|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
423-946 |
0e+00 |
|
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: 601.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 423 SSENFMSAVFELADNealfereklrflasLENLDTAVPAPHRVQDRNLPAV-AAATDSFDNTPDSDPSLPANQawgrgiL 501
Cdd:cd07125 1 ANSSFVNRIFDLEVP--------------LEALADALKAFDEKEWEAIPIInGEETETGEGAPVIDPADHERT------I 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 502 ARVpgselgkaavaaaAVSNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSD 581
Cdd:cd07125 61 GEV-------------SLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 582 PEVSEAIDFAHYYAELARELDT----------VEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSA 651
Cdd:cd07125 128 AEVREAIDFCRYYAAQARELFSdpelpgptgeLNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 652 RSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFR-----PDLPLLAETSGKNTVI 726
Cdd:cd07125 208 LIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALaerdgPILPLIAETGGKNAMI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 727 VTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLR 806
Cdd:cd07125 288 VDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIA--ERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 807 GLTELGEGETWLLKPEQLDES-GRLWSPGIRTGVrrGSEYHLTEYFGPILGVMTAA--TLEEAIDMANDIDYGLTAGLHS 883
Cdd:cd07125 366 AHTELMRGEAWLIAPAPLDDGnGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHS 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2304522532 884 LEPAEMDVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSAVGAgtKAGGPNYLIGLGNWEAV 946
Cdd:cd07125 444 RDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP--KAGGPNYLLRFGNEKTV 504
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
13-982 |
1.89e-157 |
|
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: 494.57 E-value: 1.89e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 13 AAPSAELAEQSVALVRRWLTEAAAVPVDASAAQLAGVLKDPDGLGFTVGFVDGVVRPEDIRVAARNLAALAPRVPGFLPW 92
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFLVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 93 YMRAAVRAGgILGPVVPQVVIPAARKVLREMVGHLIVDATDAKLGKAIAGIRKDNTRLNMNLLGEAVLGQHEAARRLEGT 172
Cdd:COG0506 83 ASTWGLMLT-LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 173 HALLARD-----DVDYVSIKVSSTVAPHSPWAFNEAVQHVIDSLTPLFRRAAQspVKKFINLDMEEYKDLEMTMAVFTGI 247
Cdd:COG0506 162 LEALEAIgaagvDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAARE--AGIFVTIDMEEYDRLDLTLDVFERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 248 LSQPEFKD-LEAGIVLQAYLPDALSAMVRLQEFAAARRADggaaIKVRVVKGANLPMEQVEASLHGWPLATWHTKADSDT 326
Cdd:COG0506 240 LADPELAGwPGVGIVLQAYLKRAEADLDRLAALARRGGRR----IRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 327 NYKRVINYALhpDRIKNVRIGVAGHNLFDVAFAWLLAGERGV-RDGIEFEMLLGMAAGQAE-VVRRDVGSLLLYTPVVHP 404
Cdd:COG0506 316 NYLRCARKLL--EAGDAIYPQFATHNARTIAAALALAGERGRpPDRFEFQMLYGMGEDLQRaLAAVDGGRLLLYCPVVAP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 405 AEFDVAIAYLIRRLEEGASSENFMSAVFELADNEALFEREKLRFLASLENLDTAVPAPHRVQDRNLPAVAAATDSFDNTP 484
Cdd:COG0506 394 VGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 485 DSDPSLPANQAWGRGILARVPGSELGKAAVAAAAVSNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRAD 564
Cdd:COG0506 474 AAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 565 LMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDTVEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVI 644
Cdd:COG0506 554 AAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAA 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 645 KPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLAETSGKNT 724
Cdd:COG0506 634 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 725 VIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVARSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKL 804
Cdd:COG0506 714 AAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDADLVILLLALAAA 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 805 LRGLTELGEGETWLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSL 884
Cdd:COG0506 794 AAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLAL 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 885 EPAEMDVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSAVGAGTKAGGPNYLIGLGNWEAVNGTSEAAVELPAAAPAAR 964
Cdd:COG0506 874 VLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAG 953
|
970
....*....|....*...
gi 2304522532 965 LVAAAESAGSVFTADDAA 982
Cdd:COG0506 954 TLALAAAAAAATALAAAA 971
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
520-937 |
7.02e-122 |
|
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: 384.09 E-value: 7.02e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:COG1012 40 ATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 EL--DTVEGA--------RFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRD 669
Cdd:COG1012 120 RLygETIPSDapgtrayvRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPD--LPLLAETSGKNTVIVTPSADFDLAARDVAASAFGH 747
Cdd:COG1012 200 VLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEnlKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 748 AGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLD 825
Cdd:COG1012 280 AGQRCTAASRLLVHESIY--DEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAvaEGAELLTGGRRPD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 826 -ESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVN 904
Cdd:COG1012 358 gEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWIN 437
|
410 420 430
....*....|....*....|....*....|...
gi 2304522532 905 RGITGAIVrRQPFGGWKKSAVGagtKAGGPNYL 937
Cdd:COG1012 438 DGTTGAVP-QAPFGGVKQSGIG---REGGREGL 466
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
522-937 |
1.77e-114 |
|
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: 365.39 E-value: 1.77e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL 601
Cdd:cd07124 68 KEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 D--TVEGA-------RFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQ 672
Cdd:cd07124 148 RgfPVEMVpgednryVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 673 LVQLGEKELGRQLISHPAVDRVILTGGYETA----ELFRSFRPDL----PLLAETSGKNTVIVTPSADFDLAARDVAASA 744
Cdd:cd07124 228 FLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlriyERAAKVQPGQkwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 745 FGHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELGEGETWLL---KP 821
Cdd:cd07124 308 FGFQGQKCSACSRVIVHESV--YDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLlggEV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 822 EQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNL 901
Cdd:cd07124 386 LELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNL 465
|
410 420 430
....*....|....*....|....*....|....*.
gi 2304522532 902 YVNRGITGAIVRRQPFGGWKKSavGAGTKAGGPNYL 937
Cdd:cd07124 466 YANRKITGALVGRQPFGGFKMS--GTGSKAGGPDYL 499
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
520-937 |
7.91e-109 |
|
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: 348.37 E-value: 7.91e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:pfam00171 26 ATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELD--TVEGArfvPARLTVVT--P--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVP 667
Cdd:pfam00171 106 RLDgeTLPSD---PGRLAYTRrePlgvvgaitPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 668 RDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELF--RSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAF 745
Cdd:pfam00171 183 AGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIaeAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 746 GHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQ 823
Cdd:pfam00171 263 GNAGQVCTATSRLLVHESIY--DEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAkeEGAKLLTGGEA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 824 LDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYV 903
Cdd:pfam00171 341 GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWI 420
|
410 420 430
....*....|....*....|....*....|....
gi 2304522532 904 NRGITGAIVRRqPFGGWKKSAVGagtKAGGPNYL 937
Cdd:pfam00171 421 NDYTTGDADGL-PFGGFKQSGFG---REGGPYGL 450
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
106-938 |
4.28e-96 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 330.24 E-value: 4.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 106 PVVPQvvipAARKVLREMVGHLIVDAT-DAKLGKAIAGiRKDNTRLNMNLLGEAVLGQHEAAR-------------RLEG 171
Cdd:PRK11904 163 PVIRK----AMRQAMKIMGKQFVLGRTiEEALKRARSA-RNKGYRYSFDMLGEAALTAADAERyfkayaraieaigRAAG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 172 THALLARDDVdyvSIKVSstvAPHSPWafnEAVQH--VIDSLTPLFRRAAQSPVKKFINL--DMEEYKDLEMTMAVFTGI 247
Cdd:PRK11904 238 GADLPARPGI---SIKLS---ALHPRY---EAAQRerVLAELVPRVLELARLAKEANIGLtiDAEEADRLELSLDLFEAL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 248 LSQPEFKDLEA-GIVLQAYLPDALSAMVRLQEfaaaRRADGGAAIKVRVVKGA----NLPMEQvEASLHGWPLATwhTKA 322
Cdd:PRK11904 309 FRDPSLKGWGGfGLAVQAYQKRALPVLDWLAD----LARRQGRRIPVRLVKGAywdsEIKRAQ-ELGLPGYPVFT--RKA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 323 DSDTNYKRVINYAL-HPDRIKNVrigVAGHNLFDVAFAWLLAGERGvrdgIEFEMLLGMaaGQA---EVVRRDVGSLLLY 398
Cdd:PRK11904 382 ATDVSYLACARKLLsARGAIYPQ---FATHNAHTVAAILEMAGHRG----FEFQRLHGM--GEAlydALLDAPGIPCRIY 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 399 TPV-VHPaefDVaIAYLIRRL-EEGASSenfmSAVFELADN----EALFER--EKLRFLASLENLDTAVPA----PHRV- 465
Cdd:PRK11904 453 APVgSHK---DL-LPYLVRRLlENGANS----SFVHRLVDPdvpiEELVADpvEKLRSFETLPNPKIPLPRdifgPERKn 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 466 -------QDRNLPAVAAATDSFDNTPDSDPSLPANQAWGRGILARVPGSE-LGKAAVaaaavSNEAELDAVINTAVTKSK 537
Cdd:PRK11904 525 skglnlnDRSELEPLAAAIAAFLEKQWQAGPIINGEGEARPVVSPADRRRvVGEVAF-----ADAEQVEQALAAARAAFP 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 538 AWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDTveGARFVP------ 611
Cdd:PRK11904 600 AWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFG--APEKLPgptges 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 612 ------ARLTVVT-PPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQ 684
Cdd:PRK11904 678 nelrlhGRGVFVCiSPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAA 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 685 LISHPAVDRVILTGGYETAELF-RSF----RPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVI 759
Cdd:PRK11904 758 LTADPRIAGVAFTGSTETARIInRTLaardGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLF 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 760 LVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELGEGETWLLKPEQLDES---GRLWSPgir 836
Cdd:PRK11904 838 VQEDIA--DRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGtenGHFVAP--- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 837 TGVRRGSEYHLT-EYFGPILGVMT--AATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVR 913
Cdd:PRK11904 913 TAFEIDSISQLErEVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVG 992
|
890 900
....*....|....*....|....*
gi 2304522532 914 RQPFGGWKKSavGAGTKAGGPNYLI 938
Cdd:PRK11904 993 VQPFGGQGLS--GTGPKAGGPHYLL 1015
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
521-938 |
6.76e-93 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 307.25 E-value: 6.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARE 600
Cdd:PRK03137 71 TKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 LD------TVEGAR----FVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDV 670
Cdd:PRK03137 151 LAdgkpveSRPGEHnryfYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 671 LQLVQLGEKELGRQLISHPAVDRVILTGG-------YETAE--------LFRsfrpdlpLLAETSGKNTVIVTPSADFDL 735
Cdd:PRK03137 231 VNFVPGSGSEVGDYLVDHPKTRFITFTGSrevglriYERAAkvqpgqiwLKR-------VIAEMGGKDAIVVDEDADLDL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 736 AARDVAASAFGHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPtTQMGPVIEPAAGKLLRGLTELGEGE 815
Cdd:PRK03137 304 AAESIVASAFGFSGQKCSACSRAIVHEDV--YDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEE 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 816 TWL-LKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLN 894
Cdd:PRK03137 381 GRLvLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARR 460
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2304522532 895 RISAGNLYVNRGITGAIVRRQPFGGWKKSavGAGTKAGGPNYLI 938
Cdd:PRK03137 461 EFHVGNLYFNRGCTGAIVGYHPFGGFNMS--GTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
526-937 |
2.53e-92 |
|
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: 305.64 E-value: 2.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 526 DAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELD--- 602
Cdd:TIGR01237 72 EHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAkgk 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 603 ---TVEGAR----FVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQ 675
Cdd:TIGR01237 152 pvnSREGETnqyvYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 676 LGEKELGRQLISHPAVDRVILTGG-------YETAELFRSFRPDLP-LLAETSGKNTVIVTPSADFDLAARDVAASAFGH 747
Cdd:TIGR01237 232 GSGSEVGDYLVDHPKTSLITFTGSrevgtriFERAAKVQPGQKHLKrVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 748 AGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELGEGETWLLKPEQLDES 827
Cdd:TIGR01237 312 AGQKCSAGSRAVVHEKV--YDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 828 -GRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRG 906
Cdd:TIGR01237 390 kGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRN 469
|
410 420 430
....*....|....*....|....*....|.
gi 2304522532 907 ITGAIVRRQPFGGWKKSavGAGTKAGGPNYL 937
Cdd:TIGR01237 470 ITGAIVGYQPFGGFKMS--GTDSKAGGPDYL 498
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
526-937 |
1.99e-91 |
|
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: 300.66 E-value: 1.99e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 526 DAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDTVE 605
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 606 GARFVPARLTVVTP----------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQ 675
Cdd:cd07078 81 IPSPDPGELAIVRReplgvvgaitPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 676 LGEKELGRQLISHPAVDRVILTGGYETAE-LFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCS 753
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKaIMRAAAENLkRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 754 AASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVI-EPAAGKLLRGLTELGEGETWLLK--PEQLDESGRL 830
Cdd:cd07078 241 AASRLLVHESIY--DEFVERLVERVKALKVGNPLDPDTDMGPLIsAAQLDRVLAYIEDAKAEGAKLLCggKRLEGGKGYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 831 WSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGA 910
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA 398
|
410 420
....*....|....*....|....*..
gi 2304522532 911 IVrRQPFGGWKKSAVGagtKAGGPNYL 937
Cdd:cd07078 399 EP-SAPFGGVKQSGIG---REGGPYGL 421
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
155-1138 |
2.27e-86 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 305.25 E-value: 2.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 155 LGEAVLGQHEAAR-RLEGTHALLA-------RD--DVDYVSIKVSstvAPHSPWAFneaVQH--VIDSLTP----LFRRA 218
Cdd:PRK11905 207 LGEAARTAADAERyYRDYERAIHAigkaatgRGvyDGPGISVKLS---ALHPRYER---AQRerVMAELLPrlkaLALLA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 219 AQSPVKkfINLDMEEYKDLEMTMAVFTGILSQPEFKDLEA-GIVLQAYLP------DALSAMVRlqefaaarraDGGAAI 291
Cdd:PRK11905 281 KAYDIG--LNIDAEEADRLELSLDLLEALCSDPDLAGWNGiGFVVQAYQKrcpfviDYLIDLAR----------RSGRRL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 292 KVRVVKGANLPME----QVEAsLHGWPLATwhTKADSDTNY----KRVINYalhPDRIKNvriGVAGHNLFDVAFAWLLA 363
Cdd:PRK11905 349 MVRLVKGAYWDAEikraQVDG-LEGFPVFT--RKVHTDVSYiacaRKLLAA---RDVIYP---QFATHNAQTLAAIYELA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 364 GERgvrDGIEFEMLLGMaaGQAevvrrdvgsllLYTPVVHPAEFDVA-------------IAYLIRRL-EEGASSenfmS 429
Cdd:PRK11905 420 GGK---GDFEFQCLHGM--GEP-----------LYDQVVGKEKLGRPcriyapvgthetlLAYLVRRLlENGANS----S 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 430 AVFELADN----EALFER--EKLRFLASLENLDTAVPA----PHRvqdRN-----------LPAVAAATDSFDNTP-DSD 487
Cdd:PRK11905 480 FVNRIVDEnvpvEELIADpvEKVAAMGVAPHPQIPLPRdlygPER---RNskgldlsdeatLAALDEALNAFAAKTwHAA 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 488 PSLPANQAWGRGILARVPG--SEL-GKAAVaaaavSNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRAD 564
Cdd:PRK11905 557 PLLAGGDVDGGTRPVLNPAdhDDVvGTVTE-----ASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 565 LMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDtvEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVI 644
Cdd:PRK11905 632 LFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLL--NGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 645 KPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRS-----FRPDLPLLAET 719
Cdd:PRK11905 710 KPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRtlakrSGPPVPLIAET 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 720 SGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEP 799
Cdd:PRK11905 790 GGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVA--DRVLTMLKGAMDELRIGDPWRLSTDVGPVIDA 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 800 AAGKLLRGLTELGEGETWLLKPEQLD---ESGRLWSPgirTGVRRGSEYHLT-EYFGPILGVMT--AATLEEAIDMANDI 873
Cdd:PRK11905 868 EAQANIEAHIEAMRAAGRLVHQLPLPaetEKGTFVAP---TLIEIDSISDLErEVFGPVLHVVRfkADELDRVIDDINAT 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 874 DYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSavGAGTKAGGPNYLIGLgnweavngTSEAA 953
Cdd:PRK11905 945 GYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGGPLYLGRL--------VREAP 1014
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 954 VELPAAAPAARLVAAAESAGSVFTADDAAFLRRAANSDARAwnSEFGTAKDVSALSAERNVFRYVPVPVTVRLAEGqpAA 1033
Cdd:PRK11905 1015 TPIPPAHESVDTDAAARDFLAWLDKEGKAALAAAARDARAR--SALGLEQELPGPTGESNLLSLHPRGRVLCVADT--EE 1090
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 1034 RLVRVLAAALTAGSNVSVSAAVDLPAGVR----AVLTELGLEFRVQDDAAWLASAASLTSGRVRLIggsAPALAEATGgt 1109
Cdd:PRK11905 1091 ALLRQLAAALATGNVAVVAADSGLAAALAdlpgLVAARIDWTQDWEADDPFAGALLEGDAERARAV---RQALAARPG-- 1165
|
1050 1060
....*....|....*....|....*....
gi 2304522532 1110 PDIAVyaQPVTESGRLELLPFLHEQAVSI 1138
Cdd:PRK11905 1166 AIVPL--IAAEPTDAYDLARLVEERSVSI 1192
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
474-947 |
2.36e-82 |
|
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: 277.31 E-value: 2.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 474 AAATDSFDNtpdsdpslpANQAWGRGILARVPGSelgkaavaaaavsNEAELDAVINTAVTKSKAWGALSGAERAEVLHR 553
Cdd:cd07131 10 SASGETFDS---------RNPADLEEVVGTFPLS-------------TASDVDAAVEAAREAFPEWRKVPAPRRAEYLFR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 554 AGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL--DTVEG--------ARFVPARLTVVTPPWNF 623
Cdd:cd07131 68 AAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLfgETVPSelpnkdamTRRQPIGVVALITPWNF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 624 PVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETA 703
Cdd:cd07131 148 PVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 704 ELFR--SFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSL 781
Cdd:cd07131 228 ERIGetCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVY--DEFLKRFVERAKRL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 782 KVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLD----ESGRLWSPGIRTGVRRGSEYHLTEYFGPIL 855
Cdd:cd07131 306 RVGDGLDEETDMGPLINEAQLEKVLNYNEIGkeEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 856 GVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVrRQPFGGWKKSavGAGTKAGGPN 935
Cdd:cd07131 386 ALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKS--GNGHREAGTT 462
|
490
....*....|..
gi 2304522532 936 YLIGLGNWEAVN 947
Cdd:cd07131 463 ALDAFTEWKAVY 474
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
95-1061 |
7.05e-81 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 288.37 E-value: 7.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 95 RAAVRAGGILGPVVPQVVIPAARKVLREMVGHLIVDATDAKLGKAIAGIRKDNTRLNMNLLGEAVLGQHEAARRLE---- 170
Cdd:COG4230 148 SLASGLLRLLGRLGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYayaa 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 171 ----GTHALLARDDVDYVSIKVSSTVAPHSPWAFNEAVQHVIDSLTPLFRRAAQSPVKKFINLDMEEYKDLEMTMAVFTG 246
Cdd:COG4230 228 aaaaAIAAAGGGSGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 247 ILSQPEFKDLEAGIVLQAYLPDALS-AMVRLQEFAAARRADGGAAIKVRVVKGANLPMEQVEASLHGWPlaTWHTKADSD 325
Cdd:COG4230 308 LLAALLLDGGLGGGGGVGQAVQAYAkALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYV--VYPVTTRKV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 326 TNYKRVINYALHPDRIknvRIGVAGHNLFDVAFAWLLAGERGVRDGIEFEMLLGMAAGQAEVVRRD-----------VGS 394
Cdd:COG4230 386 LYDAAALALALLLLAA---QPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVGRGklgrpcriyapVGS 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 395 ---LLlytpvvhpaefdvaiAYLIRRL-EEGASSenfmSAVFELADN----EALFER--EKLRFLASLENLDTAVPA--- 461
Cdd:COG4230 463 hedLL---------------AYLVRRLlENGANS----SFVNRIADEdvpvEELIADpvEKARALGGAPHPRIPLPRdly 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 462 -PHRvqdRN-----------LPAVAAATDSFDNTP-DSDPSLPANQAWGRGILARVP---GSELGKAAVaaaavSNEAEL 525
Cdd:COG4230 524 gPER---RNsagldlsdeavLAALSAALAAAAEKQwQAAPLIAGEAASGEARPVRNPadhSDVVGTVVE-----ATAADV 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 526 DAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDtvE 605
Cdd:COG4230 596 EAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLF--A 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 606 GARFVPARLTVVT-PPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVqLGE-KELGR 683
Cdd:COG4230 674 APTVLRGRGVFVCiSPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLL-PGDgETVGA 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 684 QLISHPAVDRVILTGGYETA-----ELFRSFRPDLPLLAETSGKNTVIVTPSAdfdLA---ARDVAASAFGHAGQKCSAA 755
Cdd:COG4230 753 ALVADPRIAGVAFTGSTETArlinrTLAARDGPIVPLIAETGGQNAMIVDSSA---LPeqvVDDVLASAFDSAGQRCSAL 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 756 SLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAA-GKLLRGLtelgegetwllkpEQLDESGRL-WSP 833
Cdd:COG4230 830 RVLCVQEDIA--DRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEArANLEAHI-------------ERMRAEGRLvHQL 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 834 GIRTGVRRG-----------SEYHLT-EYFGPILGVMT--AATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAG 899
Cdd:COG4230 895 PLPEECANGtfvaptlieidSISDLErEVFGPVLHVVRykADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVG 974
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 900 NLYVNRGITGAIVRRQPFGGWKKSavGAGTKAGGPNYLIGLgnweavngtseaavelpaaapaarlvaaaeSAGSVFTAD 979
Cdd:COG4230 975 NVYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGGPHYLLRF------------------------------ATERTVTVN 1022
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 980 DAAFLRRAANSDARAWNSEFGTAKDVSALSAERNVFRYVPvPVTVrLAEGQPAARLVRVLAAALTAGSNVSVSAAV---D 1056
Cdd:COG4230 1023 TTAAGGNASLLALGDWLASLLGALTLPGPTGERNTLTLRP-RGRV-LCLADSLEALLAQLAAALATGNRAVVAADLalaG 1100
|
....*
gi 2304522532 1057 LPAGV 1061
Cdd:COG4230 1101 LPAVL 1105
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
537-937 |
4.30e-73 |
|
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: 247.53 E-value: 4.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 537 KAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDTVEGARFVPARLTV 616
Cdd:cd06534 8 KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 617 VTP----------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLI 686
Cdd:cd06534 88 VRReplgvvgvitPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 687 SHPAVDRVILTGGYETAELFRSFRPDL--PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSV 764
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKAAAENlkPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 765 ARsqrfrnQLVDAVQSLKVgypeDPTTQMgpviepaagkllrgltelgegetwllkpeqldesgRLWspgirtgvrrgse 844
Cdd:cd06534 248 YD------EFVEKLVTVLV----DVDPDM-----------------------------------PIA------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 845 yhLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVrRQPFGGWKKSA 924
Cdd:cd06534 270 --QEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP-EAPFGGVKNSG 346
|
410
....*....|...
gi 2304522532 925 VGagtKAGGPNYL 937
Cdd:cd06534 347 IG---REGGPYGL 356
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
523-927 |
9.21e-73 |
|
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: 250.24 E-value: 9.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL- 601
Cdd:cd07097 37 EDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLs 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 -DTVEGAR---FVPAR---LTVVT--PPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQ 672
Cdd:cd07097 117 gETLPSTRpgvEVETTrepLGVVGliTPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 673 LVQLGEKELGRQLISHPAVDRVILTGGYET-AELFRS-FRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQ 750
Cdd:cd07097 197 LVMGSGSEVGQALVEHPDVDAVSFTGSTAVgRRIAAAaAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 751 KCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLD--E 826
Cdd:cd07097 277 RCTASSRLIVTEGIH--DRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIArsEGAKLVYGGERLKrpD 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 827 SGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRG 906
Cdd:cd07097 355 EGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLP 434
|
410 420
....*....|....*....|..
gi 2304522532 907 ITGaiVRRQ-PFGGWKKSAVGA 927
Cdd:cd07097 435 TAG--VDYHvPFGGRKGSSYGP 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
537-923 |
6.45e-72 |
|
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: 246.41 E-value: 6.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 537 KAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEA---IDFA-HYYAELARELDTvEGArFVPA 612
Cdd:cd07095 14 PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMagkIDISiKAYHERTGERAT-PMA-QGRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 613 RLT-------VVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQlGEKELGRQL 685
Cdd:cd07095 92 VLRhrphgvmAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ-GGRETGEAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 686 ISHPAVDRVILTGGYETAELF-RSF--RPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVG 762
Cdd:cd07095 171 AAHEGIDGLLFTGSAATGLLLhRQFagRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 763 SvARSQRFRNQLVDAVQSLKVGYP-EDPTTQMGPVIEPAAGKLLR-GLTELGEGETWLLKPEQLDESGRLWSPGI--RTG 838
Cdd:cd07095 251 G-AVGDAFLERLVEAAKRLRIGAPdAEPPFMGPLIIAAAAARYLLaQQDLLALGGEPLLAMERLVAGTAFLSPGIidVTD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 839 VrrgSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVRRqPFG 918
Cdd:cd07095 330 A---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGASSTA-PFG 405
|
....*
gi 2304522532 919 GWKKS 923
Cdd:cd07095 406 GVGLS 410
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
138-430 |
1.82e-71 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 240.47 E-value: 1.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 138 KAIAGIRKDNTRLNMNLLGEAVLGQHEAARRLEGTHALLA----------RDDVDYVSIKVSSTVAPHSPWAFNEAVQHV 207
Cdd:pfam01619 3 KTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDalgkaagpwpLGPRPGISVKLSALHPRYEPLERERVMAEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 208 IDSLTPLFRRAAQSPVkkFINLDMEEYKDLEMTMAVFTGILSQPEFKDLE-AGIVLQAYLPDALSAMVRLQEFAAARRAD 286
Cdd:pfam01619 83 LERLRPLCRLAKELGV--RLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 287 ggaaIKVRVVKGANLPMEQVEASLHGWPLATWHTKADSDTNYKRVINYAL-HPDRIknvRIGVAGHNLFDVAFAWLLAGE 365
Cdd:pfam01619 161 ----LGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLLeNHDRI---YPQFATHNARSVAAALALAEE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2304522532 366 RGV-RDGIEFEMLLGMAAGQAEVVRRDVGSLLLYTPVVHPAEFdvaIAYLIRRLEEGASSENFMSA 430
Cdd:pfam01619 234 LGIpPRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEEL---LAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
520-937 |
2.83e-71 |
|
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: 247.11 E-value: 2.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07083 52 ADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAAL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELD-----------TVEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPR 668
Cdd:cd07083 132 RLRypavevvpypgEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 669 DVLQLVQLGEKELGRQLISHPAVDRVILTGGYET--------AELFRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDV 740
Cdd:cd07083 212 GVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETgkkiyeaaARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 741 AASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELGEGETWLLK 820
Cdd:cd07083 292 VVSAFGFQGQKCSAASRLILTQGAY--EPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 821 PEQLDES-GRLWSPGIRTGVRRGSEYHLTEYFGPILGVMT--AATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRIS 897
Cdd:cd07083 370 GGKRLEGeGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRykDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFH 449
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2304522532 898 AGNLYVNRGITGAIVRRQPFGGWKKSavGAGTKAGGPNYL 937
Cdd:cd07083 450 VGNLYINRKITGALVGVQPFGGFKLS--GTNAKTGGPHYL 487
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
520-937 |
4.34e-69 |
|
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: 240.58 E-value: 4.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:TIGR01238 71 ANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELDTVEGARfvPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEK 679
Cdd:TIGR01238 151 DVLGEFSVE--SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 680 ELGRQLISHPAVDRVILTGGYETAELF-----RSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSA 754
Cdd:TIGR01238 229 DVGAALTSDPRIAGVAFTGSTEVAQLInqtlaQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 755 ASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVI-EPAAGKLLRGLTEL-GEGETWLlkpEQLDESGRLWS 832
Cdd:TIGR01238 309 LRVLCVQEDVA--DRVLTMIQGAMQELKVGVPHLLTTDVGPVIdAEAKQNLLAHIEHMsQTQKKIA---QLTLDDSRACQ 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 833 PGI---RTGVRRGSEYHLT-EYFGPILGVM--TAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRG 906
Cdd:TIGR01238 384 HGTfvaPTLFELDDIAELSeEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRN 463
|
410 420 430
....*....|....*....|....*....|.
gi 2304522532 907 ITGAIVRRQPFGGWKKSavGAGTKAGGPNYL 937
Cdd:TIGR01238 464 QVGAVVGVQPFGGQGLS--GTGPKAGGPHYL 492
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
522-937 |
3.05e-67 |
|
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: 234.47 E-value: 3.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR-- 599
Cdd:cd07088 34 AEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARri 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELDTVEGARF--------VPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVL 671
Cdd:cd07088 114 EGEIIPSDRPnenififkVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 672 QLVQLGEKELGRQLISHPAVDRVILTGGYET-AELFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAG 749
Cdd:cd07088 194 NIVTGRGSVVGDALVAHPKVGMISLTGSTEAgQKIMEAAAENItKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 750 QKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLD-E 826
Cdd:cd07088 274 QVCTCAERVYVHEDIY--DEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAveAGATLLTGGKRPEgE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 827 SGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRG 906
Cdd:cd07088 352 KGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRE 431
|
410 420 430
....*....|....*....|....*....|...
gi 2304522532 907 ITGAIvrrQPF-GGWKKSAV-GAGTKAGGPNYL 937
Cdd:cd07088 432 NFEAM---QGFhAGWKKSGLgGADGKHGLEEYL 461
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
521-932 |
7.34e-67 |
|
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: 233.61 E-value: 7.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARE 600
Cdd:cd07086 33 SPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 L--DTVEGAR--------FVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSG----AVMVEALWEAGV 666
Cdd:cd07086 113 LygLTIPSERpghrlmeqWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAiavtKILAEVLEKNGL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 667 PRDVLQLVQlGEKELGRQLISHPAVDRVILTGGYET--------AELFRsfrpdlPLLAETSGKNTVIVTPSADFDLAAR 738
Cdd:cd07086 193 PPGVVNLVT-GGGDGGELLVHDPRVPLVSFTGSTEVgrrvgetvARRFG------RVLLELGGNNAIIVMDDADLDLAVR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 739 DVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAA-GKLLRGLTEL-GEGET 816
Cdd:cd07086 266 AVLFAAVGTAGQRCTTTRRLIVHESVY--DEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAvEKYLNAIEIAkSQGGT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 817 WLLKPEQLD--ESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWL- 893
Cdd:cd07086 344 VLTGGKRIDggEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLg 423
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2304522532 894 -NRISAGNLYVNRGITGAIVrRQPFGGWKKSavGAGTKAG 932
Cdd:cd07086 424 pKGSDCGIVNVNIPTSGAEI-GGAFGGEKET--GGGRESG 460
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
522-1063 |
2.35e-65 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 242.57 E-value: 2.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARel 601
Cdd:PRK11809 681 PAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVR-- 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 DTVEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKEL 681
Cdd:PRK11809 759 DDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETV 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 682 GRQLISHPAVDRVILTGGYETAELF-RSF--------RPdLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKC 752
Cdd:PRK11809 839 GAALVADARVRGVMFTGSTEVARLLqRNLagrldpqgRP-IPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRC 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 753 SAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVI-EPAAGKLLRGL------------TELGEGETW-- 817
Cdd:PRK11809 918 SALRVLCLQDDVA--DRTLKMLRGAMAECRMGNPDRLSTDIGPVIdAEAKANIERHIqamrakgrpvfqAARENSEDWqs 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 818 -------LLKPEQLDESGRlwspgirtgvrrgseyhltEYFGPILGVM--TAATLEEAIDMANDIDYGLTAGLHS-LEPA 887
Cdd:PRK11809 996 gtfvpptLIELDSFDELKR-------------------EVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTrIDET 1056
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 888 EMDVwLNRISAGNLYVNRGITGAIVRRQPFGGWKKSavGAGTKAGGPNYLIGLGNWEAVNGTSEAAVELPAAAPAARLVA 967
Cdd:PRK11809 1057 IAQV-TGSAHVGNLYVNRNMVGAVVGVQPFGGEGLS--GTGPKAGGPLYLYRLLATRPEDALAVTLARQDAEYPVDAQLR 1133
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 968 AAESAGSVFTADDAA--FLRRAANSDARAWNSEFGTAKDVSALSAERNVFRYVPVPVTVRLAegQPAARLVRVLAAALTA 1045
Cdd:PRK11809 1134 AALLAPLTALREWAAerEPELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLA--DTEQDALTQLAAVLAV 1211
|
570 580
....*....|....*....|....*
gi 2304522532 1046 GSNV-----SVSAAV--DLPAGVRA 1063
Cdd:PRK11809 1212 GSQAlwpddALHRALvaALPAAVQA 1236
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
491-926 |
4.86e-64 |
|
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: 224.62 E-value: 4.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 491 PANQAwgrgILARVPgselgkaavaaaaVSNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMA 570
Cdd:cd07103 4 PATGE----VIGEVP-------------DAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 571 AETGKTLDQSDPEVSEAIDFAHYYAELAREL--DTVEgARFVPARLTVVT-P--------PWNFPVAIPAGSTLAALAAG 639
Cdd:cd07103 67 LEQGKPLAEARGEVDYAASFLEWFAEEARRIygRTIP-SPAPGKRILVIKqPvgvvaaitPWNFPAAMITRKIAPALAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 640 SAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAElfrsfrpdlpLLAET 719
Cdd:cd07103 146 CTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGK----------LLMAQ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 720 SG---KNT---------VIVTPSADFDLAARDVAASAFGHAGQKCSAASLVIlvgsVARS--QRFRNQLVDAVQSLKVGY 785
Cdd:cd07103 216 AAdtvKRVslelggnapFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIY----VHESiyDEFVEKLVERVKKLKVGN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 786 PEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATL 863
Cdd:cd07103 292 GLDEGTDMGPLINERAVEKVEALVEdaVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTE 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2304522532 864 EEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVrrQPFGGWKKSAVG 926
Cdd:cd07103 372 DEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLG 432
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
524-934 |
9.91e-63 |
|
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: 220.48 E-value: 9.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 524 ELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELD- 602
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 603 -----TVEG----ARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMV-EALWEAGVPRDVLQ 672
Cdd:cd07104 81 eilpsDVPGkesmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 673 LVQLGEKELGRQLISHPAVDRVILTG----GYETAELF-RSF-RPDLpllaETSGKNTVIVTPSADFDLAARDVAASAFG 746
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGstavGRHIGELAgRHLkKVAL----ELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEP-AAGKLLR--------GLTELGEGEtw 817
Cdd:cd07104 237 HQGQICMAAGRILVHESVY--DEFVEKLVAKAKALPVGDPRDPDTVIGPLINErQVDRVHAivedavaaGARLLTGGT-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 818 llkpeqldESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHS--LEPAeMDVwLNR 895
Cdd:cd07104 313 --------YEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTrdLERA-MAF-AER 382
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2304522532 896 ISAGNLYVNrGIT---GAIVrrqPFGGWKKSAVGagtKAGGP 934
Cdd:cd07104 383 LETGMVHIN-DQTvndEPHV---PFGGVKASGGG---RFGGP 417
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
521-926 |
4.99e-62 |
|
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: 219.75 E-value: 4.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGA-LSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07082 36 SALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELD--TVEGARFVPAR----------LTVV--TPPWNFPVAIPAgSTLA-ALAAGSAVVIKPARQSARSGAVMVEALWEA 664
Cdd:cd07082 116 RLDgdSLPGDWFPGTKgkiaqvrrepLGVVlaIGPFNYPLNLTV-SKLIpALIMGNTVVFKPATQGVLLGIPLAEAFHDA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 665 GVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASA 744
Cdd:cd07082 195 GFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 745 FGHAGQKCSAASLVILVGSVARsqRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPE 822
Cdd:cd07082 275 LSYSGQRCTAIKRVLVHESVAD--ELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDdaVAKGATVLNGGG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 823 QldESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLY 902
Cdd:cd07082 353 R--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVN 430
|
410 420
....*....|....*....|....*...
gi 2304522532 903 VN----RGITgaivrRQPFGGWKKSAVG 926
Cdd:cd07082 431 INskcqRGPD-----HFPFLGRKDSGIG 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
525-926 |
2.51e-60 |
|
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: 213.48 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 525 LDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAE-----LAR 599
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEnaeafLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 E-LDTVEGARFVPAR-LTVV--TPPWNFP------VAIPagstlaALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRD 669
Cdd:cd07100 81 EpIETDAGKAYVRYEpLGVVlgIMPWNFPfwqvfrFAAP------NLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGrQLISHPAVDRVILTGGyETAElfRSfrpdlplLAETSGKN---TV---------IVTPSADFDLAA 737
Cdd:cd07100 155 VFQNLLIDSDQVE-AIIADPRVRGVTLTGS-ERAG--RA-------VAAEAGKNlkkSVlelggsdpfIVLDDADLDKAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 738 RDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPViepAAGKLLRGLTE-----LG 812
Cdd:cd07100 224 KTAVKGRLQNAGQSCIAAKRFIVHEDVY--DEFLEKFVEAMAALKVGDPMDEDTDLGPL---ARKDLRDELHEqveeaVA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 813 EGETWLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVW 892
Cdd:cd07100 299 AGATLLLGGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERV 378
|
410 420 430
....*....|....*....|....*....|....*..
gi 2304522532 893 LNRISAGNLYVNrgitgAIVR---RQPFGGWKKSAVG 926
Cdd:cd07100 379 ARRLEAGMVFIN-----GMVKsdpRLPFGGVKRSGYG 410
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
521-927 |
6.88e-60 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 214.05 E-value: 6.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSE-----AIDFAHYYA 595
Cdd:PRK09457 35 TAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiAISIQAYHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 596 ---ELAREL-DTVEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVL 671
Cdd:PRK09457 115 rtgEKRSEMaDGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 672 QLVQlGEKELGRQLISHPAVDRVILTGGYETAE-LFRSF--RPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHA 748
Cdd:PRK09457 195 NLVQ-GGRETGKALAAHPDIDGLLFTGSANTGYlLHRQFagQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 749 GQKCSAASLvILVGSVARSQRFRNQLVDAVQSLKVGYP-EDPTTQMGPVI-EPAAGKLL---RGLTELGeGETwLLKPEQ 823
Cdd:PRK09457 274 GQRCTCARR-LLVPQGAQGDAFLARLVAVAKRLTVGRWdAEPQPFMGAVIsEQAAQGLVaaqAQLLALG-GKS-LLEMTQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 824 LDESGRLWSPGI--RTGVR-RGSEyhltEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGN 900
Cdd:PRK09457 351 LQAGTGLLTPGIidVTGVAeLPDE----EYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI 426
|
410 420
....*....|....*....|....*..
gi 2304522532 901 LYVNRGITGAiVRRQPFGGwkksaVGA 927
Cdd:PRK09457 427 VNWNKPLTGA-SSAAPFGG-----VGA 447
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
520-926 |
7.72e-60 |
|
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: 212.84 E-value: 7.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07149 18 ASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 EL-------DTVEGA--RF-----VPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAG 665
Cdd:cd07149 98 RLagetipfDASPGGegRIgftirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 666 VPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAF 745
Cdd:cd07149 178 LPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGAF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 746 GHAGQKCSAASLVILVGSVARSqrFRNQLVDAVQSLKVGYPEDPTTQMGPVIEP-AAGKLLRGLTE-LGEGETWLLKPEQ 823
Cdd:cd07149 258 ANAGQVCISVQRIFVHEDIYDE--FLERFVAATKKLVVGDPLDEDTDVGPMISEaEAERIEEWVEEaVEGGARLLTGGKR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 824 ldeSGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGL------HSLEPAEmdvwlnRIS 897
Cdd:cd07149 336 ---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVftndlqKALKAAR------ELE 406
|
410 420
....*....|....*....|....*....
gi 2304522532 898 AGNLYVNrGITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07149 407 VGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
520-926 |
2.50e-59 |
|
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: 211.31 E-value: 2.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07099 15 TDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 EldtVEGARFVPARLTV----------------VTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWE 663
Cdd:cd07099 95 R---VLAPRKVPTGLLMpnkkatveyrpygvvgVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 664 AGVPRDVLQLVQlGEKELGRQLISHPaVDRVILTGGYET--------AELFrsfrpdLPLLAETSGKNTVIVTPSADFDL 735
Cdd:cd07099 172 AGPPQGVLQVVT-GDGATGAALIDAG-VDKVAFTGSVATgrkvmaaaAERL------IPVVLELGGKDPMIVLADADLER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 736 AARDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGE 813
Cdd:cd07099 244 AAAAAVWGAMVNAGQTCISVERVYVHESVY--DEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDdaVAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 814 GETWLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWL 893
Cdd:cd07099 322 GAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIA 401
|
410 420 430
....*....|....*....|....*....|...
gi 2304522532 894 NRISAGNLYVNRGITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07099 402 RRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
520-926 |
4.44e-59 |
|
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: 210.48 E-value: 4.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVT--KSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAEL 597
Cdd:cd07114 16 ASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 598 ArelDTVEGArFVPAR------LTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWE 663
Cdd:cd07114 96 A---DKIEGA-VIPVDkgdylnFTRREPlgvvaaitPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 664 AGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETA-ELFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVA 741
Cdd:cd07114 172 AGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGrHIARAAAENLaPVTLELGGKSPNIVFDDADLDAAVNGVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 742 ASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLL 819
Cdd:cd07114 252 AGIFAAAGQTCVAGSRLLVQRSIY--DEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAreEGARVLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 820 KPEQLDE----SGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGlhslepaemdVWLN- 894
Cdd:cd07114 330 GGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG----------IWTRd 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2304522532 895 ---------RISAGNLYVN--RgitgAIVRRQPFGGWKKSAVG 926
Cdd:cd07114 400 larahrvarAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIG 438
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
500-928 |
1.00e-58 |
|
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: 210.07 E-value: 1.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 500 ILARVPgselgkaavaaaaVSNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQ 579
Cdd:cd07085 28 VIARVP-------------LATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 580 SDPEVS---EAIDFA---------HYYAELARELDTVEgaRFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPA 647
Cdd:cd07085 95 ARGDVLrglEVVEFAcsiphllkgEYLENVARGIDTYS--YRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 648 RQSARSGAVMVEALWEAGVPRDVLQLVQlGEKELGRQLISHPAVDRVILTGGYETAELF--RSFRPDLPLLAETSGKNTV 725
Cdd:cd07085 173 ERVPGAAMRLAELLQEAGLPDGVLNVVH-GGKEAVNALLDHPDIKAVSFVGSTPVGEYIyeRAAANGKRVQALGGAKNHA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 726 IVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLL 805
Cdd:cd07085 252 VVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEA--DEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 806 RGLTELG--EGETWLL-----KPEQLDEsGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLT 878
Cdd:cd07085 330 EGLIESGveEGAKLVLdgrgvKVPGYEN-GNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNG 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2304522532 879 AGLHSLEPAEMDVWLNRISAGNLYVNRGITgAIVRRQPFGGWKKSAVGAG 928
Cdd:cd07085 409 AAIFTRSGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGGWKGSFFGDL 457
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
520-926 |
4.06e-58 |
|
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: 207.80 E-value: 4.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDP-EVSEAIDFAHYYAELA 598
Cdd:cd07093 16 GGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFADYI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 RE-----LDTVEGAR----FVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRD 669
Cdd:cd07093 96 LQldgesYPQDGGALnyvlRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQ-LGEkELGRQLISHPAVDRVILTGGYETAELF-RSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFG 746
Cdd:cd07093 176 VVNVVHgFGP-EAGAALVAHPDVDLISFTGETATGRTImRAAAPNLkPVSLELGGKNPNIVFADADLDRAVDAAVRSSFS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLL---KP 821
Cdd:cd07093 255 NNGEVCLAGSRILVQRSIY--DEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAraEGATILTgggRP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 822 EQLDESGRLW-SPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGN 900
Cdd:cd07093 333 ELPDLEGGYFvEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGT 412
|
410 420
....*....|....*....|....*...
gi 2304522532 901 LYVNrgitGAIVR--RQPFGGWKKSAVG 926
Cdd:cd07093 413 VWVN----CWLVRdlRTPFGGVKASGIG 436
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
520-927 |
4.31e-57 |
|
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: 204.68 E-value: 4.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTASLDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELDTVEG-------ARFVParLTVVTP--PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAgVPRDV 670
Cdd:cd07106 96 PDEVIEDddtrrveLRRKP--LGVVAAivPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 671 LQLVQlGEKELGRQLISHPAVDRVILTGGYETAEL-FRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHA 748
Cdd:cd07106 173 LNVVS-GGDELGPALTSHPDIRKISFTGSTATGKKvMASAAKTLkRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 749 GQKCSAASLVIlvgsVARSQ--RFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPEQL 824
Cdd:cd07106 252 GQVCAAIKRLY----VHESIydEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEdaKAKGAKVLAGGEPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 825 DESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVN 904
Cdd:cd07106 328 DGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN 407
|
410 420
....*....|....*....|...
gi 2304522532 905 RgiTGAIVRRQPFGGWKKSAVGA 927
Cdd:cd07106 408 T--HGALDPDAPFGGHKQSGIGV 428
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
521-926 |
3.38e-56 |
|
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: 202.73 E-value: 3.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDP-EVSEAIDFAHYYAELAR 599
Cdd:cd07138 34 TAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAaQVGLGIGHLRAAADALK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELD---TVEGARFV--PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLV 674
Cdd:cd07138 114 DFEfeeRRGNSLVVrePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 675 QLGEKELGRQLISHPAVDRVILTG----GYETAELfrsfrpdlplLAET--------SGKNTVIVTPSADFDLAARDVAA 742
Cdd:cd07138 194 NGDGPVVGEALSAHPDVDMVSFTGstraGKRVAEA----------AADTvkrvalelGGKSANIILDDADLEKAVPRGVA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 743 SAFGHAGQKCSAASLVIlvgsVARSQ--RFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWL 818
Cdd:cd07138 264 ACFANSGQSCNAPTRML----VPRSRyaEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGieEGARLV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 819 L----KPEQLdESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLN 894
Cdd:cd07138 340 AggpgRPEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVAR 418
|
410 420 430
....*....|....*....|....*....|..
gi 2304522532 895 RISAGNLYVNRGITGAivrRQPFGGWKKSAVG 926
Cdd:cd07138 419 RLRAGQVHINGAAFNP---GAPFGGYKQSGNG 447
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
494-926 |
9.66e-56 |
|
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: 200.74 E-value: 9.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 494 QAWGRGILARVPgselgkaavaaaaVSNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAET 573
Cdd:cd07094 5 NPYDGEVIGKVP-------------ADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 574 GKTLDQSDPEVSEAIDFAHYYAELARELDTVE----GARFVPARLTVVTP----------PWNFPVAIPAGSTLAALAAG 639
Cdd:cd07094 72 GKPIKDARVEVDRAIDTLRLAAEEAERIRGEEipldATQGSDNRLAWTIRepvgvvlaitPFNFPLNLVAHKLAPAIATG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 640 SAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLAET 719
Cdd:cd07094 152 CPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 720 SGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEP 799
Cdd:cd07094 232 GGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELY--DEFIEAFVAAVKKLKVGDPLDEDTDVGPLISE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 800 AAGKLLRGLTE--LGEGETWLLKPEQldeSGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGL 877
Cdd:cd07094 310 EAAERVERWVEeaVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2304522532 878 TAGLHSLEPAEMDVWLNRISAGNLYVNRGiTGAIVRRQPFGGWKKSAVG 926
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
539-926 |
1.29e-55 |
|
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: 200.64 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 539 WGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDTVEGARFVPARLTVVT 618
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 619 ----------PPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISH 688
Cdd:cd07118 117 repigvvgiiTPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 689 PAVDRVILTG--GYETAELFRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVAr 766
Cdd:cd07118 197 PDVDMVSFTGstRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIA- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 767 sQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLDE-SGRLWSPGIRTGVRRGS 843
Cdd:cd07118 276 -DAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGraEGATLLLGGERLASaAGLFYQPTIFTDVTPDM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 844 EYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIvrRQPFGGWKKS 923
Cdd:cd07118 355 AIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQS 432
|
...
gi 2304522532 924 AVG 926
Cdd:cd07118 433 GIG 435
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
520-926 |
3.13e-55 |
|
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: 199.45 E-value: 3.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07090 16 AGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 EL--DTVE--GARFVPAR---LTVVTP--PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDV 670
Cdd:cd07090 96 TLsgEHVPlpGGSFAYTRrepLGVCAGigAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 671 LQLVQlGEKELGRQLISHPAVDRVILTGGYETAE-LFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHA 748
Cdd:cd07090 176 FNVVQ-GGGETGQLLCEHPDVAKVSFTGSVPTGKkVMSAAAKGIkHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 749 GQKCSAASLVIlvgsVARS--QRFRNQLVDAVQSLKVGYPEDPTTQMGPVI-EPAAGKLLR--------GLTELGEGEtw 817
Cdd:cd07090 255 GQVCSNGTRVF----VQRSikDEFTERLVERTKKIRIGDPLDEDTQMGALIsEEHLEKVLGyiesakqeGAKVLCGGE-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 818 LLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRIS 897
Cdd:cd07090 329 RVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQ 408
|
410 420 430
....*....|....*....|....*....|
gi 2304522532 898 AGNLYVNR-GITGAIVrrqPFGGWKKSAVG 926
Cdd:cd07090 409 AGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
521-945 |
5.44e-55 |
|
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: 198.29 E-value: 5.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARE 600
Cdd:cd07152 11 DAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 -----LDTVEG----ARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMV-EALWEAGVPRDV 670
Cdd:cd07152 91 pqgeiLPSAPGrlslARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLFEEAGLPAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 671 LQLVQlGEKELGRQLISHPAVDRVILTG----GYETAELFRSFRPDLPLlaETSGKNTVIVTPSADFDLAARDVAASAFG 746
Cdd:cd07152 171 LHVLP-GGADAGEALVEDPNVAMISFTGstavGRKVGEAAGRHLKKVSL--ELGGKNALIVLDDADLDLAASNGAWGAFL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEP--------------AAG-KLLRGltel 811
Cdd:cd07152 248 HQGQICMAAGRHLVHESVA--DAYTAKLAAKAKHLPVGDPATGQVALGPLINArqldrvhaivddsvAAGaRLEAG---- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 812 GEGEtwllkpeqldesGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDV 891
Cdd:cd07152 322 GTYD------------GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2304522532 892 WLNRISAGNLYVNRG--ITGAIVrrqPFGGWKKSavGAGTKAGGPNyliglgNWEA 945
Cdd:cd07152 390 LADRLRTGMLHINDQtvNDEPHN---PFGGMGAS--GNGSRFGGPA------NWEE 434
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
520-932 |
5.71e-55 |
|
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: 198.74 E-value: 5.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAwgaLSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07146 18 GTEEALREALALAASYRST---LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELD---------TVEGARFV-----PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAG 665
Cdd:cd07146 95 RDDgesfscdltANGKARKIftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 666 VPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAF 745
Cdd:cd07146 175 LPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 746 GHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPEQ 823
Cdd:cd07146 255 ANSGQRCTAVKRILVHESVA--DEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEeaIAQGARVLLGNQR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 824 ldeSGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYV 903
Cdd:cd07146 333 ---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNV 409
|
410 420
....*....|....*....|....*....
gi 2304522532 904 NrGITGAIVRRQPFGGWKKSavGAGTKAG 932
Cdd:cd07146 410 N-EVPGFRSELSPFGGVKDS--GLGGKEG 435
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
521-926 |
7.40e-55 |
|
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: 198.43 E-value: 7.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTL-DQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07115 17 SAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIrAARRLDVPRAADTFRYYAGWAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELdtveGARFVPAR-----LTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGV 666
Cdd:cd07115 97 KI----EGEVIPVRgpflnYTVREPvgvvgaivPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 667 PRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAE-LFRSFRPDLPLLA-ETSGKNTVIVTPSADFDLAARDVAASA 744
Cdd:cd07115 173 PAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRkIMQGAAGNLKRVSlELGGKSANIVFADADLDAAVRAAATGI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 745 FGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPE 822
Cdd:cd07115 253 FYNQGQMCTAGSRLLVHESIY--DEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGreEGARLLTGGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 823 QLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLY 902
Cdd:cd07115 331 RPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVW 410
|
410 420
....*....|....*....|....
gi 2304522532 903 VNrgITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07115 411 IN--TYNRFDPGSPFGGYKQSGFG 432
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
522-926 |
1.42e-54 |
|
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: 197.47 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARE- 600
Cdd:cd07102 17 LEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 LDTVEGA------RFV---PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVL 671
Cdd:cd07102 97 LADIRVPekdgfeRYIrrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 672 QLVQLGEKELGRqLISHPAVDRVILTGGYET-AELFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAG 749
Cdd:cd07102 177 QVLHLSHETSAA-LIADPRIDHVSFTGSVAGgRAIQRAAAGRFiKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 750 QKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPE---QL 824
Cdd:cd07102 256 QSCCSIERIYVHESI--YDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAdaIAKGARALIDGAlfpED 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 825 DESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVN 904
Cdd:cd07102 334 KAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMN 413
|
410 420
....*....|....*....|..
gi 2304522532 905 RGItgAIVRRQPFGGWKKSAVG 926
Cdd:cd07102 414 RCD--YLDPALAWTGVKDSGRG 433
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
520-926 |
2.39e-54 |
|
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: 196.69 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKA-WGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELA 598
Cdd:cd07109 16 GGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 relDTVEG------------ARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGV 666
Cdd:cd07109 96 ---DKLHGetiplgpgyfvyTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 667 PRDVLQLVQ-LGEkELGRQLISHPAVDRVILTGGYETAELFR--SFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAAS 743
Cdd:cd07109 173 PAGALNVVTgLGA-EAGAALVAHPGVDHISFTGSVETGIAVMraAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 744 AFGHAGQKCSAASLVIlvgsVARS--QRFRNQLVDAVQSLKVGYP-EDPttQMGPVIEPAAGKLLRGLTELGEGETWLL- 819
Cdd:cd07109 252 IIQNAGQTCSAGSRLL----VHRSiyDEVLERLVERFRALRVGPGlEDP--DLGPLISAKQLDRVEGFVARARARGARIv 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 820 ----KPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNR 895
Cdd:cd07109 326 aggrIAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARR 405
|
410 420 430
....*....|....*....|....*....|.
gi 2304522532 896 ISAGNLYVNRGITGAIVRRqPFGGWKKSAVG 926
Cdd:cd07109 406 LRAGQVFVNNYGAGGGIEL-PFGGVKKSGHG 435
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
523-934 |
1.38e-53 |
|
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: 194.47 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL- 601
Cdd:cd07150 21 QDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 ---------DTVEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQ 672
Cdd:cd07150 101 getlpsdspGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 673 LVQLGEKELGRQLISHPAVDRVILTG----GYETAElfRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHA 748
Cdd:cd07150 181 VVTGGGAEVGDELVDDPRVRMVTFTGstavGREIAE--KAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 749 GQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--------LGEGETWllk 820
Cdd:cd07150 259 GQICMSASRIIVEEPVY--DEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEdavakgakLLTGGKY--- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 821 peqldeSGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGL--HSLEPAeMDVWLnRISA 898
Cdd:cd07150 334 ------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIltNDLQRA-FKLAE-RLES 405
|
410 420 430
....*....|....*....|....*....|....*....
gi 2304522532 899 GNLYVNrgitGAIVRRQ---PFGGWKKSAVGagtKAGGP 934
Cdd:cd07150 406 GMVHIN----DPTILDEahvPFGGVKASGFG---REGGE 437
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
529-926 |
2.92e-52 |
|
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: 190.89 E-value: 2.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 529 INTAVTKSKA------WGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTL-DQSDPEVSEAIDFAHYYAELareL 601
Cdd:cd07112 26 VDRAVAAARRafesgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIsDALAVDVPSAANTFRWYAEA---I 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 DTVEG--ARFVPARLTVVT--P--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRD 669
Cdd:cd07112 103 DKVYGevAPTGPDALALITrePlgvvgavvPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELF--RSFRPDL-PLLAETSGKNTVIVTPSA-DFDLAARDVAASAF 745
Cdd:cd07112 183 VLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFleYSGQSNLkRVWLECGGKSPNIVFADApDLDAAAEAAAAGIF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 746 GHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELGEGETWLL----KP 821
Cdd:cd07112 263 WNQGEVCSAGSRLLVHESIK--DEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLvaggKR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 822 EQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGlhslepaemdVW---LNR--- 895
Cdd:cd07112 341 VLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS----------VWtsdLSRahr 410
|
410 420 430
....*....|....*....|....*....|....*
gi 2304522532 896 ----ISAGNLYVNRGITGAIvrRQPFGGWKKSAVG 926
Cdd:cd07112 411 varrLRAGTVWVNCFDEGDI--TTPFGGFKQSGNG 443
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
523-926 |
3.27e-52 |
|
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: 190.92 E-value: 3.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELDAVINTAVTKSKAWG-ALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDP-EVSEAIDFAHYYAELARE 600
Cdd:cd07089 19 ADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQVDGPIGHLRYFADLADS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 LD-----TVEGARFVPARLTVVTPP---------WNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGV 666
Cdd:cd07089 99 FPwefdlPVPALRGGPGRRVVRREPvgvvaaitpWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 667 PRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYET-AELFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASA 744
Cdd:cd07089 179 PAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVgRRIMAQAAATLkRVLLELGGKSANIVLDDADLAAAAPAAVGVC 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 745 FGHAGQKCSAASLVILVGSvaRSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLL--- 819
Cdd:cd07089 259 MHNAGQGCALTTRLLVPRS--RYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGrdEGARLVTggg 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 820 KPEQLDeSGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAE-MDVWLnRISA 898
Cdd:cd07089 337 RPAGLD-KGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRaYRVAR-RIRT 414
|
410 420
....*....|....*....|....*...
gi 2304522532 899 GNLYVNRGITGAIvrRQPFGGWKKSAVG 926
Cdd:cd07089 415 GSVGINGGGGYGP--DAPFGGYKQSGLG 440
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
520-926 |
4.91e-51 |
|
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: 187.18 E-value: 4.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTL-DQSDPEVSEAIDFAHYYAELA 598
Cdd:cd07108 16 SRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFGGLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 REL---------DTVEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAgVPRD 669
Cdd:cd07108 96 GELkgetlpfgpDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRQLISHPAVDRVILTGGYETAE-LFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASA-FG 746
Cdd:cd07108 175 VLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKiIYRAAADRLiPVSLELGGKSPMIVFPDADLDDAVDGAIAGMrFT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVILVGSVARSqrFRNQLVDAVQSLKVGYPEDPTTQMGPVIEP----------AAGKLLRGLTELGEGet 816
Cdd:cd07108 255 RQGQSCTAGSRLFVHEDIYDA--FLEKLVAKLSKLKIGDPLDEATDIGAIISEkqfakvcgyiDLGLSTSGATVLRGG-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 817 wLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRI 896
Cdd:cd07108 331 -PLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHAL 409
|
410 420 430
....*....|....*....|....*....|
gi 2304522532 897 SAGNLYVNRGitGAIVRRQPFGGWKKSAVG 926
Cdd:cd07108 410 EAGWVQVNQG--GGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
526-932 |
6.44e-51 |
|
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: 186.24 E-value: 6.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 526 DAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDTVE 605
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 606 GARFVPARLTVV--TP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQ 675
Cdd:cd07105 83 IPSDKPGTLAMVvkEPvgvvlgiaPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 676 LGEK---ELGRQLISHPAVDRVILTG----GYETAELfrSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHA 748
Cdd:cd07105 163 HSPEdapEVVEALIAHPAVRKVNFTGstrvGRIIAET--AAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 749 GQKCSAASLVILVGSVARsqRFRNQLVDAVQSLKVGypedpTTQMGPVIEPAAGKLLRGLTE--LGEGETWLL-KPEQLD 825
Cdd:cd07105 241 GQICMSTERIIVHESIAD--EFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDdaLSKGAKLVVgGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 826 ESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHS------LEPAEmdvwlnRISAG 899
Cdd:cd07105 314 PSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTrdlaraLAVAK------RIESG 387
|
410 420 430
....*....|....*....|....*....|....*..
gi 2304522532 900 NLYVNrgitGAIVRRQ---PFGGWKKSAVGA-GTKAG 932
Cdd:cd07105 388 AVHIN----GMTVHDEptlPHGGVKSSGYGRfNGKWG 420
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
538-934 |
7.65e-51 |
|
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: 187.01 E-value: 7.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 538 AWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDP-EVSEAIDFAHYYAELARELDTVEGARFVPARLTV 616
Cdd:cd07139 53 PWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRaQGPGPAALLRYYAALARDFPFEERRPGSGGGHVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 617 VT----------PPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQlGEKELGRQLI 686
Cdd:cd07139 133 VRrepvgvvaaiVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVP-ADREVGEYLV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 687 SHPAVDRVILTG--------GYETAELFRsfrpdlPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLV 758
Cdd:cd07139 212 RHPGVDKVSFTGstaagrriAAVCGERLA------RVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 759 ILvgSVARSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELGEGETWLL-----KPEQLDEsGRLWSP 833
Cdd:cd07139 286 LV--PRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEGARLvtgggRPAGLDR-GWFVEP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 834 GIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAE-MDVwLNRISAGNLYVNrGITGAIV 912
Cdd:cd07139 363 TLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERgLAV-ARRIRTGTVGVN-GFRLDFG 440
|
410 420
....*....|....*....|..
gi 2304522532 913 rrQPFGGWKKSAVGagtKAGGP 934
Cdd:cd07139 441 --APFGGFKQSGIG---REGGP 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
536-926 |
8.65e-51 |
|
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: 187.13 E-value: 8.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 536 SKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAreldTVEGARFVPA--- 612
Cdd:cd07119 50 SGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLA----TKETGEVYDVpph 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 613 --RLTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELG 682
Cdd:cd07119 126 viSRTVREPvgvcglitPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 683 RQLISHPAVDRVILTGGYETAE-LFRSFRPDLPLLA-ETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVIL 760
Cdd:cd07119 206 AELAESPDVDLVSFTGGTATGRsIMRAAAGNVKKVAlELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 761 VGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLDES----GRLWSPG 834
Cdd:cd07119 286 EESIH--DKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGkeEGARLVCGGKRPTGDelakGYFVEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 835 IRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNR-GITGAivr 913
Cdd:cd07119 364 IFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyHPYFA--- 440
|
410
....*....|...
gi 2304522532 914 RQPFGGWKKSAVG 926
Cdd:cd07119 441 EAPWGGYKQSGIG 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
521-926 |
1.13e-50 |
|
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: 186.36 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARE 600
Cdd:cd07151 30 SKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 LD------TVEGA--RFVPARLTVV--TPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWE-AGVPRD 669
Cdd:cd07151 110 MEgrilpsDVPGKenRVYREPLGVVgvISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLAKIFEeAGLPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRQLISHPaVDRVI-LTG----GYETAEL-FRSFRpdLPLLaETSGKNTVIVTPSADFDLAARDVAAS 743
Cdd:cd07151 190 VLNVVVGAGSEIGDAFVEHP-VPRLIsFTGstpvGRHIGELaGRHLK--KVAL-ELGGNNPFVVLEDADIDAAVNAAVFG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 744 AFGHAGQKCSAASLVILVGSVARSqrFRNQLVDAVQSLKVGYPEDPTTQMGPVI-EPAAGKLLR--------GLTELGEG 814
Cdd:cd07151 266 KFLHQGQICMAINRIIVHEDVYDE--FVEKFVERVKALPYGDPSDPDTVVGPLInESQVDGLLDkieqaveeGATLLVGG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 815 ETwllkpeqldeSGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLN 894
Cdd:cd07151 344 EA----------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFAR 413
|
410 420 430
....*....|....*....|....*....|....
gi 2304522532 895 RISAGNLYVNRGITG--AIVrrqPFGGWKKSAVG 926
Cdd:cd07151 414 RIDAGMTHINDQPVNdePHV---PFGGEKNSGLG 444
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
520-926 |
2.34e-50 |
|
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: 185.22 E-value: 2.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLD-QSDPEVSEAIDFAHYYAELA 598
Cdd:cd07092 16 ASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHlVRDDELPGAVDNFRFFAGAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 RELDTVEGARFVPARLTVV----------TPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEaGVPR 668
Cdd:cd07092 96 RTLEGPAAGEYLPGHTSMIrrepigvvaqIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-VLPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 669 DVLQLVQLGEKELGRQLISHPAVDRVILTGGYET-AELFRSFRPDLPLL-AETSGKNTVIVTPSADFDLAARDVAASAFG 746
Cdd:cd07092 175 GVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTgKKVARAAADTLKRVhLELGGKAPVIVFDDADLDAAVAGIATAGYY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRG-LTELGEGETWLLKPEQLD 825
Cdd:cd07092 255 NAGQDCTAACRVYVHESVY--DEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGfVERAPAHARVLTGGRRAE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 826 ESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNR 905
Cdd:cd07092 333 GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT 412
|
410 420
....*....|....*....|.
gi 2304522532 906 GITgaIVRRQPFGGWKKSAVG 926
Cdd:cd07092 413 HIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
522-926 |
4.47e-50 |
|
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: 184.48 E-value: 4.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL 601
Cdd:cd07110 18 AEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 DT-------VEGARFV------PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPR 668
Cdd:cd07110 98 DAkaeravpLPSEDFKarvrrePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 669 DVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAE-LFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFG 746
Cdd:cd07110 178 GVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSqVMQAAAQDIkPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFW 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLL---KP 821
Cdd:cd07110 258 NNGQICSATSRLLVHESIA--DAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGkeEGARLLCggrRP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 822 EQLDEsGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNL 901
Cdd:cd07110 336 AHLEK-GYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIV 414
|
410 420
....*....|....*....|....*
gi 2304522532 902 YVNrgITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07110 415 WIN--CSQPCFPQAPWGGYKRSGIG 437
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
522-937 |
3.57e-49 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 182.97 E-value: 3.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELA-RE 600
Cdd:PLN02278 61 RAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAkRV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 LDTVEGARFVPARLTVV---------TPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVL 671
Cdd:PLN02278 141 YGDIIPSPFPDRRLLVLkqpvgvvgaITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 672 QLVQLGEKELGRQLISHPAVDRVILTGGYETAELFrsfrpdLPLLAET--------SGKNTVIVTPSADFDLAARDVAAS 743
Cdd:PLN02278 221 NVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKL------MAGAAATvkrvslelGGNAPFIVFDDADLDVAVKGALAS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 744 AFGHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKP 821
Cdd:PLN02278 295 KFRNSGQTCVCANRILVQEGI--YDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQdaVSKGAKVLLGG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 822 EQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEmdVWlnRISA--- 898
Cdd:PLN02278 373 KRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQR--AW--RVSEale 448
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2304522532 899 -GNLYVNRGITGAIVrrQPFGGWKKSAVG-AGTKAGGPNYL 937
Cdd:PLN02278 449 yGIVGVNEGLISTEV--APFGGVKQSGLGrEGSKYGIDEYL 487
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
524-926 |
5.88e-49 |
|
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: 181.01 E-value: 5.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 524 ELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELD- 602
Cdd:cd07145 22 EVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 603 ---TVEGARFVPARLTVVT--P--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRD 669
Cdd:cd07145 102 etiPVDAYEYNERRIAFTVrePigvvgaitPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELF--RSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGH 747
Cdd:cd07145 182 VINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIasKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFEN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 748 AGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPEQld 825
Cdd:cd07145 262 AGQVCNAVKRILVEEEVY--DKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNdaVEKGGKILYGGKR-- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 826 ESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNR 905
Cdd:cd07145 338 DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVIND 417
|
410 420
....*....|....*....|...
gi 2304522532 906 GITgaiVRRQ--PFGGWKKSAVG 926
Cdd:cd07145 418 STR---FRWDnlPFGGFKKSGIG 437
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
520-927 |
1.35e-48 |
|
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: 180.20 E-value: 1.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:cd07101 15 STPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELDTVE---GARFVPARLTV---------VTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVP 667
Cdd:cd07101 95 RLLKPRrrrGAIPVLTRTTVnrrpkgvvgVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 668 RDVLQLVqLGE-KELGRQLISHpaVDRVILTGGYETAELF--RSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASA 744
Cdd:cd07101 175 RDLWQVV-TGPgSEVGGAIVDN--ADYVMFTGSTATGRVVaeRAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRAC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 745 FGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPE 822
Cdd:cd07101 252 FSNAGQLCVSIERIYVHESVY--DEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDdaVAKGATVLAGGR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 823 QLDESGRL-WSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNL 901
Cdd:cd07101 330 ARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTV 409
|
410 420
....*....|....*....|....*..
gi 2304522532 902 YVNRGITGAIVRRQ-PFGGWKKSAVGA 927
Cdd:cd07101 410 NVNEGYAAAWASIDaPMGGMKDSGLGR 436
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
520-927 |
8.43e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 176.61 E-value: 8.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR 599
Cdd:PRK09407 51 STAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 EL---DTVEGARFVPARLTV---------VTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVP 667
Cdd:PRK09407 131 KLlapRRRAGALPVLTKTTElrqpkgvvgVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 668 RDVLQLVqLGE-KELGRQLISHpaVDRVILTGGYET----AElfRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAA 742
Cdd:PRK09407 211 RDLWQVV-TGPgPVVGTALVDN--ADYLMFTGSTATgrvlAE--QAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 743 SAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPA---------AGKLLRGLTELGE 813
Cdd:PRK09407 286 ACFSNAGQLCISIERIYVHESIY--DEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAqletvsahvDDAVAKGATVLAG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 814 GETwllKPeqlDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWL 893
Cdd:PRK09407 364 GKA---RP---DLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIA 437
|
410 420 430
....*....|....*....|....*....|....*
gi 2304522532 894 NRISAGNLYVNRGITGAIVRRQ-PFGGWKKSAVGA 927
Cdd:PRK09407 438 ARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLGR 472
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
522-926 |
5.57e-46 |
|
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: 172.56 E-value: 5.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL 601
Cdd:cd07107 18 AADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 dtveGARFVPA-----RLTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAgVPR 668
Cdd:cd07107 98 ----KGETIPVggrnlHYTLREPygvvarivAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-LPP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 669 DVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDL--PLLAETSGKNTVIVTPSADFDLAARD-VAASAF 745
Cdd:cd07107 173 GVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGikHVTLELGGKNALIVFPDADPEAAADAaVAGMNF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 746 GHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAA-GKLLRGLTELGEGETWLL----K 820
Cdd:cd07107 253 TWCGQSCGSTSRLFVHESIY--DEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQyDRVMHYIDSAKREGARLVtgggR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 821 PEQLDESGRLW-SPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAG 899
Cdd:cd07107 331 PEGPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAG 410
|
410 420 430
....*....|....*....|....*....|
gi 2304522532 900 NLYVN---RGITGAivrrqPFGGWKKSAVG 926
Cdd:cd07107 411 YVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
551-937 |
1.37e-45 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 169.92 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 551 LHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAR--ELDTVEGAR-----FVPARLTVVTP---P 620
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryEGEIIQSDRpgeniLLFKRALGVTTgilP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 621 WNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGY 700
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 701 ETAE-LFRSFRPDLPLLA-ETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAV 778
Cdd:PRK10090 161 SAGEkIMAAAAKNITKVClELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY--DQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 779 QSLKVGYP-EDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPIL 855
Cdd:PRK10090 239 QAVQFGNPaERNDIAMGPLINAAALERVEQKVARAveEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 856 GVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIvrrQPF-GGWKKSAV-GAGTKAGG 933
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSGIgGADGKHGL 395
|
....
gi 2304522532 934 PNYL 937
Cdd:PRK10090 396 HEYL 399
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
535-937 |
4.05e-45 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 171.07 E-value: 4.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 535 KSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELDTVEGA------- 607
Cdd:PLN02467 62 KGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKApvslpme 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 608 ----RFVPARLTVV--TPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKEL 681
Cdd:PLN02467 142 tfkgYVLKEPLGVVglITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 682 GRQLISHPAVDRVILTGGYETAE-LFRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVI 759
Cdd:PLN02467 222 GAPLASHPGVDKIAFTGSTATGRkIMTAAAQMVkPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 760 LVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLL---KPEQLDEsGRLWSPG 834
Cdd:PLN02467 302 VHERIA--SEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAksEGATILCggkRPEHLKK-GFFIEPT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 835 IRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNrgITGAIVRR 914
Cdd:PLN02467 379 IITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQ 456
|
410 420
....*....|....*....|....
gi 2304522532 915 QPFGGWKKSAVGAGTKAGG-PNYL 937
Cdd:PLN02467 457 APWGGIKRSGFGRELGEWGlENYL 480
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
521-938 |
7.74e-45 |
|
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: 170.46 E-value: 7.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEAR-RADLMEVMAAETGKTLDQSDPEVS-EAIDFAHYYAELA 598
Cdd:cd07123 67 DAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKyRYELNAATMLGQGKNVWQAEIDAAcELIDFLRFNVKYA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 REL------DTVEGAR----------FVPArltvVTPpWNFpVAIpaGSTLAALAA--GSAVVIKPARQSARSGAVMVEA 660
Cdd:cd07123 147 EELyaqqplSSPAGVWnrleyrplegFVYA----VSP-FNF-TAI--GGNLAGAPAlmGNVVLWKPSDTAVLSNYLVYKI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 661 LWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYET-----------AELFRSFrpdlP-LLAETSGKNTVIVT 728
Cdd:cd07123 219 LEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTfkslwkqigenLDRYRTY----PrIVGETGGKNFHLVH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 729 PSADFDLAARDVAASAFGHAGQKCSAASLVIlvgsVARS--QRFRNQLVDAVQSLKVGYPEDPTTQMGPVI-EPAAGKLL 805
Cdd:cd07123 295 PSADVDSLVTATVRGAFEYQGQKCSAASRAY----VPESlwPEVKERLLEELKEIKMGDPDDFSNFMGAVIdEKAFDRIK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 806 R---------GLTELGEGET-----WLLKPeqldesgrlwspgirTGVRRGSEYHLT---EYFGPILGVMT--AATLEEA 866
Cdd:cd07123 371 GyidhaksdpEAEIIAGGKCddsvgYFVEP---------------TVIETTDPKHKLmteEIFGPVLTVYVypDSDFEET 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2304522532 867 IDMANDI-DYGLTAGLHSLEPAEMDVWLN--RISAGNLYVNRGITGAIVRRQPFGGWKKSavgaGT--KAGGPNYLI 938
Cdd:cd07123 436 LELVDTTsPYALTGAIFAQDRKAIREATDalRNAAGNFYINDKPTGAVVGQQPFGGARAS----GTndKAGSPLNLL 508
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
521-937 |
2.23e-44 |
|
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: 168.34 E-value: 2.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQS-DPEVSEAIDFAHYYAELAR 599
Cdd:cd07111 57 EEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ELDTvEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQlGEK 679
Cdd:cd07111 137 LLDT-ELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVT-GNG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 680 ELGRQLISHPAVDRVILTGGYETAELFRS----FRPDLPLlaETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAA 755
Cdd:cd07111 215 SFGSALANHPGVDKVAFTGSTEVGRALRRatagTGKKLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 756 SLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLDESGRLWSP 833
Cdd:cd07111 293 SRLLVQESVA--EELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGraEGADVFQPGADLPSKGPFYPP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 834 GIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGlhslepaemdVWLNRIS----------AGNLYV 903
Cdd:cd07111 371 TLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAAS----------VWSENLSlalevalslkAGVVWI 440
|
410 420 430
....*....|....*....|....*....|....*.
gi 2304522532 904 N-RGITGAIVrrqPFGGWKKSAVG-AGTKAGGPNYL 937
Cdd:cd07111 441 NgHNLFDAAA---GFGGYRESGFGrEGGKEGLYEYL 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
520-926 |
6.54e-44 |
|
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: 166.37 E-value: 6.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVT--KSKAWgALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAEL 597
Cdd:cd07120 16 GGVAEAEAAIAAARRafDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 598 ARELD----TVEGARFV-----PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEA-GVP 667
Cdd:cd07120 95 ARTEAgrmiEPEPGSFSlvlrePMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 668 RDVLQLVQLGEKELGRQLISHPAVDRVILTGGYET-AELFRSFRPDLPLLA-ETSGKNTVIVTPSADFDLAARDVAASAF 745
Cdd:cd07120 175 AGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATgRAIMAAAAPTLKRLGlELGGKTPCIVFDDADLDAALPKLERALT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 746 GHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPEQ 823
Cdd:cd07120 255 IFAGQFCMAGSRVLVQRSIA--DEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVEraIAAGAEVVLRGGP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 824 LDES---GRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGN 900
Cdd:cd07120 333 VTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGT 412
|
410 420
....*....|....*....|....*.
gi 2304522532 901 LYVNRgiTGAIVRRQPFGGWKKSAVG 926
Cdd:cd07120 413 VWIND--WNKLFAEAEEGGYRQSGLG 436
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
520-926 |
1.09e-43 |
|
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: 166.08 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSK-AWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDP-EVSEAIDFAHYYA-- 595
Cdd:cd07113 34 ATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQSANFLRYFAgw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 596 -------ELARELDTVEGARFV------PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALW 662
Cdd:cd07113 114 atkingeTLAPSIPSMQGERYTaftrrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 663 EAGVPRDVLQLVQlGEKELGRQLISHPAVDRVILTGGYETAE-LFRSFRPDLPLLA-ETSGKNTVIVTPSADFDLAARDV 740
Cdd:cd07113 194 EAGIPDGVLNVVN-GKGAVGAQLISHPDVAKVSFTGSVATGKkIGRQAASDLTRVTlELGGKNAAAFLKDADIDWVVEGL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 741 AASAFGHAGQKCSAASLVILVGSvaRSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVI-EPAAGKLLRGLTEL-GEGETWL 818
Cdd:cd07113 273 LTAGFLHQGQVCAAPERFYVHRS--KFDELVTKLKQALSSFQVGSPMDESVMFGPLAnQPHFDKVCSYLDDArAEGDEIV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 819 LKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISA 898
Cdd:cd07113 351 RGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEA 430
|
410 420
....*....|....*....|....*....
gi 2304522532 899 GNLYVN-RGITGAIVrrqPFGGWKKSAVG 926
Cdd:cd07113 431 GTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
520-926 |
3.16e-43 |
|
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: 164.89 E-value: 3.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKA-WGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQ-SDPEVSEAIDFAHYYAEL 597
Cdd:cd07144 42 AGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 598 ArelDTVEGARFV--PARL--TVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAG 665
Cdd:cd07144 122 A---DKIQGKTIPtsPNKLayTLHEPygvcgqiiPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 666 VPRDVLQLVQ-LGEKeLGRQLISHPAVDRVILTG----GYETAELFRSFRPDLPLlaETSGKNTVIVTPSADFDLAARDV 740
Cdd:cd07144 199 FPPGVVNIIPgYGAV-AGSALAEHPDVDKIAFTGstatGRLVMKAAAQNLKAVTL--ECGGKSPALVFEDADLDQAVKWA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 741 AASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAV-QSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETW 817
Cdd:cd07144 276 AAGIMYNSGQNCTATSRIYVQESIY--DKFVEKFVEHVkQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGkkEGAKL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 818 LL---KPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLN 894
Cdd:cd07144 354 VYggeKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVAR 433
|
410 420 430
....*....|....*....|....*....|..
gi 2304522532 895 RISAGNLYVNRGITGAIvrRQPFGGWKKSAVG 926
Cdd:cd07144 434 ELEAGMVWINSSNDSDV--GVPFGGFKMSGIG 463
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
535-926 |
1.13e-41 |
|
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: 160.07 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 535 KSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQS-DPEVSEAIDFAHYYAELArelDTVEGaRFVPAR 613
Cdd:cd07091 55 ETGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESaKGDVALSIKCLRYYAGWA---DKIQG-KTIPID 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 614 -----LTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQ-LGeK 679
Cdd:cd07091 131 gnflaYTRREPigvcgqiiPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPgFG-P 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 680 ELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLA---ETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAAS 756
Cdd:cd07091 210 TAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNLKKvtlELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 757 LVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLDESGRLWSPG 834
Cdd:cd07091 290 RIFVQESI--YDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGkkEGATLLTGGERHGSKGYFIQPT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 835 IRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNrgiTGAIVRR 914
Cdd:cd07091 368 VFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDA 444
|
410
....*....|...
gi 2304522532 915 Q-PFGGWKKSAVG 926
Cdd:cd07091 445 AvPFGGFKQSGFG 457
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
523-937 |
2.31e-41 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 159.30 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL- 601
Cdd:PRK11241 48 DETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIy 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 -DTVEG----ARFV----PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQ 672
Cdd:PRK11241 128 gDTIPGhqadKRLIvikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 673 LVQLGEKELGRQLISHPAVDRVILTGGYETA-ELFRSFRPDLPLLA-ETSGKNTVIVTPSADFDLAARDVAASAFGHAGQ 750
Cdd:PRK11241 208 VVTGSAGAVGGELTSNPLVRKLSFTGSTEIGrQLMEQCAKDIKKVSlELGGNAPFIVFDDADLDKAVEGALASKFRNAGQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 751 KCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVI-EPAAGKLLRGLTE-LGEGETWLLKPEQLDESG 828
Cdd:PRK11241 288 TCVCANRLYVQDGV--YDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIdEKAVAKVEEHIADaLEKGARVVCGGKAHELGG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 829 RLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGIT 908
Cdd:PRK11241 366 NFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGII 445
|
410 420 430
....*....|....*....|....*....|
gi 2304522532 909 GAIVrrQPFGGWKKSAVG-AGTKAGGPNYL 937
Cdd:PRK11241 446 SNEV--APFGGIKASGLGrEGSKYGIEDYL 473
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
520-926 |
2.89e-41 |
|
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: 159.05 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQS-DPEVSEAIDFAHYYAELA 598
Cdd:cd07559 35 STAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETlAADIPLAIDHFRYFAGVI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 R-------ELDTVEGARFVPARLTVVTP--PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAgVPRD 669
Cdd:cd07559 115 RaqegslsEIDEDTLSYHFHEPLGVVGQiiPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPD--LPLLAETSGKNTVIVTPSA-----DFDLAARDVAA 742
Cdd:cd07559 194 VVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEnlIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 743 SAFGHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLK 820
Cdd:cd07559 274 GFAFNQGEVCTCPSRALVQESI--YDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGkeEGAEVLTG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 821 PEQLDESGRL----WSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGlhslepaemdVW---L 893
Cdd:cd07559 352 GERLTLGGLDkgyfYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGG----------VWtrdI 421
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2304522532 894 NR-------ISAGNLYVNrgITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07559 422 NRalrvargIQTGRVWVN--CYHQYPAHAPFGGYKKSGIG 459
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
520-946 |
3.79e-40 |
|
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: 155.54 E-value: 3.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTL-DQSDPEV---SEAIDF--AHY 593
Cdd:cd07098 15 DTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMvDASLGEIlvtCEKIRWtlKHG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 594 YAELARE------LDTVEGAR--FVParLTVVTP--PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMV----E 659
Cdd:cd07098 95 EKALRPEsrpgglLMFYKRARveYEP--LGVVGAivSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLsiirE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 660 ALWEAGVPRDVLQLVqLGEKELGRQLISHPAVDRVILTGGYETAELF-RSFRPDL-PLLAETSGKNTVIVTPSADFDLAA 737
Cdd:cd07098 173 CLAACGHDPDLVQLV-TCLPETAEALTSHPVIDHITFIGSPPVGKKVmAAAAESLtPVVLELGGKDPAIVLDDADLDQIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 738 RDVAASAFGHAGQKCSAASLVIlvgsVARSQ--RFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGE 813
Cdd:cd07098 252 SIIMRGTFQSSGQNCIGIERVI----VHEKIydKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVAdaVEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 814 GETWL----LKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEM 889
Cdd:cd07098 328 GARLLaggkRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRA 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2304522532 890 DVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSAVGagtKAGGPNYLIGLGNWEAV 946
Cdd:cd07098 408 RRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG---RFAGEEGLRGLCNPKSV 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
521-926 |
7.31e-40 |
|
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: 154.33 E-value: 7.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARE 600
Cdd:cd07147 19 GPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 -------LDTVEGA-------RFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGV 666
Cdd:cd07147 99 iygevlpLDISARGegrqglvRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 667 PRDVLQLVQLgEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFG 746
Cdd:cd07147 179 PKGAFSVLPC-SRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETwLLKPEQL 824
Cdd:cd07147 258 QAGQSCISVQRVLVHRSVY--DEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNeaVDAGAK-LLTGGKR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 825 DesGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGL--HSLEPAeMDVWlNRISAGNLY 902
Cdd:cd07147 335 D--GALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVftRDLEKA-LRAW-DELEVGGVV 410
|
410 420
....*....|....*....|....
gi 2304522532 903 VNRgITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07147 411 IND-VPTFRVDHMPYGGVKDSGIG 433
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
521-926 |
8.84e-40 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 154.65 E-value: 8.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQS---DPeVSEAiDFAHYYAEL 597
Cdd:PRK13252 42 TPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETsvvDI-VTGA-DVLEYYAGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 598 ARELD----TVEGARFVPAR---LTVVTP--PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPR 668
Cdd:PRK13252 120 APALEgeqiPLRGGSFVYTRrepLGVCAGigAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 669 DVLQLVQlGEKELGRQLISHPAVDRVILTGGYET-----AELFRSFRpdlPLLAETSGKNTVIVTPSADFDLAArDVAAS 743
Cdd:PRK13252 200 GVFNVVQ-GDGRVGAWLTEHPDIAKVSFTGGVPTgkkvmAAAAASLK---EVTMELGGKSPLIVFDDADLDRAA-DIAML 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 744 A-FGHAGQKCSAASLVIlvgsVARS--QRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWL 818
Cdd:PRK13252 275 AnFYSSGQVCTNGTRVF----VQKSikAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGkaEGARLL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 819 LKPEQLDE----SGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLN 894
Cdd:PRK13252 351 CGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIH 430
|
410 420 430
....*....|....*....|....*....|...
gi 2304522532 895 RISAGNLYVNR-GITGAivrRQPFGGWKKSAVG 926
Cdd:PRK13252 431 QLEAGICWINTwGESPA---EMPVGGYKQSGIG 460
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
521-893 |
9.57e-40 |
|
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: 154.29 E-value: 9.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 521 NEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARE 600
Cdd:cd07130 32 TPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFAVGLSRQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 601 LD--TVEGAR--------FVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQ----SARSGAVMVEALWEAGV 666
Cdd:cd07130 112 LYglTIPSERpghrmmeqWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTtpltAIAVTKIVARVLEKNGL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 667 PRDVLQLVQlGEKELGRQLISHPAVDRVILTG--------GYETAELF-RSfrpdlplLAETSGKNTVIVTPSADFDLAA 737
Cdd:cd07130 192 PGAIASLVC-GGADVGEALVKDPRVPLVSFTGstavgrqvGQAVAARFgRS-------LLELGGNNAIIVMEDADLDLAV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 738 RDVAASAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAA-GKLLRGLTEL-GEGE 815
Cdd:cd07130 264 RAVLFAAVGTAGQRCTTTRRLIVHESIY--DEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAvDNYLAAIEEAkSQGG 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2304522532 816 TWLLKPEQLDESGRLWSPGIRTGVRRGSEYHlTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWL 893
Cdd:cd07130 342 TVLFGGKVIDGPGNYVEPTIVEGLSDAPIVK-EETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWL 418
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
524-877 |
1.01e-39 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 154.91 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 524 ELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAElareldt 603
Cdd:PLN00412 54 EVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAE------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 604 vEGARF-------------------------VPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMV 658
Cdd:PLN00412 127 -EGVRIlgegkflvsdsfpgnernkycltskIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 659 EALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPdLPLLAETSGKNTVIVTPSADFDLAAR 738
Cdd:PLN00412 206 HCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKAGM-VPLQMELGGKDACIVLEDADLDLAAA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 739 DVAASAFGHAGQKCSAASLVILVGSVArsqrfrNQLVDAVQS----LKVGYPEDpTTQMGPVIEPAAGKLLRGLTELGEG 814
Cdd:PLN00412 285 NIIKGGFSYSGQRCTAVKVVLVMESVA------DALVEKVNAkvakLTVGPPED-DCDITPVVSESSANFIEGLVMDAKE 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2304522532 815 ETWLLKPEQLDESGRLWsPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGL 877
Cdd:PLN00412 358 KGATFCQEWKREGNLIW-PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGL 419
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
522-926 |
2.27e-39 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 152.97 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL 601
Cdd:PRK09406 22 DDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 602 DTVEGA------------RFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRD 669
Cdd:PRK09406 102 LADEPAdaaavgasrayvRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRqLISHPAVDRVILTGGYETAELFRSFRPDL--PLLAETSGKNTVIVTPSADFDLAARDVAASAFGH 747
Cdd:PRK09406 182 CFQTLLVGSGAVEA-ILRDPRVAAATLTGSEPAGRAVAAIAGDEikKTVLELGGSDPFIVMPSADLDRAAETAVTARVQN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 748 AGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLKPEQLD 825
Cdd:PRK09406 261 NGQSCIAAKRFIVHADVY--DAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDdaVAAGATILCGGKRPD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 826 ESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNr 905
Cdd:PRK09406 339 GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN- 417
|
410 420
....*....|....*....|.
gi 2304522532 906 GITgAIVRRQPFGGWKKSAVG 926
Cdd:PRK09406 418 GMT-VSYPELPFGGVKRSGYG 437
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
520-926 |
4.86e-39 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 152.37 E-value: 4.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQS-DPEVSEAIDFAHYYAELA 598
Cdd:PRK13473 36 ASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAlNDEIPAIVDVFRFFAGAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 RELDTVEGARFVPAR--------LTVVT--PPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAgVPR 668
Cdd:PRK13473 116 RCLEGKAAGEYLEGHtsmirrdpVGVVAsiAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 669 DVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAE-LFRSFRPDLPLL-AETSGKNTVIVTPSADFDLAARDVAASAFG 746
Cdd:PRK13473 195 GVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKhVLSAAADSVKRThLELGGKAPVIVFDDADLDAVVEGIRTFGYY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVIlvgsVARS--QRFRNQLVDAVQSLKVGYPEDPTTQMGPVI-----EPAAGKLLRGLtELGEGETwLL 819
Cdd:PRK13473 275 NAGQDCTAACRIY----AQRGiyDDLVAKLAAAVATLKVGDPDDEDTELGPLIsaahrDRVAGFVERAK-ALGHIRV-VT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 820 KPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAglhslepaemDVWL------ 893
Cdd:PRK13473 349 GGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLAS----------SVWTrdvgra 418
|
410 420 430
....*....|....*....|....*....|....*..
gi 2304522532 894 ----NRISAGNLYVNRGITgaIVRRQPFGGWKKSAVG 926
Cdd:PRK13473 419 hrvsARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
525-926 |
1.44e-38 |
|
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: 151.14 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 525 LDAVINTAVTKSKA-----WG-ALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDP-EVSEAIDFAHYYAEL 597
Cdd:cd07143 42 TEADVDIAVEVAHAafetdWGlKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 598 A-----RELDTVEG----ARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPR 668
Cdd:cd07143 122 AdkihgQVIETDIKkltyTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 669 DVLQLVQLGEKELGRQLISHPAVDRVILTGGYETA-----ELFRSFRPDLPLlaETSGKNTVIVTPSADFDLAARDVAAS 743
Cdd:cd07143 202 GVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGrkvmeAAAKSNLKKVTL--ELGGKSPNIVFDDADLESAVVWTAYG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 744 AFGHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKP 821
Cdd:cd07143 280 IFFNHGQVCCAGSRIYVQEGI--YDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGkaEGATVETGG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 822 EQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNL 901
Cdd:cd07143 358 KRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTV 437
|
410 420
....*....|....*....|....*
gi 2304522532 902 YVNrgITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07143 438 WVN--CYNLLHHQVPFGGYKQSGIG 460
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
522-929 |
2.57e-37 |
|
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: 147.22 E-value: 2.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDP-EVSEAIDFAHYYAELAR- 599
Cdd:cd07117 37 DADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRa 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 ------ELDTVEGARFVPARLTVVTP--PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEaLWEAGVPRDVL 671
Cdd:cd07117 117 eegsanMIDEDTLSIVLREPIGVVGQiiPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAK-IIQDVLPKGVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 672 QLVQLGEKELGRQLISHPAVDRVILTG----GYETAElfRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGH 747
Cdd:cd07117 196 NIVTGKGSKSGEYLLNHPGLDKLAFTGstevGRDVAI--AAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFN 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 748 AGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLD 825
Cdd:cd07117 274 QGQVCCAGSRIFVQEGI--YDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAkeEGAKILTGGHRLT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 826 ES----GRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGlhslepaemdVWLNRISAGnL 901
Cdd:cd07117 352 ENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGG----------VFTKDINRA-L 420
|
410 420 430
....*....|....*....|....*....|....*..
gi 2304522532 902 YVNRGI-TG--------AIVRRQPFGGWKKSAVGAGT 929
Cdd:cd07117 421 RVARAVeTGrvwvntynQIPAGAPFGGYKKSGIGRET 457
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
523-926 |
8.26e-37 |
|
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: 145.95 E-value: 8.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELD-AVINTAVTKSKA-------WGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKT-LDQSDPEVSEAIDFAHY 593
Cdd:cd07141 39 QEGDkADVDKAVKAARAafklgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPfSKSYLVDLPGAIKVLRY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 594 YAELArelDTVEGaRFVPAR-----LTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEA 660
Cdd:cd07141 119 YAGWA---DKIHG-KTIPMDgdfftYTRHEPvgvcgqiiPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 661 LWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFR--SFRPDLPLLA-ETSGKNTVIVTPSADFDLAA 737
Cdd:cd07141 195 IKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQqaAGKSNLKRVTlELGGKSPNIVFADADLDYAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 738 RDVAASAFGHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGE 815
Cdd:cd07141 275 EQAHEALFFNMGQCCCAGSRTFVQESI--YDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGkkEGA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 816 TWLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNR 895
Cdd:cd07141 353 KLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNA 432
|
410 420 430
....*....|....*....|....*....|.
gi 2304522532 896 ISAGNLYVNrgITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07141 433 LRAGTVWVN--CYNVVSPQAPFGGYKMSGNG 461
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
539-926 |
8.46e-37 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 146.12 E-value: 8.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 539 WGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDP-EVSEAIDFAHYYAELArelDTVEGARFVPAR---- 613
Cdd:PLN02766 76 WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAA---DKIHGETLKMSRqlqg 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 614 LTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQL 685
Cdd:PLN02766 153 YTLKEPigvvghiiPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 686 ISHPAVDRVILTGGYETAELF--RSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVG 762
Cdd:PLN02766 233 ASHMDVDKVSFTGSTEVGRKImqAAATSNLkQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 763 SVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLKPEQLDESGRLWSPGIRTGVR 840
Cdd:PLN02766 313 GI--YDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGkrEGATLLTGGKPCGDKGYYIEPTIFTDVT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 841 RGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSlepAEMDVwLNRIS----AGNLYVNrgITGAIVRRQP 916
Cdd:PLN02766 391 EDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVT---KDLDV-ANTVSrsirAGTIWVN--CYFAFDPDCP 464
|
410
....*....|
gi 2304522532 917 FGGWKKSAVG 926
Cdd:PLN02766 465 FGGYKMSGFG 474
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
523-926 |
2.55e-36 |
|
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: 144.17 E-value: 2.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELDAV-INTAVTKSK------AWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSD-PEVSEAIDFAHYY 594
Cdd:cd07142 36 AEGDAEdVDRAVKAARkafdegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 595 AELARELD----TVEGARFV-----PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAG 665
Cdd:cd07142 116 AGWADKIHgmtlPADGPHHVytlhePIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 666 VPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSF--RPDL-PLLAETSGKNTVIVTPSADFDLAARDVAA 742
Cdd:cd07142 196 LPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLaaKSNLkPVTLELGGKSPFIVCEDADVDKAVELAHF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 743 SAFGHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLK 820
Cdd:cd07142 276 ALFFNQGQCCCAGSRTFVHESI--YDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGkeEGATLITG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 821 PEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGN 900
Cdd:cd07142 354 GDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGT 433
|
410 420
....*....|....*....|....*...
gi 2304522532 901 LYVN--RGITGAIvrrqPFGGWKKSAVG 926
Cdd:cd07142 434 VWVNcyDVFDASI----PFGGYKMSGIG 457
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
520-926 |
2.76e-36 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 143.85 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAE--- 596
Cdd:PRK13968 26 AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEhgp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 597 --LARELDTVEGARFV----PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDV 670
Cdd:PRK13968 106 amLKAEPTLVENQQAVieyrPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 671 LQLVQlGEKELGRQLISHPAVDRVILTG--------GYETAELFRSfrpdlpLLAETSGKNTVIVTPSADFDLAARDVAA 742
Cdd:PRK13968 186 YGWLN-ADNDGVSQMINDSRIAAVTVTGsvragaaiGAQAGAALKK------CVLELGGSDPFIVLNDADLELAVKAAVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 743 SAFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTE--LGEGETWLLK 820
Cdd:PRK13968 259 GRYQNTGQVCAAAKRFIIEEGIA--SAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEatLAEGARLLLG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 821 PEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGN 900
Cdd:PRK13968 337 GEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGG 416
|
410 420
....*....|....*....|....*.
gi 2304522532 901 LYVNrGITgAIVRRQPFGGWKKSAVG 926
Cdd:PRK13968 417 VFIN-GYC-ASDARVAFGGVKKSGFG 440
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
522-926 |
1.46e-35 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 142.34 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 522 EAELDAVINTA--VTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQS-DPEVSEAIDFAHYYAELA 598
Cdd:PRK09847 56 SVDIDRAVSAArgVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 REL-------DTVEGARFVPARLTVVTP--PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRD 669
Cdd:PRK09847 136 DKVygevattSSHELAMIVREPVGVIAAivPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPL---LAETSGKNTVIV-TPSADFDLAARDVAASAF 745
Cdd:PRK09847 216 VLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMkrvWLEAGGKSANIVfADCPDLQQAASATAAGIF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 746 GHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELGEGETWLLkpeqLD 825
Cdd:PRK09847 296 YNQGQVCIAGTRLLLEESIA--DEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLL----LD 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 826 ESGRLW----SPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNL 901
Cdd:PRK09847 370 GRNAGLaaaiGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSV 449
|
410 420
....*....|....*....|....*
gi 2304522532 902 YVNRGITGAIVrrQPFGGWKKSAVG 926
Cdd:PRK09847 450 FVNNYNDGDMT--VPFGGYKQSGNG 472
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
520-926 |
6.42e-33 |
|
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: 134.12 E-value: 6.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTL-DQSDPEVSEAIDFAHYYAELA 598
Cdd:cd07116 35 STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVrETLAADIPLAIDHFRYFAGCI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 599 R-------ELDTVEGARFVPARLTVVTP--PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAgVPRD 669
Cdd:cd07116 115 RaqegsisEIDENTVAYHFHEPLGVVGQiiPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 670 VLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPD--LPLLAETSGKNTVIVTPS------ADFDLAARDVA 741
Cdd:cd07116 194 VVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEniIPVTLELGGKSPNIFFADvmdaddAFFDKALEGFV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 742 ASAFgHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLL 819
Cdd:cd07116 274 MFAL-NQGEVCTCPSRALIQESI--YDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGkeEGAEVLT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 820 KPEQLDESGRL-----WSPGIRTG--VRRGSEyhltEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVW 892
Cdd:cd07116 351 GGERNELGGLLgggyyVPTTFKGGnkMRIFQE----EIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRM 426
|
410 420 430
....*....|....*....|....*....|....
gi 2304522532 893 LNRISAGNLYVNrgITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07116 427 GRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
620-927 |
3.11e-31 |
|
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: 128.11 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 620 PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEaLWEAGVPRDVLQLVQLGEKELGRQLISH---------PA 690
Cdd:cd07135 117 PWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE-LVPKYLDPDAFQVVQGGVPETTALLEQKfdkifytgsGR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 691 VDRVILTGGYETaelfrsfrpdL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVARSqr 769
Cdd:cd07135 196 VGRIIAEAAAKH----------LtPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDE-- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 770 frnqLVDAVQS-LKVGYPEDPT--TQMGPVIEPAAGKLLRGLTELGEGETWLlkPEQLDESGRLWSPGIRTGVRRGSEYH 846
Cdd:cd07135 264 ----FVEELKKvLDEFYPGGANasPDYTRIVNPRHFNRLKSLLDTTKGKVVI--GGEMDEATRFIPPTIVSDVSWDDSLM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 847 LTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07135 338 SEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDSGYG 417
|
.
gi 2304522532 927 A 927
Cdd:cd07135 418 A 418
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
520-928 |
1.14e-30 |
|
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: 127.15 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEAELDAVINTAVTKSK---AWgaLSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAE 596
Cdd:cd07148 18 VDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 597 LARELdtveGARFVPARLT------------------VVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMV 658
Cdd:cd07148 96 ELGQL----GGREIPMGLTpasagriafttrepigvvVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 659 EALWEAGVPRDVLQLVqLGEKELGRQLISHPAVDRVILTGGYETAELFRS-FRPDLPLLAETSGKNTVIVTPSADFDLAA 737
Cdd:cd07148 172 DLLHEAGLPEGWCQAV-PCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSkLAPGTRCALEHGGAAPVIVDRSADLDAMI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 738 RDVAASAFGHAGQKCSAASLVILVGSVARSqrFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAagkllrgltELGEGETW 817
Cdd:cd07148 251 PPLVKGGFYHAGQVCVSVQRVFVPAEIADD--FAQRLAAAAEKLVVGDPTDPDTEVGPLIRPR---------EVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 818 LlkPEQLDESGRLWSPGIRTGVR-----------RGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSlep 886
Cdd:cd07148 320 V--NEAVAAGARLLCGGKRLSDTtyaptvlldppRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFT--- 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2304522532 887 AEMDVWLN---RISAGNLYVNRGiTGAIVRRQPFGGWKKSAVGAG 928
Cdd:cd07148 395 KDLDVALKavrRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYGTG 438
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
520-904 |
7.81e-28 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 120.24 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 520 SNEaELDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAr 599
Cdd:PLN02419 149 TNE-EFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMA- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 eldTVEGARFVPA------RLTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAG 665
Cdd:PLN02419 227 ---TLQMGEYLPNvsngvdTYSIREPlgvcagicPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 666 VPRDVLQLVQlGEKELGRQLISHPAVdRVILTGGYETAELF---RSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAA 742
Cdd:PLN02419 304 LPDGVLNIVH-GTNDTVNAICDDEDI-RAVSFVGSNTAGMHiyaRAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 743 SAFGHAGQKCSAASLVILVGSvarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EGETWLLK 820
Cdd:PLN02419 382 AGFGAAGQRCMALSTVVFVGD---AKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGvdDGAKLLLD 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 821 PEQL----DESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRI 896
Cdd:PLN02419 459 GRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDI 538
|
....*...
gi 2304522532 897 SAGNLYVN 904
Cdd:PLN02419 539 EAGQIGIN 546
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
525-934 |
1.77e-27 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 116.95 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 525 LDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQS---------DPEVSEAIDFAHYYA 595
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAenicgdqvqLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 596 ELAREL--DTVEGARFVPARLTVVT--PPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAG-VPRDV 670
Cdd:cd07084 81 EPGNHLgqGLKQQSHGYRWPYGPVLviGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 671 LQLVQlGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLAETSGKNTVIVTPSAD-FDLAARDVAASAFGHAG 749
Cdd:cd07084 161 VTLIN-GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 750 QKCSAASlVILVGSVARSQRFrnqlVDAVQSLkVGYPEDPTTQMGPVIEPAAgklLRGLTELGEGETWLL----KPEQLD 825
Cdd:cd07084 240 QKCTAQS-MLFVPENWSKTPL----VEKLKAL-LARRKLEDLLLGPVQTFTT---LAMIAHMENLLGSVLlfsgKELKNH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 826 ESGRLWSPGIRTGV-------RRGSEYHLTEYFGPILGVM-----TAATLEEAIDMANDidyGLTAGLHSLEPAEMD-VW 892
Cdd:cd07084 311 SIPSIYGACVASALfvpideiLKTYELVTEEIFGPFAIVVeykkdQLALVLELLERMHG---SLTAAIYSNDPIFLQeLI 387
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2304522532 893 LNRISAGNLY-VNRGITGAIVRRQPFGGWKksAVGAGTKAGGP 934
Cdd:cd07084 388 GNLWVAGRTYaILRGRTGVAPNQNHGGGPA--ADPRGAGIGGP 428
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
523-919 |
3.78e-27 |
|
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: 115.70 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELDAVINTAVTKSKAWgalsgaeRAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSD-PEVS---EAIDFA--HYYAE 596
Cdd:cd07087 5 ARLRETFLTGKTRSLEW-------RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAvvlGEIDHAlkHLKKW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 597 LARE-LDTVEGARFVPARL-------TVVTPPWNFPVA---IPAgstLAALAAGSAVVIKPARQSARSGAVMVEaLWEAG 665
Cdd:cd07087 78 MKPRrVSVPLLLQPAKAYVipeplgvVLIIGPWNYPLQlalAPL---IGAIAAGNTVVLKPSELAPATSALLAK-LIPKY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 666 VPRDVLQLVQlGEKELGRQLISHPaVDRVILTGGYETAEL-FRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAAS 743
Cdd:cd07087 154 FDPEAVAVVE-GGVEVATALLAEP-FDHIFFTGSPAVGKIvMEAAAKHLtPVTLELGGKSPCIVDKDANLEVAARRIAWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 744 AFGHAGQKCSAASLVILVGSVArsQRFRNQLVDAVQSLkvgYPEDPTTQ--MGPVI-EPAAGKllrgLTELGEGETwLLK 820
Cdd:cd07087 232 KFLNAGQTCIAPDYVLVHESIK--DELIEELKKAIKEF---YGEDPKESpdYGRIInERHFDR----LASLLDDGK-VVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 821 PEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGN 900
Cdd:cd07087 302 GGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGG 381
|
410
....*....|....*....
gi 2304522532 901 LYVNRGITGAIVRRQPFGG 919
Cdd:cd07087 382 VCVNDVLLHAAIPNLPFGG 400
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
536-932 |
8.83e-27 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 116.09 E-value: 8.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 536 SKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARELD--TVEGARFVPAR 613
Cdd:PLN02315 69 AKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNgsIIPSERPNHMM 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 614 LTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQ----SARSGAVMVEALWEAGVPRDVLQLVqLGEKEL 681
Cdd:PLN02315 149 MEVWNPlgivgvitAFNFPCAVLGWNACIALVCGNCVVWKGAPTtpliTIAMTKLVAEVLEKNNLPGAIFTSF-CGGAEI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 682 GRQLISHPAVDRVILTGGYETAELFRSF---RPDLPLLaETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLV 758
Cdd:PLN02315 228 GEAIAKDTRIPLVSFTGSSKVGLMVQQTvnaRFGKCLL-ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 759 ILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGK-LLRGLTEL-GEGETWLLKPEQLDESGRLWSPGIr 836
Cdd:PLN02315 307 LLHESI--YDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKnFEKGIEIIkSQGGKILTGGSAIESEGNFVQPTI- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 837 TGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISA--GNLYVNRGITGAIVrR 914
Cdd:PLN02315 384 VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIPTNGAEI-G 462
|
410
....*....|....*...
gi 2304522532 915 QPFGGWKksAVGAGTKAG 932
Cdd:PLN02315 463 GAFGGEK--ATGGGREAG 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
529-926 |
1.64e-26 |
|
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: 114.90 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 529 INTAVTKSKA------WGALSGAERAEVLHRAGEVLEARRADLMEVMAAETG-------KTldqsdpEVSEAIDFAHYYA 595
Cdd:cd07140 45 VDRAVAAAKEafengeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGavytlalKT------HVGMSIQTFRYFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 596 ELArelDTVEGARFV--PAR------LTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVE 659
Cdd:cd07140 119 GWC---DKIQGKTIPinQARpnrnltLTKREPigvcgiviPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 660 ALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYET-AELFRS-FRPDLPLLA-ETSGKNTVIVTPSADFDLA 736
Cdd:cd07140 196 LTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIgKHIMKScAVSNLKKVSlELGGKSPLIIFADCDMDKA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 737 ARDVAASAFGHAGQKCSAASLVILVGSVarSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLRGLTELG--EG 814
Cdd:cd07140 276 VRMGMSSVFFNKGENCIAAGRLFVEESI--HDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGvkEG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 815 ETWLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGV--MTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVW 892
Cdd:cd07140 354 ATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYV 433
|
410 420 430
....*....|....*....|....*....|....
gi 2304522532 893 LNRISAGNLYVNRGITGAIVrrQPFGGWKKSAVG 926
Cdd:cd07140 434 SDKLEAGTVFVNTYNKTDVA--APFGGFKQSGFG 465
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
523-926 |
1.74e-26 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 115.29 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELDAV-INTAVTKSKA------WGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQS-DPEVSEAIDFAHYY 594
Cdd:PLN02466 90 AEGDAEdVNRAVAAARKafdegpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSaKAELPMFARLFRYY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 595 AELArelDTVEGARfVPAR-----LTVVTP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEAL 661
Cdd:PLN02466 170 AGWA---DKIHGLT-VPADgphhvQTLHEPigvagqiiPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 662 WEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSF--RPDL-PLLAETSGKNTVIVTPSADFDLAAR 738
Cdd:PLN02466 246 HEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELaaKSNLkPVTLELGGKSPFIVCEDADVDKAVE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 739 DVAASAFGHAGQKCSAASLVILvgsvarSQRFRNQLVDAVQ--SLK--VGYPEDPTTQMGPVIEPAAGKLLRGLTELG-- 812
Cdd:PLN02466 326 LAHFALFFNQGQCCCAGSRTFV------HERVYDEFVEKAKarALKrvVGDPFKKGVEQGPQIDSEQFEKILRYIKSGve 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 813 EGETWLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGL--HSLEPAEMd 890
Cdd:PLN02466 400 SGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVftQNLDTANT- 478
|
410 420 430
....*....|....*....|....*....|....*....
gi 2304522532 891 vwLNR-ISAGNLYVN--RGITGAIvrrqPFGGWKKSAVG 926
Cdd:PLN02466 479 --LSRaLRVGTVWVNcfDVFDAAI----PFGGYKMSGIG 511
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
526-927 |
1.79e-26 |
|
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: 113.86 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 526 DAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGK-----TLDQSDPEVSEAidfAHYYAELAR- 599
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKpaaevDLTEILPVLSEI---NHAIKHLKKw 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 600 -----------ELDTVEGARFVPARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPR 668
Cdd:cd07134 78 mkpkrvrtpllLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 669 DVlQLVQlGEKELGRQLIS----H------PAVDRVILTGGYETaelfrsfrpdlplLA----ETSGKNTVIVTPSADFD 734
Cdd:cd07134 158 EV-AVFE-GDAEVAQALLElpfdHifftgsPAVGKIVMAAAAKH-------------LAsvtlELGGKSPTIVDETADLK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 735 LAARDVAASAFGHAGQKCSAASLVIlvgsVARSQrfRNQLVDAVQ-SLKVGYPEDPTTQMGP----VIEPAAGKLLRGLT 809
Cdd:cd07134 223 KAAKKIAWGKFLNAGQTCIAPDYVF----VHESV--KDAFVEHLKaEIEKFYGKDAARKASPdlarIVNDRHFDRLKGLL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 810 E--LGEGETwLLKPEQLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPA 887
Cdd:cd07134 297 DdaVAKGAK-VEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKA 375
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2304522532 888 EMDVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSAVGA 927
Cdd:cd07134 376 NVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGS 415
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
523-927 |
7.73e-24 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 106.65 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 523 AELDAVINTAVTKSKAWgalsgaeRAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSD-----PEVSEaIDF--AHYYA 595
Cdd:PTZ00381 14 KKLKESFLTGKTRPLEF-------RKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKmtevlLTVAE-IEHllKHLDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 596 ELARELDTVEGARFV--------PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEaLWEAGVP 667
Cdd:PTZ00381 86 YLKPEKVDTVGVFGPgksyiipePLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAK-LLTKYLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 668 RDVLQLVQlGEKELGRQLISHPaVDRVILTGGYETAEL-FRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAF 745
Cdd:PTZ00381 165 PSYVRVIE-GGVEVTTELLKEP-FDHIFFTGSPRVGKLvMQAAAENLtPCTLELGGKSPVIVDKSCNLKVAARRIAWGKF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 746 GHAGQKCSAASLVILVGSVArsqrfrNQLVDAV-QSLKVGYPEDPTTQ--MGPVIEPAAGKLLRGLTELGEGEtwLLKPE 822
Cdd:PTZ00381 243 LNAGQTCVAPDYVLVHRSIK------DKFIEALkEAIKEFFGEDPKKSedYSRIVNEFHTKRLAELIKDHGGK--VVYGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 823 QLDESGRLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLY 902
Cdd:PTZ00381 315 EVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVV 394
|
410 420
....*....|....*....|....*
gi 2304522532 903 VNRGITGAIVRRQPFGGWKKSAVGA 927
Cdd:PTZ00381 395 INDCVFHLLNPNLPFGGVGNSGMGA 419
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
620-927 |
4.00e-21 |
|
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: 97.68 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 620 PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALweagvPR----DVLQLVQLGEKELGrQLISHpAVDRVI 695
Cdd:cd07132 109 AWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-----PKyldkECYPVVLGGVEETT-ELLKQ-RFDYIF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 696 LTGGYETAELFRSF--RPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGSVarsqrfRNQ 773
Cdd:cd07132 182 YTGSTSVGKIVMQAaaKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEV------QEK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 774 LVDAVQ-SLKVGYPEDPTT--QMGPVIEPAAGKLLRGLTELGE----GETwllkpeqlDESGRLWSPGIRTGVRRGSEYH 846
Cdd:cd07132 256 FVEALKkTLKEFYGEDPKEspDYGRIINDRHFQRLKKLLSGGKvaigGQT--------DEKERYIAPTVLTDVKPSDPVM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 847 LTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSAVG 926
Cdd:cd07132 328 QEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
.
gi 2304522532 927 A 927
Cdd:cd07132 408 A 408
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
525-885 |
1.04e-20 |
|
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: 96.84 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 525 LDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELARElDTV 604
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVRE-GSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 605 EGARFVPARLTVVTPPW-------------------NFPVA--IPAGSTLAALAAGSAVVIK--PA--RQSARSGAVMVE 659
Cdd:cd07129 80 LDARIDPADPDRQPLPRpdlrrmlvplgpvavfgasNFPLAfsVAGGDTASALAAGCPVVVKahPAhpGTSELVARAIRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 660 ALWEAGVPRDVLQLVQLGEKELGRQLISHPAVDRVILTGGYE--TAeLFR--SFRPD-LPLLAETSGKNTVIVTPSAdfd 734
Cdd:cd07129 160 ALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRggRA-LFDaaAARPEpIPFYAELGSVNPVFILPGA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 735 LAAR------DVAASAFGHAGQKCSAASLVILVGSVArSQRFRNQLVDAVQSLkvgypeDPTTQMGPVIepaAGKLLRGL 808
Cdd:cd07129 236 LAERgeaiaqGFVGSLTLGAGQFCTNPGLVLVPAGPA-GDAFIAALAEALAAA------PAQTMLTPGI---AEAYRQGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 809 TELGE-GETWLLKPEQLDESGRLWSPGI-RTGVR--RGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSL 884
Cdd:cd07129 306 EALAAaPGVRVLAGGAAAEGGNQAAPTLfKVDAAafLADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGE 385
|
.
gi 2304522532 885 E 885
Cdd:cd07129 386 E 386
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
606-927 |
1.37e-19 |
|
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: 92.93 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 606 GARFVPARLTVV-TP--------PWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGvPRDVLQLVQl 676
Cdd:cd07133 87 GLLFLPAKAEVEyQPlgvvgiivPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF-DEDEVAVVT- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 677 GEKELGRQlISHPAVDRVILTGGYETAEL-FRSFRPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSA 754
Cdd:cd07133 165 GGADVAAA-FSSLPFDHLLFTGSTAVGRHvMRAAAENLtPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 755 ASLVIlvgsVARSQrfRNQLVDAVQS-LKVGYPEDPTTQ-MGPVIEPAAGKLLRGLTE----LGEGETWLLKPEQLDESG 828
Cdd:cd07133 244 PDYVL----VPEDK--LEEFVAAAKAaVAKMYPTLADNPdYTSIINERHYARLQGLLEdaraKGARVIELNPAGEDFAAT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 829 RLWSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGIT 908
Cdd:cd07133 318 RKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
330
....*....|....*....
gi 2304522532 909 GAIVRRQPFGGwkksaVGA 927
Cdd:cd07133 398 HVAQDDLPFGG-----VGA 411
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
547-927 |
3.98e-17 |
|
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: 85.63 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 547 RAEVLHRAGEVLEARRADL----MEVMAAETGKTLDqsdpEVSEAIdfahyyaelaRELDTVEGARFVPARL-------- 614
Cdd:cd07136 30 KQAIKKYENEILEALKKDLgkseFEAYMTEIGFVLS----EINYAI----------KHLKKWMKPKRVKTPLlnfpsksy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 615 --------TVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAgVPRDVLQLVQlGEKELGRQLI 686
Cdd:cd07136 96 iyyepygvVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE-GGVEENQELL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 687 SHPaVDRVILTGG-------YETAElfrsfrPDL-PLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLV 758
Cdd:cd07136 174 DQK-FDYIFFTGSvrvgkivMEAAA------KHLtPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 759 ILVGSVarSQRFRNQLVDAVQSLkvgYPEDPTT--QMGPVIEPAAGKLLRGLTELGE----GETwllkpeqlDESGRLWS 832
Cdd:cd07136 247 LVHESV--KEKFIKELKEEIKKF---YGEDPLEspDYGRIINEKHFDRLAGLLDNGKivfgGNT--------DRETLYIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 833 PGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSlEPAEM-DVWLNRISAGNLYVNRGITGAI 911
Cdd:cd07136 314 PTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFS-EDKKVeKKVLENLSFGGGCINDTIMHLA 392
|
410
....*....|....*.
gi 2304522532 912 VRRQPFGGWKKSAVGA 927
Cdd:cd07136 393 NPYLPFGGVGNSGMGS 408
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
541-887 |
4.25e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 82.83 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 541 ALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQSDPEVSEAIDFAHYYAELAREL---------DTVEGAR--- 608
Cdd:PRK11903 59 ALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALgdarllrdgEAVQLGKdpa 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 609 ------FVPAR-LTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGV-PRDVLQLVQLGEKE 680
Cdd:PRK11903 139 fqgqhvLVPTRgVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 681 LGRQLishPAVDRVILTGGYETAELFRS----FRPDLPLLAETSGKNTVIVTP-----SADFDLAARDVAASAFGHAGQK 751
Cdd:PRK11903 219 LLDHL---QPFDVVSFTGSAETAAVLRShpavVQRSVRVNVEADSLNSALLGPdaapgSEAFDLFVKEVVREMTVKSGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 752 CSAASLVILvgSVARSQRFRNQLVDAVQSLKVGYPEDPTTQMGPVIEPAAGKLLR-GLTELGEGETWLL-----KPEQLD 825
Cdd:PRK11903 296 CTAIRRIFV--PEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRaGLAALRAQAEVLFdgggfALVDAD 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2304522532 826 ESGRLWSPGIRTGVRRG---SEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPA 887
Cdd:PRK11903 374 PAVAACVGPTLLGASDPdaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAA 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
537-871 |
4.70e-16 |
|
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: 82.70 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 537 KAWGALSGAERAEVLHRAGEVLEARRADLMEVmAAETGKTLDQSDPEVSEAIDFAHYYAELAREL---------DTVE-- 605
Cdd:cd07128 51 PALRALTFHERAAMLKALAKYLMERKEDLYAL-SAATGATRRDSWIDIDGGIGTLFAYASLGRRElpnahflveGDVEpl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 606 --GARF------VPAR-LTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGV-PRDVLQLVQ 675
Cdd:cd07128 130 skDGTFvgqhilTPRRgVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLIC 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 676 LGEKELGRQLISHpavDRVILTGGYETAELFRS----FRPDLPLLAETSGKNTVIVTPSA-----DFDLAARDVAASAFG 746
Cdd:cd07128 210 GSVGDLLDHLGEQ---DVVAFTGSAATAAKLRAhpniVARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 747 HAGQKCSAASLVI----LVGSVARSqrfrnqLVDAVQSLKVGYPEDPTTQMGPVIE--------------PAAGKLLRG- 807
Cdd:cd07128 287 KAGQKCTAIRRAFvpeaRVDAVIEA------LKARLAKVVVGDPRLEGVRMGPLVSreqredvraavatlLAEAEVVFGg 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2304522532 808 ----LTELGEGET-WLLKPEQLDESGRLWSPGIrtgvrrgseyHLTEYFGPILGVMTAATLEEAIDMAN 871
Cdd:cd07128 361 pdrfEVVGADAEKgAFFPPTLLLCDDPDAATAV----------HDVEAFGPVATLMPYDSLAEAIELAA 419
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
611-927 |
5.02e-16 |
|
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: 82.07 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 611 PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEaLWEAGVPRDVLQLVQlGEKELGRQLISHpA 690
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAK-LIPEYLDTKAIKVIE-GGVPETTALLEQ-K 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 691 VDRVILTGGYETAELFR--SFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFG-HAGQKCSAASLVILvgsvarS 767
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMaaAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGcNNGQACIAPDYVLV------E 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 768 QRFRNQLVDAVQS-LKVGYPEDP--TTQMGPVIEPAAGKLLRGLTELGEGETWLLKPEQLDESGRLWSPGIRTGVRRGSE 844
Cdd:cd07137 252 ESFAPTLIDALKNtLEKFFGENPkeSKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEPTILLDPPLDSS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 845 YHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSA 924
Cdd:cd07137 332 IMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESG 411
|
...
gi 2304522532 925 VGA 927
Cdd:cd07137 412 FGA 414
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
542-934 |
1.01e-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: 74.57 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 542 LSGAERAEVLHRAGEVLEARRADLMEVMAAETG-----------KTLDQSDPEVSEAIDFAHY-YAELARELDTVEGARF 609
Cdd:cd07077 13 NHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiAMMGCSESKLYKNIDTERGiTASVGHIQDVLLPDNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 610 ------VPARLTVVTPPWNFPVAIPAgSTLAALAAGSAVVIKP---ARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKE 680
Cdd:cd07077 93 etyvraFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPhpsAPFTNRALALLFQAADAAHGPKILVLYVPHPSDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 681 LGRQLISHPAVDRVILTGGYETAELFRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFgHAGQKCSAASLVIL 760
Cdd:cd07077 172 LAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 761 VGSVARSQRFRNQLVDAVQSLKVgypedpttqmgpviePAAGKLLRGLTelgegetwllKPEQLDEsgrlwspgirtgvr 840
Cdd:cd07077 251 VDDVLDPLYEEFKLKLVVEGLKV---------------PQETKPLSKET----------TPSFDDE-------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 841 rgseyhLTEYFGPILGVMTAATLEEAIDMANDIDY----GLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVRRQP 916
Cdd:cd07077 292 ------ALESMTPLECQFRVLDVISAVENAWMIIEsgggPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAG 365
|
410
....*....|....*...
gi 2304522532 917 FGGWKKSAVGAGTKAGGP 934
Cdd:cd07077 366 KGVERIVTSGMNNIFGAG 383
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
611-927 |
1.50e-12 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 71.23 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 611 PARLTVVTPPWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALwEAGVPRDVLQLVQLGEKELGRQLisHPA 690
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 691 VDRVILTGGYETAELFRSFRPD--LPLLAETSGKNTVIVTPSADFDLAARDVAASAFG-HAGQKCSAASLVIlvgsvaRS 767
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKhlTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYIL------TT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 768 QRFRNQLVDAVQ-SLKVGYPEDP--TTQMGPVIEPAAGKLLRGLTELGEGETWLLKPEQLDESGRLWSPGIRTGVRRGSE 844
Cdd:PLN02174 263 KEYAPKVIDAMKkELETFYGKNPmeSKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 845 YHLTEYFGPILGVMTAATLEEAIDMANDIDYGLTAGLHSLEPAEMDVWLNRISAGNLYVNRGITGAIVRRQPFGGWKKSA 924
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESG 422
|
...
gi 2304522532 925 VGA 927
Cdd:PLN02174 423 MGA 425
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
617-904 |
4.67e-12 |
|
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: 69.44 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 617 VTPPWNfPVAIPAGSTLAALAAGSAVVIKPARQSARSGA----VMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVD 692
Cdd:cd07122 102 LIPSTN-PTSTAIFKALIALKTRNAIIFSPHPRAKKCSIeaakIMREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 693 RVILTGGyetAELFRSfrpdlpllAETSGK--------NT-VIVTPSADFDLAARDVAAS-AFGHaGQKCSAASLVILVG 762
Cdd:cd07122 181 LILATGG---PGMVKA--------AYSSGKpaigvgpgNVpAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 763 SVArsqrfrNQLVDAVQSLKvGY--PEDPTTQMGPVIEPAAGKL--------------LRGLtELGEGETWLLKPEqlde 826
Cdd:cd07122 249 EIY------DEVRAELKRRG-AYflNEEEKEKLEKALFDDGGTLnpdivgksaqkiaeLAGI-EVPEDTKVLVAEE---- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 827 sgrlwspgirTGVrrGSEYHLT-EYFGPILGVMTAATLEEAIDMANDI-DY---GLTAGLHSLEPAEMDVWLNRISAGNL 901
Cdd:cd07122 317 ----------TGV--GPEEPLSrEKLSPVLAFYRAEDFEEALEKARELlEYggaGHTAVIHSNDEEVIEEFALRMPVSRI 384
|
...
gi 2304522532 902 YVN 904
Cdd:cd07122 385 LVN 387
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
525-940 |
3.77e-11 |
|
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: 66.91 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 525 LDAVINTAVTKSKAWGALSGAERAEVLHRAGEVLEARRADLMEVMAAETGKTLDQsDPEVSEAIDFAHYYAELARELDTV 604
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVE-DKVIKNHFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 605 EGARFVPARLTVVTPPWNF-----PVAIPAGST----LAALAAGSAVVIKP----ARQSARSGAVMVEALWEAGVPRDVL 671
Cdd:cd07081 80 VLTGDENGGTLIIAEPIGVvasitPSTNPTSTVifksLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 672 QLVQLGEKELGRQLISHPAVDRVILTGGYETAELFRSFRPdlPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQK 751
Cdd:cd07081 160 GWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGK--PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 752 CSAASLVILVGSVARSQRFR-----------NQLvDAVQS--LK--------VGYPEDPTTQMGPVIEPAAGKLLRG-LT 809
Cdd:cd07081 238 CASEQSVIVVDSVYDEVMRLfegqgaykltaEEL-QQVQPviLKngdvnrdiVGQDAYKIAAAAGLKVPQETRILIGeVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 810 ELGEgetwllkpeqldesgrlwspgirtgvrrgSEYHLTEYFGPILGVMTAATLEEAIDMA----NDIDYGLTAGLHSLE 885
Cdd:cd07081 317 SLAE-----------------------------HEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDN 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2304522532 886 ---PAEMDVWLNRISAGNLYVNRGIT-GAIVRRQPFGGWKKSAVGAGTKAG-------GPNYLIGL 940
Cdd:cd07081 368 ikaIENMNQFANAMKTSRFVKNGPCSqGGLGDLYNFRGWPSMTLGCGTWGGnsvsenvGPKHLVNL 433
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
619-911 |
2.62e-08 |
|
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: 57.87 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 619 PPWNfpvAIPAgsTLAALAAGSAVVIKPARQSARSGAVMV----EALWEAGV-PRDVLQLVQLGEKELGRQLISHPAVDR 693
Cdd:cd07127 206 PTWN---GYPG--LFASLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 694 VILTGGYETAELFRSFRPDLPLLAETSGKNTVIVTPSADFDLAARDVAASAFGHAGQKCSAASLV------ILVGSVARS 767
Cdd:cd07127 281 IDFTGSNAFGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIyvprdgIQTDDGRKS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 768 -QRFRNQLVDAVQSLkVGYPEDPTTQMGPVIEPAAgklLRGLTELGEGETWLLKPEQLD----ESGRLWSPGIRTGVRRG 842
Cdd:cd07127 361 fDEVAADLAAAIDGL-LADPARAAALLGAIQSPDT---LARIAEARQLGEVLLASEAVAhpefPDARVRTPLLLKLDASD 436
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2304522532 843 SEYHLTEYFGPILGVMTAATLEEAIDMANDI--DYG-LTAGLHSLEPAEMDVW--LNRISAGNLYVNrgITGAI 911
Cdd:cd07127 437 EAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDPEVVERVqeAALDAGVALSIN--LTGGV 508
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
609-871 |
4.57e-08 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 57.04 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 609 FVPARLTVVTPP---------WNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVlqLVQLGEK 679
Cdd:PLN02203 97 AFPATAEVVPEPlgvvlifssWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV--KVIEGGP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 680 ELGRQLISHPAvDRVILTGGYETAELFRSFRPD--LPLLAETSGKNTVIV---TPSADFDLAARDVAASAFGH-AGQKCS 753
Cdd:PLN02203 175 AVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKhlTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 754 AASLVILvgsvarSQRFRNQLVDAVQS-LKVGYPEDP--TTQMGPVIEPAAGKLLRGLTELGEGETWLLKPEQLDESGRL 830
Cdd:PLN02203 254 AIDYVLV------EERFAPILIELLKStIKKFFGENPreSKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLF 327
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2304522532 831 WSPGIRTGVRRGSEYHLTEYFGPILGVMTAATLEEAIDMAN 871
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFIN 368
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
617-883 |
3.21e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 54.17 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 617 VTPPWNfPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVE----ALWEAGVPRDVLQLVQLGEKELGRQLISHPAVD 692
Cdd:cd07121 104 ITPSTN-PTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVElinkAIAEAGGPDNLVVTVEEPTIETTNELMAHPDIN 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 693 RVILTGGyetaelfrsfrPDLPLLAETSGKN---------TVIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGS 763
Cdd:cd07121 183 LLVVTGG-----------PAVVKAALSSGKKaigagagnpPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 764 VArsqrfrNQLVDAVQSLKVGYpedpttqmgpVIEPAAGKLLRGLTELGEGET----WLLKPEQ--LDESGRLWSPGIRT 837
Cdd:cd07121 252 VA------DYLIAAMQRNGAYV----------LNDEQAEQLLEVVLLTNKGATpnkkWVGKDASkiLKAAGIEVPADIRL 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2304522532 838 GVRRGSEYHL---TEYFGPILGVMTAATLEEAIDMANDIDYGL--TAGLHS 883
Cdd:cd07121 316 IIVETDKDHPfvvEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHS 366
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
617-883 |
6.53e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 49.90 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 617 VTPPWNfPVAIPAGSTLAALAAGSAVVIKP----ARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQLISHPAVD 692
Cdd:PRK15398 136 VTPSTN-PTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTIETAQRLMKHPGIA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 693 RVILTGGyetaelfrsfrPDLPLLAETSGKNT---------VIVTPSADFDLAARDVAASAFGHAGQKCSAASLVILVGS 763
Cdd:PRK15398 215 LLVVTGG-----------PAVVKAAMKSGKKAigagagnppVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 764 VA-----RSQRFRNQLVDAVQSLKVgypEDPTTQMGPVIEPA-----AGKLLRGLTELGEGETWLLKPEqldesgrlwsp 833
Cdd:PRK15398 284 VAdelmrLMEKNGAVLLTAEQAEKL---QKVVLKNGGTVNKKwvgkdAAKILEAAGINVPKDTRLLIVE----------- 349
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2304522532 834 girtgVRRGSEYHLTEYFGPILGVMTAATLEEAIDMANDIDYGL--TAGLHS 883
Cdd:PRK15398 350 -----TDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHS 396
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
263-420 |
4.04e-05 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 47.39 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 263 QAYLPDALSamvRLQEfAAARRADGGAAIKVRVVKGANLPMEQVEASLHGWPLATWHTKADSDTNYKRVINYALHPDRIK 342
Cdd:PLN02681 274 QAYLKDARE---RLRL-DLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 343 NVRIGVAGHNLFDVAFAWLLAGERGVR---DGIEFEMLLGMAagqaevvrrDVGSLLL---------YTPVvhpAEFDVA 410
Cdd:PLN02681 350 DGEVMLATHNVESGELAAAKMNELGLHkgdPRVQFAQLLGMS---------DNLSFGLgnagfrvskYLPY---GPVEEV 417
|
170
....*....|
gi 2304522532 411 IAYLIRRLEE 420
Cdd:PLN02681 418 IPYLLRRAEE 427
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
606-758 |
7.01e-05 |
|
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: 46.72 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2304522532 606 GARFVPARLTVVTPpWNFPVAIPAGSTLAALAAGSAVVIKPARQSARSGAVMVEALWEAGVPRDVLQLVQLGEKELGRQL 685
Cdd:cd07126 138 GYRWPYGPVAIITP-FNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2304522532 686 IShpAVDRVIL-TGGYETAE-LFRSFRPDLPLlaETSGKNTVIVTPS-ADFDLAARDVAASAFGHAGQKCSAASLV 758
Cdd:cd07126 217 LE--ANPRMTLfTGSSKVAErLALELHGKVKL--EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSIL 288
|
|
| |
