGNS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 238 RPCSGAEHMFSH----KLDAIAPKPALHGEQCAIGTIMMMKLHGGD----WEALKKTLVTIGTPTTAQEIGIGSEFIIQS 309
Cdd:cd08175   239 RPASGAEHHLSHywemEFLRLGKPPVLHGEKVGVGTLLIAALYILEqlppPEELRELLRKAGAPTTPEDLGIDRDLLRDS 318

                         330
                  ....*....|....*
gi 2108433413 310 LMEAHTIRvDRYTIL 324
Cdd:cd08175   319 LRLAKEIR-DRYTVL 332
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
9-266 2.54e-78

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 239.90  E-value: 2.54e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   9 VGHDTLDNVGGACKRLKMEGpALIIADSNTKKIAGEAVIESLQQHNYEVLV--TTIEDATIEEVERVKVKIEDDKINLVL 86
Cdd:pfam13685   2 IGPGALGRLGEYLAELGFRR-VALVADANTYAAAGRKVAESLKRAGIEVETrlEVAGNADMETAEKLVGALRERDADAVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  87 GVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPFALIADTAIIAQAPKRINAAGCGDL 166
Cdd:pfam13685  81 GVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVDGKKRSIPAAAPFGVIADTDVIAAAPRRLLASGVGDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 167 ISNETAVLDWELAHKEKnedistYAKTLSKMTAFVIEKYA-EIISAGGEEgawhVIKALVASGVAMSIAGSSRPCSGAEH 245
Cdd:pfam13685 161 LAKITAVADWELAHAEE------VAAPLALLSAAMVMNFAdRPLRDPGDI----EALAELLSALAMGGAGSSRPASGSEH 230

                         250       260
                  ....*....|....*....|.
gi 2108433413 246 MFSHKLDAIAPKPALHGEQCA 266
Cdd:pfam13685 231 LISHALDMIAPKQALHGEQVG 251
GlyDH-like cd08550
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ...
 4-304 3.86e-29

Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.


Pssm-ID: 341480 [Multi-domain]  Cd Length: 347  Bit Score: 114.56  E-value: 3.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRL--KmegpALIIADSNTKKIAGEAVIESLQQHN--YEVLVTTIEdATIEEVERVKVKIED 79
Cdd:cd08550     1 PGRYIQEPGILAKAGEYIAPLgkK----ALIIGGKTALEAVGEKLEKSLEEAGidYEVEVFGGE-CTEENIERLAEKAKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  80 DKINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDG---HTPFALIADTAIIAQAPK 156
Cdd:cd08550    76 EGADVIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSllkRSPDLVLVDTDIIAAAPV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 157 RINAAGCGDLIS--NETAVLdwelaHKEKNEDISTYAKT-LSKMTAFVIEKYAE--IISAGGEEG--AWH-VIKALVA-S 227
Cdd:cd08550   156 RYLAAGIGDTLAkwYEARPS-----SRGGPDDLALQAAVqLAKLAYDLLLEYGVqaVEDVRQGKVtpALEdVVDAIILlA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 228 GVAMSIaGSSRPCSGAEHMFSHKLDAIAP-KPALHGEQCAIGTIMMMKLHG---GDWEALKKTLVTIGTPTTAQEIGIGS 303
Cdd:cd08550   231 GLVGSL-GGGGCRTAAAHAIHNGLTKLPEtHGTLHGEKVAFGLLVQLALEGrseEEIEELIEFLRRLGLPVTLEDLGLEL 309


                  .
gi 2108433413 304 E 304
Cdd:cd08550   310 T 310
GlyDH cd08170
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ...
 10-302 6.95e-27

Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.


Pssm-ID: 341449 [Multi-domain]  Cd Length: 351  Bit Score: 108.65  E-value: 6.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  10 GHDTLDNVGGACKRLKmeGPALIIADSNTKKIAGEAVIESLQQHNYEVLVTTIE-DATIEEVERVKVKIEDDKINLVLGV 88
Cdd:cd08170     7 GPGALDRLGEYLAPLG--KKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGgECSREEIERLAAIARANGADVVIGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  89 GGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDD-RKKSYD--GHTPFALIADTAIIAQAPKRINAAGCGD 165
Cdd:cd08170    85 GGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDgEFDEYLflPRNPDLVLVDTEIIAKAPVRFLVAGMGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 166 LISneTAvldWE-LAHKEKNEDisTYAKTLSKMTAFVI-EKYAEIISAGG-------EEGAW-----HVIKALV-ASGVA 230
Cdd:cd08170   165 ALA--TY---FEaRACARSGAP--NMAGGRPTLAALALaELCYDTLLEYGvaakaavEAGVVtpaleAVIEANTlLSGLG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108433413 231 MSIAGssrpCSGAeHMFSHKLDAI-APKPALHGEQCAIGTIMMMKLHGGDWEALKKTL---VTIGTPTTAQEIGIG 302
Cdd:cd08170   238 FESGG----LAAA-HAIHNGLTALpETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIrfcRSVGLPVTLADLGLE 308
gldA PRK09423
glycerol dehydrogenase; Provisional
 10-304 1.34e-25

glycerol dehydrogenase; Provisional


Pssm-ID: 181843  Cd Length: 366  Bit Score: 105.28  E-value: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  10 GHDTLDNVGGACKRLKMEgpALIIADSNTKKIAGEAVIESLQQHNYEVLVTTIE-DATIEEVERVKVKIEDDKINLVLGV 88
Cdd:PRK09423   14 GKGALARLGEYLKPLGKR--ALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNgECSDNEIDRLVAIAEENGCDVVIGI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  89 GGGRPIDVAKLSSFHKEVPFISVPTAASHDGIVSSRASIWVDDRK-KSYD--GHTPFALIADTAIIAQAPKRINAAGCGD 165
Cdd:PRK09423   92 GGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEfERYLflPKNPDLVLVDTAIIAKAPARFLAAGIGD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 166 LISNetavldWELAHKEKNEDISTYAKTLSKMTAFVI-EKYAEIISAGG-------EEGAwhVIKALVA--------SGV 229
Cdd:PRK09423  172 ALAT------WFEARACSRSGGTTMAGGKPTLAALALaELCYETLLEDGlkaklavEAKV--VTPALENvieantllSGL 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108433413 230 AMSIAGssrpCSGAeHMFSHKLDAIAP-KPALHGEQCAIGTIMMMKLHGGDWEALKKTL---VTIGTPTTAQEIGIGSE 304
Cdd:PRK09423  244 GFESGG----LAAA-HAIHNGLTALEDtHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIdfcHAVGLPTTLADLGLKED 317
DHQ_Fe-ADH cd07766
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 30-304 2.82e-22

Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


Pssm-ID: 341447 [Multi-domain]  Cd Length: 271  Bit Score: 94.35  E-value: 2.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  30 ALIIADSNTKKIAGEAVIESLQQH-NYEVLVTTIEDATIEEVERVKVKIEDDKINLVLGVGGGRPIDVAK---LSSFHKe 105
Cdd:cd07766    25 ALVVSDEGVVKGVGEKVADSLKKGlAVAIFDFVGENPTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKavaALLNRG- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 106 VPFISVPTAASHDGIVSSRASIWVDDRKKSYDG--HTPFALIADTAIIAQAPKRINAAGCGDLISNetavldwelahkek 183
Cdd:cd07766   104 IPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGphYNPDVVFVDTDITKGLPPRQVASGGVDALAH-------------- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 184 nedistyaktlskmtafviekyaeiisaggeegaWHVIKALVASGVAMSIAGSSRPCSGAEHMFSHKLDAIapKPALHGE 263
Cdd:cd07766   170 ----------------------------------AVELEKVVEAATLAGMGLFESPGLGLAHAIGHALTAF--EGIPHGE 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2108433413 264 QCAIGTIMMMKLH-------GGDWEALKKTLVTIGTPTTAQEIGIGSE 304
Cdd:cd07766   214 AVAVGLPYVLKVAndmnpepEAAIEAVFKFLEDLGLPTHLADLGVSKE 261
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
4-165 8.09e-16

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 77.26  E-value: 8.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLKMegPALIIADSNTKKI-AGEAVIESLQQHNYEVLV--TTIEDATIEEVERVKVKIEDD 80
Cdd:pfam00465   1 PTRIVFGAGALAELGEELKRLGA--RALIVTDPGSLKSgLLDKVLASLEEAGIEVVVfdGVEPEPTLEEVDEAAALAREA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  81 KINLVLGVGGGRPIDVAKLSSF------------------HKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYDGHTPF 142
Cdd:pfam00465  79 GADVIIAVGGGSVIDTAKAIALlltnpgdvwdylggkpltKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPK 158

                         170       180
                  ....*....|....*....|....*..
gi 2108433413 143 AL----IADTAIIAQAPKRINAAGCGD 165
Cdd:pfam00465 159 LLpdlaILDPELTLTLPPRLTAATGMD 185
GlyDH-like cd08171
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 42-323 8.55e-14

Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.


Pssm-ID: 341450  Cd Length: 345  Bit Score: 71.40  E-value: 8.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  42 AGEAVIESLQQHNYEVLVTTI--EDATIEEVERVKVKIEDDKINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTAASHDG 119
Cdd:cd08171    37 AKPKLRAALEGSGLEITDFIWygGEATYENVEKLKANPEVQEADMIFAVGGGKAIDTVKVLADRLNKPVFTFPTIASNCA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 120 IVSSRASIWVDDR--KKSYDGHTP--FALIaDTAIIAQAPKRINAAGCGDLISNETAVL----DWELAHkeknedISTYA 191
Cdd:cd08171   117 AVTAVSVMYNPDGsfKEYYFLKRPpvHTFI-DTEIIAEAPEKYLWAGIGDTLAKYYEVEfsarGDELDH------TNALG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 192 KTLSKMTAFVIEKYAE---------IISAGGEEGAWHVIkalVASGVAmSIAGSSRPCSGAEHMFSHKLDAI--APKPAL 260
Cdd:cd08171   190 VAISKMCSEPLLKYGVqaledcranKVSDALEQVVLDII---VTTGLV-SNLVEPDYNSSLAHALYYGLTTLpqIEEEHL 265

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108433413 261 HGEQCAIGTIMMMKLHgGDWEALKKTLV---TIGTPTTAQEIGIGSEF---IIQSLMEAHTIRVDRYTI 323
Cdd:cd08171   266 HGEVVSYGVLVLLTVD-GQFEELEKVYAfnkSIGLPTCLADLGLTVEDlekVLDKALKTKDLRHSPYPI 333
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
 7-293 2.86e-12

Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.


Pssm-ID: 341448 [Multi-domain]  Cd Length: 328  Bit Score: 66.66  E-value: 2.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   7 VLVGHDTLDNVGGAcKRLKMEGPALIIADSNTKKIAGEAVIESLQQH-NYEVLVTTI--EDATIEEVERVKVKIEDDKIN 83
Cdd:cd08169     4 VFFGEGVFESVNSY-IPRDAFDQCLIIVDSGVPDLIVNYLAEYFGYYlEVHVFIIQGgeAYKTFQTVVEELERAAALHLN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  84 ---LVLGVGGGRPIDVA--KLSSFHKEVPFISVPTA--ASHDGIVSSRASIwvDDRK-KSYDG--HTPFALIADTAIIAQ 153
Cdd:cd08169    83 rhsAVVAVGGGATGDVVgfAAATYFRGIAFIRVPTTllAQSDSSVGIKVGI--NTRGgKNLLGafYPPRAVFADFSFLKT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 154 APKRINAAGCGDLISNetAVLdwelAHKEKNEDISTYA--------KTLSKMTAFVIEKYAEIISAGGEEgawhvikalv 225
Cdd:cd08169   161 LPFRQVRAGMAELVKM--ALI----ADNDFFEFLEDKAnsatvyspEQLEKLINKCISLKLDVVVADEDE---------- 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108433413 226 asgvamsiAGSSRPCSGAeHMFSHKLDAIAPKPALHGEQCAIGTIM---------MMKLHggDWEALKKTLVTIGTP 293
Cdd:cd08169   225 --------QGKRRGLNYG-HTFGHALELASGYKIPHGEAVAVGMAYaakianrlgLLPEH--DVSRIIWLLNKLGLP 290
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 4-115 6.46e-11

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


Pssm-ID: 341481 [Multi-domain]  Cd Length: 372  Bit Score: 62.85  E-value: 6.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLKMeGPALIIADSNTKKI-AGEAVIESLQQHNYEVLV-TTIE-DATIEEVERVKVKIEDD 80
Cdd:cd08551     1 PTRIVFGAGALARLGEELKALGG-KKVLLVTDPGLVKAgLLDKVLESLKAAGIEVEVfDDVEpNPTVETVEAAAELAREE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2108433413  81 KINLVLGVGGGRPIDVAKLSSF------------------HKEVPFISVPTAA 115
Cdd:cd08551    80 GADLVIAVGGGSVLDTAKAIAVlatnggsirdyegigkvpKPGLPLIAIPTTA 132
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
3-161 1.99e-10

Alcohol dehydrogenase, class IV [Energy production and conversion];


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 61.29  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   3 LPREVLVGHDTLDNVGGACKRLKMEgPALIIADSNTKKI-AGEAVIESLQQHNYEVLV--TTIEDATIEEVERVKVKIED 79
Cdd:COG1454     7 LPTRIVFGAGALAELGEELKRLGAK-RALIVTDPGLAKLgLLDRVLDALEAAGIEVVVfdDVEPNPTVETVEAGAAAARE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  80 DKINLVLGVGGGRPIDVAKLSSF------------------HKEVPFISVPT---AASHdgiVSSRASIWVDDRKKSYDG 138
Cdd:COG1454    86 FGADVVIALGGGSAIDAAKAIALlatnpgdledylgikkvpGPPLPLIAIPTtagTGSE---VTPFAVITDPETGVKKGI 162

                         170       180
                  ....*....|....*....|....*...
gi 2108433413 139 HTPfALIADTAII-----AQAPKRINAA 161
Cdd:COG1454   163 ADP-ELLPDVAILdpeltLTLPPSLTAA 189
GlyDH-like cd08172
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ...
 65-165 6.16e-10

Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.


Pssm-ID: 341451 [Multi-domain]  Cd Length: 346  Bit Score: 59.84  E-value: 6.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  65 ATIEEVERVKVKIEDDKINLVLGVGGGRPIDVAKLSSFHKEVPFISVPTaashdgIVSSRA-----SIWVDD----RKKS 135
Cdd:cd08172    59 CSYEEIDRLAEEAKEHQADVIIGIGGGKVLDTAKAVADKLNIPLILIPT------LASNCAawtplSVIYDEdgefIGYD 132

                          90       100       110
                  ....*....|....*....|....*....|
gi 2108433413 136 YDGHTPFALIADTAIIAQAPKRINAAGCGD 165
Cdd:cd08172   133 YFPRSAYLVLVDPRLLLDSPKDYFVAGIGD 162
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
 6-113 4.71e-09

3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440106  Cd Length: 355  Bit Score: 57.02  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   6 EVLVGHDTLDNVGGACKRLKMEGPALIIADSNTKKIAGEAVIESLQQHNYEVLVTTIEDA----TIEEVERV-----KVK 76
Cdd:COG0337    14 DIRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAAGFEVHLLVLPDGeaskTLETLERIldallEAG 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2108433413  77 IE-DDkinLVLGVGGGRPIDVAKL--SSFHKEVPFISVPT 113
Cdd:COG0337    94 LDrDD---LVVALGGGVVGDLAGFaaATYLRGVPFIQVPT 130
Fe-ADH-like cd14863
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 1-115 1.07e-07

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341485 [Multi-domain]  Cd Length: 380  Bit Score: 52.92  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   1 MELPREVLVGHDTLDNVGGACKRLKMEgPALIIADSNTKKiAG--EAVIESLQQHNYEVLV-TTIE-DATIEEVERVKVK 76
Cdd:cd14863     2 YSQLTPVIFGAGAVEQIGELLKELGCK-KVLLVTDKGLKK-AGivDKIIDLLEEAGIEVVVfDDVEpDPPDEIVDEAAEI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2108433413  77 IEDDKINLVLGVGGGRPIDVAKL-------------------SSFHKEVPFISVPTAA 115
Cdd:cd14863    80 AREEGADGVIGIGGGSVLDTAKAiavlltnpgpiidyalagpPVPKPGIPLIAIPTTA 137
Fe-ADH-like cd14862
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 30-107 9.52e-07

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341484 [Multi-domain]  Cd Length: 375  Bit Score: 49.92  E-value: 9.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  30 ALIIADSNTKKIAG-EAVIESLQQHNYEVLV--TTIEDATIEEVERVKVKIEDDKINLVLGVGGGRPIDVAKLSSFHKEV 106
Cdd:cd14862    27 ALIVTDKVLVKLGLlKKVLKRLLQAGFEVEVfdEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAKAAWVLYER 106


                  .
gi 2108433413 107 P 107
Cdd:cd14862   107 P 107
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 4-115 1.76e-06

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.


Pssm-ID: 341473 [Multi-domain]  Cd Length: 378  Bit Score: 49.07  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLKMEGPaLIIADSNTKKI-AGEAVIESLQQHN--YEVLVTTIEDATIEEVERVKVKIEDD 80
Cdd:cd08194     1 PRTIIIGGGALEELGEEAASLGGKRA-LIVTDKVMVKLgLVDKVTQLLAEAGiaYAVFDDVVSEPTDEMVEEGLALYKEG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2108433413  81 KINLVLGVGGGRPIDVAK-----------LSSFHKE-------VPFISVPTAA 115
Cdd:cd08194    80 GCDFIVALGGGSPIDTAKaiavlatnggpIRDYMGPrkvdkpgLPLIAIPTTA 132
Fe-ADH-like cd14864
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 3-238 2.29e-06

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341486 [Multi-domain]  Cd Length: 376  Bit Score: 48.84  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   3 LPREVLVGHDTLDNVGGACKRLKMEgpALIIADSNTK--KIAGEaVIESLQQHNYEVLV-TTIED-ATIEEVERVKVKIE 78
Cdd:cd14864     3 IPPNIVFGADSLERIGEEVKEYGSR--FLLITDPVLKesGLADK-IVSSLEKAGISVIVfDEIPAsATSDTIDEAAELAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  79 DDKINLVLGVGGGRPIDVAKLSSF------------------HKEVPFISVPTAAsHDGIVSSRASIWVDDRKKS----- 135
Cdd:cd14864    80 KAGADGIIAVGGGKVLDTAKAVAIlanndggaydflegakpkKKPLPLIAVPTTP-RSGFEFSDRFPVVDSRSREvkllk 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 136 YDGHTPFALIADTAIIAQA-PKRINAAGCGDL-------ISNETAVLDWELAHKEknedISTYAKTLSKMTA-FVIEKYA 206
Cdd:cd14864   159 AQPGLPKAVIVDPNLMASLtGNQTAAMALAALalaveayLSKKSNFFSDALALKA----IELVSENLDGALAdPKNTPAE 234

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2108433413 207 EIISAGGeegawhVIKALVAS------GVAMSIAGSSR 238
Cdd:cd14864   235 ELLAQAG------CLAGLAASssspglATALALAVNSR 266
NADPH_BDH cd08179
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ...
 3-267 3.50e-06

NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.


Pssm-ID: 341458 [Multi-domain]  Cd Length: 379  Bit Score: 48.34  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   3 LPREVLVGHDTLD---NVGGacKRlkmegpALIIADSNTKKIAG--EAVIESLQQHNYEVLV-TTIE-DATIEEVERVKV 75
Cdd:cd08179     4 VPRDIYFGEGALEylkTLKG--KR------AFIVTGGGSMKRNGflDKVEDYLKEAGMEVKVfEGVEpDPSVETVEKGAE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  76 KIEDDKINLVLGVGGGRPIDVAK---------------------LSSFHKEVPFISVPT---AASHdgivSSRASIWVDD 131
Cdd:cd08179    76 AMREFEPDWIIAIGGGSVIDAAKamwvfyeypeltfedalvpfpLPELRKKARFIAIPStsgTGSE----VTRASVITDT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 132 RKKSYDGHTPFALIADTAII-----AQAPKRInAAGCG-DLISN--ETAVldwelahkekNEDISTYAKTLSKMTAFVIE 203
Cdd:cd08179   152 EKGIKYPLASFEITPDVAILdpeltMTMPPHV-TANTGmDALTHaiEAYV----------STLANDFTDALALGAILDIF 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108433413 204 KYAEIISAGGEEgawhvIKA----LVASGVA-MSIAGSsrpCSGAEHMFSHKLDAIAPKPalHGEQCAI 267
Cdd:cd08179   221 ENLPKSYNGGKD-----LEArekmHNASCLAgMAFSNS---GLGIVHSMAHKGGAFFGIP--HGLANAI 279
EEVS cd08199
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ...
 28-113 4.38e-06

2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.


Pssm-ID: 341478  Cd Length: 349  Bit Score: 47.91  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  28 GPALIIADSNTKKIAGEAVIESLQQHN----YEVLVTTIEDATIEEVERVKVKIEDDKIN---LVLGVGGGRPIDVAKL- 99
Cdd:cd08199    27 RRRLVVVDENVDRLYGARIRAYFAAHGieatILVLPGGEANKTMETVLRIVDALDDFGLDrrePVIAIGGGVLLDVVGFa 106

                          90
                  ....*....|....*
gi 2108433413 100 -SSFHKEVPFISVPT 113
Cdd:cd08199   107 aSLYRRGVPYIRVPT 121
Fe-ADH-like cd08196
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 1-151 4.77e-06

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341475 [Multi-domain]  Cd Length: 367  Bit Score: 47.96  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   1 MELPREVLVGHDTLDNVGGACKRLKMEGPaLIIADSNTKKiagEAVIESLQQHNYEVLVTTIEDA----TIEEVERVKVK 76
Cdd:cd08196     3 YYQPVKIIFGEGILKELPDIIKELGGKRG-LLVTDPSFIK---SGLAKRIVESLKGRIVAVFSDVepnpTVENVDKCARL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  77 IEDDKINLVLGVGGGRPIDVAKLSS-------------------FHKEVPFISVPTAASHDGIVSSRASIWVDDRKKSYD 137
Cdd:cd08196    79 ARENGADFVIAIGGGSVLDTAKAAAclaktdgsiedylegkkkiPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAP 158

                         170
                  ....*....|....
gi 2108433413 138 GHTPFaLIADTAII 151
Cdd:cd08196   159 LVSPG-FYPDIAIV 171
PLN02834 PLN02834
3-dehydroquinate synthase
 30-271 5.42e-06

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 47.84  E-value: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  30 ALIIADSNTKKIAGEAVIESLQQHNYEVLVTTI------EDATIEEVERVKVK-IED--DKINLVLGVGGGRPIDVAKL- 99
Cdd:PLN02834  103 VLVVTNETVAPLYLEKVVEALTAKGPELTVESVilpdgeKYKDMETLMKVFDKaLESrlDRRCTFVALGGGVIGDMCGFa 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 100 -SSFHKEVPFISVPTA--ASHDGIVSSRASiwVDDR-KKSYDG--HTPFALIADTAIIAQAPKRINAAGCGDLIS----N 169
Cdd:PLN02834  183 aASYQRGVNFVQIPTTvmAQVDSSVGGKTG--VNHPlGKNMIGafYQPQCVLIDTDTLATLPDRELASGIAEVVKygliR 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413 170 ETAVLDWELAHKEK----NEDISTYAKTLSkmtafvIEKYAEIISAGGEEgawhvikalvaSGVamsiagssRPCSGAEH 245
Cdd:PLN02834  261 DAEFFEWQEANMEKllarDPGALAYAIKRS------CENKAEVVSLDEKE-----------SGL--------RATLNLGH 315

                         250       260
                  ....*....|....*....|....*..
gi 2108433413 246 MFSHKLDA-IAPKPALHGEQCAIGTIM 271
Cdd:PLN02834  316 TFGHAIETgPGYGEWLHGEAVAAGTVM 342
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
 6-113 1.09e-05

Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.


Pssm-ID: 341474  Cd Length: 343  Bit Score: 46.67  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   6 EVLVGHDTLDNVGgACKRLKMEGPALIIADSNTKKIAGEAVIESLQQHNYEVLVTTIEDA----TIEEVERVKVKIEDDK 81
Cdd:cd08195     3 PILIGSGLLDKLG-ELLELKKGSKVVIVTDENVAKLYGELLLKSLEAAGFKVEVIVIPAGekskSLETVERIYDFLLEAG 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2108433413  82 IN---LVLGVGGGRPID----VAklSSFHKEVPFISVPT 113
Cdd:cd08195    82 LDrdsLLIALGGGVVGDlagfVA--STYMRGIPFIQVPT 118
Fe-ADH-like cd08189
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 6-115 1.31e-05

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.


Pssm-ID: 341468 [Multi-domain]  Cd Length: 378  Bit Score: 46.31  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   6 EVLVGHDTLDNVGGACKRLKMEGPaLIIADSNTKKiAG--EAVIESLQQHNYEVLV--TTIEDATIEEVERVKVKIEDDK 81
Cdd:cd08189     7 ELFEGAGSLLQLPEALKKLGIKRV-LIVTDKGLVK-LGllDPLLDALKKAGIEYVVfdGVVPDPTIDNVEEGLALYKENG 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2108433413  82 INLVLGVGGGRPIDVAK-------------------LSSFHKEVPFISVPTAA 115
Cdd:cd08189    85 CDAIIAIGGGSVIDCAKviaaraanpkksvrklkglLKVRKKLPPLIAVPTTA 137
HEPD cd08182
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ...
 4-151 1.54e-05

Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.


Pssm-ID: 341461 [Multi-domain]  Cd Length: 370  Bit Score: 46.06  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLKMEGPALIIADSNTKKIAGEAVIESLQQHnyeVLVTTIEDA----TIEEVERVKVKIED 79
Cdd:cd08182     1 PVKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGGR---IPVVVFSDFspnpDLEDLERGIELFRE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  80 DKINLVLGVGGGRPIDVAKLSSFHKE--------------------VPFISVPTAA---SHdgiVSSRASIWVDDRKKSY 136
Cdd:cd08182    78 SGPDVIIAVGGGSVIDTAKAIAALLGspgenllllrtgekapeenaLPLIAIPTTAgtgSE---VTPFATIWDEAEGKKY 154

                         170
                  ....*....|....*
gi 2108433413 137 DGHTPfALIADTAII 151
Cdd:cd08182   155 SLAHP-SLYPDAAIL 168
Fe-ADH-like cd08185
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 1-115 8.05e-05

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341464 [Multi-domain]  Cd Length: 379  Bit Score: 44.03  E-value: 8.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   1 MELPREVLVGHDTLDNVGGACKRL--KmegpALIIADSNTKKIAG--EAVIESLQQHNYEV----------LVTTIEDAt 66
Cdd:cd08185     1 YYQPTRILFGAGKLNELGEEALRPgkK----ALIVTGKGSSKKTGllDRVKKLLEKAGVEVvvfdkvepnpLTTTVMEG- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108433413  67 ieeVERVKvkieDDKINLVLGVGGGRPIDVAKLSSF----------------------HKEVPFISVPTAA 115
Cdd:cd08185    76 ---AALAK----EEGCDFVIGLGGGSSMDAAKAIAFmatnpgdiwdyifggtgkgpppEKALPIIAIPTTA 139
PDD cd08180
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ...
 3-113 1.39e-04

1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.


Pssm-ID: 341459 [Multi-domain]  Cd Length: 333  Bit Score: 43.25  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   3 LPREVLVGHDTLDNVggacKRLKMEGpALIIADSNTKKIAG-EAVIESLQQHN-YEVLVTTIEDATIEEVERVKVKIEDD 80
Cdd:cd08180     3 LKTKIYSGEDSLERL----KELKGKR-VFIVTDPFMVKSGMvDKVTDELDKSNeVEIFSDVVPDPSIEVVAKGLAKILEF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2108433413  81 KINLVLGVGGGRPIDVAK--------LSSFHKEVPFISVPT 113
Cdd:cd08180    78 KPDTIIALGGGSAIDAAKaiiyfalkQKGNIKKPLFIAIPT 118
Fe-ADH-like cd08191
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 3-115 2.82e-04

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.


Pssm-ID: 341470 [Multi-domain]  Cd Length: 392  Bit Score: 42.22  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   3 LPREVLVGHDTLDNVGGACKRLKMEgpALIIADSNTKKIAG-EAVIESLQQHNYEVLVttiEDATIEEVERVKVKIE--- 78
Cdd:cd08191     3 SPSRLLFGPGARRALGRVAARLGSR--VLIVTDPRLASTPLvAELLAALTAAGVAVEV---FDGGQPELPVSTVADAaaa 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2108433413  79 --DDKINLVLGVGGGRPIDVAKL-----------SSFHKE-------VPFISVPTAA 115
Cdd:cd08191    78 arAFDPDVVIGLGGGSNMDLAKVvalllahggdpRDYYGEdrvpgpvLPLIAVPTTA 134
Fe-ADH-like cd08183
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 4-115 2.97e-04

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341462 [Multi-domain]  Cd Length: 377  Bit Score: 42.10  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLkmEGPALIIADSNT-KKIAGEAVIESLQQHNYEV-LVTTIEDATIEEVERVKVKIEDDK 81
Cdd:cd08183     1 PPRIVFGRGSLQELGELAAEL--GKRALLVTGRSSlRSGRLARLLEALEAAGIEVaLFSVSGEPTVETVDAAVALAREAG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2108433413  82 INLVLGVGGGRPIDVAK----------------------LSSFHKEVPFISVPTAA 115
Cdd:cd08183    79 CDVVIAIGGGSVIDAAKaiaalltnegsvldylevvgkgRPLTEPPLPFIAIPTTA 134
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
 10-99 3.35e-04

Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.


Pssm-ID: 341469 [Multi-domain]  Cd Length: 412  Bit Score: 42.15  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  10 GHDTLDNVGGACKRLKMEGPaLIIADSNTKKIAG-EAVIESLQQHNYEVLV---TTIE--DATIEEVERVkvkIEDDKIN 83
Cdd:cd08190     7 GPGATRELGMDLKRLGAKKV-LVVTDPGLAKLGLvERVLESLEKAGIEVVVydgVRVEptDESFEEAIEF---AKEGDFD 82

                          90
                  ....*....|....*.
gi 2108433413  84 LVLGVGGGRPIDVAKL 99
Cdd:cd08190    83 AFVAVGGGSVIDTAKA 98
Fe-ADH-like cd14865
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 4-115 1.05e-03

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341487 [Multi-domain]  Cd Length: 383  Bit Score: 40.60  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLKMEGPaLIIADSNTKKiAG--EAVIESLQQHNYEVLV--TTIEDATIEEVERVKVKIED 79
Cdd:cd14865     6 PTKIVSGAGALENLPAELARLGARRP-LIVTDKGLAA-AGllKKVEDALGDAIEIVGVfdDVPPDSSVAVVNEAAARARE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2108433413  80 DKINLVLGVGGGRPIDVAK---------------LSSF----HKEVPFISVPTAA 115
Cdd:cd14865    84 AGADGIIAVGGGSVIDTAKgvnillseggddlddYGGAnrltRPLKPLIAIPTTA 138
HVD cd08193
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ...
 4-115 2.35e-03

5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.


Pssm-ID: 341472 [Multi-domain]  Cd Length: 379  Bit Score: 39.42  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   4 PREVLVGHDTLDNVGGACKRLKMeGPALIIADSNTKKiAG--EAVIESLQQHNYEVLVTT--IEDATIEEVERVKVKIED 79
Cdd:cd08193     4 VPRIICGAGAAARLGELLRELGA-RRVLLVTDPGLVK-AGlaDPALAALEAAGIAVTVFDdvVADPPEAVVEAAVEQARE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2108433413  80 DKINLVLGVGGGRPIDVAKLSSF------------------HKEVPFISVPTAA 115
Cdd:cd08193    82 AGADGVIGFGGGSSMDVAKLVALlagsdqplddiygvgkatGPRLPLILVPTTA 135
PDDH cd08188
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ...
 3-115 5.82e-03

1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.


Pssm-ID: 341467 [Multi-domain]  Cd Length: 377  Bit Score: 38.26  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   3 LPREVLVGHDTLDNVGGACKRLKMEgPALIIADSNTKKIA-GEAVIESLQQHN--YEVLVTTIEDATIEEVERVKVKIED 79
Cdd:cd08188     5 IPPVNLFGPGCLKEIGDELKKLGGK-KALIVTDKGLVKLGlVKKVTDVLEEAGieYVIFDGVQPNPTVTNVNEGLELFKE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2108433413  80 DKINLVLGVGGGRPIDVAKL------------------SSFHKEVPFISVPTAA 115
Cdd:cd08188    84 NGCDFIISVGGGSAHDCAKAigilatnggeiedyegvdKSKKPGLPLIAINTTA 137
Fe-ADH-like cd17814
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 6-115 9.33e-03

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341489 [Multi-domain]  Cd Length: 374  Bit Score: 37.52  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413   6 EVLVGHDTLDNVGGACKRLKMEGPaLIIADSNTKKiAG--EAVIESLQQHNYEVLVTT--IEDATIEEVERVKVKIEDDK 81
Cdd:cd17814     6 EFIFGVGARKLAGRYAKNLGARKV-LVVTDPGVIK-AGwvDEVLDSLEAEGLEYVVFSdvTPNPRDFEVMEGAELYREEG 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2108433413  82 INLVLGVGGGRPIDVAK----LSSFHKEV--------------PFISVPTAA 115
Cdd:cd17814    84 CDGIVAVGGGSPIDCAKgigiVVSNGGHIldyegvdkvrrplpPLICIPTTA 135
PRK10586 PRK10586
putative oxidoreductase; Provisional
 85-174 9.38e-03

putative oxidoreductase; Provisional


Pssm-ID: 182570  Cd Length: 362  Bit Score: 37.40  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108433413  85 VLGVGGGRPIDVAKLSSFHKEVPFISVPTAAShdgivSSRA----SIWVDD-----RKKSYDGHTpFALIADTAIIAQAP 155
Cdd:PRK10586   90 VIGVGGGALLDTAKALARRLGLPFVAIPTIAA-----TCAAwtplSVWYNDagqalHFEIFDDAN-FLVLVEPRIILNAP 163

                          90       100
                  ....*....|....*....|.
gi 2108433413 156 KRINAAGCGDLISN--ETAVL 174
Cdd:PRK10586  164 QEYLLAGIGDTLAKwyEAVVL 184
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH