|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
490-998 |
0e+00 |
|
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: 800.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 490 FVNSSDRDYAIDQEREAAQTALQQVRRQLGKTYLPIINGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKN 569
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 570 AFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGVQRNLPGEDN 649
Cdd:cd07124 81 AFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 650 TYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHL 729
Cdd:cd07124 161 RYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 730 VKHPDVHLIAFTGSQQVGCQIVTEASILRPKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSR 809
Cdd:cd07124 241 VEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 810 AIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVPN---HGFYVPPTIF 886
Cdd:cd07124 321 VIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLElaaEGYFVQPTIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 887 GDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHP 966
Cdd:cd07124 401 ADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQP 480
|
490 500 510
....*....|....*....|....*....|..
gi 1320983422 967 FGGFKLSGIGSKAGGRDYLLQFLEPRSITENT 998
Cdd:cd07124 481 FGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
492-997 |
0e+00 |
|
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: 721.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 492 NSSDRDYAIDQEREAAQTALQQVRRQLGKTYLPIINGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAF 571
Cdd:TIGR01237 3 HEPFTDFADEENRQAFFKALATVKEQLGKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 572 SLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERL-ESGVQRNLPGEDNT 650
Cdd:TIGR01237 83 EAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELaKGKPVNSREGETNQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 651 YIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLV 730
Cdd:TIGR01237 163 YVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 731 KHPDVHLIAFTGSQQVGCQIVTEASILRPKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRA 810
Cdd:TIGR01237 243 DHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 811 IVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGE-VPNHGFYVPPTIFGDV 889
Cdd:TIGR01237 323 VVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCgDDSKGYFIGPTIFADV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 890 DPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGG 969
Cdd:TIGR01237 403 DRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGG 482
|
490 500
....*....|....*....|....*...
gi 1320983422 970 FKLSGIGSKAGGRDYLLQFLEPRSITEN 997
Cdd:TIGR01237 483 FKMSGTDSKAGGPDYLALFMQAKTVTEM 510
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
497-996 |
0e+00 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 693.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 497 DYAIDQEREAAQTALQQVRRQLGKTYLPIINGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKK 576
Cdd:PRK03137 12 DFSVEENVEAFEEALKKVEKELGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 577 LSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGVQRN-LPGEDNTYIYQP 655
Cdd:PRK03137 92 WSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVEsRPGEHNRYFYIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 656 RGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDV 735
Cdd:PRK03137 172 LGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 736 HLIAFTGSQQVGCQIVTEASILRPKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAP 815
Cdd:PRK03137 252 RFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHED 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 816 VYDNFMERLVEATRSLKVGEAHLPDtKFSAVIDGSAQQNILNYIAKGKETATLAFEGEV-PNHGFYVPPTIFGDVDPDSV 894
Cdd:PRK03137 332 VYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGdDSKGYFIQPTIFADVDPKAR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 895 IAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSG 974
Cdd:PRK03137 411 IMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 490
|
490 500
....*....|....*....|..
gi 1320983422 975 IGSKAGGRDYLLQFLEPRSITE 996
Cdd:PRK03137 491 TDSKAGGPDYLLLFLQAKTVSE 512
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
136-1002 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 615.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 136 LAKRYICGENLSEATKSIEKLRRDRFGFTMDLLGEAVISEVEAGEYLNRYIGMMEDLSNKAKNWGLIDqidkadgeelkR 215
Cdd:PRK11904 176 MGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADLPA-----------R 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 216 VQVSVKLSAFYSQFDPLDPVKTTEKVSEPARILLRKAQALGCGIHFDMEQYEFKSLTLQILKQVLMEPEFRDRTDVGITL 295
Cdd:PRK11904 245 PGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLAV 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 296 QGYLRDSEQDLRDLVEWAKLRGKPVTVRLVKGAYWDRETIRSYQQGWS-LPVFSDKVSTDANYERLIQILLENYQYLYAA 374
Cdd:PRK11904 325 QAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPgYPVFTRKAATDVSYLACARKLLSARGAIYPQ 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 375 IGSHNARSLAkaiAIVQNMNipSRAFETQCLYGMGDK-FAKAIADMGYRVRVYCPFG---DLIPgmsYLIRRLLENTANS 450
Cdd:PRK11904 405 FATHNAHTVA---AILEMAG--HRGFEFQRLHGMGEAlYDALLDAPGIPCRIYAPVGshkDLLP---YLVRRLLENGANS 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 451 SFL-RISGEGVDISKLIAAPVMTERDANYNGAPAL----NIF-DGFVNSSDRDYAIDQEREAAQTALQQVRRQLGKTYlP 524
Cdd:PRK11904 477 SFVhRLVDPDVPIEELVADPVEKLRSFETLPNPKIplprDIFgPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAG-P 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 525 IINGQAveteTYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWI 604
Cdd:PRK11904 556 IINGEG----EARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALC 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 605 CWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGVQRnLP---GEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIA 681
Cdd:PRK11904 632 VREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEK-LPgptGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALA 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 682 AGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQI-----VTEASI 756
Cdd:PRK11904 711 AGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInrtlaARDGPI 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 757 LrPkqkhmkrVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEA 836
Cdd:PRK11904 791 V-P-------LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDP 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 837 HLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVPN---HGFYVPPTIFgDVDPDSVIaQEEIFGPVLAVI--KAQ 911
Cdd:PRK11904 863 RLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAgteNGHFVAPTAF-EIDSISQL-EREVFGPILHVIryKAS 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 912 SFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGSKAGGRDYLLQFLEP 991
Cdd:PRK11904 941 DLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATE 1020
|
890
....*....|.
gi 1320983422 992 RSITENTQRQG 1002
Cdd:PRK11904 1021 KTVTVNTTAAG 1031
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
520-998 |
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: 579.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 520 KTYLPIINGQAVETET--YIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKR 597
Cdd:COG1012 4 PEYPLFIGGEWVAAASgeTFDVINPATG-EVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 598 EELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGVQRN-LPGEDNTYIYQPRGVVVVISPWNFPFAIALGMS 676
Cdd:COG1012 83 EELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSdAPGTRAYVRREPLGVVGAITPWNFPLALAAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 677 VAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASi 756
Cdd:COG1012 163 APALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 757 lrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEA 836
Cdd:COG1012 242 -----ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 837 HLPDTKFSAVIDGSAQQNILNYIAKGKET-ATLAFEGEVPNH--GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSF 913
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEgAELLTGGRRPDGegGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 914 DEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGAlVDRHPFGGFKLSGIGSKaGGRDYLLQFLEPRS 993
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGLEEYTETKT 474
|
....*
gi 1320983422 994 ITENT 998
Cdd:COG1012 475 VTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
537-994 |
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: 554.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:pfam00171 9 IEVINPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSV 696
Cdd:pfam00171 88 GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 697 IGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNG 776
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA------QNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 777 IIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNIL 856
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 857 NYIAKGKET-ATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSR 934
Cdd:pfam00171 322 KYVEDAKEEgAKLLTGGEaGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTS 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 935 TPSHIERAYREFEVGNLYINRGITGAlVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSI 994
Cdd:pfam00171 402 DLERALRVARRLEAGMVWINDYTTGD-ADGLPFGGFKQSGFG-REGGPYGLEEYTEVKTV 459
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
504-1002 |
6.50e-177 |
|
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: 525.22 E-value: 6.50e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 504 REAAQTALQQVRRQLGKTYlPIINGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERG 583
Cdd:cd07125 16 LEALADALKAFDEKEWEAI-PIINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 584 DMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGVQRNLP-GEDNTYIYQPRGVVVVI 662
Cdd:cd07125 95 EILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPtGELNGLELHGRGVFVCI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 663 SPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTG 742
Cdd:cd07125 175 SPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 743 SQQVGCQIvteASILRPKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFME 822
Cdd:cd07125 255 STETAKLI---NRALAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 823 RLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVP-NHGFYVPPTIFGDVDPDSViaQEEIF 901
Cdd:cd07125 332 MLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDdGNGYFVAPGIIEIVGIFDL--TTEVF 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 902 GPVLAVIKAQSF--DEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGSKA 979
Cdd:cd07125 410 GPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKA 489
|
490 500
....*....|....*....|...
gi 1320983422 980 GGRDYLLQFLEPRSITENTQRQG 1002
Cdd:cd07125 490 GGPNYLLRFGNEKTVSLNTTAAG 512
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
136-991 |
4.57e-173 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 537.91 E-value: 4.57e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 136 LAKRYICGENLSEATKSIEKLRRDRFGFTMDLLGEAVISEVEAGEYLNRYIgmmedlsnKAknwglIDQIDKA-DGEELK 214
Cdd:PRK11905 175 MGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYE--------RA-----IHAIGKAaTGRGVY 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 215 RVQ-VSVKLSA-----FYSQ----FDPLDPvktteKVSEpariLLRKAQALGCGIHFDMEQYEFKSLTLQILKQVLMEPE 284
Cdd:PRK11905 242 DGPgISVKLSAlhpryERAQrervMAELLP-----RLKA----LALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 285 FRDRTDVGITLQGYLRDSEQDLRDLVEWAKLRGKPVTVRLVKGAYWDRETIRSYQQGWS-LPVFSDKVSTDANYERLIQI 363
Cdd:PRK11905 313 LAGWNGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEgFPVFTRKVHTDVSYIACARK 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 364 LLENYQYLYAAIGSHNARSLAkaiAIVQnMNIPSRAFETQCLYGMGDKFAKAI---ADMGYRVRVYCPFG---DLIPgms 437
Cdd:PRK11905 393 LLAARDVIYPQFATHNAQTLA---AIYE-LAGGKGDFEFQCLHGMGEPLYDQVvgkEKLGRPCRIYAPVGtheTLLA--- 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 438 YLIRRLLENTANSSFL-RISGEGVDISKLIAAPVMTERDA--NYNGAPAL--NIF-DGFVNSSDRDYAIDQEREAAQTAL 511
Cdd:PRK11905 466 YLVRRLLENGANSSFVnRIVDENVPVEELIADPVEKVAAMgvAPHPQIPLprDLYgPERRNSKGLDLSDEATLAALDEAL 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 512 QQVRRQLGKTYlPIINGQAVETETYiESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAAD 591
Cdd:PRK11905 546 NAFAAKTWHAA-PLLAGGDVDGGTR-PVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAAD 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 592 IMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGVQRnlpgedntyiyQPRGVVVVISPWNFPFAI 671
Cdd:PRK11905 624 LMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGH-----------KPLGPVVCISPWNFPLAI 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 672 ALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcqiv 751
Cdd:PRK11905 693 FTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVA---- 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 752 teASILRPKQKHMKR---VIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACsRAIVLAP-VYDNFMERLVEA 827
Cdd:PRK11905 769 --RLIQRTLAKRSGPpvpLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSAL-RVLCLQEdVADRVLTMLKGA 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 828 TRSLKVGE-AHLpDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVP---NHGFYVPPTIFgDVDPDSVIaQEEIFGP 903
Cdd:PRK11905 846 MDELRIGDpWRL-STDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPaetEKGTFVAPTLI-EIDSISDL-EREVFGP 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 904 VLAVI--KAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGSKAGG 981
Cdd:PRK11905 923 VLHVVrfKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGG 1002
|
890
....*....|
gi 1320983422 982 RDYLLQFLEP 991
Cdd:PRK11905 1003 PLYLGRLVRE 1012
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
143-1002 |
2.17e-170 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 529.51 E-value: 2.17e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 143 GENLSEATKSIEKLRRDRFGFTMDLLGEAVISEVEAGEYLNRYIgmmEDLSNKAKNwglidqidKADGEELKRVQVSVKL 222
Cdd:COG4230 183 GFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYA---AAAAAAIAA--------AGGGSGGPGPSISSSL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 223 SAFYSQFDPLDPVKTTEKVSEPARILLRKAQALGCGIHFDMEQYEFKSLTLqILKQVLMEPEFRDRTDVGITLQGYLRDS 302
Cdd:COG4230 252 SVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLL-LLLLDLLAALLLDGGLGGGGGVGQAVQA 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 303 EQ-DLRDLVEWAKLRGKPVTVRLVKGAYWDRETIRSYQQGWSL-----PVFSDKVSTDANYERLIQILLENYQYLYAaig 376
Cdd:COG4230 331 YAkALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLgyvvyPVTTRKVLYDAAALALALLLLAAQPAFAP--- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 377 sHNARSLAKAIAIVQNMNIPsRAFETQCLYGMGDKFAKAIADM--GYRVRVYCPFG---DLIPgmsYLIRRLLENTANSS 451
Cdd:COG4230 408 -QFATHAAATAAAAAAAGGG-GEFEFQCLHGMGEYLYDQVGRGklGRPCRIYAPVGsheDLLA---YLVRRLLENGANSS 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 452 FL-RISGEGVDISKLIAAPVmtERDANYNGAP----AL--NIF-DGFVNSSDRDYAIDQEREAAQTALQQvrrQLGKTYL 523
Cdd:COG4230 483 FVnRIADEDVPVEELIADPV--EKARALGGAPhpriPLprDLYgPERRNSAGLDLSDEAVLAALSAALAA---AAEKQWQ 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 524 --PIINGQAVETETyIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELI 601
Cdd:COG4230 558 aaPLIAGEAASGEA-RPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 602 AWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLEsgvqrnlpgeDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIA 681
Cdd:COG4230 637 ALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLF----------AAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALA 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 682 AGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIvteasilrpkQ 761
Cdd:COG4230 707 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI----------N 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 762 KHM-KR------VIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACsRaIVLAP--VYDNFMERLVEATRSLK 832
Cdd:COG4230 777 RTLaARdgpivpLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSAL-R-VLCVQedIADRVLEMLKGAMAELR 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 833 VGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVP---NHGFYVPPTIFgDVDPDSVIaQEEIFGPVLAVI- 908
Cdd:COG4230 855 VGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPeecANGTFVAPTLI-EIDSISDL-EREVFGPVLHVVr 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 909 -KAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGSKAGGRDYLLQ 987
Cdd:COG4230 933 yKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLR 1012
|
890
....*....|....*
gi 1320983422 988 FLEPRSITENTQRQG 1002
Cdd:COG4230 1013 FATERTVTVNTTAAG 1027
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
19-1008 |
6.16e-167 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 515.37 E-value: 6.16e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 19 SKYEAKTQEIAKKILSGNEKSSFWsklsqikdelrLDDKLMAWTMENEGLRVQLFRLIDCLPALQSKAEIARHMQEYLA- 97
Cdd:COG0506 7 EALRARAVALARRLVEAIRAAPEG-----------GVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 98 SDAVEVPALRALLNFStdNPNSIPATAAATTLSTAVATLAKRYICGENLSEATKSIEKLRRDRFGFTMDLLGEAVISEVE 177
Cdd:COG0506 76 SPSFLVNASTWGLMLT--LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 178 AGEYLNRYIGmmedlsnkaknwgLIDQIDKAdgeELKRVQVSVKLSAFYSQFDPLDPVKTTEKVSEPARILLRKAQALGC 257
Cdd:COG0506 154 AERYLDAYLE-------------ALEAIGAA---GVDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAGI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 258 GIHFDMEQYEFKSLTLQILKQVLMEPEFRDRTDVGITLQGYLRDSEQDLRDLVEWAKLRGKPVTVRLVKGAYWDRETIRS 337
Cdd:COG0506 218 FVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAYWDPEIVRA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 338 YQQGWSLPVFSDKVSTDANYERLIQILLENYQYLYAAIGSHNARSLAKAIAIVQNMNIPSRAFETQCLYGMGDKFAKAIA 417
Cdd:COG0506 298 QVHGWPYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGERGRPPDRFEFQMLYGMGEDLQRALA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 418 D-MGYRVRVYCPFGDLIPGMSYLIRRLLENTANSSFLR-ISGEGVDISKLIAAPVMTERD-----ANYNGAPALNIFDGF 490
Cdd:COG0506 378 AvDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNfFVADFDDDEDLLEFPREPPRFlaalaAPTPPPPPPLRRQRR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 491 VNSSDRDYAIDQEREAAQTALQQVRRQLGKTYLPIINGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNA 570
Cdd:COG0506 458 RRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAA 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 571 FSLWK-KLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGVQRNLPGedN 649
Cdd:COG0506 538 AAAAAaAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPG--G 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 650 TYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFtylpakgstVGSHL 729
Cdd:COG0506 616 LVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAG---------GGVLV 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 730 VKHPDVHLIAFTGSQQVGCQIVTEASILRPKQKHMKRVIAEMGGKNGIIIDE-------SADLDQAVVGVMNSAFGFAGQ 802
Cdd:COG0506 687 LGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGgaaaaaaAAAAAAAVAAVAASAAASASA 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 803 KCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVP---NHGF 879
Cdd:COG0506 767 SASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGgplVPGL 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 880 YVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITG 959
Cdd:COG0506 847 LTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGG 926
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*....
gi 1320983422 960 ALVDRHPFGGFKLSGIGSKAGGRDYLLQFLEPRSITENTQRQGFAPLDG 1008
Cdd:COG0506 927 GGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAAA 975
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
504-997 |
3.22e-161 |
|
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: 484.00 E-value: 3.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 504 REAAQTALQQVRRQLGKTYlPIINGQA-VETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKER 582
Cdd:cd07083 1 RRAMREALRRVKEEFGRAY-PLVIGGEwVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 583 GDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESG--VQRNLPGEDNTYIYQPRGVVV 660
Cdd:cd07083 80 ARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPavEVVPYPGEDNESFYVGLGAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 661 VISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAF 740
Cdd:cd07083 160 VISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 741 TGSQQVGCQIVTEASILRPKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNF 820
Cdd:cd07083 240 TGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 821 MERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVPN-HGFYVPPTIFGDVDPDSVIAQEE 899
Cdd:cd07083 320 LERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEgEGYFVAPTVVEEVPPKARIAQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 900 IFGPVLAVI--KAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGS 977
Cdd:cd07083 400 IFGPVLSVIryKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNA 479
|
490 500
....*....|....*....|
gi 1320983422 978 KAGGRDYLLQFLEPRSITEN 997
Cdd:cd07083 480 KTGGPHYLRRFLEMKAVAER 499
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
561-996 |
1.81e-157 |
|
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: 471.69 E-value: 1.81e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 561 EAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLEsGV 640
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLH-GE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 641 QRNL--PGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYL 718
Cdd:cd07078 80 VIPSpdPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 719 PAKGSTVGSHLVKHPDVHLIAFTGSQQVGcQIVTEASilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFG 798
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVG-KAIMRAA-----AENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 799 FAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGEVP-- 875
Cdd:cd07078 234 NAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKaEGAKLLCGGKRLeg 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 876 NHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINR 955
Cdd:cd07078 314 GKGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1320983422 956 GITGAlVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSITE 996
Cdd:cd07078 394 YSVGA-EPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
522-988 |
2.95e-146 |
|
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: 444.00 E-value: 2.95e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 522 YLPIINGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELI 601
Cdd:cd07097 1 YRNYIDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 602 AWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLeSGvqRNLPGED-NTYIY---QPRGVVVVISPWNFPFAIALGMSV 677
Cdd:cd07097 81 RLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRL-SG--ETLPSTRpGVEVEttrEPLGVVGLITPWNFPIAIPAWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 678 AAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASil 757
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 758 rpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAH 837
Cdd:cd07097 236 ----ARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 838 LPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGEV---PNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSF 913
Cdd:cd07097 312 DEGVDIGPVVSERQLEKDLRYIEIARsEGAKLVYGGERlkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDY 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1320983422 914 DEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGalVDRH-PFGGFKLSGIGSKAGGRdYLLQF 988
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGE-AALEF 464
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
526-997 |
1.05e-141 |
|
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: 432.54 E-value: 1.05e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE--TETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAW 603
Cdd:cd07131 3 IGGEWVDsaSGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 ICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESG-VQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAA 682
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGEtVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 683 GNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqK 762
Cdd:cd07131 163 GNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA------R 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 763 HMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTK 842
Cdd:cd07131 237 PNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 843 FSAVIDGSAQQNILNYIAKGK-ETATLAFEGEVPNH-----GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEA 916
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKeEGATLLLGGERLTGggyekGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 917 LAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVdrH-PFGGFKLSGIGSKAGGRDYLLQFLEPRSIT 995
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV--HlPFGGVKKSGNGHREAGTTALDAFTEWKAVY 474
|
..
gi 1320983422 996 EN 997
Cdd:cd07131 475 VD 476
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
149-454 |
6.92e-134 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 404.95 E-value: 6.92e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 149 ATKSIEKLRRDRFGFTMDLLGEAVISEVEAGEYLNRYIGMMEDLSNKAKNWGLIDqidkadgeelkRVQVSVKLSAFYSQ 228
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGP-----------RPGISVKLSALHPR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 229 FDPLDPVKTTEKVSEPARILLRKAQALGCGIHFDMEQYEFKSLTLQILKQVLMEPEFRDRTDVGITLQGYLRDSEQDLRD 308
Cdd:pfam01619 70 YEPLERERVMAELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 309 LVEWAKLRGKPVTVRLVKGAYWDRETIRSYQQGWSLPVFSDKVSTDANYERLIQILLENYQYLYAAIGSHNARSLAKAIA 388
Cdd:pfam01619 150 LLELARRRGRPLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1320983422 389 IVQNMNIPSRAFETQCLYGMGDKFAKAIADMGYRVRVYCPFGDLIPGMSYLIRRLLENTANSSFLR 454
Cdd:pfam01619 230 LAEELGIPPRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVR 295
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
138-992 |
1.79e-133 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 435.17 E-value: 1.79e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 138 KRYICGENLSEATKSIEKLRRDRFGFTMDLLGEAVISEVEAGEYLNRY------IGmmedlsnKAKNW-GlidqIDKADG 210
Cdd:PRK11809 257 EQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYeqaihaIG-------KASNGrG----IYEGPG 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 211 eelkrvqVSVKLSAF---YS--QFDpldpvKTTEKVSEPARILLRKAQALGCGIHFDMEQYEFKSLTLQILKQVLMEPEF 285
Cdd:PRK11809 326 -------ISIKLSALhprYSraQYD-----RVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 286 RDRTDVGITLQGYLRDSEQDLRDLVEWAKLRGKPVTVRLVKGAYWDRETIRSYQQGWS-LPVFSDKVSTDANYERLIQIL 364
Cdd:PRK11809 394 AGWNGIGFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEgYPVYTRKVYTDVSYLACARKL 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 365 LENYQYLYAAIGSHNARSLAkAIAIVQNMNIPSRAFETQCLYGMG----DKFAKAIAD--MGYRVRVYCPFGDLIPGMSY 438
Cdd:PRK11809 474 LAVPNLIYPQFATHNAHTLA-AIYHLAGQNYYPGQYEFQCLHGMGeplyEQVVGKVADgkLNRPCRIYAPVGTHETLLAY 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 439 LIRRLLENTANSSFL-RISGEGVDISKLIAAPVMT----ERDANYNGAPALNI-------FDGFVNSSDRDYAIDQEREA 506
Cdd:PRK11809 553 LVRRLLENGANTSFVnRIADTSLPLDELVADPVEAveklAQQEGQLGLPHPKIplprdlyGKGRANSAGLDLANEHRLAS 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 507 AQTALQQVRRQLGKTyLPIInGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDML 586
Cdd:PRK11809 633 LSSALLASAHQKWQA-APML-EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAIL 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 587 RKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERlesgvqrnlpGEDNTyIYQPRGVVVVISPWN 666
Cdd:PRK11809 711 ERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRD----------DFDND-THRPLGPVVCISPWN 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 667 FPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQV 746
Cdd:PRK11809 780 FPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEV 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 747 GCQIV-TEASILRPkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLV 825
Cdd:PRK11809 860 ARLLQrNLAGRLDP-QGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLR 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 826 EATRSLKVGEahlPD---TKFSAVIDGSAQQNILNYI----AKGKETATLAF-EGEVPNHGFYVPPTIfgdVDPDSVIA- 896
Cdd:PRK11809 939 GAMAECRMGN---PDrlsTDIGPVIDAEAKANIERHIqamrAKGRPVFQAAReNSEDWQSGTFVPPTL---IELDSFDEl 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 897 QEEIFGPVLAVI--KAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSG 974
Cdd:PRK11809 1013 KREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSG 1092
|
890
....*....|....*...
gi 1320983422 975 IGSKAGGRDYLLQFLEPR 992
Cdd:PRK11809 1093 TGPKAGGPLYLYRLLATR 1110
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
526-997 |
3.59e-125 |
|
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: 389.23 E-value: 3.59e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE-TETYIESVNPANSSQVVGkIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWI 604
Cdd:cd07086 3 IGGEWVGsGGETFTSRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 605 CWEVAKPIREGDGEVSEAIDFCRYYAKEMERLE-SGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAG 683
Cdd:cd07086 82 SLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYgLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 684 NTVILKPAEQSSVIGAK----IAEVLQAAGLPTGVFTyLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcQIVTEASilrp 759
Cdd:cd07086 162 NTVVWKPSETTPLTAIAvtkiLAEVLEKNGLPPGVVN-LVTGGGDGGELLVHDPRVPLVSFTGSTEVG-RRVGETV---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 760 kQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLP 839
Cdd:cd07086 236 -ARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 840 DTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGEVPNH---GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDE 915
Cdd:cd07086 315 GTLVGPLINQAAVEKYLNAIEIAKsQGGTVLTGGKRIDGgepGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 916 ALAIANGTNFALTGGLYSRTPSHIERAYREF--EVGNLYINRGITGALVdrH-PFGGFKLSGIGSKAgGRDYLLQFLEPR 992
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTSGAEI--GgAFGGEKETGGGRES-GSDAWKQYMRRS 471
|
....*
gi 1320983422 993 SITEN 997
Cdd:cd07086 472 TCTIN 476
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
567-996 |
2.09e-124 |
|
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: 383.12 E-value: 2.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 567 AKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLE-SGVQRNLP 645
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGgPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 646 GEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTV 725
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 726 GSHLVKHPDVHLIAFTGSQQVGcQIVTEASilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCS 805
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVG-KAIMKAA-----AENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 806 ACSRAIVLAPVYDNFMERLVeatrslkvgeahlpdtkfsavidgsaqqnilnyiakgketatlafegevpnhgfyvppTI 885
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV----------------------------------------------------------TV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 886 FGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGAlVDRH 965
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GPEA 337
|
410 420 430
....*....|....*....|....*....|.
gi 1320983422 966 PFGGFKLSGIGSkAGGRDYLLQFLEPRSITE 996
Cdd:cd06534 338 PFGGVKNSGIGR-EGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
539-995 |
2.24e-122 |
|
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: 381.14 E-value: 2.24e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 539 SVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREG-DG 617
Cdd:cd07093 1 NFNPATG-EVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 618 EVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIaLGMSVA-AIAAGNTVILKPAEQSSV 696
Cdd:cd07093 80 DIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLML-LTWKIApALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 697 IGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNG 776
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA------PNLKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 777 IIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNIL 856
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 857 NYIAKGK-ETATLAFEGEVPNH-----GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGG 930
Cdd:cd07093 313 GYVELARaEGATILTGGGRPELpdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320983422 931 LYSRTPSHIERAYREFEVGNLYINRGITGALvdRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSIT 995
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGTVWVNCWLVRDL--RTPFGGVKASGIG-REGGDYSLEFYTELKNVC 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
526-995 |
3.54e-121 |
|
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: 378.38 E-value: 3.54e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVETET--YIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAW 603
Cdd:cd07138 3 IDGAWVAPAGteTIDVINPATE-EVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 ICWEVAKPIR-EGDGEVSEAIDFCRYYAKEMERLESGVQRNlpgeDNTYIYQPRGVVVVISPWNFPF-AIALGMsVAAIA 681
Cdd:cd07138 82 ITLEMGAPITlARAAQVGLGIGHLRAAADALKDFEFEERRG----NSLVVREPIGVCGLITPWNWPLnQIVLKV-APALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 682 AGNTVILKPAEQ---SSVIgakIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilr 758
Cdd:cd07138 157 AGCTVVLKPSEVaplSAII---LAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 759 pkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHL 838
Cdd:cd07138 231 ---DTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 839 PDTKFSAVIDGSAQQNILNYIAKG-KETATLAFEG----EVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSF 913
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGiEEGARLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 914 DEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgitGALVDRH-PFGGFKLSGIGsKAGGRDYLLQFLEPR 992
Cdd:cd07138 388 DEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG-REWGRYGLEEFLEVK 462
|
...
gi 1320983422 993 SIT 995
Cdd:cd07138 463 SIQ 465
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
540-995 |
3.77e-121 |
|
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: 377.93 E-value: 3.77e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 540 VNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEV 619
Cdd:cd07103 2 INPATG-EVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 620 SEAIDFCRYYAKEMERLE-SGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFA-IALGMSvAAIAAGNTVILKPAEQSSVI 697
Cdd:cd07103 81 DYAASFLEWFAEEARRIYgRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAmITRKIA-PALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 698 GAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGI 777
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA------DTVKRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 778 IIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILN 857
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 858 YI----AKGketATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLY 932
Cdd:cd07103 314 LVedavAKG---AKVLTGGKrLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1320983422 933 SRTPSHIERAYREFEVGNLYINRG-ITGALVdrhPFGGFKLSGIGSKaGGRDYLLQFLEPRSIT 995
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGlISDAEA---PFGGVKESGLGRE-GGKEGLEEYLETKYVS 450
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
539-994 |
4.83e-115 |
|
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: 361.87 E-value: 4.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 539 SVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFS--LWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:cd07114 1 SINPATG-EPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLESGVqrnLPGEDNTYI----YQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAE 692
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAV---IPVDKGDYLnftrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 693 QSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMG 772
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA------ENLAPVTLELG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 773 GKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQ 852
Cdd:cd07114 231 GKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 853 QNILNYIAKGK-ETATLAFEGEVPNH-----GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFA 926
Cdd:cd07114 311 EKVERYVARAReEGARVLTGGERPSGadlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1320983422 927 LTGGLYSRTPSHIERAYREFEVGNLYINrgiTGALVDRH-PFGGFKLSGIGsKAGGRDYLLQFLEPRSI 994
Cdd:cd07114 391 LAAGIWTRDLARAHRVARAIEAGTVWVN---TYRALSPSsPFGGFKDSGIG-RENGIEAIREYTQTKSV 455
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
526-994 |
1.81e-114 |
|
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: 360.81 E-value: 1.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVETET--YIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAW 603
Cdd:cd07088 2 INGEFVPSSSgeTIDVLNPATG-EVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 ICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGV-QRNLPGEdNTYIY-QPRGVVVVISPWNFPFAIALGMSVAAIA 681
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIiPSDRPNE-NIFIFkVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 682 AGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkq 761
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 762 KHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDT 841
Cdd:cd07088 234 ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 842 KFSAVIDGSAQQNILNYIAKGKET-ATLAFEGEVPN--HGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALA 918
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAgATLLTGGKRPEgeKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1320983422 919 IANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHpfGGFKLSGIGSkAGGRDYLLQFLEPRSI 994
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLGG-ADGKHGLEEYLQTKVV 466
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
560-995 |
1.88e-113 |
|
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: 356.84 E-value: 1.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 560 AEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYyAKEMERLESG 639
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILRE-AAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 640 --VQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALgMSVA-AIAAGNTVILKPAEQSSV-IGAKIAEVLQAAGLPTGVF 715
Cdd:cd07104 81 eiLPSDVPGKESMVRRVPLGVVGVISPFNFPLILAM-RSVApALALGNAVVLKPDSRTPVtGGLLIAEIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 716 TYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAV-VGVMn 794
Cdd:cd07104 160 NVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG------RHLKKVALELGGNNPLIVLDDADLDLAVsAAAF- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 795 SAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGE 873
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVaAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 874 VpnHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYI 953
Cdd:cd07104 313 Y--EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1320983422 954 NrGIT---GALVdrhPFGGFKLSGIGSkAGGRDYLLQFLEPRSIT 995
Cdd:cd07104 391 N-DQTvndEPHV---PFGGVKASGGGR-FGGPASLEEFTEWQWIT 430
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
526-995 |
4.11e-113 |
|
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: 357.67 E-value: 4.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE--TETYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAF--SLWKKLSAKERGDMLRKAADIMEEKREELI 601
Cdd:cd07091 8 INNEFVDsvSGKTFPTINPATE-EVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 602 AWICWEVAKPIREG-DGEVSEAIDFCRYYAKEMERLESgvqRNLPGEDNTYIY---QPRGVVVVISPWNFPFAIALGMSV 677
Cdd:cd07091 87 ALESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQG---KTIPIDGNFLAYtrrEPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 678 AAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASil 757
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAA-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 758 rpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAH 837
Cdd:cd07091 242 ---KSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 838 LPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDE 915
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKkEGATLLTGGErHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 916 ALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgiTGALVDRH-PFGGFKLSGIGsKAGGRDYLLQFLEPRSI 994
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSGFG-RELGEEGLEEYTQVKAV 474
|
.
gi 1320983422 995 T 995
Cdd:cd07091 475 T 475
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
500-992 |
6.55e-111 |
|
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: 352.68 E-value: 6.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 500 IDQEREAAQTAlQQVRRQLGKTY--LPIINGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKL 577
Cdd:TIGR01238 15 LDNESELKPLE-AQIHAWADKTWqaAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNAT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 578 SAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEmerlesgVQRNLPGEDntyiYQPRG 657
Cdd:TIGR01238 94 PAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQ-------VRDVLGEFS----VESRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 658 VVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHL 737
Cdd:TIGR01238 163 VFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 738 IAFTGSQQVGcQIVTEAsiLRPKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVY 817
Cdd:TIGR01238 243 VAFTGSTEVA-QLINQT--LAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 818 DNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYI----AKGKETATLAFEGEVP-NHGFYVPPTIFGDVDPD 892
Cdd:TIGR01238 320 DRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIehmsQTQKKIAQLTLDDSRAcQHGTFVAPTLFELDDIA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 893 SViaQEEIFGPVLAVI--KAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGF 970
Cdd:TIGR01238 400 EL--SEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQ 477
|
490 500
....*....|....*....|..
gi 1320983422 971 KLSGIGSKAGGRDYLLQFLEPR 992
Cdd:TIGR01238 478 GLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
534-990 |
3.68e-109 |
|
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: 346.51 E-value: 3.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 534 ETYiESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSL--WKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKP 611
Cdd:cd07112 2 ETF-ATINPATG-RVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 612 IREG-DGEVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKP 690
Cdd:cd07112 80 ISDAlAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 691 AEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkQKHMKRVIAE 770
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSG-----QSNLKRVWLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 771 MGGKN-GIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDG 849
Cdd:cd07112 235 CGGKSpNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 850 SAQQNILNYIAKGK-ETATLAFEGE---VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNF 925
Cdd:cd07112 315 AHFDKVLGYIESGKaEGARLVAGGKrvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320983422 926 ALTGGLYSRTPSHIERAYREFEVGNLYINrgITGALVDRHPFGGFKLSGigskaGGRDYLLQFLE 990
Cdd:cd07112 395 GLAASVWTSDLSRAHRVARRLRAGTVWVN--CFDEGDITTPFGGFKQSG-----NGRDKSLHALD 452
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
542-995 |
1.81e-108 |
|
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: 344.71 E-value: 1.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 542 PANSsQVVGKIGLANIDQAEAAVQVAKNAFSL--WKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEV 619
Cdd:cd07118 4 PAHG-VVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 620 SEAIDFCRYYAkemerlesGVQRNLPGEDNTYI---------YQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKP 690
Cdd:cd07118 83 EGAADLWRYAA--------SLARTLHGDSYNNLgddmlglvlREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 691 AEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAE 770
Cdd:cd07118 155 SEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA------RNLKKVSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 771 MGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGS 850
Cdd:cd07118 229 LGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 851 AQQNILNYIAKGK-ETATLAFEGEVPNH--GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFAL 927
Cdd:cd07118 309 QLAKITDYVDAGRaEGATLLLGGERLASaaGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320983422 928 TGGLYSRTPSHIERAYREFEVGNLYINRGITGAlvDRHPFGGFKLSGIGSKAgGRDYLLQFLEPRSIT 995
Cdd:cd07118 389 SAGVWSKDIDTALTVARRIRAGTVWVNTFLDGS--PELPFGGFKQSGIGREL-GRYGVEEYTELKTVH 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
537-976 |
4.53e-108 |
|
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: 343.42 E-value: 4.53e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:cd07149 1 IEVISPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLeSGVQRNL---PGEDNT---YIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKP 690
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRL-AGETIPFdasPGGEGRigfTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 691 AEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASIlrpkqkhmKRVIAE 770
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGL--------KKVTLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 771 MGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGS 850
Cdd:cd07149 231 LGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 851 AQQNILNYIAKGKET-ATLAFEGEvpNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTG 929
Cdd:cd07149 311 EAERIEEWVEEAVEGgARLLTGGK--RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1320983422 930 GLYSRTPSHIERAYREFEVGNLYINrGITGALVDRHPFGGFKLSGIG 976
Cdd:cd07149 389 GVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
539-994 |
4.02e-107 |
|
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: 340.96 E-value: 4.02e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 539 SVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREG-DG 617
Cdd:cd07115 1 TLNPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 618 EVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVI 697
Cdd:cd07115 80 DVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 698 GAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcqivteASILRPKQKHMKRVIAEMGGKNGI 777
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVG------RKIMQGAAGNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 778 IIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILN 857
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 858 YIAKG-KETATLAFEGEVPN-HGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRT 935
Cdd:cd07115 314 YVDVGrEEGARLLTGGKRPGaRGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1320983422 936 PSHIERAYREFEVGNLYINrgITGALVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSI 994
Cdd:cd07115 394 LGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEVKSV 449
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
526-976 |
4.72e-107 |
|
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: 341.42 E-value: 4.72e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE--TETYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAW 603
Cdd:cd07085 5 INGEWVEskTTEWLDVYNPATG-EVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 ICWEVAKPIREGDGEVS---EAIDFCryyakemerleSGVQRNLPGE---------DNTYIYQPRGVVVVISPWNFPFAI 671
Cdd:cd07085 84 ITLEHGKTLADARGDVLrglEVVEFA-----------CSIPHLLKGEylenvargiDTYSYRQPLGVVAGITPFNFPAMI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 672 ALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVgSHLVKHPDVHLIAFTGSQQVGCQIV 751
Cdd:cd07085 153 PLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 752 TEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSL 831
Cdd:cd07085 232 ERAA------ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 832 KVGEAHLPDTKFSAVIDGSAQQNILNYIAKG-KETATLAFEG---EVPNH--GFYVPPTIFGDVDPDSVIAQEEIFGPVL 905
Cdd:cd07085 306 KVGAGDDPGADMGPVISPAAKERIEGLIESGvEEGAKLVLDGrgvKVPGYenGNFVGPTILDNVTPDMKIYKEEIFGPVL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1320983422 906 AVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITgALVDRHPFGGFKLSGIG 976
Cdd:cd07085 386 SIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGGWKGSFFG 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
541-980 |
9.37e-107 |
|
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: 340.05 E-value: 9.37e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 541 NPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVS 620
Cdd:cd07090 3 EPATG-EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 621 EAIDFCRYYAKEMERLeSGVQRNLPGEDNTYI-YQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGA 699
Cdd:cd07090 82 SSADCLEYYAGLAPTL-SGEHVPLPGGSFAYTrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 700 KIAEVLQAAGLPTGVFTYLPAKGSTvGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIII 779
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA------KGIKHVTLELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 780 DESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYI 859
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 860 AKGK-ETATLAFEGEVP------NHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLY 932
Cdd:cd07090 314 ESAKqEGAKVLCGGERVvpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1320983422 933 SRtpsHIERAYR---EFEVGNLYINR-GITGALVdrhPFGGFKLSGIGSKAG 980
Cdd:cd07090 394 TR---DLQRAHRviaQLQAGTCWINTyNISPVEV---PFGGYKQSGFGRENG 439
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
539-980 |
1.10e-106 |
|
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: 339.60 E-value: 1.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 539 SVNPANSsQVVGKIGLANIDQAEAAVQVAKNAF-SLWKKLSAKERGDMLRKAADIMEEKREELiAWI-CWEVAKPIREGD 616
Cdd:cd07109 1 VFDPSTG-EVFARIARGGAADVDRAVQAARRAFeSGWLRLSPAERGRLLLRIARLIREHADEL-ARLeSLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIaLGMSVA-AIAAGNTVILKPAEQSS 695
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQI-TGRSVApALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 696 VIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcqivteASILRPKQKHMKRVIAEMGGKN 775
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETG------IAVMRAAAENVVPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 776 GIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAhLPDTKFSAVIDGSAQQNI 855
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPG-LEDPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 856 LNYIAKGKET-ATLAFEGEV----PNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGG 930
Cdd:cd07109 311 EGFVARARARgARIVAGGRIaegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1320983422 931 LYSRTPSHIERAYREFEVGNLYINRGITGALVDRhPFGGFKLSGIGSKAG 980
Cdd:cd07109 391 VWTRDGDRALRVARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSGHGREKG 439
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
526-995 |
5.71e-106 |
|
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: 338.40 E-value: 5.71e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE--TETYIESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAF--SLWKKLSAKERGDMLRKAADIMEEKREELI 601
Cdd:cd07139 3 IGGRWVApsGSETIDVVSPA-TEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 602 AWICWEVAKPIR-EGDGEVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYI-YQPRGVVVVISPWNFPFAIALGMSVAA 679
Cdd:cd07139 82 RLWTAENGMPISwSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVrREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 680 IAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAkGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrp 759
Cdd:cd07139 162 LAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 760 kqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLP 839
Cdd:cd07139 237 --ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 840 DTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGEVPNH---GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDE 915
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRaEGARLVTGGGRPAGldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 916 ALAIANGTNFALTGGLYSRTPshiERAY---REFEVGNLYINrgitGALVDRH-PFGGFKLSGIGsKAGGRDYLLQFLEP 991
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADV---ERGLavaRRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGPEGLDAYLET 466
|
....
gi 1320983422 992 RSIT 995
Cdd:cd07139 467 KSIY 470
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
532-976 |
2.57e-104 |
|
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: 333.89 E-value: 2.57e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 532 ETETYIESVNPANSSqVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKP 611
Cdd:cd07151 7 TSERTIDVLNPYTGE-TLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 612 IREGDGEVSEAIDFCRYYAKEMERLESG-VQRNLPGEDNtYIY-QPRGVVVVISPWNFPFAIALgMSVA-AIAAGNTVIL 688
Cdd:cd07151 86 RIKANIEWGAAMAITREAATFPLRMEGRiLPSDVPGKEN-RVYrEPLGVVGVISPWNFPLHLSM-RSVApALALGNAVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 689 KPAEQSSVIGAK-IAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRV 767
Cdd:cd07151 164 KPASDTPITGGLlLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG------RHLKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 768 IAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVI 847
Cdd:cd07151 238 ALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 848 DGSAQQNILNYIAKGK-ETATLAFEGEVpnHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFA 926
Cdd:cd07151 318 NESQVDGLLDKIEQAVeEGATLLVGGEA--EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYG 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1320983422 927 LTGGLYSRTPSHIERAYREFEVGNLYINRGItgalVDRHP---FGGFKLSGIG 976
Cdd:cd07151 396 LSGAVFTSDLERGVQFARRIDAGMTHINDQP----VNDEPhvpFGGEKNSGLG 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
540-996 |
5.42e-104 |
|
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: 332.78 E-value: 5.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 540 VNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEV 619
Cdd:cd07110 2 INPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 620 SEAIDFCRYYAKEMERLESGVQRNLPGEDNTY----IYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSS 695
Cdd:cd07110 81 DDVAGCFEYYADLAEQLDAKAERAVPLPSEDFkarvRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 696 VIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKN 775
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA------QDIKPVSLELGGKS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 776 GIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNI 855
Cdd:cd07110 235 PIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 856 LNYIAKGKET-ATLAFEGEVPNH---GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGL 931
Cdd:cd07110 315 LSFIARGKEEgARLLCGGRRPAHlekGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1320983422 932 YSRTPSHIERAYREFEVGNLYINrgITGALVDRHPFGGFKLSGIGSKAG--GrdyLLQFLEPRSITE 996
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIGRELGewG---LDNYLEVKQITR 456
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
540-994 |
1.00e-103 |
|
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: 332.29 E-value: 1.00e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 540 VNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWK-KLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIR-EGDG 617
Cdd:cd07089 2 INPA-TEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 618 EVSEAIDFCRYYA---KEMERLESGVQRNLPGEDNTYI--YQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAE 692
Cdd:cd07089 81 QVDGPIGHLRYFAdlaDSFPWEFDLPVPALRGGPGRRVvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 693 QSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASILrpkqkhMKRVIAEMG 772
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT------LKRVLLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 773 GKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQ 852
Cdd:cd07089 235 GKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 853 QNILNYIAKGK-ETATLAFEGEVPNH---GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALT 928
Cdd:cd07089 315 DRVEGYIARGRdEGARLVTGGGRPAGldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1320983422 929 GGLYSRTPshiERAY---REFEVGNLYINrGITGALVDRhPFGGFKLSGIGsKAGGRDYLLQFLEPRSI 994
Cdd:cd07089 395 GGVWSADV---DRAYrvaRRIRTGSVGIN-GGGGYGPDA-PFGGYKQSGLG-RENGIEGLEEFLETKSI 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
526-999 |
2.58e-103 |
|
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: 331.97 E-value: 2.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE--TETYIESVNPANSSqVVGKIGLANIDQAEAAVQVAKNAF--SLWKKLSAKERGDMLRKAADIMEEKREELI 601
Cdd:cd07119 2 IDGEWVEaaSGKTRDIINPANGE-VIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 602 AWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERlESGVQRNLPGEDNTYI-YQPRGVVVVISPWNFPFAIALGMSVAAI 680
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATK-ETGEVYDVPPHVISRTvREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 681 AAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcqivteASILRPK 760
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATG------RSIMRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 761 QKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPD 840
Cdd:cd07119 234 AGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 841 TKFSAVIdgSAQQ--NILNYIAKGK-ETATLAFEGEVPN-----HGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQS 912
Cdd:cd07119 314 TEMGPLV--SAEHreKVLSYIQLGKeEGARLVCGGKRPTgdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 913 FDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgitgalvDRH------PFGGFKLSGIGsKAGGRDYLL 986
Cdd:cd07119 392 EEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN--------DYHpyfaeaPWGGYKQSGIG-RELGPTGLE 462
|
490
....*....|...
gi 1320983422 987 QFLEPRSITENTQ 999
Cdd:cd07119 463 EYQETKHININLS 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
538-995 |
6.66e-103 |
|
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: 329.68 E-value: 6.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 538 ESVNPANSSqVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDG 617
Cdd:cd07150 2 DDLNPADGS-VYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 618 EVSEAIDFCRYYAKEMERLESGVQRNL-PGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSV 696
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRGETLPSDsPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 697 IGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNG 776
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 777 IIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNIL 856
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 857 NYI----AKGketATLAFEGEVpnHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLY 932
Cdd:cd07150 315 RQVedavAKG---AKLLTGGKY--DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1320983422 933 SRtpsHIERAY---REFEVGNLYINrGITgALVDRH-PFGGFKLSGIGsKAGGRDYLLQFLEPRSIT 995
Cdd:cd07150 390 TN---DLQRAFklaERLESGMVHIN-DPT-ILDEAHvPFGGVKASGFG-REGGEWSMEEFTELKWIT 450
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
537-994 |
1.77e-102 |
|
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: 328.54 E-value: 1.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:cd07145 1 IEVRNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLESGVQR--NLPGEDNTYIY---QPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPA 691
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPvdAYEYNERRIAFtvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 692 EQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASILrpkqkhMKRVIAEM 771
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGT------GKKVALEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 772 GGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSA 851
Cdd:cd07145 234 GGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 852 QQNILNYIAKGKET-ATLAFEGEVPNhGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGG 930
Cdd:cd07145 314 VERMENLVNDAVEKgGKILYGGKRDE-GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1320983422 931 LYSrtpSHIERAYR---EFEVGNLYINrGITGALVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSI 994
Cdd:cd07145 393 VFT---NDINRALKvarELEAGGVVIN-DSTRFRWDNLPFGGFKKSGIG-REGVRYTMLEMTEEKTI 454
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
560-976 |
1.33e-101 |
|
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: 325.18 E-value: 1.33e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 560 AEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESG 639
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 640 VQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLP 719
Cdd:cd07100 81 EPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 720 AKGSTVgSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGF 799
Cdd:cd07100 161 IDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAG------KNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 800 AGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFS-----AVIDGSAQQnILNYIAKGketATLAFEGEV 874
Cdd:cd07100 234 AGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGplarkDLRDELHEQ-VEEAVAAG---ATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 875 PNH-GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYI 953
Cdd:cd07100 310 PDGpGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFI 389
|
410 420
....*....|....*....|...
gi 1320983422 954 NrGITGALVdRHPFGGFKLSGIG 976
Cdd:cd07100 390 N-GMVKSDP-RLPFGGVKRSGYG 410
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
519-980 |
2.18e-101 |
|
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: 326.67 E-value: 2.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 519 GKTYL-PI---INGQ---AVETETyIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAF-SLWKKLSAKERGDMLRKAA 590
Cdd:cd07144 1 GKSYDqPTglfINNEfvkSSDGET-IKTVNPSTG-EVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 591 DIMEEKREELIAWICWEVAKPIREG-DGEVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPF 669
Cdd:cd07144 79 DLVEKNRDLLAAIEALDSGKPYHSNaLGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 670 AIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcQ 749
Cdd:cd07144 159 AMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATG-R 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 750 IVTEASilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAV----VGVM-NSafgfaGQKCSACSRAIVLAPVYDNFMERL 824
Cdd:cd07144 238 LVMKAA-----AQNLKAVTLECGGKSPALVFEDADLDQAVkwaaAGIMyNS-----GQNCTATSRIYVQESIYDKFVEKF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 825 VEATRS-LKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGEV----PNHGFYVPPTIFGDVDPDSVIAQE 898
Cdd:cd07144 308 VEHVKQnYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKkEGAKLVYGGEKapegLGKGYFIPPTIFTDVPQDMRIVKE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 899 EIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRtpsHIERAYR---EFEVGNLYINRGITGALvdRHPFGGFKLSGI 975
Cdd:cd07144 388 EIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTK---DIRRAHRvarELEAGMVWINSSNDSDV--GVPFGGFKMSGI 462
|
....*
gi 1320983422 976 GSKAG 980
Cdd:cd07144 463 GRELG 467
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
503-997 |
1.63e-100 |
|
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: 325.70 E-value: 1.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 503 EREAAQTALQQVRRQlgKTYLP-IINGQAVETETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKE 581
Cdd:cd07123 15 ERAKLQEALAELKSL--TVEIPlVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 582 RGDMLRKAADIME-EKREELIAWICWEVAKPIREGDGEVS-EAIDFCRYYAKEMERLESGvQ--RNLPGEDNTYIYQP-R 656
Cdd:cd07123 93 RAAIFLKAADLLSgKYRYELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYAEELYAQ-QplSSPAGVWNRLEYRPlE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 657 GVVVVISPWNFPfAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVH 736
Cdd:cd07123 172 GFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 737 LIAFTGS--------QQVGCQIVTEASIlrPkqkhmkRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACS 808
Cdd:cd07123 251 GLHFTGStptfkslwKQIGENLDRYRTY--P------RIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAAS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 809 RAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYI--AKGKETATLAFEGEVPNH-GFYVPPTI 885
Cdd:cd07123 323 RAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIdhAKSDPEAEIIAGGKCDDSvGYFVEPTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 886 FGDVDPDSVIAQEEIFGPVLA--VIKAQSFDEALAIANGTN-FALTGGLYSRTPSHIERAYRE--FEVGNLYINRGITGA 960
Cdd:cd07123 403 IETTDPKHKLMTEEIFGPVLTvyVYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDAlrNAAGNFYINDKPTGA 482
|
490 500 510
....*....|....*....|....*....|....*..
gi 1320983422 961 LVDRHPFGGFKLSGIGSKAGGRDYLLQFLEPRSITEN 997
Cdd:cd07123 483 VVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKET 519
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
541-995 |
1.77e-99 |
|
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: 320.85 E-value: 1.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 541 NPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIR-EGDGEV 619
Cdd:cd07108 3 NPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 620 SEAIDFCRYYAKemerLESGVQ-RNLPGEDNTYIY---QPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSS 695
Cdd:cd07108 82 AVLADLFRYFGG----LAGELKgETLPFGPDVLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 696 VIGAKIAEVLQAAgLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKN 775
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA------DRLIPVSLELGGKS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 776 GIIIDESADLDQAVVGVMNSA-FGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQN 854
Cdd:cd07108 231 PMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 855 ILNYIAKGKET--ATLAFEGEVP-----NHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFAL 927
Cdd:cd07108 311 VCGYIDLGLSTsgATVLRGGPLPgegplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320983422 928 TGGLYSRTPSHIERAYREFEVGNLYINRGitGALVDRHPFGGFKLSGIGSKAGGRDYLLQFLEPRSIT 995
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLGREASLEGMLEHFTQKKTVN 456
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
540-995 |
8.47e-98 |
|
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: 316.09 E-value: 8.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 540 VNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEV 619
Cdd:cd07099 1 RNPATG-EVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 620 SEAIDFCRYYAKEMERL--ESGVQRNL--PGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSS 695
Cdd:cd07099 80 LLALEAIDWAARNAPRVlaPRKVPTGLlmPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 696 VIGAKIAEVLQAAGLPTGVFTYLPAKGSTvGSHLVKHPdVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKN 775
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAA------ERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 776 GIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGS----A 851
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARqldiV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 852 QQNILNYIAKGketATLAFEGEVPN-HGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGG 930
Cdd:cd07099 312 RRHVDDAVAKG---AKALTGGARSNgGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320983422 931 LYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGSKaGGRDYLLQFLEPRSIT 995
Cdd:cd07099 389 VFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRR-HGAEGLREFCRPKAIA 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
526-976 |
2.35e-96 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 313.36 E-value: 2.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE--TETYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAW 603
Cdd:PRK13252 11 IDGAYVEatSGETFEVINPATG-EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 ICWEVAKPIREGD-GEVSEAIDFCRYYAKEMERLEsGVQRNLPGEDNTY-IYQPRGVVVVISPWNFPFAIALGMSVAAIA 681
Cdd:PRK13252 90 ETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALE-GEQIPLRGGSFVYtRREPLGVCAGIGAWNYPIQIACWKSAPALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 682 AGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGStVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkq 761
Cdd:PRK13252 169 AGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA------ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 762 KHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDT 841
Cdd:PRK13252 242 ASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 842 KFSAVIDGSAQQNILNYIAKGK-ETATLAFEGEVPN-----HGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDE 915
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKaEGARLLCGGERLTeggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320983422 916 ALAIANGTNFALTGGLYSRTpshIERAYR---EFEVGNLYINR-GITGALVdrhPFGGFKLSGIG 976
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTAD---LSRAHRvihQLEAGICWINTwGESPAEM---PVGGYKQSGIG 460
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
539-995 |
1.59e-95 |
|
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: 310.08 E-value: 1.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 539 SVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGE 618
Cdd:cd07107 1 VINPATG-QVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 619 VSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIG 698
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 699 AKIAEVLQAAgLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSqqvgcqIVTEASILRPKQKHMKRVIAEMGGKNGII 778
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGS------VPTGRAIMRAAAEGIKHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 779 IDESADLDQAVVGV---MNsaFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNI 855
Cdd:cd07107 233 VFPDADPEAAADAAvagMN--FTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 856 LNYIAKGK-ETATLAF-----EGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTG 929
Cdd:cd07107 311 MHYIDSAKrEGARLVTgggrpEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 930 GLYSRTPSHIERAYREFEVGNLYINRgitgalVDRH----PFGGFKLSGIGSKAgGRDYLLQFLEPRSIT 995
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWING------SSRHflgaPFGGVKNSGIGREE-CLEELLSYTQEKNVN 453
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
540-984 |
2.62e-95 |
|
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: 309.26 E-value: 2.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 540 VNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREG-DGE 618
Cdd:cd07092 2 VDPA-TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVrDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 619 VSEAIDFCRYYAKEMERLESGVQRN-LPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVI 697
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEyLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 698 GAKIAEVLqAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGI 777
Cdd:cd07092 161 TLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA------DTLKRVHLELGGKAPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 778 IIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIdgSAQQ--NI 855
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLN--SAAQreRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 856 LNYIAKGKETATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSR 934
Cdd:cd07092 312 AGFVERAPAHARVLTGGRrAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1320983422 935 TPSHIERAYREFEVGNLYINRGITgaLVDRHPFGGFKLSGIG---SKAGGRDY 984
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYGkdlSIYALEDY 442
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
540-994 |
3.48e-95 |
|
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: 308.69 E-value: 3.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 540 VNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEV 619
Cdd:cd07106 2 INPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 620 SEAIDFCRYYAkEMERLESGVQRNlpgeDNTYI---YQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSV 696
Cdd:cd07106 81 GGAVAWLRYTA-SLDLPDEVIEDD----DTRRVelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 697 IGAKIAEVLQAAgLPTGVFTYLPAKGStVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNG 776
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAA------KTLKRVTLELGGNDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 777 IIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVidgsaqQN-- 854
Cdd:cd07106 228 AIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPV------QNkm 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 855 ----ILNYIAKGK-ETATLAFEGEVPN-HGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALT 928
Cdd:cd07106 302 qydkVKELVEDAKaKGAKVLAGGEPLDgPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLG 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1320983422 929 GGLYSrtpSHIERAY---REFEVGNLYINRgiTGALVDRHPFGGFKLSGIGSkAGGRDYLLQFLEPRSI 994
Cdd:cd07106 382 ASVWS---SDLERAEavaRRLEAGTVWINT--HGALDPDAPFGGHKQSGIGV-EFGIEGLKEYTQTQVI 444
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
526-976 |
1.70e-94 |
|
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: 308.12 E-value: 1.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVETET--YIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAW 603
Cdd:cd07559 5 INGEWVAPSKgeYFDNYNPVNG-KVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 ICWEVAKPIREGDG-EVSEAIDFCRYYAKEMeRLESGVQRNLPGEDNTYI-YQPRGVVVVISPWNFPFAIALGMSVAAIA 681
Cdd:cd07559 84 ETLDNGKPIRETLAaDIPLAIDHFRYFAGVI-RAQEGSLSEIDEDTLSYHfHEPLGVVGQIIPWNFPLLMAAWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 682 AGNTVILKPAEQSSVIGAKIAEVLQAAgLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkq 761
Cdd:cd07559 163 AGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 762 KHMKRVIAEMGGKNGIII-----DESADLDQAVVGVMnsaFGFA---GQKCSACSRAIVLAPVYDNFMERLVEATRSLKV 833
Cdd:cd07559 236 ENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQ---LGFAfnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 834 GEAHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATL------AFEGEVPNHGFYVPPTIFGdVDPDSVIAQEEIFGPVLA 906
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKeEGAEVltggerLTLGGLDKGYFYEPTLIKG-GNNDMRIFQEEIFGPVLA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1320983422 907 VIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgiTGALVDRH-PFGGFKLSGIG 976
Cdd:cd07559 392 VITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN---CYHQYPAHaPFGGYKKSGIG 459
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
520-997 |
1.48e-93 |
|
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: 305.26 E-value: 1.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 520 KTYlpiINGQAVETET-YIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKK-LSAKERGDMLRKAADIMEEKR 597
Cdd:cd07082 3 KYL---INGEWKESSGkTIEVYSPIDG-EVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 598 EELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLEsgvQRNLPGE-----DNTY-IYQ--PRGVVVVISPWNFPF 669
Cdd:cd07082 79 EEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLD---GDSLPGDwfpgtKGKIaQVRrePLGVVLAIGPFNYPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 670 AIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQ 749
Cdd:cd07082 156 NLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 750 IVteasilrpKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATR 829
Cdd:cd07082 236 LK--------KQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 830 SLKVGEAHLPDTKFSAVIDGSA----QQNILNYIAKGketATLAFEG--EVPNhgfYVPPTIFGDVDPDSVIAQEEIFGP 903
Cdd:cd07082 308 KLKVGMPWDNGVDITPLIDPKSadfvEGLIDDAVAKG---ATVLNGGgrEGGN---LIYPTLLDPVTPDMRLAWEEPFGP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 904 VLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYIN----RGItgalvDRHPFGGFKLSGIGSKa 979
Cdd:cd07082 382 VLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIGTQ- 455
|
490
....*....|....*...
gi 1320983422 980 GGRDYLLQFLEPRSITEN 997
Cdd:cd07082 456 GIGDALRSMTRRKGIVIN 473
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
526-985 |
2.05e-89 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 294.51 E-value: 2.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVETETYIESV-NPANSSqVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWI 604
Cdd:PRK13473 7 INGELVAGEGEKQPVyNPATGE-VLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 605 CWEVAKPIREG-DGEVSEAIDFCRYYAkemerlesGVQRNLPG-------EDNT-YIYQ-PRGVVVVISPWNFPfaiaLG 674
Cdd:PRK13473 86 SLNCGKPLHLAlNDEIPAIVDVFRFFA--------GAARCLEGkaageylEGHTsMIRRdPVGVVASIAPWNYP----LM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 675 MSV----AAIAAGNTVILKPAEQSSVIGAKIAEVLQAAgLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQI 750
Cdd:PRK13473 154 MAAwklaPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 751 VTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRS 830
Cdd:PRK13473 233 LSAAA------DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVAT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 831 LKVGEAHLPDTKFSAVIdgSAQQ--NILNYI--AKGKETATLAFEGEVPNH-GFYVPPTIFGDVDPDSVIAQEEIFGPVL 905
Cdd:PRK13473 307 LKVGDPDDEDTELGPLI--SAAHrdRVAGFVerAKALGHIRVVTGGEAPDGkGYYYEPTLLAGARQDDEIVQREVFGPVV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 906 AVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITgaLVDRHPFGGFKLSGIG---SKAGGR 982
Cdd:PRK13473 385 SVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYGkdmSLYGLE 462
|
...
gi 1320983422 983 DYL 985
Cdd:PRK13473 463 DYT 465
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
526-995 |
4.03e-89 |
|
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: 293.87 E-value: 4.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQ---AVETETYiESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSL---WKKLSAKERGDMLRKAADIMEEKREE 599
Cdd:cd07141 11 INNEwhdSVSGKTF-PTINPATG-EKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 600 LIAWICWEVAKPIREG-DGEVSEAIDFCRYYAKEMERLESgvqRNLPGEDNTYIY---QPRGVVVVISPWNFPFAIALGM 675
Cdd:cd07141 89 LASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHG---KTIPMDGDFFTYtrhEPVGVCGQIIPWNFPLLMAAWK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 676 SVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcQIVTEAS 755
Cdd:cd07141 166 LAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVG-KLIQQAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 756 ilrpKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGE 835
Cdd:cd07141 245 ----GKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 836 AHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSF 913
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKkEGAKLECGGKrHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 914 DEALAIANGTNFALTGGLYSRtpsHIERAY---REFEVGNLYINrgITGALVDRHPFGGFKLSGIGSKAgGRDYLLQFLE 990
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTK---DIDKAItfsNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNGREL-GEYGLQEYTE 474
|
....*
gi 1320983422 991 PRSIT 995
Cdd:cd07141 475 VKTVT 479
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
525-980 |
2.89e-88 |
|
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: 291.32 E-value: 2.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 525 IINGQ---AVETETYiESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSL--WKKLSAKERGDMLRKAADIMEEKREE 599
Cdd:cd07142 7 FINGQfvdAASGKTF-PTIDPRNG-EVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 600 LIAWICWEVAKPIREGD-GEVSEAIDFCRYYAKEMERLESgvqRNLPGEDNTYIY---QPRGVVVVISPWNFPFaIALGM 675
Cdd:cd07142 85 LAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHG---MTLPADGPHHVYtlhEPIGVVGQIIPWNFPL-LMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 676 SVA-AIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEA 754
Cdd:cd07142 161 KVGpALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 755 SilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVG 834
Cdd:cd07142 241 A-----KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 835 EAHLPDTKFSAVIDGSAQQNILNYIAKGKET-ATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQS 912
Cdd:cd07142 316 DPFRKGVEQGPQVDKEQFEKILSYIEHGKEEgATLITGGDrIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1320983422 913 FDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYIN-RGITGALVdrhPFGGFKLSGIGSKAG 980
Cdd:cd07142 396 VDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
539-995 |
6.52e-88 |
|
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: 289.63 E-value: 6.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 539 SVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAF--SLWKKlSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:cd07120 1 SIDPA-TGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAH-DPRLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKeMERLESG-VQRNLPGEDNTYIYQPRGVVVVISPWNFPfAIALGMSVA-AIAAGNTVILKPAEQS 694
Cdd:cd07120 79 FEISGAISELRYYAG-LARTEAGrMIEPEPGSFSLVLREPMGVAGIIVPWNSP-VVLLVRSLApALAAGCTVVVKPAGQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 695 SVIGAKIAEVL-QAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGG 773
Cdd:cd07120 157 AQINAAIIRILaEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA------PTLKRLGLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 774 KNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQ 853
Cdd:cd07120 231 KTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 854 NILNYIAKGKET-ATLAFEGEVPNH----GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVikaQSFD---EALAIANGTNF 925
Cdd:cd07120 311 RVDRMVERAIAAgAEVVLRGGPVTEglakGAFLRPTLLEVDDPDADIVQEEIFGPVLTL---ETFDdeaEAVALANDTDY 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 926 ALTGGLYSRTPSHIERAYREFEVGNLYINRgiTGALVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSIT 995
Cdd:cd07120 388 GLAASVWTRDLARAMRVARAIRAGTVWIND--WNKLFAEAEEGGYRQSGLG-RLHGVAALEDFIEYKHIY 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
537-993 |
2.04e-87 |
|
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: 288.37 E-value: 2.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:cd07147 1 LEVTNPY-TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLESGVQRnLPGEDNTYIYQ------PRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKP 690
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRIYGEVLP-LDISARGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 691 AEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKgSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEAsilrPKqkhmKRVIAE 770
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARA----GK----KKVVLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 771 MGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGS 850
Cdd:cd07147 230 LGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 851 AQQNILNYI----AKGketATLAFEGEVpnHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFA 926
Cdd:cd07147 310 EAERVEGWVneavDAG---AKLLTGGKR--DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFG 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1320983422 927 LTGGLYSRTPSHIERAYREFEVGNLYINRgITGALVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRS 993
Cdd:cd07147 385 LQAGVFTRDLEKALRAWDELEVGGVVIND-VPTFRVDHMPYGGVKDSGIG-REGVRYAIEEMTEPRL 449
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
547-1001 |
2.24e-87 |
|
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: 287.65 E-value: 2.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 547 QVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFC 626
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 627 RYyAKEMERLESGVQrnLPGEDNTYIY---QPRGVVVVISPWNFPFAIALgMSVA-AIAAGNTVILKPAEQSSVI-GAKI 701
Cdd:cd07152 82 HE-AAGLPTQPQGEI--LPSAPGRLSLarrVPLGVVGVISPFNFPLILAM-RSVApALALGNAVVLKPDPRTPVSgGVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 702 AEVLQAAGLPTGVFTYLPAkGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDE 781
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAG------RHLKKVSLELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 782 SADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNIL----N 857
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHaivdD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 858 YIAKGketATLAFEGEvpNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPS 937
Cdd:cd07152 311 SVAAG---ARLEAGGT--YDGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVG 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320983422 938 HIERAYREFEVGNLYINRGItgALVDRH-PFGGFKLSGIGSKAGGrdyllqflePRSITENTQRQ 1001
Cdd:cd07152 386 RAMALADRLRTGMLHINDQT--VNDEPHnPFGGMGASGNGSRFGG---------PANWEEFTQWQ 439
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
519-980 |
4.82e-87 |
|
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: 288.27 E-value: 4.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 519 GKTYLPI---INGQAVET--ETYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAF-SLW-KKLSAKERGDMLRKAAD 591
Cdd:cd07143 1 GKYEQPTglfINGEFVDSvhGGTVKVYNPSTG-KLITKIAEATEADVDIAVEVAHAAFeTDWgLKVSGSKRGRCLSKLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 592 IMEEKREELIAWICWEVAKPIRE-GDGEVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFA 670
Cdd:cd07143 80 LMERNLDYLASIEALDNGKTFGTaKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 671 IALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQI 750
Cdd:cd07143 160 MCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 751 VTEASilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRS 830
Cdd:cd07143 240 MEAAA-----KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 831 LKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVI 908
Cdd:cd07143 315 LKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKaEGATVETGGKrHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1320983422 909 KAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgITGALVDRHPFGGFKLSGIGSKAG 980
Cdd:cd07143 395 KFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSGIGRELG 464
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
501-990 |
7.69e-87 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 288.13 E-value: 7.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 501 DQEREAAQTALQQVRRQ-LGKTYlPIINGQAVETE--TYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKL 577
Cdd:PLN02278 4 RASSMDAQSALVKLRNAgLLRTQ-GLIGGKWTDAYdgKTFPVYNPATG-EVIANVPCMGRAETNDAIASAHDAFPSWSKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 578 SAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGV-QRNLPGEDNTYIYQPR 656
Cdd:PLN02278 82 TASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIiPSPFPDRRLLVLKQPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 657 GVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVH 736
Cdd:PLN02278 162 GVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 737 LIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPV 816
Cdd:PLN02278 242 KITFTGSTAVGKKLMAGAA------ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 817 YDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNY----IAKGketATLAFEGEVPNHG--FYvPPTIFGDVD 890
Cdd:PLN02278 316 YDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHvqdaVSKG---AKVLLGGKRHSLGgtFY-EPTVLGDVT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 891 PDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVdrHPFGGF 970
Cdd:PLN02278 392 EDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFGGV 469
|
490 500
....*....|....*....|
gi 1320983422 971 KLSGIGsKAGGRDYLLQFLE 990
Cdd:PLN02278 470 KQSGLG-REGSKYGIDEYLE 488
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
540-994 |
2.90e-86 |
|
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: 284.91 E-value: 2.90e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 540 VNPANSSqVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEV 619
Cdd:cd07102 1 ISPIDGS-VIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 620 SEAIDFCRYYAKEMER-LESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIG 698
Cdd:cd07102 80 RGMLERARYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 699 AKIAEVLQAAGLPTGVFTYLPAKGSTvGSHLVKHPDVHLIAFTGSQQVGcqivteASILRPKQKHMKRVIAEMGGKNGII 778
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGG------RAIQRAAAGRFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 779 IDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNY 858
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 859 I----AKGketATLAFEG----EVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGG 930
Cdd:cd07102 313 IadaiAKG---ARALIDGalfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTAS 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320983422 931 LYSRtpsHIERAYR---EFEVGNLYINRGItgaLVD-RHPFGGFKLSGIGSkAGGRDYLLQFLEPRSI 994
Cdd:cd07102 390 VWTK---DIARAEAlgeQLETGTVFMNRCD---YLDpALAWTGVKDSGRGV-TLSRLGYDQLTRPKSY 450
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
515-980 |
8.05e-86 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 285.47 E-value: 8.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 515 RRQLgktylpIINGQAVETET--YIESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSL-----WKKLSAKERGDMLR 587
Cdd:PLN02467 7 RRQL------FIGGEWREPVLgkRIPVVNPA-TEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 588 KAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLEsGVQR---NLPGE--DNTYIYQPRGVVVVI 662
Cdd:PLN02467 80 AIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALD-AKQKapvSLPMEtfKGYVLKEPLGVVGLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 663 SPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTG 742
Cdd:PLN02467 159 TPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 743 SQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFME 822
Cdd:PLN02467 239 STATGRKIMTAAA------QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 823 RLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGEVPNH---GFYVPPTIFGDVDPDSVIAQE 898
Cdd:PLN02467 313 KLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKsEGATILCGGKRPEHlkkGFFIEPTIITDVTTSMQIWRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 899 EIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgITGALVDRHPFGGFKLSGIGSK 978
Cdd:PLN02467 393 EVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFGRE 470
|
..
gi 1320983422 979 AG 980
Cdd:PLN02467 471 LG 472
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
502-991 |
1.37e-85 |
|
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: 284.29 E-value: 1.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 502 QEREAAQTALQQVRRQLGktylPIINGQ--AVETETYIESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSA 579
Cdd:cd07111 6 ESAACALAWLDAHDRSFG----HFINGKwvKPENRKSFPTINPA-TGEVLASVLQAEEEDVDAAVAAARTAFESWSALPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 580 KERGDMLRKAADIMEEKREELIAWICWEVAKPIREG-DGEVSEAIDFCRYYAKEMERLESgvqrNLPGedntyiYQPRGV 658
Cdd:cd07111 81 HVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLLDT----ELAG------WKPVGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 659 VVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTvGSHLVKHPDVHLI 738
Cdd:cd07111 151 VGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 739 AFTGSQQVGcqivteASILRPKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYD 818
Cdd:cd07111 230 AFTGSTEVG------RALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 819 NFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFE--GEVPNHGFYVPPTIFGDVDPDSVIA 896
Cdd:cd07111 304 ELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQpgADLPSKGPFYPPTLFTNVPPASRIA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 897 QEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYS-RTPSHIERAYReFEVGNLYINrgiTGALVD-RHPFGGFKLSG 974
Cdd:cd07111 384 QEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSeNLSLALEVALS-LKAGVVWIN---GHNLFDaAAGFGGYRESG 459
|
490
....*....|....*..
gi 1320983422 975 IGsKAGGRDYLLQFLEP 991
Cdd:cd07111 460 FG-REGGKEGLYEYLRP 475
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
537-982 |
2.30e-85 |
|
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: 282.71 E-value: 2.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPANSSqVVGKIGLANIDQAEAAVQVAKNAFSlwkKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:cd07146 1 LEVRNPYTGE-VVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLESGVQR--NLPGEDNTYIY---QPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPA 691
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFScdLTANGKARKIFtlrEPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 692 EQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqkhMKRVIAEM 771
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 772 GGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSA 851
Cdd:cd07146 229 GGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 852 ----QQNILNYIAKGketATLAFEGEvpNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFAL 927
Cdd:cd07146 309 aiqiENRVEEAIAQG---ARVLLGNQ--RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1320983422 928 TGGLYSRTPSHIERAYREFEVGNLYINrGITGALVDRHPFGGFKLSGIGSKAGGR 982
Cdd:cd07146 384 SSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEGVR 437
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
527-941 |
1.25e-83 |
|
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: 278.71 E-value: 1.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 527 NGQAVETETYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICW 606
Cdd:cd07130 4 DGEWGGGGGVVTSISPANG-EPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 607 EVAKPIREGDGEVSEAIDFCRY--------YAKEM--ERlesgvqrnlPGEDNTYIYQPRGVVVVISPWNFPFAIALGMS 676
Cdd:cd07130 83 EMGKILPEGLGEVQEMIDICDFavglsrqlYGLTIpsER---------PGHRMMEQWNPLGVVGVITAFNFPVAVWGWNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 677 VAAIAAGNTVILKPAEQ---SSVIGAKI-AEVLQAAGLPTGVFTyLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcQIVT 752
Cdd:cd07130 154 AIALVCGNVVVWKPSPTtplTAIAVTKIvARVLEKNGLPGAIAS-LVCGGADVGEALVKDPRVPLVSFTGSTAVG-RQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 753 EASilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLK 832
Cdd:cd07130 232 QAV-----AARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 833 VGEAHLPDTKFSAVIDGSAQQNILNYIAKGKET-ATLAFEGEV-PNHGFYVPPTIFgDVDPDSVIAQEEIFGPVLAVIKA 910
Cdd:cd07130 307 IGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQgGTVLFGGKViDGPGNYVEPTIV-EGLSDAPIVKEETFAPILYVLKF 385
|
410 420 430
....*....|....*....|....*....|.
gi 1320983422 911 QSFDEALAIANGTNFALTGGLYSRTPSHIER 941
Cdd:cd07130 386 DTLEEAIAWNNEVPQGLSSSIFTTDLRNAFR 416
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
537-995 |
1.75e-82 |
|
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: 274.70 E-value: 1.75e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPANSSqVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:cd07094 1 LDVHNPYDGE-VIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMER-----LESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPA 691
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERirgeeIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 692 EQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASIlrpkqkhmKRVIAEM 771
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------KRIALEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 772 GGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSA 851
Cdd:cd07094 232 GGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 852 QQNILNYIAKG-KETATLAFEGEvpNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGG 930
Cdd:cd07094 312 AERVERWVEEAvEAGARLLCGGE--RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1320983422 931 LYSRTPSHIERAYREFEVGNLYINRGiTGALVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSIT 995
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVG-REGVPYAMEEMTEEKTVV 452
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
526-976 |
2.28e-82 |
|
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: 275.49 E-value: 2.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVETET--YIESVNPANssqvvGKIgLANIDQA-----EAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKRE 598
Cdd:cd07117 5 INGEWVKGSSgeTIDSYNPAN-----GET-LSEITDAtdadvDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 599 ELIAWICWEVAKPIREGDG-EVSEAIDFCRYYAKEMeRLESGvQRNLPGED--NTYIYQPRGVVVVISPWNFPFAIALGM 675
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVI-RAEEG-SANMIDEDtlSIVLREPIGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 676 SVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAgLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEAS 755
Cdd:cd07117 157 LAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 756 ilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGE 835
Cdd:cd07117 236 ------KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 836 AHLPDTKFSAVIDGSAQQNILNYIAKGKET-ATLAFEGE-----VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIK 909
Cdd:cd07117 310 PLDPDTQMGAQVNKDQLDKILSYVDIAKEEgAKILTGGHrltenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIK 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320983422 910 AQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgiTGALVDRH-PFGGFKLSGIG 976
Cdd:cd07117 390 FKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN---TYNQIPAGaPFGGYKKSGIG 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
526-995 |
7.07e-82 |
|
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: 274.37 E-value: 7.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVETE---TYiESVNPANSSqVVGKIGLANIDQAEAAVQVAKNAF--SLWKKLSAKERGDMLRKAADIMEEKREEL 600
Cdd:cd07140 10 INGEFVDAEggkTY-NTINPTDGS-VICKVSLATVEDVDRAVAAAKEAFenGEWGKMNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 601 iAWIcwevaKPIREG-------DGEVSEAIDFCRYYAKEMERLESG---VQRNLPGEDNTYIY-QPRGVVVVISPWNFPF 669
Cdd:cd07140 88 -ATI-----ESLDSGavytlalKTHVGMSIQTFRYFAGWCDKIQGKtipINQARPNRNLTLTKrEPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 670 AIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQ 749
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 750 IVTEASIlrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATR 829
Cdd:cd07140 242 IMKSCAV-----SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 830 SLKVGE------AHLPDTKfSAVIDgsaqqNILNYIAKG-KETATLAFEG-EVPNHGFYVPPTIFGDVDPDSVIAQEEIF 901
Cdd:cd07140 317 KMKIGDpldrstDHGPQNH-KAHLD-----KLVEYCERGvKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 902 GPVLAVIKAQS--FDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgiTGALVD-RHPFGGFKLSGIGsK 978
Cdd:cd07140 391 GPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN---TYNKTDvAAPFGGFKQSGFG-K 466
|
490
....*....|....*..
gi 1320983422 979 AGGRDYLLQFLEPRSIT 995
Cdd:cd07140 467 DLGEEALNEYLKTKTVT 483
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
559-995 |
1.12e-81 |
|
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: 271.76 E-value: 1.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 559 QAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLES 638
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 639 G-VQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTY 717
Cdd:cd07105 81 GsIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 718 L---PAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMN 794
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAA------KHLKPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 795 SAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPdtkfSAVIDGSAQQN---ILNYIAKGketATLAF- 870
Cdd:cd07105 235 GAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVLG----SLVSAAAADRVkelVDDALSKG---AKLVVg 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 871 -EGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRtpsHIERAYR---EF 946
Cdd:cd07105 308 gLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTR---DLARALAvakRI 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1320983422 947 EVGNLYINrGITgaLVDRH--PFGGFKLSGIGsKAGGRDYLLQFLEPRSIT 995
Cdd:cd07105 385 ESGAVHIN-GMT--VHDEPtlPHGGVKSSGYG-RFNGKWGIDEFTETKWIT 431
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
559-974 |
1.98e-81 |
|
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: 271.07 E-value: 1.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 559 QAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIdfcryyAKEMERLES 638
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMA------GKIDISIKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 639 gvQRNLPGEDNTYI--------YQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGL 710
Cdd:cd07095 75 --YHERTGERATPMaqgravlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 711 PTGVFTyLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIvteasilrpKQK---HMKRVIA-EMGGKNGIIIDESADLD 786
Cdd:cd07095 153 PPGVLN-LVQGGRETGEALAAHEGIDGLLFTGSAATGLLL---------HRQfagRPGKILAlEMGGNNPLVVWDVADID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 787 QAVVGVMNSAFGFAGQKCSACSRAIVL-APVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNY----IAK 861
Cdd:cd07095 223 AAAYLIVQSAFLTAGQRCTCARRLIVPdGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAqqdlLAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 862 GKETaTLAFEGEVPNHGFYVPPTIfgDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIER 941
Cdd:cd07095 303 GGEP-LLAMERLVAGTAFLSPGII--DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFER 379
|
410 420 430
....*....|....*....|....*....|...
gi 1320983422 942 AYREFEVGNLYINRGITGAlVDRHPFGGFKLSG 974
Cdd:cd07095 380 FLARIRAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
526-990 |
5.85e-80 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 269.46 E-value: 5.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 ING---QAVETETYiESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFS--LWKKLSAKERGDMLRKAADIMEEKREEL 600
Cdd:PRK09847 24 INGeytAAAENETF-ETVDPV-TQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 601 IAWICWEVAKPIREG-DGEVSEAIDFCRYYAKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAA 679
Cdd:PRK09847 102 ALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 680 IAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrp 759
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 760 kQKHMKRVIAEMGGKNG-IIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHL 838
Cdd:PRK09847 258 -DSNMKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 839 PDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALA 918
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQ 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1320983422 919 IANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVdrHPFGGFKLSGigskaGGRDYLLQFLE 990
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSG-----NGRDKSLHALE 481
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
526-994 |
1.15e-79 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 268.61 E-value: 1.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQ---AVETETYiESVNPaNSSQVVGKIGLANIDQAEAAVQVAKNAFS--LWKKLSAKERGDMLRKAADIMEEKREEL 600
Cdd:PLN02766 25 INGEfvdAASGKTF-ETRDP-RTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 601 IAWICWEVAKPIREGDG-EVSEAIDFCRYYAKEMERLESGVQRnLPGEDNTY-IYQPRGVVVVISPWNFPFAIALGMSVA 678
Cdd:PLN02766 103 AALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLK-MSRQLQGYtLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 679 AIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilr 758
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAA--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 759 pkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHL 838
Cdd:PLN02766 259 --TSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 839 PDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEA 916
Cdd:PLN02766 337 PRARQGPQVDKQQFEKILSYIEHGKrEGATLLTGGKpCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320983422 917 LAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgITGALVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSI 994
Cdd:PLN02766 417 IKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFG-RDQGMDALDKYLQVKSV 491
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
526-985 |
2.04e-79 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 267.54 E-value: 2.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVETET--YIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAW 603
Cdd:PRK11241 15 INGEWLDANNgeVIDVTNPANG-DKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 ICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGVqrnLPGEDN----TYIYQPRGVVVVISPWNFPFAIALGMSVAA 679
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDT---IPGHQAdkrlIVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 680 IAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrp 759
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCA---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 760 kqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLP 839
Cdd:PRK11241 247 --KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 840 DTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVPNH--GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEAL 917
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHElgGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1320983422 918 AIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVdrHPFGGFKLSGI---GSKAGGRDYL 985
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIKASGLgreGSKYGIEDYL 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
526-995 |
5.94e-78 |
|
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: 263.15 E-value: 5.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAV--ETETYIESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAF-SLWKKLSAKERGDMLRKAADIMEEKREELIA 602
Cdd:cd07113 4 IDGRPVagQSEKRLDITNPA-TEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 603 WICWEVAKPIREGDG-EVSEAIDFCRYYAKEMERLE-SGVQRNLP---GEDNTYIY--QPRGVVVVISPWNFPFAIALGM 675
Cdd:cd07113 83 LETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINgETLAPSIPsmqGERYTAFTrrEPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 676 SVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGStVGSHLVKHPDVHLIAFTGSQQVGCQIVTEAS 755
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 756 ilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGE 835
Cdd:cd07113 242 ------SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 836 AHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSF 913
Cdd:cd07113 316 PMDESVMFGPLANQPHFDKVCSYLDDARaEGDEIVRGGEaLAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 914 DEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgiTGALVDRH-PFGGFKLSGIGsKAGGRDYLLQFLEPR 992
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDPAvPFGGMKQSGIG-REFGSAFIDDYTELK 471
|
...
gi 1320983422 993 SIT 995
Cdd:cd07113 472 SVM 474
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
561-996 |
4.32e-75 |
|
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: 254.54 E-value: 4.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 561 EAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESGV 640
Cdd:cd07101 21 EAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERLLKPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 641 QRN--LPG-EDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTY 717
Cdd:cd07101 101 RRRgaIPVlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 718 LPAKGSTVGSHLVKHPDvhLIAFTGSQQVGCQIVTEASilrpkqkhmKRVI---AEMGGKNGIIIDESADLDQAVVGVMN 794
Cdd:cd07101 181 VTGPGSEVGGAIVDNAD--YVMFTGSTATGRVVAERAG---------RRLIgcsLELGGKNPMIVLEDADLDKAAAGAVR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 795 SAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYI--AKGKETATLAFEG 872
Cdd:cd07101 250 ACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVddAVAKGATVLAGGR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 873 EVPNHG--FYvPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGN 950
Cdd:cd07101 330 ARPDLGpyFY-EPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGT 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1320983422 951 LYINRGITGAL--VDRhPFGGFKLSGIGSKAgGRDYLLQFLEPRSITE 996
Cdd:cd07101 409 VNVNEGYAAAWasIDA-PMGGMKDSGLGRRH-GAEGLLKYTETQTVAV 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
547-1009 |
6.44e-74 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 253.65 E-value: 6.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 547 QVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFC 626
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 627 RYYAKEMERL-----ESGVqrnLPG-EDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAK 700
Cdd:PRK09407 123 RYYARRAPKLlaprrRAGA---LPVlTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 701 IAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDvhLIAFTGSQQVGCQIVTEASilrpkqkhmKRVI---AEMGGKNGI 777
Cdd:PRK09407 200 AVELLYEAGLPRDLWQVVTGPGPVVGTALVDNAD--YLMFTGSTATGRVLAEQAG---------RRLIgfsLELGGKNPM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 778 IIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVG--------------EAHLpDTKF 843
Cdd:PRK09407 269 IVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGagydysadmgslisEAQL-ETVS 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 844 SAVIDGsaqqnilnyIAKGketATLAFEGEV-PNHG--FYvPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIA 920
Cdd:PRK09407 348 AHVDDA---------VAKG---ATVLAGGKArPDLGplFY-EPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 921 NGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGAL--VDRhPFGGFKLSGIGSKAgGRDYLLQFLEPRSITenT 998
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWgsVDA-PMGGMKDSGLGRRH-GAEGLLKYTESQTIA--T 490
|
490
....*....|..
gi 1320983422 999 QR-QGFAPLDGI 1009
Cdd:PRK09407 491 QRvLPLAPPPGM 502
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
525-980 |
1.27e-72 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 250.50 E-value: 1.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 525 IINGQAVETET--YIESVNPaNSSQVVGKIGLANIDQAEAAVQVAKNAFSL--WKKLSAKERGDMLRKAADIMEEKREEL 600
Cdd:PLN02466 61 LINGQFVDAASgkTFPTLDP-RTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 601 IAWICWEVAKPIREGDG-EVSEAIDFCRYYAKEMERLESGVqrnLPGEDNTYI---YQPRGVVVVISPWNFP---FAIAL 673
Cdd:PLN02466 140 AALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLT---VPADGPHHVqtlHEPIGVAGQIIPWNFPllmFAWKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 674 GmsvAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGcQIVTE 753
Cdd:PLN02466 217 G---PALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTG-KIVLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 754 ASilrpKQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERlvEATRSLK- 832
Cdd:PLN02466 293 LA----AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEK--AKARALKr 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 833 -VGEAHLPDTKFSAVIDGSAQQNILNYIAKGKET-ATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIK 909
Cdd:PLN02466 367 vVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESgATLECGGDrFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILK 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1320983422 910 AQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYIN-RGITGALVdrhPFGGFKLSGIGSKAG 980
Cdd:PLN02466 447 FKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
526-976 |
1.40e-71 |
|
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: 245.82 E-value: 1.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE--TETYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAW 603
Cdd:cd07116 5 IGGEWVApvKGEYFDNITPVTG-KVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 ICWEVAKPIREGDG-EVSEAIDFCRYYAKEMeRLESGVQRNLPGEDNTY-IYQPRGVVVVISPWNFPFAIALGMSVAAIA 681
Cdd:cd07116 84 ETWDNGKPVRETLAaDIPLAIDHFRYFAGCI-RAQEGSISEIDENTVAYhFHEPLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 682 AGNTVILKPAEQSSVIGAKIAEVLQAAgLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkq 761
Cdd:cd07116 163 AGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 762 KHMKRVIAEMGGKN-GIIIDESAD-----LDQAVVGVMNSAFGfAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGE 835
Cdd:cd07116 236 ENIIPVTLELGGKSpNIFFADVMDaddafFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 836 AHLPDTKFSAVIDGSAQQNILNYIAKGK-ETATL------AFEGEVPNHGFYVPPTIFGDvdPDSVIAQEEIFGPVLAVI 908
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDIGKeEGAEVltggerNELGGLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1320983422 909 KAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINrgiTGALVDRH-PFGGFKLSGIG 976
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN---CYHLYPAHaAFGGYKQSGIG 458
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
526-974 |
5.91e-70 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 241.40 E-value: 5.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVE-TETYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWI 604
Cdd:PRK09457 5 INGDWIAgQGEAFESRNPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 605 CWEVAKPIREGDGEVSE-----AIDFCRYYakemERleSGVQRNlPGEDNTYI--YQPRGVVVVISPWNFPFAIALGMSV 677
Cdd:PRK09457 84 ARETGKPLWEAATEVTAminkiAISIQAYH----ER--TGEKRS-EMADGAAVlrHRPHGVVAVFGPYNFPGHLPNGHIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 678 AAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAkGSTVGSHLVKHPDVHLIAFTGSQQVGcqivteasIL 757
Cdd:PRK09457 157 PALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTG--------YL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 758 RPKQ--KHMKRVIA-EMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVY-DNFMERLVEATRSLKV 833
Cdd:PRK09457 228 LHRQfaGQPEKILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 834 GEAHLPDTKF-SAVIDGSAQQNIL----NYIAKGKEtATLAFEGEVPNHGFYVPPTIfgDVDPDSVIAQEEIFGPVLAVI 908
Cdd:PRK09457 308 GRWDAEPQPFmGAVISEQAAQGLVaaqaQLLALGGK-SLLEMTQLQAGTGLLTPGII--DVTGVAELPDEEYFGPLLQVV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1320983422 909 KAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRhPFGGFKLSG 974
Cdd:PRK09457 385 RYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGASSAA-PFGGVGASG 449
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
540-997 |
1.78e-69 |
|
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: 239.51 E-value: 1.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 540 VNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD-GE 618
Cdd:cd07098 1 YDPA-TGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 619 VSEAIDFCRYYAKEME---RLES-GVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQ- 693
Cdd:cd07098 80 ILVTCEKIRWTLKHGEkalRPESrPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 694 ---SSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTvGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAE 770
Cdd:cd07098 160 awsSGFFLSIIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAA------ESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 771 MGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGS 850
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 851 A----QQNILNYIAKGketATLAFEGEVPNH-----GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIAN 921
Cdd:cd07098 313 RfdrlEELVADAVEKG---ARLLAGGKRYPHpeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1320983422 922 GTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGsKAGGRDYLLQFLEPRSITEN 997
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTED 464
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
586-990 |
2.27e-69 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 237.33 E-value: 2.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 586 LRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEMERLESG-VQRNLPGEdNTYIY-QPRGVVVVIS 663
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEiIQSDRPGE-NILLFkRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 664 PWNFPF-AIALGMSvAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTG 742
Cdd:PRK10090 80 PWNFPFfLIARKMA-PALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 743 SQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFME 822
Cdd:PRK10090 159 SVSAGEKIMAAAA------KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 823 RLVEATRSLKVGE-AHLPDTKFSAVIDGSAQQNILNYIAKGKET-ATLAFEGEVPN-HGFYVPPTIFGDVDPDSVIAQEE 899
Cdd:PRK10090 233 RLGEAMQAVQFGNpAERNDIAMGPLINAAALERVEQKVARAVEEgARVALGGKAVEgKGYYYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 900 IFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHpfGGFKLSGIGSkA 979
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSGIGG-A 389
|
410
....*....|.
gi 1320983422 980 GGRDYLLQFLE 990
Cdd:PRK10090 390 DGKHGLHEYLQ 400
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
537-984 |
8.27e-68 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 234.63 E-value: 8.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:PRK09406 3 IATINPATG-ETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLESGVQRNLP--GEDNTYI-YQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQ 693
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADEPADAAavGASRAYVrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 694 SSVIGAKIAEVLQAAGLPTGVFTYLPAkGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGG 773
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLLV-GSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAG------DEIKKTVLELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 774 KNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQ 853
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 854 NILNYIAKGKET-ATLAFEGEVPNH-GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGL 931
Cdd:PRK09406 315 EVEKQVDDAVAAgATILCGGKRPDGpGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1320983422 932 YSRTPSHIERAYREFEVGNLYINrGITGALVDRhPFGGFKLSGIG---SKAGGRDY 984
Cdd:PRK09406 395 WTRDEAEQERFIDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
568-980 |
4.84e-64 |
|
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: 223.26 E-value: 4.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 568 KNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD-----GEVSEAIDFCRYYAKEMERLESGVQR 642
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilPVLSEINHAIKHLKKWMKPKRVRTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 643 NLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYlpAKG 722
Cdd:cd07134 88 LLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVF--EGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 723 STVGSHLVKHPDVHlIAFTGSQQVGcQIVTEASilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQ 802
Cdd:cd07134 166 AEVAQALLELPFDH-IFFTGSPAVG-KIVMAAA-----AKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 803 KCSACSRAIVLAPVYDNFMERLVEA-TRSLKVGEAHLPDTKFSAVIDGSAQQNILNYI----AKGketATLAFEGEVPNH 877
Cdd:cd07134 239 TCIAPDYVFVHESVKDAFVEHLKAEiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLddavAKG---AKVEFGGQFDAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 878 GFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGI 957
Cdd:cd07134 316 QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVV 395
|
410 420
....*....|....*....|...
gi 1320983422 958 TGALVDRHPFGGFKLSGIGSKAG 980
Cdd:cd07134 396 LHFLNPNLPFGGVNNSGIGSYHG 418
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
535-976 |
8.31e-64 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 223.58 E-value: 8.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 535 TYIESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIRE 614
Cdd:PRK13968 7 THAISVNPATG-EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 615 GDGEVSEAIDFCRYYAKE---MERLESGVQRNlpgEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPA 691
Cdd:PRK13968 86 ARAEVAKSANLCDWYAEHgpaMLKAEPTLVEN---QQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 692 EQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVgSHLVKHPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEM 771
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAG------AALKKCVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 772 GGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVG-----EAHL-PDTKFSa 845
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGdprdeENALgPMARFD- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 846 vIDGSAQQNILNYIAKGketATLAFEGE-VPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTN 924
Cdd:PRK13968 315 -LRDELHHQVEATLAEG---ARLLLGGEkIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSE 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1320983422 925 FALTGGLYSRTPSHIERAYREFEVGNLYINrGITgALVDRHPFGGFKLSGIG 976
Cdd:PRK13968 391 FGLSATIFTTDETQARQMAARLECGGVFIN-GYC-ASDARVAFGGVKKSGFG 440
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
537-978 |
1.26e-59 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 212.69 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:PLN00412 33 VAITNPS-TRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMER-LESG---VQRNLPGED-NTYIYQ---PRGVVVVISPWNFPFAIALGMSVAAIAAGNTVIL 688
Cdd:PLN00412 112 TEVVRSGDLISYTAEEGVRiLGEGkflVSDSFPGNErNKYCLTskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 689 KPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSqQVGCQIVTEASILrPKQkhmkrvi 768
Cdd:PLN00412 192 KPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAISKKAGMV-PLQ------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 769 AEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHlPDTKFSAVID 848
Cdd:PLN00412 263 MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE-DDCDITPVVS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 849 GSAQQNILNYIAKGKET-ATlaFEGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFAL 927
Cdd:PLN00412 342 ESSANFIEGLVMDAKEKgAT--FCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGL 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1320983422 928 TGGLYSRTpshIERAYR---EFEVGNLYIN----RGitgalVDRHPFGGFKLSGIGSK 978
Cdd:PLN00412 420 QGCVFTRD---INKAILisdAMETGTVQINsapaRG-----PDHFPFQGLKDSGIGSQ 469
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
512-979 |
1.81e-57 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 209.22 E-value: 1.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 512 QQVRRQLGKTYLPIINGQAVETET--YIESVNPAnSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKA 589
Cdd:PLN02419 104 QSTQPQMPPRVPNLIGGSFVESQSssFIDVINPA-TQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKF 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 590 ADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYyAKEMERLESGvqRNLP----GEDNTYIYQPRGVVVVISPW 665
Cdd:PLN02419 183 QELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEH-ACGMATLQMG--EYLPnvsnGVDTYSIREPLGVCAGICPF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 666 NFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGShLVKHPDVHLIAFTGSQQ 745
Cdd:PLN02419 260 NFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNT 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 746 VGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVyDNFMERLV 825
Cdd:PLN02419 339 AGMHIYARAA------AKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDA-KSWEDKLV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 826 EATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKG-KETATLAFEGE---VPNH--GFYVPPTIFGDVDPDSVIAQEE 899
Cdd:PLN02419 412 ERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGvDDGAKLLLDGRdivVPGYekGNFIGPTILSGVTPDMECYKEE 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 900 IFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALvdrhPFGGFKlsgiGSKA 979
Cdd:PLN02419 492 IFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPL----PFFSFT----GNKA 563
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
563-980 |
2.67e-56 |
|
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: 201.22 E-value: 2.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 563 AVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIA----------WICW--EVAKPIREgdgevseaIDF-CRYY 629
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAalyadlgkppAEAYltEIAVVLGE--------IDHaLKHL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 630 AKEMERLESGVQRNLPGEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQaag 709
Cdd:cd07087 75 KKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIP--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 710 lptgvfTYLPAK-------GSTVGSHLVKHP-DvhLIAFTGSQQVGcQIVTEASilrpkQKHMKRVIAEMGGKNGIIIDE 781
Cdd:cd07087 152 ------KYFDPEavavvegGVEVATALLAEPfD--HIFFTGSPAVG-KIVMEAA-----AKHLTPVTLELGGKSPCIVDK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 782 SADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLkVGEAHLPDTKFSAVIDGSAQQNILNYIAK 861
Cdd:cd07087 218 DANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 862 GKetatLAFEGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIER 941
Cdd:cd07087 297 GK----VVIGGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQER 372
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1320983422 942 AYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGS---KAG 980
Cdd:cd07087 373 VLAETSSGGVCVNDVLLHAAIPNLPFGGVGNSGMGAyhgKAG 414
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
537-997 |
4.20e-55 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 200.06 E-value: 4.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPANSsQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD 616
Cdd:PLN02315 36 VSSVNPANN-QPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 617 GEVSEAIDFCRYYAKEMERLESGVqrnLPGEDNTY----IYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAE 692
Cdd:PLN02315 115 GEVQEIIDMCDFAVGLSRQLNGSI---IPSERPNHmmmeVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 693 QSSVIGAK----IAEVLQAAGLPTGVFTYLpAKGSTVGSHLVKHPDVHLIAFTGSQQVGcQIVTEASilrpKQKHMKRVI 768
Cdd:PLN02315 192 TTPLITIAmtklVAEVLEKNNLPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVG-LMVQQTV----NARFGKCLL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 769 aEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVID 848
Cdd:PLN02315 266 -ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 849 GSAQQNILNYIAKGKETATLAFEG--EVPNHGFYVPPTIFgDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFA 926
Cdd:PLN02315 345 PESKKNFEKGIEIIKSQGGKILTGgsAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQG 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1320983422 927 LTGGLYSRTPSHIER--AYREFEVGNLYINRGITGALVDrHPFGGFKLSGIGSKAGGrDYLLQFLEPRSITEN 997
Cdd:PLN02315 424 LSSSIFTRNPETIFKwiGPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS-DSWKQYMRRSTCTIN 494
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
555-977 |
3.19e-53 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 194.09 E-value: 3.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 555 ANIDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD--------GEVSEAIDFC 626
Cdd:PTZ00381 4 DNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlltvAEIEHLLKHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 627 RYYAKEMERLESGVQrnLPGEdnTYI-YQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVL 705
Cdd:PTZ00381 84 DEYLKPEKVDTVGVF--GPGK--SYIiPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 706 QaaglptgvfTYLPAK-------GSTVGSHLVKHPDVHLIaFTGSQQVGcQIVTEASilrpkQKHMKRVIAEMGGKNGII 778
Cdd:PTZ00381 160 T---------KYLDPSyvrviegGVEVTTELLKEPFDHIF-FTGSPRVG-KLVMQAA-----AENLTPCTLELGGKSPVI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 779 IDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEAtRSLKVGEAHLPDTKFSAVIDGSAQQNILNY 858
Cdd:PTZ00381 224 VDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEA-IKEFFGEDPKKSEDYSRIVNEFHTKRLAEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 859 IA--KGKetatLAFEGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTP 936
Cdd:PTZ00381 303 IKdhGGK----VVYGGEVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDK 378
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1320983422 937 SHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGS 977
Cdd:PTZ00381 379 RHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMGA 419
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
537-976 |
1.41e-52 |
|
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: 191.48 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 537 IESVNPANSSqVVGKIGLANIDQAEAAVQVAKNAF---SLWkkLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIR 613
Cdd:cd07148 1 LEVVNPFDLK-PIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 614 EGDGEVSEAIDFCRYYAKEMERLEsGVQRNL---PGEDNTYIY---QPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVI 687
Cdd:cd07148 78 DAKVEVTRAIDGVELAADELGQLG-GREIPMgltPASAGRIAFttrEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 688 LKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKgSTVGSHLVKHPDVHLIAFTGSQQVGCQivteasiLRPKQKHMKRV 767
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWM-------LRSKLAPGTRC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 768 IAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVI 847
Cdd:cd07148 229 ALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 848 DGSAQQNILNYI----AKGketATLAFEGEVPNHGFYvPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGT 923
Cdd:cd07148 309 RPREVDRVEEWVneavAAG---ARLLCGGKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1320983422 924 NFALTGGLYSRTPSHIERAYREFEVGNLYINRGiTGALVDRHPFGGFKLSGIG 976
Cdd:cd07148 385 PVAFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
557-996 |
1.68e-51 |
|
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: 187.43 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 557 IDQAEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGD-GEVSEAIDFCRYYAKEM-- 633
Cdd:cd07135 4 LDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 634 ----ERLESGVQRNLPGedNTYIY-QPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAA 708
Cdd:cd07135 84 wakdEKVKDGPLAFMFG--KPRIRkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 709 gLPTGVFTYLPAKGSTVGSHLVKHPDvhLIAFTGSQQVGcQIVTEASilrpkQKHMKRVIAEMGGKNGIIIDESADLDQA 788
Cdd:cd07135 162 -LDPDAFQVVQGGVPETTALLEQKFD--KIFYTGSGRVG-RIIAEAA-----AKHLTPVTLELGGKSPVIVTKNADLELA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 789 VVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHlPDTKFSAVIDGSAQQNILNYIAKGKetATL 868
Cdd:cd07135 233 AKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGAN-ASPDYTRIVNPRHFNRLKSLLDTTK--GKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 869 AFEGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEV 948
Cdd:cd07135 310 VIGGEMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1320983422 949 GNLYINRGITGALVDRHPFGGFKLSGIGSKaGGRDYLLQFLEPRSITE 996
Cdd:cd07135 390 GGVVINDTLIHVGVDNAPFGGVGDSGYGAY-HGKYGFDTFTHERTVVK 436
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
578-977 |
3.52e-47 |
|
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: 174.98 E-value: 3.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 578 SAKERGDMLRKAADIMEEKREELIAWIcwevAK-----PIREGD-GEVSEAIDFCRYYAKEM------ERLESGVQrnLP 645
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAI----SAdfghrSRHETLlAEILPSIAGIKHARKHLkkwmkpSRRHVGLL--FL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 646 GEDNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPT--GVFTylpaKGS 723
Cdd:cd07133 92 PAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDevAVVT----GGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 724 TVGSHLVKHPDVHLIaFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGFAGQK 803
Cdd:cd07133 168 DVAAAFSSLPFDHLL-FTGSTAVGRHVMRAAA------ENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 804 CsacsraivLAPVY--------DNFMERLVEATRSLKVGEAHLPDtkFSAVIDGSAQQNILNYI----AKGKETATLAFE 871
Cdd:cd07133 241 C--------VAPDYvlvpedklEEFVAAAKAAVAKMYPTLADNPD--YTSIINERHYARLQGLLedarAKGARVIELNPA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 872 GEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALtgGLY--SRTPSHIERAYREFEVG 949
Cdd:cd07133 311 GEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPL--ALYyfGEDKAEQDRVLRRTHSG 388
|
410 420
....*....|....*....|....*...
gi 1320983422 950 NLYINRGITGALVDRHPFGGFKLSGIGS 977
Cdd:cd07133 389 GVTINDTLLHVAQDDLPFGGVGASGMGA 416
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
561-977 |
5.92e-47 |
|
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: 174.72 E-value: 5.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 561 EAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREgdgEVSEAIDFCRYYAKE-MERLESG 639
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFE---AVLSEILLVKNEIKYaISNLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 640 VQRNLPGE------DNTYIY-QPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAaglpt 712
Cdd:cd07132 78 MKPEPVKKnlatllDDVYIYkEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPK----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 713 gvftYLPAK-------GSTVGSHLVKHPDVHlIAFTGSQQVGcQIVTEASilrpkQKHMKRVIAEMGGKNGIIIDESADL 785
Cdd:cd07132 153 ----YLDKEcypvvlgGVEETTELLKQRFDY-IFYTGSTSVG-KIVMQAA-----AKHLTPVTLELGGKSPCYVDKSCDI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 786 DQAVVGVMNSAFGFAGQKCSA-----CSRAIvlapvydnfMERLVEATR-SLK--VGE--AHLPDtkFSAVIDGSAQQNI 855
Cdd:cd07132 222 DVAARRIAWGKFINAGQTCIApdyvlCTPEV---------QEKFVEALKkTLKefYGEdpKESPD--YGRIINDRHFQRL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 856 LNYIAKGKetatLAFEGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRT 935
Cdd:cd07132 291 KKLLSGGK----VAIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN 366
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1320983422 936 PSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGS 977
Cdd:cd07132 367 KKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMGA 408
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
643-977 |
1.53e-44 |
|
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: 167.68 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 643 NLPGEDntYIY-QPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAaglptgVFtylPAK 721
Cdd:cd07136 89 NFPSKS--YIYyEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEE------TF---DEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 722 -------GSTVGSHLVKHPDVHlIAFTGSQQVGcQIVTEASilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVmn 794
Cdd:cd07136 158 yvavvegGVEENQELLDQKFDY-IFFTGSVRVG-KIVMEAA-----AKHLTPVTLELGGKSPCIVDEDANLKLAAKRI-- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 795 sAFG-F--AGQKCSACSRAIVLAPVYDNFMERLVEATRSLKvGEAHLPDTKFSAVIDGSAQQNILNYIAKGKetatLAFE 871
Cdd:cd07136 229 -VWGkFlnAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFY-GEDPLESPDYGRIINEKHFDRLAGLLDNGK----IVFG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 872 GEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNL 951
Cdd:cd07136 303 GNTDRETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGG 382
|
330 340
....*....|....*....|....*.
gi 1320983422 952 YINRGITGALVDRHPFGGFKLSGIGS 977
Cdd:cd07136 383 CINDTIMHLANPYLPFGGVGNSGMGS 408
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
561-933 |
3.16e-40 |
|
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: 155.01 E-value: 3.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 561 EAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGDGEVSEAIDFCRYYAKEME------ 634
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRegswld 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 635 -RLESG-VQRN-LPGEDNTYIYQPRGVVVVISPWNFPFA--IALGMSVAAIAAGNTVILK--PA--EQSSVIGAKIAEVL 705
Cdd:cd07129 82 aRIDPAdPDRQpLPRPDLRRMLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAhpGTSELVARAIRAAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 706 QAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQQVGCQIVTEASiLRPkqkHMKRVIAEMGGKN------GIII 779
Cdd:cd07129 162 RATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAA-ARP---EPIPFYAELGSVNpvfilpGALA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 780 DESADLDQAVVGVMnsAFGfAGQKCSACSRAIVLA-PVYDNFMERLVEATRslkvgeAHLPDTKFSAVIDGSAQQNILNy 858
Cdd:cd07129 238 ERGEAIAQGFVGSL--TLG-AGQFCTNPGLVLVPAgPAGDAFIAALAEALA------AAPAQTMLTPGIAEAYRQGVEA- 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1320983422 859 iAKGKETATLAFEGEVPNHGFYVPPTIFGdVDPDSVIA----QEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYS 933
Cdd:cd07129 308 -LAAAPGVRVLAGGAAAEGGNQAAPTLFK-VDAAAFLAdpalQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHG 384
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
560-980 |
1.30e-38 |
|
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: 149.87 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 560 AEAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREG-DGEVSEAIDFCRYYAKEMERLES 638
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 639 GVQRNLP-------GEdntYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQaaglp 711
Cdd:cd07137 81 PEKVKTPlttfpakAE---IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 712 tgvfTYLPAK-------GSTVGSHLVKHP-DVhlIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESA 783
Cdd:cd07137 153 ----EYLDTKaikviegGVPETTALLEQKwDK--IFFTGSPRVGRIIMAAAA------KHLTPVTLELGGKCPVIVDSTV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 784 DLDQAVVGVMNSAFGF-AGQKCsacsraivLAPVY----DNFMERLVEATRS-LK--VGEAHLPDTKFSAVIDGSAQQNI 855
Cdd:cd07137 221 DLKVAVRRIAGGKWGCnNGQAC--------IAPDYvlveESFAPTLIDALKNtLEkfFGENPKESKDLSRIVNSHHFQRL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 856 LNYIAKGKETATLAFEGEVPNHGFYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRT 935
Cdd:cd07137 293 SRLLDDPSVADKIVHGGERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKN 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1320983422 936 PSHIERAYREFEVGNLYINRGITGALVDRHPFGGFKLSGIGSKAG 980
Cdd:cd07137 373 KELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFGAYHG 417
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
561-994 |
5.87e-36 |
|
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: 142.38 E-value: 5.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 561 EAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREgdgevseAIDFC------RYYAKEme 634
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMF-------AENICgdqvqlRARAFV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 635 rLESGVQRNLPGE--------DNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQ 706
Cdd:cd07084 73 -IYSYRIPHEPGNhlgqglkqQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 707 AAG-LPTGVFTYLPAKGSTvGSHLVKHPDVHLIAFTGSQQVGcqivtEASILRPKQkhmKRVIAEMGGKNGIIIDESADL 785
Cdd:cd07084 152 YAGlLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA-----EKLALDAKQ---ARIYLELAGFNWKVLGPDAQA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 786 DQAVV-GVMNSAFGFAGQKCSACSRAIVLA-----PVYDNFMERLveATRSLKvgeahlpDTKFSAVIDGSAQQNILNyi 859
Cdd:cd07084 223 VDYVAwQCVQDMTACSGQKCTAQSMLFVPEnwsktPLVEKLKALL--ARRKLE-------DLLLGPVQTFTTLAMIAH-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 860 AKGKETATLAFEG-EVPNH------GFYVPPTIFGDVDPD---SVIAQEEIFGPVLAVIKAQSFDEALAIANGTNF--AL 927
Cdd:cd07084 292 MENLLGSVLLFSGkELKNHsipsiyGACVASALFVPIDEIlktYELVTEEIFGPFAIVVEYKKDQLALVLELLERMhgSL 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1320983422 928 TGGLYSRTPSHIERAYREFEV-GNLY-INRGITGALVDRHPFGGFKLSGIGSKAGGRDYLLQFLEPRSI 994
Cdd:cd07084 372 TAAIYSNDPIFLQELIGNLWVaGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
654-976 |
5.91e-32 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 131.00 E-value: 5.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 654 QPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQaaglptgvfTYLPAK-------GSTVG 726
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIP---------KYLDSKavkviegGPAVG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 727 SHLVKHP-DVhlIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIID---ESADLDQAVVGVMNSAFGF-AG 801
Cdd:PLN02203 178 EQLLQHKwDK--IFFTGSPRVGRIIMTAAA------KHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 802 QKCSACSRAIvlapVYDNFMERLVEATRS-LK--VGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVPNHG 878
Cdd:PLN02203 250 QACIAIDYVL----VEERFAPILIELLKStIKkfFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 879 FYVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGIT 958
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAII 405
|
330
....*....|....*...
gi 1320983422 959 GALVDRHPFGGFKLSGIG 976
Cdd:PLN02203 406 QYACDSLPFGGVGESGFG 423
|
|
| PutA_N |
pfam18083 |
Proline utilization A N-terminal domain; This domain is found in Proline utilization A (PutA) ... |
22-116 |
2.11e-29 |
|
Proline utilization A N-terminal domain; This domain is found in Proline utilization A (PutA) proteins present in Geobacter sulfurreducens. PutA are bifunctional peripheral membrane flavoenzymes that catalyze the oxidation of l-proline to l-glutamate and couple the oxidation of imported proline imported to the reduction of membrane-associated quinones. This domain is located at the N-terminus and is referred to as the alpha domain. The hydrocarbon tail of Zwittergent 3-12 binds to an exposed hydrophobic patch of the alpha domain which contains aromatic and nonpolar residues. The domain may be involved in membrane association.
Pssm-ID: 436258 Cd Length: 113 Bit Score: 113.22 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 22 EAKTQEIAKKILSGneKSSFWSKLsqiKDELRLDDKLMAWTMENEGLRVQLFRLIDCLPALQSKAEIARHMQEYLASDAV 101
Cdd:pfam18083 1 EARTQRIGRELFAA--LSGERPSL---FDRRWWDDKLMEWAMKDEQLKVQLFRFVDVLPALKTPAEVARHLREYLGDVQD 75
|
90
....*....|....*
gi 1320983422 102 EVPALRALLNFSTDN 116
Cdd:pfam18083 76 ELPQPLRWALRAADG 90
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
652-980 |
1.99e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 111.29 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 652 IYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTylpAKGSTVGSHLVK 731
Cdd:PLN02174 109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRV---VEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 732 HPDVHLIAFTGSQQVGCQIVTEASilrpkqKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFGF-AGQKCSACSRA 810
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAA------KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGCnNGQACISPDYI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 811 IV---LAPVYDNFMERLVEATrslkVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGEVPNHGFYVPPTIFG 887
Cdd:PLN02174 260 LTtkeYAPKVIDAMKKELETF----YGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 888 DVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERAYREFEVGNLYINRGITGALVDRHPF 967
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPF 415
|
330
....*....|...
gi 1320983422 968 GGFKLSGIGSKAG 980
Cdd:PLN02174 416 GGVGESGMGAYHG 428
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
526-941 |
1.97e-24 |
|
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: 108.51 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVETETYIESVNPANSSQVVGKIGLANIDQAeAAVQVA--KNAFSLwKKLSAKERGDMLRKAADIMEEKREELIAw 603
Cdd:cd07128 5 VAGQWHAGTGDGRTLHDAVTGEVVARVSSEGLDFA-AAVAYAreKGGPAL-RALTFHERAAMLKALAKYLMERKEDLYA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 604 icweVAkpIREGDGEVSEAID--------FcrYYAKeMERLESGVQRNLP-------GEDNTY----IYQPR-GVVVVIS 663
Cdd:cd07128 82 ----LS--AATGATRRDSWIDidggigtlF--AYAS-LGRRELPNAHFLVegdveplSKDGTFvgqhILTPRrGVAVHIN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 664 PWNFP-------FAIALgmsvaaiAAGNTVILKPAEQSS-VIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGSHLvKHPDV 735
Cdd:cd07128 153 AFNFPvwgmlekFAPAL-------LAGVPVIVKPATATAyLTEAVVKDIVESGLLPEGALQLICGSVGDLLDHL-GEQDV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 736 hlIAFTGSQQVGCQIVTEASILRpkqkHMKRVIAEMGGKNGIIIDESA-----DLDQAVVGVMNSAFGFAGQKCSACSRA 810
Cdd:cd07128 225 --VAFTGSAATAAKLRAHPNIVA----RSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 811 IVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAF--------EGEVPNHGFYVP 882
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFggpdrfevVGADAEKGAFFP 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1320983422 883 PTIFGDVDPDSVIA--QEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIER 941
Cdd:cd07128 379 PTLLLCDDPDAATAvhDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
557-941 |
2.48e-23 |
|
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: 104.27 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 557 IDQAEAAVQVAKNAFSLWkklSAKERGDMLRKAADIMEEKREELIAWICWEVAKPIREGdgEVSEAIDFCRY-YAKEMER 635
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCK---SQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVED--KVIKNHFAAEYiYNVYKDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 636 LESGVqrnLPGEDN---TYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKP---AEQSSVIGAKIaeVLQA-- 707
Cdd:cd07081 76 KTCGV---LTGDENggtLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKVTQRAATL--LLQAav 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 708 -AGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGSQqvgcqivteaSILRPKQKHMKRVIAEMGGKNGIIIDESADLD 786
Cdd:cd07081 151 aAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATGGP----------AVVKAAYSSGKPAIGVGAGNTPVVIDETADIK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 787 QAVVGVMNSAFGFAGQKCSACSRAIVLAPVYDNFMER-------LVEATRSLKVGEAHLPDTKFSAVIDGSAQQNIlnyi 859
Cdd:cd07081 221 RAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLfegqgayKLTAEELQQVQPVILKNGDVNRDIVGQDAYKI---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 860 akgketATLAfegevpnhGFYVPPT---IFGDVdpdSVIAQEEIFG-----PVLAVIKAQSFDEALAIA----NGTNFAL 927
Cdd:cd07081 297 ------AAAA--------GLKVPQEtriLIGEV---TSLAEHEPFAheklsPVLAMYRAANFADADAKAlalkLEGGCGH 359
|
410
....*....|....
gi 1320983422 928 TGGLYSRTPSHIER 941
Cdd:cd07081 360 TSAMYSDNIKAIEN 373
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
577-942 |
2.68e-22 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.09 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 577 LSAKERGDMLRKAADIMEEKREELIAwICWEVAKPIReGDG--EVSEAIDFCRYYAKEMERLesGVQRNLP-------GE 647
Cdd:PRK11903 60 LTYAQRAALLAAIVKVLQANRDAYYD-IATANSGTTR-NDSavDIDGGIFTLGYYAKLGAAL--GDARLLRdgeavqlGK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 648 DNTYIYQ-----PRGVVVVISPWNFPfaiALGM---SVAAIAAGNTVILKPAEQSSVIGAK-IAEVLQAAGLPTGVFTYL 718
Cdd:PRK11903 136 DPAFQGQhvlvpTRGVALFINAFNFP---AWGLwekAAPALLAGVPVIVKPATATAWLTQRmVKDVVAAGILPAGALSVV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 719 PAKGSTVGSHLvKHPDVhlIAFTGSQQVGCQIVTEASILRpkqkHMKRVIAEMGGKNGIII--DESAD---LDQAVVGVM 793
Cdd:PRK11903 213 CGSSAGLLDHL-QPFDV--VSFTGSAETAAVLRSHPAVVQ----RSVRVNVEADSLNSALLgpDAAPGseaFDLFVKEVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 794 NSAFGFAGQKCSACSRAIVLAPVYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQNILNYIAKGKETATLAFEGE 873
Cdd:PRK11903 286 REMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGG 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320983422 874 V-------PNHGFYVPPTIFGDVDPDSVIA--QEEIFGPVLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIERA 942
Cdd:PRK11903 366 GfalvdadPAVAACVGPTLLGASDPDAATAvhDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAA 443
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
143-446 |
1.74e-21 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 99.01 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 143 GENLSEATKSIEKLRRDRFGFTMDLLGEAVISEVEAGEYLNRYIGMMEDLSNKAKNWG--------------------LI 202
Cdd:PLN02681 91 GEDAEEAARTVRRLWELGLGGILDYAAEDAGDNAACDRNLEKFLAAIRAAATLPPSSSsaavkitalcppsllervsdLL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 203 DQIDKADGEELKRVQVSVKLSAFYSQF-------DPLDP--VKTTEKVSEPARILLRKAQALGCGIHFDMEQYEFK---- 269
Cdd:PLN02681 171 RWQDRDPNGKLPWKQWSFPLFADSSPLyhatsepEPLTAeeERLLELAHERLQKLCERAAQLGVPLLIDAEYTSLQpaid 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 270 --SLTLQIlkqvlmepEF---RDRTDVGITLQGYLRDSEQDLRDLVEWAKLRGKPVTVRLVKGAYWDRETIRSYQQGWSL 344
Cdd:PLN02681 251 yiTYDLAR--------EFnkgKDRPIVYGTYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 345 PVFSDKVSTDANYERLIQILLENYQYLYAAI--GSHNARSLAKAIAIVQNMNIP---SRAFETQcLYGMGDKFAKAIADM 419
Cdd:PLN02681 323 PVHDTIQDTHACYNRCAEFLLEKASNGDGEVmlATHNVESGELAAAKMNELGLHkgdPRVQFAQ-LLGMSDNLSFGLGNA 401
|
330 340 350
....*....|....*....|....*....|
gi 1320983422 420 GYRVRVYCPFG---DLIPgmsYLIRRLLEN 446
Cdd:PLN02681 402 GFRVSKYLPYGpveEVIP---YLLRRAEEN 428
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
648-969 |
4.31e-21 |
|
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: 98.32 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 648 DNTYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKP---AEQSSVIGAKIA-EVLQAAGL-PTGVFTYLPAKG 722
Cdd:cd07127 186 EKTFTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPhpaAILPLAITVQVArEVLAEAGFdPNLVTLAADTPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 723 STVGSHLVKHPDVHLIAFTGSQQVGCQIVTEAsilRPKQkhmkrVIAEMGGKNGIIIDESADLdqavVGVM-NSAFGFA- 800
Cdd:cd07127 266 EPIAQTLATRPEVRIIDFTGSNAFGDWLEANA---RQAQ-----VYTEKAGVNTVVVDSTDDL----KAMLrNLAFSLSl 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 801 --GQKCSACSraIVLAPV-----------YDNFMERLVEATRSLkvgeahLPDTKFSAVIDGSAQ-QNILNYIAKGKETA 866
Cdd:cd07127 334 ysGQMCTTPQ--NIYVPRdgiqtddgrksFDEVAADLAAAIDGL------LADPARAAALLGAIQsPDTLARIAEARQLG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 867 TLAFEGEVPNHGFY------VPPTIFGDVDPDSVIAQEEiFGPVLAVIKAQSFDEALAIANG---TNFALTGGLYSRTPS 937
Cdd:cd07127 406 EVLLASEAVAHPEFpdarvrTPLLLKLDASDEAAYAEER-FGPIAFVVATDSTDHSIELAREsvrEHGAMTVGVYSTDPE 484
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1320983422 938 HIER---AYREFEV-------GNLYINRgiTGALVDRHPFGG 969
Cdd:cd07127 485 VVERvqeAALDAGValsinltGGVFVNQ--SAAFSDFHGTGA 524
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
650-954 |
1.43e-17 |
|
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: 86.39 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 650 TYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKP---AEQSSVIGAKI-AEVLQAAGLPTGVFTYLPAKGSTV 725
Cdd:cd07122 90 VEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 726 GSHLVKHPDVHLIAFTGSQQVgcqiVTEA-SILRPkqkhmkrviAEMGGK-NG-IIIDESADLDQAVVGVMNS-AFGFaG 801
Cdd:cd07122 170 TQELMKHPDVDLILATGGPGM----VKAAySSGKP---------AIGVGPgNVpAYIDETADIKRAVKDIILSkTFDN-G 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 802 QKCSACSRAIVLAPVYDNFMERL-------VEATRSLKVGEAHLPDTKF--SAVIDGSAQQnilnyIAKgketatLAfeg 872
Cdd:cd07122 236 TICASEQSVIVDDEIYDEVRAELkrrgayfLNEEEKEKLEKALFDDGGTlnPDIVGKSAQK-----IAE------LA--- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 873 evpnhGFYVPPTI------FGDVDPDSVIAQEEIFgPVLAVIKAQSFDEALAIANG-TNFA---LTGGLYSRTPSHIERA 942
Cdd:cd07122 302 -----GIEVPEDTkvlvaeETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKARElLEYGgagHTAVIHSNDEEVIEEF 375
|
330
....*....|..
gi 1320983422 943 YREFEVGNLYIN 954
Cdd:cd07122 376 ALRMPVSRILVN 387
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
555-947 |
1.48e-15 |
|
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: 80.36 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 555 ANIDQAEAAvqvAKNAFSLWKKLSAKERgdmlrkaADIMEEKREELIAWICwEVAKPIREGDGevseaidfcryyakeME 634
Cdd:cd07121 4 ATVDDAVAA---AKAAQKQYRKCTLADR-------EKIIEAIREALLSNAE-ELAEMAVEETG---------------MG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 635 RLESGVQRNL------PGE----------DN---TYIYQPRGVVVVISPWNFPFAIALGMSVAAIAAGNTVILKPAEQSS 695
Cdd:cd07121 58 RVEDKIAKNHlaaektPGTedltttawsgDNgltLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 696 VIGA----KIAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPDVHLIAFTGsqqvGCQIVTEAsilrpkQKHMKRVIAEM 771
Cdd:cd07121 138 KVSAyaveLINKAIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAA------LSSGKKAIGAG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 772 GGKNGIIIDESADLDQAVVGVMNSAfGFAGQ-KCSACSRAIVLAPVYDNFMERLVeatrslKVGEAHLPDTKFSAVIDGS 850
Cdd:cd07121 208 AGNPPVVVDETADIEKAARDIVQGA-SFDNNlPCIAEKEVIAVDSVADYLIAAMQ------RNGAYVLNDEQAEQLLEVV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 851 AQQNILNYIAK---GKETATLAFEGEVPNHGfyVPPTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEA--LAIANGTNF 925
Cdd:cd07121 281 LLTNKGATPNKkwvGKDASKILKAAGIEVPA--DIRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAieLAVELEHGN 358
|
410 420
....*....|....*....|..
gi 1320983422 926 ALTGGLYSRTPSHIERAYREFE 947
Cdd:cd07121 359 RHTAIIHSKNVENLTKMARAMQ 380
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
526-945 |
5.49e-15 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 78.79 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 526 INGQAVET---ETYIESVNPANSSQVVGKIGLANIDQAEAAVQVAKNAFSLWKKLSAKERgdmlRKAADIMeekREELIA 602
Cdd:PRK15398 1 MNQQDIEQvvkAVLAEMLSSQTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYQQKSLAMR----QRIIDAI---REALLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 603 WICwEVAKPIREGDGevseaidfcryyakeMERLESGVQRNL------PG-EDNT------------YIYQPRGVVVVIS 663
Cdd:PRK15398 74 HAE-ELAELAVEETG---------------MGRVEDKIAKNVaaaektPGvEDLTtealtgdngltlIEYAPFGVIGAVT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 664 PWNFPFAIALGMSVAAIAAGNTVILKP---AEQSSVIG-AKIAEVLQAAGLPTGVFTYL--PAKGSTvgSHLVKHPDVHL 737
Cdd:PRK15398 138 PSTNPTETIINNAISMLAAGNSVVFSPhpgAKKVSLRAiELLNEAIVAAGGPENLVVTVaePTIETA--QRLMKHPGIAL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 738 IAFTGsqqvGCQIVTEAsilrpkQKHMKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAfGFAGQ-KCSACSRAIVLAPV 816
Cdd:PRK15398 216 LVVTG----GPAVVKAA------MKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGA-SFDNNlPCIAEKEVIVVDSV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 817 YDNFMERL------------VEATRSLKVGEAHLPDTKFSavidgsaqqnilnyiakGKETATLAFE--GEVPNHgfyvP 882
Cdd:PRK15398 285 ADELMRLMekngavlltaeqAEKLQKVVLKNGGTVNKKWV-----------------GKDAAKILEAagINVPKD----T 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1320983422 883 PTIFGDVDPDSVIAQEEIFGPVLAVIKAQSFDEALAIA----NGtnFALTGGLYSRTPSHIERAYRE 945
Cdd:PRK15398 344 RLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAvkleHG--NRHTAIMHSRNVDNLNKMARA 408
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
525-941 |
1.56e-14 |
|
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: 77.54 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 525 IINGQAVETETYIESVNPANSSQVvgkIGLANIDQAE------AAVQVAKNAfsLWKKLSAKER----GDMLRKAADIME 594
Cdd:cd07126 2 LVAGKWKGASNYTTLLDPLNGDKF---ISVPDTDEDEinefvdSLRQCPKSG--LHNPLKNPERyllyGDVSHRVAHELR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 595 E-KREELIAWICWEVA-KPIREGDGEV--------SEAIDFCRYYAKEMErlesgVQRNLPGEDNTYIYQPRGVVVVISP 664
Cdd:cd07126 77 KpEVEDFFARLIQRVApKSDAQALGEVvvtrkfleNFAGDQVRFLARSFN-----VPGDHQGQQSSGYRWPYGPVAIITP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 665 WNFPFAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAAGLPTGVFTYLPAKGSTVGShLVKHPDVHLIAFTGSQ 744
Cdd:cd07126 152 FNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK-ILLEANPRMTLFTGSS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 745 QVGcqivteasilrpkqkhmKRVIAEMGGKNGIiidESADLDQAVVG--VMN----------SAFGFAGQKCSACSraIV 812
Cdd:cd07126 231 KVA-----------------ERLALELHGKVKL---EDAGFDWKILGpdVSDvdyvawqcdqDAYACSGQKCSAQS--IL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 813 LApvYDNFMERLVEATRSLKVGEAHLPDTKFSAVIDGSAQQnILNYIAK--GKETATLAFEG-EVPNHGFyvpPTIFGDV 889
Cdd:cd07126 289 FA--HENWVQAGILDKLKALAEQRKLEDLTIGPVLTWTTER-ILDHVDKllAIPGAKVLFGGkPLTNHSI---PSIYGAY 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320983422 890 DPDSV--------------IAQEEIFGP--VLAVIKAQSFDEALAIANGTNFALTGGLYSRTPSHIER 941
Cdd:cd07126 363 EPTAVfvpleeiaieenfeLVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQE 430
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
647-824 |
2.47e-13 |
|
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: 73.03 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 647 EDNTYIYQ---PRGVVVVISPWNFPfAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAA---GLPTGVFTYLPA 720
Cdd:cd07077 89 PDNGETYVrafPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 721 KGSTVGSHLVKHPDVHLIAFTGSQQVgcqivteasiLRPKQKH--MKRVIAEMGGKNGIIIDESADLDQAVVGVMNSAFg 798
Cdd:cd07077 168 PSDELAEELLSHPKIDLIVATGGRDA----------VDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF- 236
|
170 180
....*....|....*....|....*.
gi 1320983422 799 FAGQKCSACSRAIVLAPVYDNFMERL 824
Cdd:cd07077 237 FDQNACASEQNLYVVDDVLDPLYEEF 262
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
561-807 |
1.52e-06 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 51.67 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 561 EAAVQVAKNAFSLWKKLSAKERGDMLRKAADIMEEKREELIAwicwEVAKPIREG-DGEVSEA-IDfcRYYAKEmERLES 638
Cdd:cd07079 1 EELAKRAKAASRALATLSTEQKNAALLAIADALEANRDEILE----ANAKDLAAArEAGLSEAlLD--RLLLTP-ERIEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 639 ---GVQR--NLP---GE--DNTY------IYQ---PRGVVVVIspwnfpF---------AIALgmsvaAIAAGNTVILKP 690
Cdd:cd07079 74 maeGLRQvaALPdpvGEvlRGWTlpnglqIEKvrvPLGVIGII------YesrpnvtvdAAAL-----CLKSGNAVILRG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 691 ---AEQSSVIGAK-IAEVLQAAGLPTGVFTYLPAKGSTVGSHLVKHPD-VHLIAFTGSQQVGCQIVTEASIlrPkqkhmk 765
Cdd:cd07079 143 gseALHSNRALVEiIQEALEEAGLPEDAVQLIPDTDREAVQELLKLDDyIDLIIPRGGAGLIRFVVENATI--P------ 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1320983422 766 rVIAEMGGKNGIIIDESADLDQAVVGVMNSafgfagqKC---SAC 807
Cdd:cd07079 215 -VIKHGDGNCHVYVDESADLEMAVRIVVNA-------KTqrpSVC 251
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
677-833 |
2.50e-04 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 44.67 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 677 VAAIA--AGNTVILKP---AEQSS-VIGAKIAEVLQAAGLPTGVFTYLPAKG-STVGS--HLVKHPDV-------HLIAF 740
Cdd:PRK00197 133 AAALClkSGNAVILRGgseAIHSNrALVAVIQEALEEAGLPADAVQLVETTDrAAVGEllKLDGYVDViiprggaGLIRR 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320983422 741 tgsqqvgcqIVTEASIlrPkqkhmkrVIAEMGGKNGIIIDESADLDQAVVGVMNSAFgfagQKCSACSRA---IVLAPVY 817
Cdd:PRK00197 213 ---------VVENATV--P-------VIEHGDGICHIYVDESADLDKALKIVLNAKT----QRPSVCNALetlLVHEAIA 270
|
170
....*....|....*.
gi 1320983422 818 DNFMERLVEATRSLKV 833
Cdd:PRK00197 271 EEFLPKLAEALAEAGV 286
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
641-708 |
8.32e-04 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 43.39 E-value: 8.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1320983422 641 QRNLP---GEDNTYIYQPRGVVVVISPWNfpfAIALGMSVAAIAAGNTVILKPAEQSSVIGAKIAEVLQAA 708
Cdd:COG4230 1045 ALTLPgptGERNTLTLRPRGRVLCLADSL---EALLAQLAAALATGNRAVVAADLALAGLPAVLLPPFDAV 1112
|
|
| |
