|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
555-1009 |
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: 614.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 555 TDPSRPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEI 634
Cdd:cd07125 51 IDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 635 SEAIDFCEFYPLTVNH----------WAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVA 704
Cdd:cd07125 131 REAIDFCRYYAAQARElfsdpelpgpTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 705 AMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVR-----PDLHLLAETGGKNATIVTA 779
Cdd:cd07125 211 ARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALaerdgPILPLIAETGGKNAMIVDS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 780 MADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVfdDPKFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKTLTRGMK 859
Cdd:cd07125 291 TALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEI--AERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 860 TLEDDETWLVAPEHI-VGQPNLYRPGVKWNVapGSFSHLTELFGPVLGVMPFSR--LEEAIEIVRSTGYGLTSGLESLDD 936
Cdd:cd07125 369 ELMRGEAWLIAPAPLdDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712455972 937 REIELWKQSIHAGNLYINRSTTGAIVLRQPFGGVGLSAYGPgvKAGGPHYVLALMRITdsgqttpsTDSVSTT 1009
Cdd:cd07125 447 REIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP--KAGGPNYLLRFGNEK--------TVSLNTT 509
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
500-992 |
2.70e-123 |
|
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: 390.43 E-value: 2.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 500 YVNEPDTDWSVPANSVWAEQTLQKWKDQCGDQatvVPLWVGDQQV-TPEpdqMRESTDPSRPGCVVCRYPMASLDQVQQA 578
Cdd:cd07124 1 FRNEPFTDFADEENRAAFRAALARVREELGRE---YPLVIGGKEVrTEE---KIESRNPADPSEVLGTVQKATKEEAEAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 579 VSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYPLTVNHWAQQAGVD 658
Cdd:cd07124 75 VQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 659 IC---------SRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDE 729
Cdd:cd07124 155 VPgednryvyrPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 730 VAESGLVKDGRVETVILTG----GTSTAKRMLAVRPDL----HLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQK 801
Cdd:cd07124 235 EVGDYLVEHPDVRFIAFTGsrevGLRIYERAAKVQPGQkwlkRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 802 CSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPP---------------GKTLTRGMKTLEDDET 866
Cdd:cd07124 315 CSACSRVIVHESVYD--EFLERLVERTKALKVGDPEDPEVYMGPVIDKGardrirryieigkseGRLLLGGEVLELAAEG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 867 WLVAPeHIVGQpnlyrpgvkwnVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSI 946
Cdd:cd07124 393 YFVQP-TIFAD-----------VPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREF 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1712455972 947 HAGNLYINRSTTGAIVLRQPFGGVGLSayGPGVKAGGPHYVLALMR 992
Cdd:cd07124 461 EVGNLYANRKITGALVGRQPFGGFKMS--GTGSKAGGPDYLLQFMQ 504
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
535-994 |
1.74e-116 |
|
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: 371.00 E-value: 1.74e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 535 VPLWVGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGD 614
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 615 MIGAMVAEGGKTIPEADPEISEAIDFCEFY----------------PLTVNHWAQQAgvdicsRGVVAVITPWNFPLAIP 678
Cdd:COG1012 85 LAALLTLETGKPLAEARGEVDRAADFLRYYagearrlygetipsdaPGTRAYVRREP------LGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 679 AGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLA 758
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 759 VRPD--LHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSA 836
Cdd:COG1012 239 AAAEnlKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDE--FVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 837 WDLETKMGPLIAPPGKTLTRGM--KTLEDDETWLVAPEHI-VGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRL 913
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYieDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 914 EEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAiVLRQPFGGVGLSAYGpgvKAGGPHYVLALMRI 993
Cdd:COG1012 397 EEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIG---REGGREGLEEYTET 472
|
.
gi 1712455972 994 T 994
Cdd:COG1012 473 K 473
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
544-993 |
3.24e-113 |
|
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: 361.46 E-value: 3.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 544 VTPEPDQMrESTDPSrPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEG 623
Cdd:pfam00171 2 VDSESETI-EVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 624 GKTIPEADPEISEAIDFCEFY--------PLTVNhwaQQAGVDICSR----GVVAVITPWNFPLAIPAGGIAAALACGNT 691
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYaglarrldGETLP---SDPGRLAYTRreplGVVGAITPWNFPLLLPAWKIAPALAAGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 692 VILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRmLAVRPDLHL---LAE 768
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRH-IAEAAAQNLkrvTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 769 TGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIA 848
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDE--FVEKLVEAAKKLKVGDPLDPDTDMGPLIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 849 PpgKTLTRGMKTLED--DETWLVAP--EHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTG 924
Cdd:pfam00171 314 K--AQLERVLKYVEDakEEGAKLLTggEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712455972 925 YGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRqPFGGVGLSAYGpgvKAGGPHYVLALMRI 993
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG---REGGPYGLEEYTEV 456
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
22-990 |
2.02e-99 |
|
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: 339.33 E-value: 2.02e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 22 DRSDVDRAIQLAADLLERAAELQtpqERRQQAELDRMVKHQTDKATMVEMTDQAFRTYSPARVADQLTHLLDvqGIPRFF 101
Cdd:COG0506 6 DEALRARAVALARRLVEAIRAAP---EGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--KSPSFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 102 SPVEQAMLRGFqSFGEYLPGVAVPLVKEKMRRETANVILPAEPELLTQHLRNRQSHGVGMNVNLLGEAVLGEDEVRNRMR 181
Cdd:COG0506 81 VNASTWGLMLT-LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 182 RYTEALRLDDVRC-----MSVKISTMDSQVSSLARQHTIDKVSDRLETLYRTAdREIDpstgnsKFIYLDMEEYRDLYLT 256
Cdd:COG0506 160 AYLEALEAIGAAGvdrpgVSVKLSALGPRYSPAQRERVVEELLERLRPLARAA-REAG------IFVTIDMEEYDRLDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 257 ADVLCQTLDRPGLEQ-TRAGIALQAYVPDSYPVMQRLIEWSTKRVAdgctGLTIRLVKGANLEMERVESSIGGHRQSPYM 335
Cdd:COG0506 233 LDVFERLLADPELAGwPGVGIVLQAYLKRAEADLDRLAALARRGGR----RIRVRLVKGAYWDPEIVRAQVHGWPYPVFT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 336 SKVETDANYKRMLRDLVAAArsGIVHIGLASHNLFDVALGLIWAGDL-VHTDAIQIEMLEGMANHQRRAI-GDHVENLLL 413
Cdd:COG0506 309 RKADTDANYLRCARKLLEAG--DAIYPQFATHNARTIAAALALAGERgRPPDRFEFQMLYGMGEDLQRALaAVDGGRLLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 414 YAPACRQDEFLNAIGYLIRRLDENTGPQNFLRHSYRLKPGSPEFKRLADDFRQSYAMIDSVSSAPRRNverkDAPEQPPV 493
Cdd:COG0506 387 YCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRR----QRRRRRRA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 494 AEHWSLYVNEPDTDWSVPANSVWAEQTLQKWkdqcgdqatvvPLWVGDQQVTPEPDQMRESTDPSRPGCVVcrypmASLD 573
Cdd:COG0506 463 RGGALAAALAAAAAAAALAAAAAAAAALAAA-----------AAGAAAAAAAAAVAVVPAAAAAVVAAAAA-----AAAA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 574 QVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFY-------PL 646
Cdd:COG0506 527 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAaaaaaarAA 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 647 TVNHWAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVcDAFWDAGVPRDALQMLPC 726
Cdd:COG0506 607 APPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAA-AALAALLLLLGGAGGGVL 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 727 EDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPDLHLLAETGGKNATIVTAM-------ADRDLAVKHVVQSAFGHAG 799
Cdd:COG0506 686 VLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGaaaaaaaAAAAAAVAAVAASAAASAS 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 800 QKCSATSLLLLEQEVFDDPKFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKTLTRGMKTLEDDETWLVAPEHIVGQPN 879
Cdd:COG0506 766 ASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPG 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 880 LYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTG 959
Cdd:COG0506 846 LLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGG 925
|
970 980 990
....*....|....*....|....*....|.
gi 1712455972 960 AIVLRQPFGGVGLSAYGPGVKAGGPHYVLAL 990
Cdd:COG0506 926 GGGGGGGGGGGGGGGGGGGGGGGGGGAGTLA 956
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
500-991 |
3.95e-96 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 317.26 E-value: 3.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 500 YVNEPDTDWSVPANSVWAEQTLQKWKDQCGDQatvVPLWVGDQQVTPEpDQMrESTDPSRPGCVVCRYPMASLDQVQQAV 579
Cdd:PRK03137 5 YKHEPFTDFSVEENVEAFEEALKKVEKELGQD---YPLIIGGERITTE-DKI-VSINPANKSEVVGRVSKATKELAEKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 580 SIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYPLTVNHWAQqaGVDI 659
Cdd:PRK03137 80 QAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLAD--GKPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 660 CSR------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCE 727
Cdd:PRK03137 158 ESRpgehnryfyiplGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 728 DEVAESGLVKDGRVETVILTG----GTSTAKRMLAVRP-DLHL---LAETGGKNATIVTAMADRDLAVKHVVQSAFGHAG 799
Cdd:PRK03137 238 GSEVGDYLVDHPKTRFITFTGsrevGLRIYERAAKVQPgQIWLkrvIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 800 QKCSATSLLLLEQEVFDDpkfqsLLADAVE---SLPVGSAWDlETKMGPLIAPpgKTLTRGMKTLE--DDETWLVAPEHI 874
Cdd:PRK03137 318 QKCSACSRAIVHEDVYDE-----VLEKVVEltkELTVGNPED-NAYMGPVINQ--ASFDKIMSYIEigKEEGRLVLGGEG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 875 VGQPNLY-RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYI 953
Cdd:PRK03137 390 DDSKGYFiQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYF 469
|
490 500 510
....*....|....*....|....*....|....*...
gi 1712455972 954 NRSTTGAIVLRQPFGGVGLSayGPGVKAGGPHYVLALM 991
Cdd:PRK03137 470 NRGCTGAIVGYHPFGGFNMS--GTDSKAGGPDYLLLFL 505
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
500-992 |
5.61e-91 |
|
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: 302.94 E-value: 5.61e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 500 YVNEPDTDWSVPANSVWAEQTLQKWKDQCGDQatvVPLWVGDQQVtpEPDQMRESTDPSRPGCVVCRYPMASLDQVQQAV 579
Cdd:TIGR01237 1 YKHEPFTDFADEENRQAFFKALATVKEQLGKT---YPLVINGERV--ETENKIVSINPCDKSEVVGTVSKASQEHAEHAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 580 SIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYPLTVNHWAQQAGVD- 658
Cdd:TIGR01237 76 QAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNs 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 659 ---------ICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDE 729
Cdd:TIGR01237 156 regetnqyvYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 730 VAESGLVKDGRVETVILTG----GTSTAKRMLAVRP-DLHL---LAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQK 801
Cdd:TIGR01237 236 EVGDYLVDHPKTSLITFTGsrevGTRIFERAAKVQPgQKHLkrvIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 802 CSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKTLTRGMKTLEDDETWLVAPEHIVGQPNLY 881
Cdd:TIGR01237 316 CSAGSRAVVHEKVYD--EVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDSKGYF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 882 -RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGA 960
Cdd:TIGR01237 394 iGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGA 473
|
490 500 510
....*....|....*....|....*....|..
gi 1712455972 961 IVLRQPFGGVGLSayGPGVKAGGPHYVLALMR 992
Cdd:TIGR01237 474 IVGYQPFGGFKMS--GTDSKAGGPDYLALFMQ 503
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
196-988 |
1.49e-90 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 315.60 E-value: 1.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 196 SVKISTMDSQVSSLARQHTIDKVSDRLETLYRTAdREIDPStgnskfIYLDMEEYRDLYLTADVLCQTLDRPGLEQ-TRA 274
Cdd:PRK11904 248 SIKLSALHPRYEAAQRERVLAELVPRVLELARLA-KEANIG------LTIDAEEADRLELSLDLFEALFRDPSLKGwGGF 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 275 GIALQAYVPDSYPVmqrlIEWSTKRVADGCTGLTIRLVKGANLEMERVESSIGGHRQSP-YMSKVETDANY----KRMLr 349
Cdd:PRK11904 321 GLAVQAYQKRALPV----LDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPvFTRKAATDVSYlacaRKLL- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 350 dlvaAARSgivHI--GLASHNLFDVALGLIWAGDlvhtDAIQIEMLEGMANHQRRAIGDHVE-NLLLYAPACRQDEFLna 426
Cdd:PRK11904 396 ----SARG---AIypQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALLDAPGiPCRIYAPVGSHKDLL-- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 427 iGYLIRRLDENTGPQNFLrHsyrlkpgspefkRLADdfrqSYAMIDSVSSAPRRNVERKDAPEQPPVAEHWSLY----VN 502
Cdd:PRK11904 463 -PYLVRRLLENGANSSFV-H------------RLVD----PDVPIEELVADPVEKLRSFETLPNPKIPLPRDIFgperKN 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 503 EPDTDWSVPANSVWAEQTLQKWKDQcgdQATVVPLWVGDQQVtpepdqmRESTDPSRPGCVVCRYPMASLDQVQQAVSIA 582
Cdd:PRK11904 525 SKGLNLNDRSELEPLAAAIAAFLEK---QWQAGPIINGEGEA-------RPVVSPADRRRVVGEVAFADAEQVEQALAAA 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 583 ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYpltvnhwAQQA------- 655
Cdd:PRK11904 595 RAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYY-------AAQArrlfgap 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 656 -------GVD----ICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQML 724
Cdd:PRK11904 668 eklpgptGESnelrLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 725 PCEDEVAESGLVKDGRVETVILTGGTSTAK---RMLAVR--PDLHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAG 799
Cdd:PRK11904 748 PGDGATVGAALTADPRIAGVAFTGSTETARiinRTLAARdgPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAG 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 800 QKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLI-APPGKTLTRGMKTLEDDETWLVAPEhivgqp 878
Cdd:PRK11904 828 QRCSALRVLFVQEDIAD--RVIEMLKGAMAELKVGDPRLLSTDVGPVIdAEAKANLDAHIERMKREARLLAQLP------ 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 879 nlyRPGVKWN---VAP-----GSFSHLT-ELFGPVLGVMPF--SRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIH 947
Cdd:PRK11904 900 ---LPAGTENghfVAPtafeiDSISQLErEVFGPILHVIRYkaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVR 976
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1712455972 948 AGNLYINRSTTGAIVLRQPFGGVGLSAYGPgvKAGGPHYVL 988
Cdd:PRK11904 977 VGNVYVNRNQIGAVVGVQPFGGQGLSGTGP--KAGGPHYLL 1015
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
275-1204 |
2.05e-89 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 314.88 E-value: 2.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 275 GIALQAYVPDSYPVMQRLIEWSTKrvadgcTG--LTIRLVKGA--NLEMERveSSIGGHRQSP-YMSKVETDANYKRMLR 349
Cdd:PRK11905 320 GFVVQAYQKRCPFVIDYLIDLARR------SGrrLMVRLVKGAywDAEIKR--AQVDGLEGFPvFTRKVHTDVSYIACAR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 350 DLVAAArsGIVHIGLASHNLFDVALGLIWAGDlvhTDAIQIEMLEGM-----------ANHQRRA-----IGDHvENLLl 413
Cdd:PRK11905 392 KLLAAR--DVIYPQFATHNAQTLAAIYELAGG---KGDFEFQCLHGMgeplydqvvgkEKLGRPCriyapVGTH-ETLL- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 414 yapacrqdeflnaiGYLIRRLDENTGPQNFLrhsyrlkpgspefKRLADDfRQSyamIDSVSSAPRRNVER-KDAPeQPP 492
Cdd:PRK11905 465 --------------AYLVRRLLENGANSSFV-------------NRIVDE-NVP---VEELIADPVEKVAAmGVAP-HPQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 493 VAEHWSLYVNEPDTDWSVPANSvwaEQTLQKWKDQCgdQATVVPLWVGDQQV--TPEPDQMRESTDPSRPGCVVCRYPMA 570
Cdd:PRK11905 513 IPLPRDLYGPERRNSKGLDLSD---EATLAALDEAL--NAFAAKTWHAAPLLagGDVDGGTRPVLNPADHDDVVGTVTEA 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 571 SLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYpltvnh 650
Cdd:PRK11905 588 SAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYY------ 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 651 wAQQA-----GVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLP 725
Cdd:PRK11905 662 -AAQArrllnGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLP 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 726 CEDEVAESGLVKDGRVETVILTGGTSTAK---RMLAVR--PDLHLLAETGGKNATIV--TAMADRdlAVKHVVQSAFGHA 798
Cdd:PRK11905 741 GDGRTVGAALVADPRIAGVMFTGSTEVARliqRTLAKRsgPPVPLIAETGGQNAMIVdsSALPEQ--VVADVIASAFDSA 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 799 GQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKtltrgmKTLEDdetwlvapeHI---- 874
Cdd:PRK11905 819 GQRCSALRVLCLQEDVAD--RVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQ------ANIEA---------HIeamr 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 875 -VGQPnLYRPGVKWNVAPGSF-----------SHLT-ELFGPVLGVMPF--SRLEEAIEIVRSTGYGLTSGLES-LDDRe 938
Cdd:PRK11905 882 aAGRL-VHQLPLPAETEKGTFvaptlieidsiSDLErEVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSrIDET- 959
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 939 IELWKQSIHAGNLYINRSTTGAIVLRQPFGGVGLSAYGPgvKAGGPHYVLALMRiTDSGQTTPSTDSVSTTVAPStlgsk 1018
Cdd:PRK11905 960 IAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGP--KAGGPLYLGRLVR-EAPTPIPPAHESVDTDAAAR----- 1031
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 1019 ptdALTRWVGELSGTGIDDELRRSLMQMVDECSRAMQVEfSGSHDTVRLLGQDNLrryLSVkgltirveaGDSQSDLLSA 1098
Cdd:PRK11905 1032 ---DFLAWLDKEGKAALAAAARDARARSALGLEQELPGP-TGESNLLSLHPRGRV---LCV---------ADTEEALLRQ 1095
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 1099 VIAAVSVQTPVTLSIDPkVPDEWIEWLDAAADAVPGLVDPIdETDSDLADRIAAGDVTRLRRLtpsvpgSGSLAACCEHF 1178
Cdd:PRK11905 1096 LAAALATGNVAVVAADS-GLAAALADLPGLVAARIDWTQDW-EADDPFAGALLEGDAERARAV------RQALAARPGAI 1167
|
970 980
....*....|....*....|....*.
gi 1712455972 1179 VTVIsePVLSCAAIECLRYLDEQSIS 1204
Cdd:PRK11905 1168 VPLI--AAEPTDAYDLARLVEERSVS 1191
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
546-1033 |
2.84e-88 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 311.10 E-value: 2.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 546 PEPDQMRESTDPSRPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGK 625
Cdd:COG4230 566 AASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 626 TIPEADPEISEAIDFCEFYpltvnhwAQQA------GVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASE 699
Cdd:COG4230 646 TLPDAIAEVREAVDFCRYY-------AAQArrlfaaPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQ 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 700 TVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAK---RMLAVR--PDLHLLAETGGKNA 774
Cdd:COG4230 719 TPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinRTLAARdgPIVPLIAETGGQNA 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 775 TIV--TAMADRdlAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIappgk 852
Cdd:COG4230 799 MIVdsSALPEQ--VVDDVLASAFDSAGQRCSALRVLCVQEDIAD--RVLEMLKGAMAELRVGDPADLSTDVGPVI----- 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 853 tltrgmktleDDETWLVAPEHI-----VGQPnLYRPGVKWN------VAP-----GSFSHLT-ELFGPVLGVMPFSR--L 913
Cdd:COG4230 870 ----------DAEARANLEAHIermraEGRL-VHQLPLPEEcangtfVAPtlieiDSISDLErEVFGPVLHVVRYKAdeL 938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 914 EEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQPFGGVGLSAYGPgvKAGGPHYVLALMri 993
Cdd:COG4230 939 DKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGP--KAGGPHYLLRFA-- 1014
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1712455972 994 tdsgqtTPSTDSVSTTvapSTLGSKPTDALTRWVGELSGT 1033
Cdd:COG4230 1015 ------TERTVTVNTT---AAGGNASLLALGDWLASLLGA 1045
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
576-993 |
3.07e-87 |
|
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: 289.88 E-value: 3.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 576 QQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYPLTVNHWA--- 652
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 653 -------QQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLP 725
Cdd:cd07078 81 ipspdpgELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 726 CEDEVAESGLVKDGRVETVILTGGTSTAKR-MLAVRPDL-HLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCS 803
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAiMRAAAENLkRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 804 ATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAP---------------PGKTLTRGMKTLEDDETWL 868
Cdd:cd07078 241 AASRLLVHESIYD--EFVERLVERVKALKVGNPLDPDTDMGPLISAaqldrvlayiedakaEGAKLLCGGKRLEGGKGYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 869 VAPeHIVgqpnlyrpgvkWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHA 948
Cdd:cd07078 319 VPP-TVL-----------TDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEA 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1712455972 949 GNLYINRSTTGAiVLRQPFGGVGLSAYGpgvKAGGPHYVLALMRI 993
Cdd:cd07078 387 GTVWINDYSVGA-EPSAPFGGVKQSGIG---REGGPYGLEEYTEP 427
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
525-988 |
2.97e-81 |
|
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: 275.61 E-value: 2.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 525 KDQCGDQATVVPLWVGDQQVTPEPDQMreSTDPSRPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGA 604
Cdd:cd07083 9 RRVKEEFGRAYPLVIGGEWVDTKERMV--SVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 605 AQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFY-----------PLTVNHWAQQAGVDICSRGVVAVITPWNF 673
Cdd:cd07083 87 ADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYaraalrlrypaVEVVPYPGEDNESFYVGLGAGVVISPWNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 674 PLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTA 753
Cdd:cd07083 167 PVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 754 K---RMLAVRPD-----LHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFddPKFQSLLA 825
Cdd:cd07083 247 KkiyEAAARLAPgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAY--EPVLERLL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 826 DAVESLPVGSAWDLETKMGPLIAPPGK--------------TLTRGMKtLEDDETWLVAPEHIVGQPNLYRPGVKwnvap 891
Cdd:cd07083 325 KRAERLSVGPPEENGTDLGPVIDAEQEakvlsyiehgknegQLVLGGK-RLEGEGYFVAPTVVEEVPPKARIAQE----- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 892 gsfshltELFGPVLGVM--PFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQPFGG 969
Cdd:cd07083 399 -------EIFGPVLSVIryKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGG 471
|
490
....*....|....*....
gi 1712455972 970 VGLSayGPGVKAGGPHYVL 988
Cdd:cd07083 472 FKLS--GTNAKTGGPHYLR 488
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
539-994 |
7.53e-77 |
|
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: 262.28 E-value: 7.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 539 VGDQQVTPEPDQMRESTDPSRPGCVVCRYPMASLDQVQQAVSiAASDSNP-WKDTSLEHRHEVLRGAAQRMRQRRGDMIG 617
Cdd:cd07131 3 IGGEWVDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVE-AAREAFPeWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 618 AMVAEGGKTIPEADPEISEAIDFCEFYPLTVNHwaqQAGVDICS-------------RGVVAVITPWNFPLAIPAGGIAA 684
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRR---LFGETVPSelpnkdamtrrqpIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 685 ALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRM--LAVRPD 762
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIgeTCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 763 LHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETK 842
Cdd:cd07131 239 KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYD--EFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 843 MGPLIAPPG--KTLT-------RGMKTLEDDEtwlVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRL 913
Cdd:cd07131 317 MGPLINEAQleKVLNyneigkeEGATLLLGGE---RLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 914 EEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVlRQPFGGVGLSayGPGVKAGGPHYVLALMRI 993
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKS--GNGHREAGTTALDAFTEW 470
|
.
gi 1712455972 994 T 994
Cdd:cd07131 471 K 471
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
550-993 |
1.54e-75 |
|
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: 259.46 E-value: 1.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 550 QMRESTDPSRPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPE 629
Cdd:TIGR01238 51 EAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 630 ADPEISEAIDFCEFYPLTVNHWAQQAGVDicSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCD 709
Cdd:TIGR01238 131 AIAEVREAVDFCRYYAKQVRDVLGEFSVE--SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 710 AFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRM---LAVR--PDLHLLAETGGKNATIVTAMADRD 784
Cdd:TIGR01238 209 LMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqtLAQRedAPVPLIAETGGQNAMIVDSTALPE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 785 LAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLI-------------APPG 851
Cdd:TIGR01238 289 QVVRDVLRSAFDSAGQRCSALRVLCVQEDVAD--RVLTMIQGAMQELKVGVPHLLTTDVGPVIdaeakqnllahieHMSQ 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 852 KTLTRGMKTLEDDETW----LVAPEHIvgqpnlyrpgvkwnvAPGSFSHLT-ELFGPVLGVMPFSR--LEEAIEIVRSTG 924
Cdd:TIGR01238 367 TQKKIAQLTLDDSRACqhgtFVAPTLF---------------ELDDIAELSeEVFGPVLHVVRYKAreLDQIVDQINQTG 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712455972 925 YGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQPFGGVGLSAYGPgvKAGGPHYVLALMRI 993
Cdd:TIGR01238 432 YGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGP--KAGGPHYLYRLTQV 498
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
552-977 |
1.60e-75 |
|
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: 258.72 E-value: 1.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 552 RESTDPSRPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRgDMIGAMVA-EGGKTIPEA 630
Cdd:cd07097 16 EENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARK-EELARLLTrEEGKTLPEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 631 DPEISEAIDFCEFYPLTVNHW------AQQAGVDICSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASET 700
Cdd:cd07097 95 RGEVTRAGQIFRYYAGEALRLsgetlpSTRPGVEVETTreplGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 701 VWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKR--MLAVRPDLHLLAETGGKNATIVT 778
Cdd:cd07097 175 PASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRiaAAAAARGARVQLEMGGKNPLVVL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 779 AMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPPgktltrgm 858
Cdd:cd07097 255 DDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHD--RFVEALVERTKALKVGDALDEGVDIGPVVSER-------- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 859 kTLEDDETWL-----VAPEHIVGQPNLYRPGVKWNVAPGSFSHLT--------ELFGPVLGVMPFSRLEEAIEIVRSTGY 925
Cdd:cd07097 325 -QLEKDLRYIeiarsEGAKLVYGGERLKRPDEGYYLAPALFAGVTndmriareEIFGPVAAVIRVRDYDEALAIANDTEF 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1712455972 926 GLTSGLESLDDREIELWKQSIHAGNLYINRSTTGaIVLRQPFGGVGLSAYGP 977
Cdd:cd07097 404 GLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG-VDYHVPFGGRKGSSYGP 454
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
307-1165 |
3.01e-75 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 273.77 E-value: 3.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 307 LTIRLVKGANLEMERVESSIGGHRQSP-YMSKVETDANYKRMLRDLVAAarSGIVHIGLASHNLFDVALGLIWAGDLVHT 385
Cdd:PRK11809 428 LMIRLVKGAYWDSEIKRAQVDGLEGYPvYTRKVYTDVSYLACARKLLAV--PNLIYPQFATHNAHTLAAIYHLAGQNYYP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 386 DAIQIEMLEGMANH-QRRAIGDHVENLL-----LYAPACRQDEFLnaiGYLIRRLDENTGPQNFLrhsyrlkpgspefKR 459
Cdd:PRK11809 506 GQYEFQCLHGMGEPlYEQVVGKVADGKLnrpcrIYAPVGTHETLL---AYLVRRLLENGANTSFV-------------NR 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 460 LADDfrqSYAMIDSVSSaPRRNVERKDAPEQPPVAEH------WSLY----VNEPDTDWsvpAN--------SVWAEQTL 521
Cdd:PRK11809 570 IADT---SLPLDELVAD-PVEAVEKLAQQEGQLGLPHpkiplpRDLYgkgrANSAGLDL---ANehrlaslsSALLASAH 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 522 QKWKdqcgdqatVVPLwVGDQQVTPEPDQMRestDPSRPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVL 601
Cdd:PRK11809 643 QKWQ--------AAPM-LEDPVAAGEMSPVI---NPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAIL 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 602 RGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYpltvnhwAQQAGVDICSR-----GVVAVITPWNFPLA 676
Cdd:PRK11809 711 ERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYY-------AGQVRDDFDNDthrplGPVVCISPWNFPLA 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 677 IPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAK-- 754
Cdd:PRK11809 784 IFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARll 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 755 -RMLAVRPD-----LHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAV 828
Cdd:PRK11809 864 qRNLAGRLDpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVAD--RTLKMLRGAM 941
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 829 ESLPVGSAWDLETKMGPLIAPPGKT-LTRGMKTLEDDETwlvaPEHIVGQPNlyrpGVKWN----VAP-----GSFSHLT 898
Cdd:PRK11809 942 AECRMGNPDRLSTDIGPVIDAEAKAnIERHIQAMRAKGR----PVFQAAREN----SEDWQsgtfVPPtlielDSFDELK 1013
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 899 -ELFGPVLGVMPFSR--LEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQPFGGVGLSAY 975
Cdd:PRK11809 1014 rEVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGT 1093
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 976 GPgvKAGGPHYVLALMritdsgQTTPStDSVSTTVApSTLGSKPTDALTRWVGELSGTGIDDELRRSLMQMVDECSRAMQ 1055
Cdd:PRK11809 1094 GP--KAGGPLYLYRLL------ATRPE-DALAVTLA-RQDAEYPVDAQLRAALLAPLTALREWAAEREPELAALCDQYAE 1163
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 1056 VEFSGshdTVRLL----GQDNLRRYLSVKgltiRVEA-GDSQSDLLSAVIAAVSVQTPVTLSIDPkVPDEWIEWLDAAAD 1130
Cdd:PRK11809 1164 LAQAG---TTRLLpgptGERNTYTLLPRE----RVLClADTEQDALTQLAAVLAVGSQALWPDDA-LHRALVAALPAAVQ 1235
|
890 900 910
....*....|....*....|....*....|....*
gi 1712455972 1131 AVPGLVDPIDETDSDLADRIAAGDVTRLRRLTPSV 1165
Cdd:PRK11809 1236 ARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQV 1270
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
589-993 |
9.64e-71 |
|
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: 241.36 E-value: 9.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 589 WKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYPLTVNHWAqqaGVDICS------- 661
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLG---GPELPSpdpggea 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 662 ------RGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGL 735
Cdd:cd06534 87 yvrrepLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 736 VKDGRVETVILTGGTSTAKR-MLAVRPDL-HLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQE 813
Cdd:cd06534 167 LSHPRVDKISFTGSTAVGKAiMKAAAENLkPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHES 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 814 VFDdpKFQSLLAdaveslpvgsawdletkmgpliappgktltrgmktleddetwlvapehivgqpnlyrpGVKWNVAPGS 893
Cdd:cd06534 247 IYD--EFVEKLV----------------------------------------------------------TVLVDVDPDM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 894 FSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAiVLRQPFGGVGLS 973
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GPEAPFGGVKNS 345
|
410 420
....*....|....*....|
gi 1712455972 974 AYGpgvKAGGPHYVLALMRI 993
Cdd:cd06534 346 GIG---REGGPYGLEEYTRT 362
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
539-970 |
4.77e-68 |
|
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: 237.46 E-value: 4.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 539 VGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRgDMIGA 618
Cdd:cd07086 2 VIGGEWVGSGGETFTSRNPAN-GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKK-EALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 619 MVA-EGGKTIPEADPEISEAIDFCEF--------YPLTV-----NHWAQQAGVDIcsrGVVAVITPWNFPLAIPAGGIAA 684
Cdd:cd07086 80 LVSlEMGKILPEGLGEVQEMIDICDYavglsrmlYGLTIpserpGHRLMEQWNPL---GVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 685 ALACGNTVILKPASETVWVA----AMVCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKR---ML 757
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAiavtKILAEVLEKNGLPPGVVNLVTGGGDGGEL-LVHDPRVPLVSFTGSTEVGRRvgeTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 758 AVRPDLHLLaETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAW 837
Cdd:cd07086 236 ARRFGRVLL-ELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYD--EFLERLVKAYKQVRIGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 838 DLETKMGPLIAPPG-KTLTRGMKTL-EDDETWLVAPEHIVGQP--NLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRL 913
Cdd:cd07086 313 DEGTLVGPLINQAAvEKYLNAIEIAkSQGGTVLTGGKRIDGGEpgNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 914 EEAIEIVRSTGYGLTSGLESLDDREIELW--KQSIHAGNLYINRSTTGA-IVLrqPFGGV 970
Cdd:cd07086 393 EEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAeIGG--AFGGE 450
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
149-446 |
1.10e-65 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 224.29 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 149 QHLRNRQSHGVGMNVNLLGEAVLGEDEVRNRMRRYTEALRLDDVRC----------MSVKISTMDSQVSSLARQHTIDKV 218
Cdd:pfam01619 3 KTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAgpwplgprpgISVKLSALHPRYEPLERERVMAEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 219 SDRLETLYRTAdREIDpstgnsKFIYLDMEEYRDLYLTADVLCQTLDRPGLEQ-TRAGIALQAYVPDSYPVMQRLIEWST 297
Cdd:pfam01619 83 LERLRPLCRLA-KELG------VRLNIDAEEADRLDLTLDLFERLLAEPELRGwNGVGITLQAYLKDALAVLDWLLELAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 298 KRvadgCTGLTIRLVKGANLEMERVESSIGGhRQSP-YMSKVETDANYKRMLRDLVAAarSGIVHIGLASHNLFDVALGL 376
Cdd:pfam01619 156 RR----GRPLGVRLVKGAYWDSEIKRAQQGG-WPYPvFTRKEATDANYEACARFLLEN--HDRIYPQFATHNARSVAAAL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712455972 377 IWAGDL-VHTDAIQIEMLEGMANHQRRAIGDHVENLLLYAPACRQDEFLnaiGYLIRRLDENTGPQNFLRH 446
Cdd:pfam01619 229 ALAEELgIPPRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEELL---AYLVRRLLENTANSSFVRR 296
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
575-984 |
9.62e-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: 9.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 575 VQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFC------------E 642
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILreaaglprrpegE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 643 FYPltvnhwAQQAGVDICSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASET-VWVAAMVCDAFWDAGVP 717
Cdd:cd07104 82 ILP------SDVPGKESMVRrvplGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTpVTGGLLIAEIFEEAGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 718 RDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAkRMLAVRPDLHL---LAETGGKNATIVTAMADRDLAVKHVVQSA 794
Cdd:cd07104 156 KGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVG-RHIGELAGRHLkkvALELGGNNPLIVLDDADLDLAVSAAAFGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 795 FGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPpgKTLTRGMKTLED---DETWLVAP 871
Cdd:cd07104 235 FLHQGQICMAAGRILVHESVYDE--FVEKLVAKAKALPVGDPRDPDTVIGPLINE--RQVDRVHAIVEDavaAGARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 872 EHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREIELWKQsIHAGN 950
Cdd:cd07104 311 GTYEG--LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlERAMAFAER-LETGM 387
|
410 420 430
....*....|....*....|....*....|....*.
gi 1712455972 951 LYINRSTT--GAIVlrqPFGGVGLSAYGpgvKAGGP 984
Cdd:cd07104 388 VHINDQTVndEPHV---PFGGVKASGGG---RFGGP 417
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
561-980 |
4.05e-62 |
|
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: 219.39 E-value: 4.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDF 640
Cdd:cd07149 9 GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 641 CEF------------YPL--TVNHWAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAM 706
Cdd:cd07149 89 LRLsaeeakrlagetIPFdaSPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 707 VCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTA---KRMLAVRPdlhLLAETGGKNATIVTAMADR 783
Cdd:cd07149 169 LAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGeaiARKAGLKK---VTLELGSNAAVIVDADADL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 784 DLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPpgKTLTRGMKTLE- 862
Cdd:cd07149 246 EKAVERCVSGAFANAGQVCISVQRIFVHEDIYDE--FLERFVAATKKLVVGDPLDEDTDVGPMISE--AEAERIEEWVEe 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 863 --DDETWLVAPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGL--ESLDD-- 936
Cdd:cd07149 322 avEGGARLLTGGKRDG--AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVftNDLQKal 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1712455972 937 ---REIElwkqsihAGNLYINRSTTgaivLR---QPFGGVGLSAYG-PGVK 980
Cdd:cd07149 400 kaaRELE-------VGGVMINDSST----FRvdhMPYGGVKESGTGrEGPR 439
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
552-985 |
9.95e-61 |
|
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: 215.27 E-value: 9.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 552 RESTDPSrPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEAD 631
Cdd:cd07150 1 FDDLNPA-DGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 632 PEISEAIDFCEfypltvnhwaQQAGVdiCSR----------------------GVVAVITPWNFPLAIPAGGIAAALACG 689
Cdd:cd07150 80 FETTFTPELLR----------AAAGE--CRRvrgetlpsdspgtvsmsvrrplGVVAGITPFNYPLILATKKVAFALAAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 690 NTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAkRMLAVRPDLHL---L 766
Cdd:cd07150 148 NTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG-REIAEKAGRHLkkiT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 767 AETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPL 846
Cdd:cd07150 227 LELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE--FVKKFVARASKLKVGDPRDPDTVIGPL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 847 IAPP---------GKTLTRGMKtleddetwLVAPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAI 917
Cdd:cd07150 305 ISPRqverikrqvEDAVAKGAK--------LLTGGKYDG--NFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEAL 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712455972 918 EIVRSTGYGLTSGLESLD-DREIELwKQSIHAGNLYINRST--TGAIVlrqPFGGVGLSAYGpgvKAGGPH 985
Cdd:cd07150 375 ELANDTEYGLSAAILTNDlQRAFKL-AERLESGMVHINDPTilDEAHV---PFGGVKASGFG---REGGEW 438
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
554-976 |
3.26e-60 |
|
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: 213.97 E-value: 3.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 554 STDPSRpGCVVCRYPMASLDQVQQAVSiAASDSNP-WKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADP 632
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVA-AAKEAFPgWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 633 -EISEAIDFCEFYPLTVNH-----WAQQAG-VDICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVW 702
Cdd:cd07093 79 rDIPRAAANFRFFADYILQldgesYPQDGGaLNYVLRqpvGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 703 VAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKR-MLAVRPDL-HLLAETGGKNATIVTAM 780
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTiMRAAAPNLkPVSLELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 781 ADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPP---------- 850
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDE--FLERFVERAKALKVGDPLDPDTEVGPLISKEhlekvlgyve 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 851 -----GKTLTRGMKtleddetwlVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGY 925
Cdd:cd07093 317 laraeGATILTGGG---------RPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1712455972 926 GLTSGLESLDDREIELWKQSIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07093 388 GLAAYVWTRDLGRAHRVARRLEAGTVWVN--CWLVRDLRTPFGGVKASGIG 436
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
563-985 |
1.39e-57 |
|
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: 206.13 E-value: 1.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 563 VVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCE 642
Cdd:cd07103 9 VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 643 FYpltvnhwAQQA----GVDICSR-------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAA 705
Cdd:cd07103 89 WF-------AEEArriyGRTIPSPapgkrilvikqpvGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 706 MVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLA------VRPDLhllaETGGkNA-TIVT 778
Cdd:cd07103 162 ALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAqaadtvKRVSL----ELGG-NApFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 779 AMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPpgKTLTRgM 858
Cdd:cd07103 237 DDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYD--EFVEKLVERVKKLKVGNGLDEGTDMGPLINE--RAVEK-V 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 859 KTLEDDE-----TWLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLES 933
Cdd:cd07103 312 EALVEDAvakgaKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1712455972 934 LDDREIelWK--QSIHAGNLYINRSTTGAIVLrqPFGGVGLSAYGpgvKAGGPH 985
Cdd:cd07103 392 RDLARA--WRvaEALEAGMVGINTGLISDAEA--PFGGVKESGLG---REGGKE 438
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
559-976 |
1.76e-57 |
|
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: 205.92 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 559 RPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAI 638
Cdd:cd07099 4 ATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 639 DFCEFY----------------PLTVNHWAQqagVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVW 702
Cdd:cd07099 84 EAIDWAarnaprvlaprkvptgLLMPNKKAT---VEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 703 VAAMVCDAFWDAGVPRDALQMLPCEDEVAEsGLVkDGRVETVILTGGTSTAKRML--AVRPDLHLLAETGGKNATIVTAM 780
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGA-ALI-DAGVDKVAFTGSVATGRKVMaaAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 781 ADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPP---------G 851
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDE--FVARLVAKARALRPGADDIGDADIGPMTTARqldivrrhvD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 852 KTLTRGMKTleddetwLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGL 931
Cdd:cd07099 317 DAVAKGAKA-------LTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1712455972 932 ESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07099 390 FSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
569-984 |
5.80e-57 |
|
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: 204.45 E-value: 5.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 569 MASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFC-EFYPLT 647
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELhEAAGLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 648 VNHWAQ----QAG-VDICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASET-VWVAAMVCDAFWDAGVPR 718
Cdd:cd07152 89 TQPQGEilpsAPGrLSLARRvplGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTpVSGGVVIARLFEEAGLPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 719 DALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKRMLAVRPDL----HLlaETGGKNATIVTAMADRDLAVKHVVQSA 794
Cdd:cd07152 169 GVLHVLPGGADAGEA-LVEDPNVAMISFTGSTAVGRKVGEAAGRHlkkvSL--ELGGKNALIVLDDADLDLAASNGAWGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 795 FGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAppGKTLTRGMKTLED---DETWLVAP 871
Cdd:cd07152 246 FLHQGQICMAAGRHLVHESVAD--AYTAKLAAKAKHLPVGDPATGQVALGPLIN--ARQLDRVHAIVDDsvaAGARLEAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 872 EHIVGQpnLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREIELWKQsIHAGN 950
Cdd:cd07152 322 GTYDGL--FYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDvGRAMALADR-LRTGM 398
|
410 420 430
....*....|....*....|....*....|....
gi 1712455972 951 LYINRSTTGAIVLrQPFGGVGLSayGPGVKAGGP 984
Cdd:cd07152 399 LHINDQTVNDEPH-NPFGGMGAS--GNGSRFGGP 429
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
544-955 |
6.01e-57 |
|
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: 204.81 E-value: 6.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 544 VTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEG 623
Cdd:cd07088 7 VPSSSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 624 GKTIPEADPEISEAIDFCEFYPltvnHWAQQAGVDICS--------------RGVVAVITPWNFPLAIPAGGIAAALACG 689
Cdd:cd07088 86 GKTLSLARVEVEFTADYIDYMA----EWARRIEGEIIPsdrpnenififkvpIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 690 NTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKR-MLAVRPDL-HLLA 767
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKiMEAAAENItKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 768 ETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLI 847
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDE--FMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 848 APPGKTLTRGM--KTLEDDETWLV---APEhiVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRS 922
Cdd:cd07088 320 NEAALDKVEEMveRAVEAGATLLTggkRPE--GEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430
....*....|....*....|....*....|...
gi 1712455972 923 TGYGLTSGLESLDDREIELWKQSIHAGNLYINR 955
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
574-973 |
6.24e-57 |
|
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: 203.66 E-value: 6.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 574 QVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAI--------DFCEFYP 645
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAgkidisikAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 646 LTVNHWAQ-QAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQML 724
Cdd:cd07095 81 ERATPMAQgRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 725 PCEDEVAESgLVKDGRVETVILTGGTSTAK---RMLAVRPDLHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQK 801
Cdd:cd07095 161 QGGRETGEA-LAAHEGIDGLLFTGSAATGLllhRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 802 CSATSLLLLEQEVFDDPKFQSLLAdAVESLPVGSAWDLETKMGPLI--APPGKTLTRGMKTLEDDETWLVAPEHIVGQPN 879
Cdd:cd07095 240 CTCARRLIVPDGAVGDAFLERLVE-AAKRLRIGAPDAEPPFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMERLVAGTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 880 LYRPGV----KWNVAPGSfshltELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINR 955
Cdd:cd07095 319 FLSPGIidvtDAADVPDE-----EIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNR 393
|
410
....*....|....*...
gi 1712455972 956 STTGAiVLRQPFGGVGLS 973
Cdd:cd07095 394 PTTGA-SSTAPFGGVGLS 410
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
568-980 |
2.80e-54 |
|
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: 196.80 E-value: 2.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 568 PMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFC------ 641
Cdd:cd07145 16 PSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFklaaee 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 642 ------EFYPLTvNHWAQQAGVDICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFW 712
Cdd:cd07145 96 akvlrgETIPVD-AYEYNERRIAFTVRepiGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 713 DAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTG----GTSTAKRmlAVRPDLHLLAETGGKNATIVTAMADRDLAVK 788
Cdd:cd07145 175 EAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGstavGLLIASK--AGGTGKKVALELGGSDPMIVLKDADLERAVS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 789 HVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPpgKTLTRGMKTLEDDET-- 866
Cdd:cd07145 253 IAVRGRFENAGQVCNAVKRILVEEEVYD--KFLKLLVEKVKKLKVGDPLDESTDLGPLISP--EAVERMENLVNDAVEkg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 867 --WLVAPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQ 944
Cdd:cd07145 329 gkILYGGKRDEG--SFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVAR 406
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1712455972 945 SIHAGNLYINRSTTgaivLRQ---PFGGVGLSAYG-PGVK 980
Cdd:cd07145 407 ELEAGGVVINDSTR----FRWdnlPFGGFKKSGIGrEGVR 442
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
568-976 |
2.53e-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: 191.30 E-value: 2.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 568 PMASLDQVQQAVSIA--ASDSNPWKdTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADP--------EISEA 637
Cdd:cd07089 14 PDAGAADVDAAIAAArrAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmqvdgpigHLRYF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 638 IDFCEFYP----LTVNHWAQQAGVDICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDA 710
Cdd:cd07089 93 ADLADSFPwefdLPVPALRGGPGRRVVRRepvGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 711 FWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPDL--HLLAETGGKNATIVTAMADRDLAVK 788
Cdd:cd07089 173 IAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATlkRVLLELGGKSANIVLDDADLAAAAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 789 HVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKTLTRGMKTLEDDE--T 866
Cdd:cd07089 253 AAVGVCMHNAGQGCALTTRLLVPRSRYDE--VVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEgaR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 867 WLVAPEHIVGQPNLY--RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREIELWK 943
Cdd:cd07089 331 LVTGGGRPAGLDKGFyvEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADvDRAYRVAR 410
|
410 420 430
....*....|....*....|....*....|....*
gi 1712455972 944 QsIHAGNLYINrsttGAIVLR--QPFGGVGLSAYG 976
Cdd:cd07089 411 R-IRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
550-976 |
2.86e-52 |
|
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: 191.63 E-value: 2.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 550 QMRESTDPSRP------GCVVCRYPMASLDQVQQAVSIA-ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAE 622
Cdd:cd07082 9 EWKESSGKTIEvyspidGEVIGSVPALSALEILEAAETAyDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 623 GGKTIPEADPEISEAIDFCEF-----------YPLTVNHWAQQAGVDICSR---GVVAVITPWNFPLAIPAGGIAAALAC 688
Cdd:cd07082 89 IGKTLKDALKEVDRTIDYIRDtieelkrldgdSLPGDWFPGTKGKIAQVRReplGVVLAIGPFNYPLNLTVSKLIPALIM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 689 GNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPDLHLLAE 768
Cdd:cd07082 169 GNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRLVLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 769 TGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIA 848
Cdd:cd07082 249 LGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVAD--ELVELLKEEVAKLKVGMPWDNGVDITPLID 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 849 PpgKTLTRGMKTLEDDET---WLVAPEHIVGqPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGY 925
Cdd:cd07082 327 P--KSADFVEGLIDDAVAkgaTVLNGGGREG-GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNY 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1712455972 926 GLTSGLESLDDREIELWKQSIHAGNLYINRSTT-GAIVLrqPFGGVGLSAYG 976
Cdd:cd07082 404 GLQASIFTKDINKARKLADALEVGTVNINSKCQrGPDHF--PFLGRKDSGIG 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
575-976 |
7.98e-52 |
|
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: 188.82 E-value: 7.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 575 VQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFY---------P 645
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYaenaeaflaD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 646 LTVNHWAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLP 725
Cdd:cd07100 81 EPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 726 CEDEVAESgLVKDGRVETVILTGGT-------STAKRML--AVrpdlhllAETGGKNATIVTAMADRDLAVKHVVQSAFG 796
Cdd:cd07100 161 IDSDQVEA-IIADPRVRGVTLTGSEragravaAEAGKNLkkSV-------LELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 797 HAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPL----------------IApPGKTLTRGMKT 860
Cdd:cd07100 233 NAGQSCIAAKRFIVHEDVYDE--FLEKFVEAMAALKVGDPMDEDTDLGPLarkdlrdelheqveeaVA-AGATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 861 LEDDETWlvapehivgqpnlYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIE 940
Cdd:cd07100 310 PDGPGAF-------------YPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAE 376
|
410 420 430
....*....|....*....|....*....|....*..
gi 1712455972 941 LWKQSIHAGNLYINR-STTGAivlRQPFGGVGLSAYG 976
Cdd:cd07100 377 RVARRLEAGMVFINGmVKSDP---RLPFGGVKRSGYG 410
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
561-980 |
1.01e-51 |
|
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: 189.18 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAID- 639
Cdd:cd07094 9 GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 640 -----------FCEFYPL--TVNHWAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAM 706
Cdd:cd07094 89 lrlaaeeaeriRGEEIPLdaTQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 707 VCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPDLHLLAETGGKNATIVTAMADRDLA 786
Cdd:cd07094 169 LAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 787 VKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKTLTRGM--KTLEDD 864
Cdd:cd07094 249 IEALAKGGFYHAGQVCISVQRIYVHEELYD--EFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWveEAVEAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 865 ETWLVApehivGQPN--LYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREIEL 941
Cdd:cd07094 327 ARLLCG-----GERDgaLFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDlNVAFKA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1712455972 942 WKQsIHAGNLYINRSTtgaiVLR---QPFGGVGLSAYG-PGVK 980
Cdd:cd07094 402 AEK-LEVGGVMVNDSS----AFRtdwMPFGGVKESGVGrEGVP 439
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
556-976 |
3.38e-51 |
|
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: 187.83 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 556 DPSRpGCVVCRYPMASLDQVQQAVSIA--ASDSNpWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPE 633
Cdd:cd07109 3 DPST-GEVFARIARGGAADVDRAVQAArrAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 634 ISEAIDFCEFYPLTV-----NHWAQQAGVDICSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVA 704
Cdd:cd07109 81 VEAAARYFEYYGGAAdklhgETIPLGPGYFVYTVrephGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 705 AMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRML--AVRPDLHLLAETGGKNATIVTAMAD 782
Cdd:cd07109 161 LRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMraAAENVVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 783 RDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDlETKMGPLIAPPGKTLTRGM-KTL 861
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDE--VLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFvARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 862 EDDETWLVAPEHIVGQPNL----YRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-D 936
Cdd:cd07109 318 RARGARIVAGGRIAEGAPAggyfVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDgD 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1712455972 937 REIELwKQSIHAGNLYINRSTTGAIVLRqPFGGVGLSAYG 976
Cdd:cd07109 398 RALRV-ARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSGHG 435
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
561-976 |
4.06e-51 |
|
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: 187.54 E-value: 4.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAI 638
Cdd:cd07118 7 GVVVARYAEGTVEDVDAAVAAArkAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 639 DFCEF--------YPLTVNHWAQQAgVDICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMV 707
Cdd:cd07118 87 DLWRYaaslartlHGDSYNNLGDDM-LGLVLRepiGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLML 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 708 CDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPD-LHLLA-ETGGKNATIVTAMADRDL 785
Cdd:cd07118 166 AELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARnLKKVSlELGGKNPQIVFADADLDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 786 AVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPpgktltRGMKTLED-- 863
Cdd:cd07118 246 AADAVVFGVYFNAGECCNSGSRLLVHESIAD--AFVAAVVARSRKVRVGDPLDPETKVGAIINE------AQLAKITDyv 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 864 ----DE--TWLVAPEHIVGQPNLY-RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDD 936
Cdd:cd07118 318 dagrAEgaTLLLGGERLASAAGLFyQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1712455972 937 REIELWKQSIHAGNLYINRSTTGAIVLrqPFGGVGLSAYG 976
Cdd:cd07118 398 DTALTVARRIRAGTVWVNTFLDGSPEL--PFGGFKQSGIG 435
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
561-976 |
7.88e-51 |
|
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: 186.88 E-value: 7.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEA-DPEISEAID 639
Cdd:cd07115 7 GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPRAAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 640 FCEFYpltvNHWA-QQAGVDICSR------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAM 706
Cdd:cd07115 87 TFRYY----AGWAdKIEGEVIPVRgpflnytvrepvGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 707 VCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRML-AVRPDLHLLA-ETGGKNATIVTAMADRD 784
Cdd:cd07115 163 IAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMqGAAGNLKRVSlELGGKSANIVFADADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 785 LAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAppGKTLTRGMKTLE-- 862
Cdd:cd07115 243 AAVRAAATGIFYNQGQMCTAGSRLLVHESIYDE--FLERFTSLARSLRPGDPLDPKTQMGPLVS--QAQFDRVLDYVDvg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 863 -DDETWLVAPEHIVGQPNLY-RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIE 940
Cdd:cd07115 319 rEEGARLLTGGKRPGARGFFvEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 1712455972 941 LWKQSIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07115 399 RVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFG 432
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
561-980 |
7.63e-50 |
|
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: 183.60 E-value: 7.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAID- 639
Cdd:cd07147 9 GEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 640 -----------FCEFYPLTVNhwAQQAGVDICSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVA 704
Cdd:cd07147 89 friaaeeatriYGEVLPLDIS--ARGEGRQGLVRrfpiGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 705 AMVCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKRMLAVRPDLHLLAETGGKNATIVTAMADRD 784
Cdd:cd07147 167 LILGEVLAETGLPKGAFSVLPCSRDDADL-LVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 785 LAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPpgktltrgmKTLEDD 864
Cdd:cd07147 246 FAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDE--FKSRLVARVKALKTGDPKDDATDVGPMISE---------SEAERV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 865 ETW----------LVAPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESL 934
Cdd:cd07147 315 EGWvneavdagakLLTGGKRDG--ALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1712455972 935 DDREI-ELWKQsIHAGNLYINRSTTgaivLR---QPFGGVGLSAYG-PGVK 980
Cdd:cd07147 393 DLEKAlRAWDE-LEVGGVVINDVPT----FRvdhMPYGGVKDSGIGrEGVR 438
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
537-973 |
1.11e-49 |
|
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: 183.47 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMI 616
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 617 GAMVAEGGKTIPEADP--------EISEAIDFCEFYPltvnhWAQQAGVDICSR---GVVAVITPWNFPLAIPAGGIAAA 685
Cdd:cd07138 80 QAITLEMGAPITLARAaqvglgigHLRAAADALKDFE-----FEERRGNSLVVRepiGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 686 LACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPD--- 762
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADtvk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 763 -LHLlaETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLET 841
Cdd:cd07138 235 rVAL--ELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYA--EAEEIAAAAAEAYVVGDPRDPAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 842 KMGPLIAPPGKTLTRGM--KTLEDDETwLVA--PEHIVGQPNLY--RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEE 915
Cdd:cd07138 311 TLGPLASAAQFDRVQGYiqKGIEEGAR-LVAggPGRPEGLERGYfvKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1712455972 916 AIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRsttGAIVLRQPFGGVGLS 973
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING---AAFNPGAPFGGYKQS 444
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
561-982 |
1.26e-49 |
|
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: 182.94 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAAsdsNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAID- 639
Cdd:cd07146 9 GEVVGTVPAGTEEALREALALAA---SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 640 --FC---------EFYPLTVNHWAQQAGVDICSR--GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAM 706
Cdd:cd07146 86 lrFAaaealrddgESFSCDLTANGKARKIFTLREplGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 707 VCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPDLHLLAETGGKNATIVTAMADRDLA 786
Cdd:cd07146 166 LADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADLERA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 787 VKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKTL--TRGMKTLEDD 864
Cdd:cd07146 246 ATLAVAGSYANSGQRCTAVKRILVHESVADE--FVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQieNRVEEAIAQG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 865 ETWLVAPEHivgQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREIELWK 943
Cdd:cd07146 324 ARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDlDTIKRLVE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1712455972 944 QsIHAGNLYIN-----RSTTgaivlrQPFGGVGLSayGPGVKAG 982
Cdd:cd07146 401 R-LDVGTVNVNevpgfRSEL------SPFGGVKDS--GLGGKEG 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
535-926 |
4.08e-49 |
|
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: 182.33 E-value: 4.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 535 VPLWVGDQQVTPEPDQMRESTDPSrPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGD 614
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 615 MIGAMVAEGGKTIPEADPEISEAIDFCEFyPLTVNHWAQ-------QAGVDICSR----GVVAVITPWNFPLAIPAGGIA 683
Cdd:cd07085 80 LARLITLEHGKTLADARGDVLRGLEVVEF-ACSIPHLLKgeylenvARGIDTYSYrqplGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 684 AALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAEsGLVKDGRVETVILTGGTSTAKRM--LAVRP 761
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEYIyeRAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 762 DLHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLET 841
Cdd:cd07085 238 GKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEAD--EWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 842 KMGPLIAPPGKT-----LTRGMK---TLEDDETWLVAPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRL 913
Cdd:cd07085 316 DMGPVISPAAKErieglIESGVEegaKLVLDGRGVKVPGYENG--NFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
|
410
....*....|...
gi 1712455972 914 EEAIEIVRSTGYG 926
Cdd:cd07085 394 DEAIAIINANPYG 406
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
518-988 |
7.85e-49 |
|
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: 182.79 E-value: 7.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 518 EQTLQKWKDQCgdqaTVVPLWVGDQQVtpEPDQMRESTDPSRPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHR 597
Cdd:cd07123 20 QEALAELKSLT----VEIPLVIGGKEV--RTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 598 HEVLRGAAQRMR-QRRGDMIGA-MVAEGgKTIPEAdpEI---SEAIDFCEFYPltvnHWAQQ--------AGVDICSR-- 662
Cdd:cd07123 94 AAIFLKAADLLSgKYRYELNAAtMLGQG-KNVWQA--EIdaaCELIDFLRFNV----KYAEElyaqqplsSPAGVWNRle 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 -----GVVAVITPWNFplaipaGGIAAALAC-----GNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAE 732
Cdd:cd07123 167 yrpleGFVYAVSPFNF------TAIGGNLAGapalmGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 733 SGLVKDGRVETVILTGGTSTAKRM---LAVRPDLH-----LLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSA 804
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLwkqIGENLDRYrtyprIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 805 TSLLLLEQEVFddPKFQSLLADAVESLPVGSAWDLETKMGPLI----------------APPGKTLTRGMKTlEDDETWL 868
Cdd:cd07123 321 ASRAYVPESLW--PEVKERLLEELKEIKMGDPDDFSNFMGAVIdekafdrikgyidhakSDPEAEIIAGGKC-DDSVGYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 869 VapehivgQPNLYRpgvkwNVAPGSFSHLTELFGPVLG--VMPFSRLEEAIEIVRSTG-YGLTSGLESLDDREIELWKQS 945
Cdd:cd07123 398 V-------EPTVIE-----TTDPKHKLMTEEIFGPVLTvyVYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDA 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1712455972 946 IH--AGNLYINRSTTGAIVLRQPFGGVGLSayGPGVKAGGPHYVL 988
Cdd:cd07123 466 LRnaAGNFYINDKPTGAVVGQQPFGGARAS--GTNDKAGSPLNLL 508
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
568-969 |
6.67e-48 |
|
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: 178.27 E-value: 6.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 568 PMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCE---FY 644
Cdd:cd07151 27 PAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITReaaTF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 645 PLTVNhwaqqaGVDICS-------------RGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASET-VWVAAMVCDA 710
Cdd:cd07151 107 PLRME------GRILPSdvpgkenrvyrepLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTpITGGLLLAKI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 711 FWDAGVPRDALQMLpcedeVAESGLVKDGRVETVI-----LTGGTSTAKRM--LAVRPDLHLLAETGGKNATIVTAMADR 783
Cdd:cd07151 181 FEEAGLPKGVLNVV-----VGAGSEIGDAFVEHPVprlisFTGSTPVGRHIgeLAGRHLKKVALELGGNNPFVVLEDADI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 784 DLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAppGKTLTRGMKTLE- 862
Cdd:cd07151 256 DAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDE--FVEKFVERVKALPYGDPSDPDTVVGPLIN--ESQVDGLLDKIEq 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 863 --DDETWLVAPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREI 939
Cdd:cd07151 332 avEEGATLLVGGEAEG--NVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDlERGV 409
|
410 420 430
....*....|....*....|....*....|..
gi 1712455972 940 ELWKQsIHAGNLYINRSTTG--AIVlrqPFGG 969
Cdd:cd07151 410 QFARR-IDAGMTHINDQPVNdePHV---PFGG 437
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
574-976 |
1.36e-47 |
|
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: 176.61 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 574 QVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFYPLTVNhwaQ 653
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLIT---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 654 QAGVDICSR-------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKpASE----TVWvaaMVCDAFWDAGV 716
Cdd:cd07105 78 IIGGSIPSDkpgtlamvvkepvGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLK-ASElsprTHW---LIGRVFHEAGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 717 PRDALQMLPC--ED--EVAESgLVKDGRVETVILTGGTSTAKR--MLAVRpdlHL---LAETGGKNATIVTAMADRDLAV 787
Cdd:cd07105 154 PKGVLNVVTHspEDapEVVEA-LIAHPAVRKVNFTGSTRVGRIiaETAAK---HLkpvLLELGGKAPAIVLEDADLDAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 788 KHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSawdleTKMGPLIAPPGKT---------LTRGM 858
Cdd:cd07105 230 NAALFGAFLNSGQICMSTERIIVHESIAD--EFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADrvkelvddaLSKGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 859 KTLeddetwLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DR 937
Cdd:cd07105 303 KLV------VGGLADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlAR 376
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1712455972 938 EIELWKQsIHAGNLYINRSTTG--AIVlrqPFGGVGLSAYG 976
Cdd:cd07105 377 ALAVAKR-IESGAVHINGMTVHdePTL---PHGGVKSSGYG 413
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
556-976 |
2.94e-47 |
|
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: 176.39 E-value: 2.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 556 DPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEIS 635
Cdd:cd07110 3 NPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 636 EAIDFCEFYPLTVNHWAQQAGVDI----------CSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKP---ASE 699
Cdd:cd07110 82 DVAGCFEYYADLAEQLDAKAERAVplpsedfkarVRRepvGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPselTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 700 TVWVAAMVCDAfwdAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKR-MLA----VRPdlhLLAETGGKNA 774
Cdd:cd07110 162 TELELAEIAAE---AGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQvMQAaaqdIKP---VSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 775 TIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLI-APPGKT 853
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIAD--AFLERLATAAEAIRVGDPLEEGVRLGPLVsQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 854 LTRGMKTLEDDETWLVA----PEHIvGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTS 929
Cdd:cd07110 314 VLSFIARGKEEGARLLCggrrPAHL-EKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1712455972 930 GLESLDDREIELWKQSIHAGNLYINRSTtgAIVLRQPFGGVGLSAYG 976
Cdd:cd07110 393 AVISRDAERCDRVAEALEAGIVWINCSQ--PCFPQAPWGGYKRSGIG 437
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
537-984 |
4.38e-47 |
|
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: 176.23 E-value: 4.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMRESTDPSrPGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGD 614
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPA-TEEVVGRVPEATPADVDAAVAAArrAFDNGPWPRLSPAERAAVLRRLADALEARADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 615 MIGAMVAEGGKTIPEADPEISEAI--------DFCEFYPLTVNHWAQQAGVDICSR---GVVAVITPWNFPLAIPAGGIA 683
Cdd:cd07139 80 LARLWTAENGMPISWSRRAQGPGPaallryyaALARDFPFEERRPGSGGGHVLVRRepvGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 684 AALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKRMLAVRPDl 763
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEY-LVRHPGVDKVSFTGSTAAGRRIAAVCGE- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 764 hLLA----ETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDL 839
Cdd:cd07139 238 -RLArvtlELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDE--VVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 840 ETKMGPLIAPPGKTLTRG-MKTLEDDETWLVA----PEHiVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLE 914
Cdd:cd07139 315 ATQIGPLASARQRERVEGyIAKGRAEGARLVTgggrPAG-LDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712455972 915 EAIEIVRSTGYGLTSGLESLD-DREIELWKQsIHAGNLYIN--RSTTGAivlrqPFGGVGLSAYGpgvKAGGP 984
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADvERGLAVARR-IRTGTVGVNgfRLDFGA-----PFGGFKQSGIG---REGGP 457
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
554-976 |
5.30e-47 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 175.82 E-value: 5.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 554 STDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPE 633
Cdd:PRK13968 11 SVNPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 634 ISEAIDFCEFY-----------PLTVNHwaQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVW 702
Cdd:PRK13968 90 VAKSANLCDWYaehgpamlkaePTLVEN--QQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 703 VAAMVCDAFWDAGVPRDALQMLPCEDEvAESGLVKDGRVETVILTG----GTSTAKRMLAVRPDLHLlaETGGKNATIVT 778
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADND-GVSQMINDSRIAAVTVTGsvraGAAIGAQAGAALKKCVL--ELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 779 AMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLiappGKTLTRG- 857
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASA--FTERFVAAAAALKMGDPRDEENALGPM----ARFDLRDe 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 858 -----MKTLEDDETWLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLE 932
Cdd:PRK13968 319 lhhqvEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1712455972 933 SLDDREIELWKQSIHAGNLYIN-RSTTGAivlRQPFGGVGLSAYG 976
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINgYCASDA---RVAFGGVKKSGFG 440
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
554-976 |
5.69e-47 |
|
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: 175.43 E-value: 5.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 554 STDPSRpGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEAD 631
Cdd:cd07114 1 SINPAT-GEPWARVPEASAADVDRAVAAAraAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 632 PEISEAIDFCEFYpltvnhwaqqAGV-----------------DICSR---GVVAVITPWNFPLAIPAGGIAAALACGNT 691
Cdd:cd07114 80 AQVRYLAEWYRYY----------AGLadkiegavipvdkgdylNFTRReplGVVAAITPWNSPLLLLAKKLAPALAAGNT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 692 VILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRM--LAVRPDLHLLAET 769
Cdd:cd07114 150 VVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIarAAAENLAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 770 GGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAP 849
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYD--EFVERLVARARAIRVGDPLDPETQMGPLATE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 850 P---------------GKTLTRGMKTLEDDETwlvapehivGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLE 914
Cdd:cd07114 308 RqlekveryvarareeGARVLTGGERPSGADL---------GAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712455972 915 EAIEIVRSTGYGLTSGLESLD-DREIELWKQsIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07114 379 EAIALANDSEYGLAAGIWTRDlARAHRVARA-IEAGTVWVN--TYRALSPSSPFGGFKDSGIG 438
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
551-973 |
6.84e-46 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 173.22 E-value: 6.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 551 MRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRgDMIGAMVA-EGGKTIPE 629
Cdd:PRK09457 16 AFESRNPVS-GEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENK-EELAEVIArETGKPLWE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 630 ADPEISE-----AIDFCEFYPLTVNHWAQQAGVDICSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASET 700
Cdd:PRK09457 94 AATEVTAminkiAISIQAYHERTGEKRSEMADGAAVLRhrphGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 701 VWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTA---KRMLAVRPDLHLLAETGGKNATIV 777
Cdd:PRK09457 174 PWVAELTVKLWQQAGLPAGVLNLVQGGRETGKA-LAAHPDIDGLLFTGSANTGyllHRQFAGQPEKILALEMGGNNPLVI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 778 TAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDPkFQSLLADAVESLPVGsAWDLETK--MGPLI-APPGKTL 854
Cdd:PRK09457 253 DEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDA-FLARLVAVAKRLTVG-RWDAEPQpfMGAVIsEQAAQGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 855 TRGMKTLEDD-ETWLVAPEHIVGQPNLYRPGV--KWNVA--PGSfshltELFGPVLGVMPFSRLEEAIEIVRSTGYGLTS 929
Cdd:PRK09457 331 VAAQAQLLALgGKSLLEMTQLQAGTGLLTPGIidVTGVAelPDE-----EYFGPLLQVVRYDDFDEAIRLANNTRFGLSA 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1712455972 930 GLESLDDREIELWKQSIHAGNLYINRSTTGAiVLRQPFGGVGLS 973
Cdd:PRK09457 406 GLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGAS 448
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
554-976 |
2.59e-45 |
|
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: 170.63 E-value: 2.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 554 STDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGD--MIGAMvaEGGKTIPEAD 631
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEElaLIDAL--DCGNPVSAML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 632 PEISEAIDFCEFY------------PLTVNHWAQqagvdicSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILK 695
Cdd:cd07107 78 GDVMVAAALLDYFaglvtelkgetiPVGGRNLHY-------TLrepyGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 696 PAsETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPDL--HLLAETGGKN 773
Cdd:cd07107 151 PP-EQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGikHVTLELGGKN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 774 ATIVTAMADRDLAVKHVVQSA-FGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAppGK 852
Cdd:cd07107 230 ALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDE--VLARVVERVAAIKVGDPTDPATTMGPLVS--RQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 853 TLTRGMKTLEDDET---WLVA----PEHIVGQPNLY-RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTG 924
Cdd:cd07107 306 QYDRVMHYIDSAKRegaRLVTgggrPEGPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1712455972 925 YGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAivLRQPFGGVGLSAYG 976
Cdd:cd07107 386 YGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHF--LGAPFGGVKNSGIG 435
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
555-976 |
5.41e-45 |
|
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: 169.25 E-value: 5.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 555 TDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEI 634
Cdd:cd07106 2 INPAT-GEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 635 SEAIDFCEFYP---LTVNHWAQQAGVDICSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMV 707
Cdd:cd07106 81 GGAVAWLRYTAsldLPDEVIEDDDTRRVELRrkplGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 708 CDAFWDAgVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKR-MLAVRPDL-HLLAETGGKNATIVTAMADRDL 785
Cdd:cd07106 161 GELAQEV-LPPGVLNVVSGGDELGPA-LTSHPDIRKISFTGSTATGKKvMASAAKTLkRVTLELGGNDAAIVLPDVDIDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 786 AVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPL---------------IAPP 850
Cdd:cd07106 239 VAPKLFWGAFINSGQVCAAIKRLYVHESIYDE--FCEALVALAKAAVVGDGLDPGTTLGPVqnkmqydkvkelvedAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 851 GKTLTRGMKTLEDDETWlvapehivgqpnlYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSG 930
Cdd:cd07106 317 GAKVLAGGEPLDGPGYF-------------IPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGAS 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1712455972 931 LESLD-DREIELWKQsIHAGNLYINRSttGAIVLRQPFGGVGLSAYG 976
Cdd:cd07106 384 VWSSDlERAEAVARR-LEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
556-976 |
7.00e-45 |
|
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: 169.04 E-value: 7.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 556 DPSrPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPE-ADPEI 634
Cdd:cd07092 3 DPA-TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLvRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 635 SEAIDFCEFYPLTVNHWAQQAGVD-------ICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVA 704
Cdd:cd07092 82 PGAVDNFRFFAGAARTLEGPAAGEylpghtsMIRRepiGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 705 AMVCDAFWDaGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPD----LHLlaETGGKNATIVTAM 780
Cdd:cd07092 162 LLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADtlkrVHL--ELGGKAPVIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 781 ADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPpgKTLTRGMKT 860
Cdd:cd07092 239 ADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYD--EFVAALVEAVSAIRVGDPDDEDTEMGPLNSA--AQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 861 LEDdetwlvAPEHIV---------GQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGL 931
Cdd:cd07092 315 VER------APAHARvltggrraeGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1712455972 932 ESLD-DREIELWKQsIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07092 389 WTRDvGRAMRLSAR-LDFGTVWVN--THIPLAAEMPHGGFKQSGYG 431
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
561-976 |
7.20e-45 |
|
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: 169.03 E-value: 7.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDF 640
Cdd:cd07101 6 GEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 641 CEFYPLTVNHW----AQQAGVDICSR--------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVC 708
Cdd:cd07101 86 ARYYARRAERLlkprRRRGAIPVLTRttvnrrpkGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 709 DAFWDAGVPRDALQMLPCEDEVAESGLVKdgRVETVILTGGTSTAkRMLAVRPDLHLL---AETGGKNATIVTAMADRDL 785
Cdd:cd07101 166 ELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATG-RVVAERAGRRLIgcsLELGGKNPMIVLEDADLDK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 786 AVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPpgktltRGMKTLE--- 862
Cdd:cd07101 243 AAAGAVRACFSNAGQLCVSIERIYVHESVYDE--FVRRFVARTRALRLGAALDYGPDMGSLISQ------AQLDRVTahv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 863 DDETWLVAPEHIVGQ------PNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDD 936
Cdd:cd07101 315 DDAVAKGATVLAGGRarpdlgPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1712455972 937 REIELWKQSIHAGNLYIN---RSTTGAIvlRQPFGGVGLSAYG 976
Cdd:cd07101 395 ARGRRIAARLRAGTVNVNegyAAAWASI--DAPMGGMKDSGLG 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
561-976 |
9.38e-45 |
|
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: 168.93 E-value: 9.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEA-DPEISEA 637
Cdd:cd07112 12 GRVLAEVAACDAADVDRAVAAArrAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAlAVDVPSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 638 IDFCEFY------------PLTVNHWAqqagvdICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVW 702
Cdd:cd07112 92 ANTFRWYaeaidkvygevaPTGPDALA------LITReplGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 703 VAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRML--AVRPDL-HLLAETGGKNATIVTA 779
Cdd:cd07112 166 TALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLeySGQSNLkRVWLECGGKSPNIVFA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 780 MA-DRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAppGKTLTRGM 858
Cdd:cd07112 246 DApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDE--FLEKVVAAAREWKPGDPLDPATRMGALVS--EAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 859 KTLE---DDETWLVA---PEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLE 932
Cdd:cd07112 322 GYIEsgkAEGARLVAggkRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVW 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1712455972 933 SLD-DREIELWKQsIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07112 402 TSDlSRAHRVARR-LRAGTVWVN--CFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
544-976 |
9.40e-45 |
|
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: 169.41 E-value: 9.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 544 VTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVA 621
Cdd:cd07119 7 VEAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAArrAFDSGEWPHLPAQERAALLFRIADKIREDAEELARLETL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 622 EGGKTIPEADPEISEAIDFCEFYP--LTVNHWAQ-QAGVDICSR------GVVAVITPWNFPLAIPAGGIAAALACGNTV 692
Cdd:cd07119 86 NTGKTLRESEIDIDDVANCFRYYAglATKETGEVyDVPPHVISRtvrepvGVCGLITPWNYPLLQAAWKLAPALAAGNTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 693 ILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKR-MLAVRPDLHLLA-ETG 770
Cdd:cd07119 166 VIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSiMRAAAGNVKKVAlELG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 771 GKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLI--- 847
Cdd:cd07119 246 GKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHD--KFVAALAERAKKIKLGNGLDADTEMGPLVsae 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 848 ------------APPGKTLTRGMKTLEDDEtwlvapehivgqpnlYRPGvkWNVAPGSFSHLT--------ELFGPVLGV 907
Cdd:cd07119 324 hrekvlsyiqlgKEEGARLVCGGKRPTGDE---------------LAKG--YFVEPTIFDDVDrtmrivqeEIFGPVLTV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712455972 908 MPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07119 387 ERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN--DYHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
554-954 |
1.15e-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: 168.68 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 554 STDPSRpGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSlEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEAD 631
Cdd:cd07120 1 SIDPAT-GEVIGTYADGGVAEAEAAIAAArrAFDETDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 632 PEISEAIDFCEFYPLTVNHWAQQAG------VDICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVW 702
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIepepgsFSLVLRepmGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 703 VAAMVCDAFWDA-GVPRDALQMlpcedeVAESG------LVKDGRVETVILTGGTSTAKR-MLAVRPDLHLLA-ETGGKN 773
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNL------FTESGsegaahLVASPDVDVISFTGSTATGRAiMAAAAPTLKRLGlELGGKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 774 ATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKT 853
Cdd:cd07120 233 PCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADE--VRDRLAARLAAVKVGPGLDPASDMGPLIDRANVD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 854 LTRGM--KTLEDDETWLVAPEHIVGQPN---LYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLT 928
Cdd:cd07120 311 RVDRMveRAIAAGAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLA 390
|
410 420
....*....|....*....|....*..
gi 1712455972 929 SGLESLD-DREIELwKQSIHAGNLYIN 954
Cdd:cd07120 391 ASVWTRDlARAMRV-ARAIRAGTVWIN 416
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
555-976 |
4.56e-44 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 166.84 E-value: 4.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 555 TDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEI 634
Cdd:TIGR01780 2 YNPAT-GEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 635 SEAIDFCEFYP---------LTVNHWAQQAGVDICSR-GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVA 704
Cdd:TIGR01780 81 LYAASFLEWFAeeakrvygdTIPSPQSDKRLIVIKQPvGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 705 AMVCDAFWDAGVPRDALQMLPCEDEVAESG-LVKDGRVETVILTGGTSTAKRMLAVRPDL--HLLAETGGKNATIVTAMA 781
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGSRAKEVGNvLTTSPLVRKISFTGSTNVGKILMKQSASTvkKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 782 DRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPPG--KTLTRGMK 859
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYD--EFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAveKVEKHIAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 860 TLEDDETWLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREI 939
Cdd:TIGR01780 319 AVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRI 398
|
410 420 430
....*....|....*....|....*....|....*..
gi 1712455972 940 ELWKQSIHAGNLYINRSTTGAIVLrqPFGGVGLSAYG 976
Cdd:TIGR01780 399 WRVAEALEYGMVGINTGLISNVVA--PFGGVKQSGLG 433
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
553-942 |
9.91e-44 |
|
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: 166.23 E-value: 9.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 553 ESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMiGAMVA-EGGKTIPEAD 631
Cdd:cd07130 15 TSISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEAL-GKLVSlEMGKILPEGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 632 PEISEAIDFCEFyplTVNHWAQQAGVDICSR-------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPAS 698
Cdd:cd07130 93 GEVQEMIDICDF---AVGLSRQLYGLTIPSErpghrmmeqwnplGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 699 ET----VWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKR---MLAVRPDLHLLaETGG 771
Cdd:cd07130 170 TTpltaIAVTKIVARVLEKNGLPGAIASLVCGGADVGEA-LVKDPRVPLVSFTGSTAVGRQvgqAVAARFGRSLL-ELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 772 KNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPPG 851
Cdd:cd07130 248 NNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDE--VLERLKKAYKQVRIGDPLDDGTLVGPLHTKAA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 852 -KTLTRGMKTLEDDE-TWLVAPEHIVGQPNLYRPGVKWNVAPGSFSHlTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTS 929
Cdd:cd07130 326 vDNYLAAIEEAKSQGgTVLFGGKVIDGPGNYVEPTIVEGLSDAPIVK-EETFAPILYVLKFDTLEEAIAWNNEVPQGLSS 404
|
410
....*....|...
gi 1712455972 930 GLESLDDREIELW 942
Cdd:cd07130 405 SIFTTDLRNAFRW 417
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
561-976 |
1.13e-43 |
|
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: 165.50 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDF 640
Cdd:cd07102 6 GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 641 CEFYpLTVnhwAQQAGVDICSR--------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAM 706
Cdd:cd07102 86 ARYM-ISI---AEEALADIRVPekdgferyirreplGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 707 VCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKRM--LAVRPDLHLLAETGGKNATIVTAMADRD 784
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLSHETSAA-LIADPRIDHVSFTGSVAGGRAIqrAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 785 LAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPPGK---------TLT 855
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDA--FVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAAdfvraqiadAIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 856 RGMKTLEDDETWLVAPEHivgqPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD 935
Cdd:cd07102 319 KGARALIDGALFPEDKAG----GAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1712455972 936 -DREIELWKQsIHAGNLYINRST--------TGaivLRQPFGGVGLSAYG 976
Cdd:cd07102 395 iARAEALGEQ-LETGTVFMNRCDyldpalawTG---VKDSGRGVTLSRLG 440
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
561-985 |
6.56e-43 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 164.13 E-value: 6.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIA-ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKT--------IPEAD 631
Cdd:TIGR03216 24 GRVIARVHEAGAAEVDAAVAAArAALKGPWGKMTVAERADLLYAVADEIERRFDDFLAAEVADTGKPrslashldIPRGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 632 PEISEAIDFCEFYPLTVNHWAQQAGVDICS------RGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAA 705
Cdd:TIGR03216 104 ANFRVFADVVKNAPTECFEMATPDGKGALNyavrkpLGVVGVISPWNLPLLLMTWKVGPALACGNTVVVKPSEETPGTAT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 706 MVCDAFWDAGVPRDALQML----PcedEVAESGLVKDGRVETVILTGGTSTAKRMLA-----VRPdlhLLAETGGKNATI 776
Cdd:TIGR03216 184 LLGEVMNAVGVPKGVYNVVhgfgP---DSAGEFLTRHPGVDAITFTGETRTGSAIMKaaadgVKP---VSFELGGKNAAI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 777 VTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPP--GKTL 854
Cdd:TIGR03216 258 VFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFD--RFVAALKARAESLKIGVPDDPATNMGPLISAEhrDKVL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 855 TRGMKTLEDDETwLVAPEHIVGQPNLYRPGVkWnVAPGSFSHLT--------ELFGPVLGVMPFSRLEEAIEIVRSTGYG 926
Cdd:TIGR03216 336 SYYALAVEEGAT-VVTGGGVPDFGDALAGGA-W-VQPTIWTGLPdsarvvteEIFGPCCHIAPFDSEEEVIALANDTPYG 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712455972 927 LTSGLESLDDREIELWKQSIHAGNLYIN----RSttgaivLRQPFGGVGLSAYGpgvKAGGPH 985
Cdd:TIGR03216 413 LAASVWTEDLSRAHRVARQMEVGIVWVNswflRD------LRTPFGGSKLSGIG---REGGVH 466
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
561-985 |
3.08e-41 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 159.47 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDF 640
Cdd:PLN02278 50 GEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 641 CEFYpltvnhwAQQA----GVDICSR-------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWV 703
Cdd:PLN02278 130 LEYF-------AEEAkrvyGDIIPSPfpdrrllvlkqpvGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 704 AAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLA-----VRpdlHLLAETGGKNATIVT 778
Cdd:PLN02278 203 ALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAgaaatVK---RVSLELGGNAPFIVF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 779 AMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPPG------- 851
Cdd:PLN02278 280 DDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYD--KFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAvqkvesh 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 852 --KTLTRGMKTLeddetwLVAPEHIVGqPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTS 929
Cdd:PLN02278 358 vqDAVSKGAKVL------LGGKRHSLG-GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAA 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1712455972 930 GLESLDDReiELWK--QSIHAGNLYINRSTTGAIVlrQPFGGVGLSAYGpgvKAGGPH 985
Cdd:PLN02278 431 YIFTRDLQ--RAWRvsEALEYGIVGVNEGLISTEV--APFGGVKQSGLG---REGSKY 481
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
568-976 |
3.06e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 156.96 E-value: 3.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 568 PMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAidfcefyPLT 647
Cdd:PRK09407 49 PVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDV-------ALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 648 VNHWAQQA-----------GVDICSR--------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVC 708
Cdd:PRK09407 122 ARYYARRApkllaprrragALPVLTKttelrqpkGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 709 DAFWDAGVPRDALQMLPCEDEVAESGLVKdgRVETVILTGGTSTAkRMLAVRPDLHLL---AETGGKNATIVTAMADRDL 785
Cdd:PRK09407 202 ELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATG-RVLAEQAGRRLIgfsLELGGKNPMIVLDDADLDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 786 AVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPP--------------- 850
Cdd:PRK09407 279 AAAGAVRACFSNAGQLCISIERIYVHESIYDE--FVRAFVAAVRAMRLGAGYDYSADMGSLISEAqletvsahvddavak 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 851 GKTLTRGMKTLEDdetwlvapehiVGqPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSG 930
Cdd:PRK09407 357 GATVLAGGKARPD-----------LG-PLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNAS 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1712455972 931 LESLDDREIELWKQSIHAGNLYINRS------TTGAivlrqPFGGVGLSAYG 976
Cdd:PRK09407 425 VWTGDTARGRAIAARIRAGTVNVNEGyaaawgSVDA-----PMGGMKDSGLG 471
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
561-976 |
8.77e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 154.13 E-value: 8.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDF 640
Cdd:PRK09406 11 GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 641 CEFY--------------PLTVNhwAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAM 706
Cdd:PRK09406 91 FRYYaehaealladepadAAAVG--ASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 707 VCDAFWDAGVPRDALQMLPCEDEVAEsGLVKDGRVETVILTGGTSTAKRMLAVRPDL--HLLAETGGKNATIVTAMADRD 784
Cdd:PRK09406 169 LADLFRRAGFPDGCFQTLLVGSGAVE-AILRDPRVAAATLTGSEPAGRAVAAIAGDEikKTVLELGGSDPFIVMPSADLD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 785 LAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPPGKTltrGMKTLEDD 864
Cdd:PRK09406 248 RAAETAVTARVQNNGQSCIAAKRFIVHADVYDA--FAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD---EVEKQVDD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 865 E-----TWLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREI 939
Cdd:PRK09406 323 AvaagaTILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQ 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 1712455972 940 ELWKQSIHAGNLYINRSTTGAIVLrqPFGGVGLSAYG 976
Cdd:PRK09406 403 ERFIDDLEAGQVFINGMTVSYPEL--PFGGVKRSGYG 437
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
559-976 |
1.29e-38 |
|
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: 150.92 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 559 RPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAI 638
Cdd:cd07090 5 ATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 639 DFCEFYP-----LTVNHWAQQAGVDICSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCD 709
Cdd:cd07090 85 DCLEYYAglaptLSGEHVPLPGGSFAYTRreplGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 710 AFWDAGVPRDALQMLPCEDEVAEsGLVKDGRVETVILTGGTSTAKRMLAVRPD--LHLLAETGGKNATIVTAMADRDLAV 787
Cdd:cd07090 165 ILTEAGLPDGVFNVVQGGGETGQ-LLCEHPDVAKVSFTGSVPTGKKVMSAAAKgiKHVTLELGGKSPLIIFDDADLENAV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 788 KHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPP--GKTLTRGMKTLEDDE 865
Cdd:cd07090 244 NGAMMANFLSQGQVCSNGTRVFVQRSIKD--EFTERLVERTKKIRIGDPLDEDTQMGALISEEhlEKVLGYIESAKQEGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 866 TWLVAPEHIVGQPNLYRPGVkwnVAPGSFSHLT--------ELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-- 935
Cdd:cd07090 322 KVLCGGERVVPEDGLENGFY---VSPCVLTDCTddmtivreEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDlq 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1712455972 936 --DREIElwkqSIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07090 399 raHRVIA----QLQAGTCWIN--TYNISPVEVPFGGYKQSGFG 435
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
537-976 |
1.75e-38 |
|
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: 151.02 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIA-ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRgDM 615
Cdd:cd07144 10 LFINNEFVKSSDGETIKTVNPST-GEVIASVYAAGEEDVDKAVKAArKAFESWWSKVTGEERGELLDKLADLVEKNR-DL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 616 IGAMVA-EGGKTI-PEADPEISEAIDFCEFY------------PLTVNHWAQQAGVDIcsrGVVAVITPWNFPLAIPAGG 681
Cdd:cd07144 88 LAAIEAlDSGKPYhSNALGDLDEIIAVIRYYagwadkiqgktiPTSPNKLAYTLHEPY---GVCGQIIPWNYPLAMAAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 682 IAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVR- 760
Cdd:cd07144 165 LAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 761 ---PDLHLlaETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAV-ESLPVGSA 836
Cdd:cd07144 245 qnlKAVTL--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYD--KFVEKFVEHVkQNYKVGSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 837 WDLETKMGPLIAPP-----------GKtlTRGMKTLEDDEtwlVAPEHIvGQPNLYRPGVKWNVAPGSFSHLTELFGPVL 905
Cdd:cd07144 321 FDDDTVVGPQVSKTqydrvlsyiekGK--KEGAKLVYGGE---KAPEGL-GKGYFIPPTIFTDVPQDMRIVKEEIFGPVV 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712455972 906 GVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIvlRQPFGGVGLSAYG 976
Cdd:cd07144 395 VISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSGIG 463
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
555-976 |
1.80e-38 |
|
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: 150.20 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 555 TDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTI-PEADPE 633
Cdd:cd07108 2 INPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 634 ISEAIDFCEFYP--------LTVNHWAQQagVDICSR---GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASE--- 699
Cdd:cd07108 81 AAVLADLFRYFGglagelkgETLPFGPDV--LTYTVReplGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDapl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 700 TVWVAAMVCDAFWDAGVprdaLQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPD--LHLLAETGGKNATIV 777
Cdd:cd07108 159 AVLLLAEILAQVLPAGV----LNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADrlIPVSLELGGKSPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 778 TAMADRDLAVKHVVQSA-FGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAP------- 849
Cdd:cd07108 235 FPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDA--FLEKLVAKLSKLKIGDPLDEATDIGAIISEkqfakvc 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 850 ---------PGKTLTRGMKTLEDD---ETWLVAPEHIVGQPNlyrpgvKWNVAPgsfshlTELFGPVLGVMPFSRLEEAI 917
Cdd:cd07108 313 gyidlglstSGATVLRGGPLPGEGplaDGFFVQPTIFSGVDN------EWRLAR------EEIFGPVLCAIPWKDEDEVI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1712455972 918 EIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSttGAIVLRQPFGGVGLSAYG 976
Cdd:cd07108 381 AMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
553-976 |
1.44e-37 |
|
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: 148.13 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 553 ESTDPSRpGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRgDMIGAMVA-EGGKTIPE 629
Cdd:cd07091 22 PTINPAT-EEVICQVAEADEEDVDAAVKAAraAFETGWWRKMDPRERGRLLNKLADLIERDR-DELAALESlDNGKPLEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 630 -ADPEISEAIDFCEFY------------PLTVNHWAQQAGVDIcsrGVVAVITPWNFPLAIPAGGIAAALACGNTVILKP 696
Cdd:cd07091 100 sAKGDVALSIKCLRYYagwadkiqgktiPIDGNFLAYTRREPI---GVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 697 ASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRML--AVRPDL-HLLAETGGKN 773
Cdd:cd07091 177 AEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMeaAAKSNLkKVTLELGGKS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 774 ATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPpgKT 853
Cdd:cd07091 257 PNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYD--EFVEKFKARAEKRVVGDPFDPDTFQGPQVSK--AQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 854 LTRGMKTLED--DE--TWLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTS 929
Cdd:cd07091 333 FDKILSYIESgkKEgaTLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAA 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1712455972 930 GLESLD-DREIELWKQsIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07091 413 GVFTKDiNKALRVSRA-LKAGTVWVN--TYNVFDAAVPFGGFKQSGFG 457
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
537-985 |
4.20e-37 |
|
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: 146.77 E-value: 4.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRM--RQRRGD 614
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIqkHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 615 MIGAMVaeGGKTIPEadpeiSEAIDFcefyPLTVNH------WAQQAGVDICSR---GVVAVITPWNFPLAIPAGGIAAA 685
Cdd:cd07111 103 VLESLD--NGKPIRE-----SRDCDI----PLVARHfyhhagWAQLLDTELAGWkpvGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 686 LACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAK---RMLA-VRP 761
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSA-LANHPGVDKVAFTGSTEVGRalrRATAgTGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 762 DLHLlaETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLET 841
Cdd:cd07111 251 KLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEE--LIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 842 KMGPLIAPPGKTLTRGMKTLEDDETWLV--APEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEI 919
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVfqPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVAL 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712455972 920 VRSTGYGLTSGLESLD-DREIELwKQSIHAGNLYINrsTTGAIVLRQPFGGVGLSAYGpgvKAGGPH 985
Cdd:cd07111 407 ANNTPYGLAASVWSENlSLALEV-ALSLKAGVVWIN--GHNLFDAAAGFGGYRESGFG---REGGKE 467
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
567-976 |
7.70e-37 |
|
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: 145.52 E-value: 7.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 567 YPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRgAAQRMRQRRGDMIgAMVA--EGGKTIPEAD-PEI---SEAIDF 640
Cdd:cd07098 12 VPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLR-SLLKYILENQEEI-CRVAcrDTGKTMVDASlGEIlvtCEKIRW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 641 C----------EFYPLTVNHWAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAA----M 706
Cdd:cd07098 90 TlkhgekalrpESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGfflsI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 707 VCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKRMLAVRPDlHL---LAETGGKNATIVTAMADR 783
Cdd:cd07098 170 IRECLAACGHDPDLVQLVTCLPETAEA-LTSHPVIDHITFIGSPPVGKKVMAAAAE-SLtpvVLELGGKDPAIVLDDADL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 784 DLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAP-------------- 849
Cdd:cd07098 248 DQIASIIMRGTFQSSGQNCIGIERVIVHEKIYD--KLLEILTDRVQALRQGPPLDGDVDVGAMISParfdrleelvadav 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 850 -PGKTLTRGMKTLeddetwlVAPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLT 928
Cdd:cd07098 326 eKGARLLAGGKRY-------PHPEYPQG--HYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1712455972 929 SGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG 444
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
568-976 |
2.60e-36 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 144.88 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 568 PMASLDQVQQAVSIA-----ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCE 642
Cdd:PLN02467 40 PAATAEDVDAAVEAArkafkRNKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 643 FYpltvnhwAQQA-GVDICSR-------------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKP---ASE 699
Cdd:PLN02467 120 YY-------ADLAeALDAKQKapvslpmetfkgyvlkeplGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPselASV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 700 TVWVAAMVCDafwDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLA-----VRPdlhLLAETGGKNA 774
Cdd:PLN02467 193 TCLELADICR---EVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTaaaqmVKP---VSLELGGKSP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 775 TIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVfdDPKFQSLLADAVESLPVGSAWDLETKMGPLIAppGKTL 854
Cdd:PLN02467 267 IIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERI--ASEFLEKLVKWAKNIKISDPLEEGCRLGPVVS--EGQY 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 855 TRGMKTLE----DDETWL---VAPEHIvgQPNLY-RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYG 926
Cdd:PLN02467 343 EKVLKFIStaksEGATILcggKRPEHL--KKGFFiEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYG 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1712455972 927 LTSGLESLDDREIELWKQSIHAGNLYINRSTtgAIVLRQPFGGVGLSAYG 976
Cdd:PLN02467 421 LAGAVISNDLERCERVSEAFQAGIVWINCSQ--PCFCQAPWGGIKRSGFG 468
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
537-976 |
2.83e-35 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 141.20 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMReSTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMI 616
Cdd:PRK13473 5 LLINGELVAGEGEKQP-VYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 617 GAMVAEGGKTIPEA-DPEISEAIDFCEFYPLTVNHW-AQQAG---VDICS--R----GVVAVITPWNFPLAIPAGGIAAA 685
Cdd:PRK13473 83 RLESLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLeGKAAGeylEGHTSmiRrdpvGVVASIAPWNYPLMMAAWKLAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 686 LACGNTVILKPASET----VWVAAMVCDAFwdagvPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRP 761
Cdd:PRK13473 163 LAAGNTVVLKPSEITpltaLKLAELAADIL-----PPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 762 D----LHLlaETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAW 837
Cdd:PRK13473 238 DsvkrTHL--ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDD--LVAKLAAAVATLKVGDPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 838 DLETKMGPLI----------------APPGKTLTRGMKTLEddetwlvapehivGQPNLYRPGVKWNVAPGSFSHLTELF 901
Cdd:PRK13473 314 DEDTELGPLIsaahrdrvagfverakALGHIRVVTGGEAPD-------------GKGYYYEPTLLAGARQDDEIVQREVF 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712455972 902 GPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREIELWKQsIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:PRK13473 381 GPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDvGRAHRVSAR-LQYGCTWVN--THFMLVSEMPHGGQKQSGYG 453
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
568-978 |
1.90e-34 |
|
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: 138.32 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 568 PMASLDQVQQAVSIAAS---DSNPWkdTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEfy 644
Cdd:cd07148 16 PTVDWAAIDKALDTAHAlflDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 645 pLTVNHWAQQAGVDIC-----------------SRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETvwvaAMV 707
Cdd:cd07148 92 -LAADELGQLGGREIPmgltpasagriafttrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALAT----PLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 708 CDAFWD----AGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKRMLA-VRPDLHLLAETGGKNATIVTAMAD 782
Cdd:cd07148 167 CLAFVDllheAGLPEGWCQAVPCENAVAEK-LVTDPRVAFFSFIGSARVGWMLRSkLAPGTRCALEHGGAAPVIVDRSAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 783 RDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAP------------- 849
Cdd:cd07148 246 LDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADD--FAQRLAAAAEKLVVGDPTDPDTEVGPLIRPrevdrveewvnea 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 850 --PGKTLTRGMKTLEDdetwlvapehivgqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGL 927
Cdd:cd07148 324 vaAGARLLCGGKRLSD---------------TTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAF 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1712455972 928 TSgleSLDDREIELWKQSIH---AGNLYINRSTTgaivLR---QPFGGVGLSAYGPG 978
Cdd:cd07148 389 QA---AVFTKDLDVALKAVRrldATAVMVNDHTA----FRvdwMPFAGRRQSGYGTG 438
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
535-954 |
6.81e-34 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 137.32 E-value: 6.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 535 VPLWVGDQQVTPEPDQMRESTDPSrPGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGD 614
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPA-TNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 615 MIGAMVAEGGKTIPEADPEISEAIDF----CEFYPLTVNHWAQQAG--VDICS----RGVVAVITPWNFPLAIPAGGIAA 684
Cdd:TIGR01722 80 IAELITAEHGKTHSDALGDVARGLEVvehaCGVNSLLKGETSTQVAtrVDVYSirqpLGVCAGITPFNFPAMIPLWMFPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 685 ALACGNTVILKPaSETVWVAAM-VCDAFWDAGVPRDALQMLPcEDEVAESGLVKDGRVETVILTGGTSTAKRML--AVRP 761
Cdd:TIGR01722 160 AIACGNTFVLKP-SEKVPSAAVkLAELFSEAGAPDGVLNVVH-GDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHttGSAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 762 DLHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVfddPKFQSLLADAVESLPVGSAWDLET 841
Cdd:TIGR01722 238 GKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA---DEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 842 KMGPLIAPPGKT---------LTRGMKTLEDDETWLVA--PE-HIVGqpnlyrPGVKWNVAPGSFSHLTELFGPVLGVMP 909
Cdd:TIGR01722 315 EMGPLITPQAKDrvasliaggAAEGAEVLLDGRGYKVDgyEEgNWVG------PTLLERVPPTMKAYQEEIFGPVLCVLE 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1712455972 910 FSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYIN 954
Cdd:TIGR01722 389 ADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN 433
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
537-976 |
2.65e-33 |
|
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: 135.26 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMRESTDPSrPGCVVCRYPMASLDQVQQAVSIA-ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDM 615
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPA-TEQVIASVASATEADVDAAVASAwRAFVSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 616 IGAMVAEGGKTIPEADP-EISEAIDFCEFYPltvnHWA-----QQAGVDICSR--------------GVVAVITPWNFPL 675
Cdd:cd07113 81 AQLETLCSGKSIHLSRAfEVGQSANFLRYFA----GWAtkingETLAPSIPSMqgerytaftrrepvGVVAGIVPWNFSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 676 AIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKR 755
Cdd:cd07113 157 MIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQ-LISHPDVAKVSFTGSVATGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 756 M--LAVRPDLHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPV 833
Cdd:cd07113 236 IgrQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDE--LVTKLKQALSSFQV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 834 GSAWDLETKMGPLIAPP---------------GKTLTRGMKTLeDDETWLVAPEHIvgqpnlyrpgvkwnVAPGSFSHLT 898
Cdd:cd07113 314 GSPMDESVMFGPLANQPhfdkvcsylddaraeGDEIVRGGEAL-AGEGYFVQPTLV--------------LARSADSRLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 899 --ELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTgaIVLRQPFGGVGLSAYG 976
Cdd:cd07113 379 reETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTF--LDPAVPFGGMKQSGIG 456
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
601-955 |
5.62e-33 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 132.94 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 601 LRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFypltVNHWAQQAGVDICSR--------------GVVA 666
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDY----MAEWARRYEGEIIQSdrpgenillfkralGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 667 VITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVIL 746
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 747 TGGTST-AKRMLAVRPDLHLLA-ETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLL 824
Cdd:PRK10090 157 TGSVSAgEKIMAAAAKNITKVClELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD--QFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 825 ADAVESLPVGS-AWDLETKMGPLIAPPGKTLTRGM--KTLEDDETWLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELF 901
Cdd:PRK10090 235 GEAMQAVQFGNpAERNDIAMGPLINAAALERVEQKvaRAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1712455972 902 GPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINR 955
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR 368
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
561-976 |
8.85e-33 |
|
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: 133.81 E-value: 8.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 561 GCVVCRYPMASLDQVQQAVSIA-ASDSNPW-KDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADP-EISEA 637
Cdd:cd07143 32 GKLITKIAEATEADVDIAVEVAhAAFETDWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 638 IDFCEFYpltvNHWA-----QQAGVDIC----SR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVA 704
Cdd:cd07143 112 ADTFRYY----GGWAdkihgQVIETDIKkltyTRhepiGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 705 AMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRML--AVRPDL-HLLAETGGKNATIVTAMA 781
Cdd:cd07143 188 LYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMeaAAKSNLkKVTLELGGKSPNIVFDDA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 782 DRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPpgKTLTRGMKTL 861
Cdd:cd07143 268 DLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYD--KFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQ--IQYERIMSYI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 862 EDDETwLVAPEHIVGQpnlyRPGVK-WNVAPGSFSHLT--------ELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLE 932
Cdd:cd07143 344 ESGKA-EGATVETGGK----RHGNEgYFIEPTIFTDVTedmkivkeEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVF 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1712455972 933 SLD-DREIELwKQSIHAGNLYINRSTTgaIVLRQPFGGVGLSAYG 976
Cdd:cd07143 419 TNNiNNAIRV-ANALKAGTVWVNCYNL--LHHQVPFGGYKQSGIG 460
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
537-969 |
1.76e-32 |
|
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: 132.85 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRgDMI 616
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENL-ELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 617 gAMVA--EGGKTIPEadpeiSEAIDFcefyPLTVNHWAQQAGV---------DICSR----------GVVAVITPWNFPL 675
Cdd:cd07559 81 -AVAEtlDNGKPIRE-----TLAADI----PLAIDHFRYFAGViraqegslsEIDEDtlsyhfheplGVVGQIIPWNFPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 676 AIPAGGIAAALACGNTVILKPASETvwvaamvcdafwdagvPRDALQMLPCEDEVAESGLVKdgrvetvILTGGTSTAKR 755
Cdd:cd07559 151 LMAAWKLAPALAAGNTVVLKPASQT----------------PLSILVLMELIGDLLPKGVVN-------VVTGFGSEAGK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 756 MLAVRPDLHLLA------------------------ETGGKNATIV--TAMADRDLAVKHVVQSAFGHA---GQKCSATS 806
Cdd:cd07559 208 PLASHPRIAKLAftgsttvgrlimqyaaenlipvtlELGGKSPNIFfdDAMDADDDFDDKAEEGQLGFAfnqGEVCTCPS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 807 LLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPP----------------GKTLTRGMKTLEDDET--WL 868
Cdd:cd07559 288 RALVQESIYD--EFIERAVERFEAIKVGNPLDPETMMGAQVSKDqlekilsyvdigkeegAEVLTGGERLTLGGLDkgYF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 869 VAPEHIVGQPNLYRpgvkwnVAPgsfshlTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHA 948
Cdd:cd07559 366 YEPTLIKGGNNDMR------IFQ------EEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQT 433
|
490 500
....*....|....*....|.
gi 1712455972 949 GNLYINrsTTGAIVLRQPFGG 969
Cdd:cd07559 434 GRVWVN--CYHQYPAHAPFGG 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
663-976 |
3.00e-32 |
|
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: 132.47 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVE 742
Cdd:cd07141 147 GVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDID 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 743 TVILTGGTSTAKRML--AVRPDLHLLA-ETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpK 819
Cdd:cd07141 227 KVAFTGSTEVGKLIQqaAGKSNLKRVTlELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYD--E 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 820 FQSLLADAVESLPVGSAWDLETKMGPLIAPPG-KTLTRGMKTLEDDETWLVAPEHIVGQPNLYrpgvkwnVAPGSFSHLT 898
Cdd:cd07141 305 FVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQfKKILELIESGKKEGAKLECGGKRHGDKGYF-------IQPTVFSDVT 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 899 --------ELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREIELwKQSIHAGNLYINrsTTGAIVLRQPFGG 969
Cdd:cd07141 378 ddmriakeEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDiDKAITF-SNALRAGTVWVN--CYNVVSPQAPFGG 454
|
....*..
gi 1712455972 970 VGLSAYG 976
Cdd:cd07141 455 YKMSGNG 461
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
537-976 |
1.17e-31 |
|
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: 130.27 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRgDMI 616
Cdd:cd07117 3 LFINGEWVKGSSGETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENK-ELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 617 gAMVA--EGGKTIPEadpeiSEAIDFcefyPLTVNHWAQQAGV----------------DICSR---GVVAVITPWNFPL 675
Cdd:cd07117 81 -AMVEtlDNGKPIRE-----TRAVDI----PLAADHFRYFAGViraeegsanmidedtlSIVLRepiGVVGQIIPWNFPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 676 AIPAGGIAAALACGNTVILKPASETvwvaamvcdafwdagvPRDALQMLPCEDEVAESGLVKdgrvetvILTGGTSTAKR 755
Cdd:cd07117 151 LMAAWKLAPALAAGNTVVIKPSSTT----------------SLSLLELAKIIQDVLPKGVVN-------IVTGKGSKSGE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 756 MLAVRPDLHLLA------------------------ETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLE 811
Cdd:cd07117 208 YLLNHPGLDKLAftgstevgrdvaiaaakklipatlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 812 QEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPP----------------GKTLTRGMKTLED--DETWLVAPEH 873
Cdd:cd07117 288 EGIYD--EFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDqldkilsyvdiakeegAKILTGGHRLTENglDKGFFIEPTL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 874 IVGQPNLYRpgvkwnVAPgsfshlTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLD-DREIELwKQSIHAGNLY 952
Cdd:cd07117 366 IVNVTNDMR------VAQ------EEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDiNRALRV-ARAVETGRVW 432
|
490 500
....*....|....*....|....
gi 1712455972 953 INrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07117 433 VN--TYNQIPAGAPFGGYKKSGIG 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
553-976 |
1.15e-30 |
|
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: 127.61 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 553 ESTDPsRPGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEA 630
Cdd:cd07142 22 PTIDP-RNGEVIAHVAEGDAEDVDRAVKAArkAFDEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 631 D-PEISEAIDFCEFY------------PLTVNHWAQQAGVDIcsrGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPA 697
Cdd:cd07142 101 RyAEVPLAARLFRYYagwadkihgmtlPADGPHHVYTLHEPI---GVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 698 SETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPDLHLLA---ETGGKNA 774
Cdd:cd07142 178 EQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPvtlELGGKSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 775 TIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPPG--K 852
Cdd:cd07142 258 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYD--EFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQfeK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 853 TLTRGMKTLEDDETWLVAPEHIvGQPNLYrpgvkwnVAPGSFSHLT--------ELFGPVLGVMPFSRLEEAIEIVRSTG 924
Cdd:cd07142 336 ILSYIEHGKEEGATLITGGDRI-GSKGYY-------IQPTIFSDVKddmkiardEIFGPVQSILKFKTVDEVIKRANNSK 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1712455972 925 YGLTSGLESLDDREIELWKQSIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07142 408 YGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGIG 457
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
570-982 |
1.71e-29 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 124.56 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 570 ASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRgDMIGAMVA-EGGKTIPEADPEISEAIDFCEFyplTV 648
Cdd:PLN02315 53 ASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKL-DYLGRLVSlEMGKILAEGIGEVQEIIDMCDF---AV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 649 NHWAQQAGVDICSR-------------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASET----VWVAAMVCDAF 711
Cdd:PLN02315 129 GLSRQLNGSIIPSErpnhmmmevwnplGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTplitIAMTKLVAEVL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 712 WDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTstaKRMLAVRPDLH-----LLAETGGKNATIVTAMADRDLA 786
Cdd:PLN02315 209 EKNNLPGAIFTSFCGGAEIGEA-IAKDTRIPLVSFTGSS---KVGLMVQQTVNarfgkCLLELSGNNAIIVMDDADIQLA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 787 VKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPPGK-TLTRGMKTLEDDE 865
Cdd:PLN02315 285 VRSVLFAAVGTAGQRCTTCRRLLLHESIYDD--VLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKkNFEKGIEIIKSQG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 866 -TWLVAPEHIVGQPNLYRPGVKwNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELW-- 942
Cdd:PLN02315 363 gKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWig 441
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1712455972 943 KQSIHAGNLYINRSTTGAIVlrqpfGGV--GLSAYGPGVKAG 982
Cdd:PLN02315 442 PLGSDCGIVNVNIPTNGAEI-----GGAfgGEKATGGGREAG 478
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
570-976 |
7.91e-29 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 121.80 E-value: 7.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 570 ASLDQVQQAVSIA--ASDSNPW-KDTSLehRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTI-----PEADPEISE---AI 638
Cdd:TIGR04284 34 ATAADMDAAIAAArrAFDETDWsRDTAL--RVRCLRQLRDALRAHVEELRELTIAEVGAPRmltagAQLEGPVDDlgfAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 639 DFCEFYPltvnhWAQQAGV----DICSR--------GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAM 706
Cdd:TIGR04284 112 DLAESYA-----WTTDLGVaspmGIPTRrtlrreavGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWCAAV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 707 VCDAFWD-AGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKR-MLAVRPDL-HLLAETGGKNATIVTAMADR 783
Cdd:TIGR04284 187 LGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRAvMADAAATLkKVFLELGGKSAFIVLDDADL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 784 DLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDPkfQSLLADAVESLPVGSAWDLETKMGPLI---------------- 847
Cdd:TIGR04284 267 AAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEA--VAAAAATMGSIKPGDPADPGTVCGPVIsarqrdrvqsyldlav 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 848 APPGKTLTRGMKTLEDDETWLVAPEHIVGQPNLYRPGVKwnvapgsfshltELFGPVLGVMPFSRLEEAIEIVRSTGYGL 927
Cdd:TIGR04284 345 AEGGRFACGGGRPADRDRGFFVEPTVIAGLDNNARVARE------------EIFGPVLTVIAHDGDDDAVRIANDSPYGL 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1712455972 928 TSGLESLDDREIELWKQSIHAGNLYINrsttGAIVLRQ--PFGGVGLSAYG 976
Cdd:TIGR04284 413 SGTVFGADPERAAAVAARVRTGTVNVN----GGVWYSAdaPFGGYKQSGIG 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
553-976 |
1.05e-28 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 121.85 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 553 ESTDPsRPGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTipea 630
Cdd:PLN02766 39 ETRDP-RTGEVIARIAEGDKEDVDLAVKAAreAFDHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKL---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 631 dPEISEAIDFcefyPLTVNHWAQQAG--------VDICSR-----------GVVAVITPWNFPLAIPAGGIAAALACGNT 691
Cdd:PLN02766 114 -FALGKAVDI----PAAAGLLRYYAGaadkihgeTLKMSRqlqgytlkepiGVVGHIIPWNFPSTMFFMKVAPALAAGCT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 692 VILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRML--AVRPDLHLLA-E 768
Cdd:PLN02766 189 MVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMqaAATSNLKQVSlE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 769 TGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLI- 847
Cdd:PLN02766 269 LGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYD--EFVKKLVEKAKDWVVGDPFDPRARQGPQVd 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 848 --------------APPGKTLTRGMKTLEDDETWLvapehivgqpnlyRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRL 913
Cdd:PLN02766 347 kqqfekilsyiehgKREGATLLTGGKPCGDKGYYI-------------EPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712455972 914 EEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFG 474
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
568-987 |
1.16e-28 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 121.55 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 568 PMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEF---- 643
Cdd:PRK11241 43 PKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWfaee 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 644 ----YPLTV-NHWAQQAGVDICSR-GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVP 717
Cdd:PRK11241 123 gkriYGDTIpGHQADKRLIVIKQPiGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 718 RDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLA-VRPDLHLLA-ETGGKNATIVTAMADRDLAVKHVVQSAF 795
Cdd:PRK11241 203 AGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEqCAKDIKKVSlELGGNAPFIVFDDADLDKAVEGALASKF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 796 GHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVESLPVGSAWDLETKMGPLIAPPG---------KTLTRGMKTLEDDEt 866
Cdd:PRK11241 283 RNAGQTCVCANRLYVQDGVYD--RFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAvakveehiaDALEKGARVVCGGK- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 867 wlvaPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSI 946
Cdd:PRK11241 360 ----AHELGG--NFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEAL 433
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1712455972 947 HAGNLYINrstTGAIVLR-QPFGGVGLSAYG-PGVKAGGPHYV 987
Cdd:PRK11241 434 EYGIVGIN---TGIISNEvAPFGGIKASGLGrEGSKYGIEDYL 473
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
575-984 |
3.29e-28 |
|
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: 119.26 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 575 VQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEA---------DPEISEAIDFCEFYP 645
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAenicgdqvqLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 646 LTVNH----WAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDAL 721
Cdd:cd07084 81 EPGNHlgqgLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 722 QMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRMLAVRPDLHLLAETGGKNATIVTAMADR-DLAVKHVVQSAFGHAGQ 800
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTACSGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 801 KCSATSLLLLEQEVFDDPKFQSLLADAVESLPVGSAwdletkMGPLIAPpgKTLTRGMKTLEDDETWLV---APEHIVGQ 877
Cdd:cd07084 241 KCTAQSMLFVPENWSKTPLVEKLKALLARRKLEDLL------LGPVQTF--TTLAMIAHMENLLGSVLLfsgKELKNHSI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 878 PNLYRPgvkwNVAPGSF-----------SHLTELFGPVLGVMPFSRLEEA--IEIVRSTGYGLTSGLESLDDREI-ELWK 943
Cdd:cd07084 313 PSIYGA----CVASALFvpideilktyeLVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLqELIG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1712455972 944 QSIHAGNLY-INRSTTGAIVLRqpFGGVGLSAYGPGVKAGGP 984
Cdd:cd07084 389 NLWVAGRTYaILRGRTGVAPNQ--NHGGGPAADPRGAGIGGP 428
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
519-976 |
4.25e-28 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 120.00 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 519 QTLQKWKDQCGDQATVVPLWVGDQQVTPEPDQMRESTDPS--RPGCVVCRYPMASLDQVQQAVSiAASDSNPWKDTSLEH 596
Cdd:PRK09847 4 HHLAYWQDKALSLAIENRLFINGEYTAAAENETFETVDPVtqAPLAKIARGKSVDIDRAVSAAR-GVFERGDWSLSSPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 597 RHEVLRGAAQRMRQRRGDMIGAMVAEGGKTI--------PEADPEI---SEAID--FCEFYPLTVNHWAQQAGVDIcsrG 663
Cdd:PRK09847 83 RKAVLNKLADLMEAHAEELALLETLDTGKPIrhslrddiPGAARAIrwyAEAIDkvYGEVATTSSHELAMIVREPV---G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 664 VVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVET 743
Cdd:PRK09847 160 VIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 744 VILTGGTSTAKRMLAVRPDLHL---LAETGGKNATIVTA-MADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpk 819
Cdd:PRK09847 240 IAFTGSTRTGKQLLKDAGDSNMkrvWLEAGGKSANIVFAdCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADE-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 820 FQSLLADAVESLPVGSAWDLETKMGPLI-APPGKTLTRGMKTLEDDETWLVAPEHiVGQPNLYRPGVKWNVAPGSFSHLT 898
Cdd:PRK09847 318 FLALLKQQAQNWQPGHPLDPATTMGTLIdCAHADSVHSFIREGESKGQLLLDGRN-AGLAAAIGPTIFVDVDPNASLSRE 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712455972 899 ELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLrqPFGGVGLSAYG 976
Cdd:PRK09847 397 EIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTV--PFGGYKQSGNG 472
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
537-976 |
9.14e-28 |
|
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: 118.75 E-value: 9.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 537 LWVGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGD 614
Cdd:cd07140 8 LFINGEFVDAEGGKTYNTINPTD-GSVICKVSLATVEDVDRAVAAAkeAFENGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 615 MI-------GAMVAEG-----------------------GKTIPEADPEISEAIDFCEFYPLtvnhwaqqagvdicsrGV 664
Cdd:cd07140 87 LAtiesldsGAVYTLAlkthvgmsiqtfryfagwcdkiqGKTIPINQARPNRNLTLTKREPI----------------GV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 665 VAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETV 744
Cdd:cd07140 151 CGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 745 ILTGGTSTAKRMLAVRPDLHLLA---ETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQ 821
Cdd:cd07140 231 GFTGSTPIGKHIMKSCAVSNLKKvslELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDE--FV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 822 SLLADAVESLPVGSAWDLETKMGPL--IAPPGKTLTRGMKTLEDDETWLVAPEHiVGQPNLY-RPGVKWNVAPGSFSHLT 898
Cdd:cd07140 309 RRVVEEVKKMKIGDPLDRSTDHGPQnhKAHLDKLVEYCERGVKEGATLVYGGKQ-VDRPGFFfEPTVFTDVEDHMFIAKE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 899 ELFGPVLGVMPF--SRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07140 388 ESFGPIMIISKFddGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDVAAPFGGFKQSGFG 465
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
535-954 |
7.08e-27 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 117.54 E-value: 7.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 535 VPLWVGDQQVTPEPDQMRESTDPSRPGcVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGD 614
Cdd:PLN02419 114 VPNLIGGSFVESQSSSFIDVINPATQE-VVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 615 MIGAMVAEGGKTIPEADPEISEAIDF----CEFYPLTVNHWAQQA--GVDICS----RGVVAVITPWNFPLAIPAGGIAA 684
Cdd:PLN02419 193 LAMNITTEQGKTLKDSHGDIFRGLEVvehaCGMATLQMGEYLPNVsnGVDTYSirepLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 685 ALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKRML--AVRPD 762
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYarAAAKG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 763 LHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLeqeVFDDPKFQSLLADAVESLPVGSAWDLETK 842
Cdd:PLN02419 352 KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVF---VGDAKSWEDKLVERAKALKVTCGSEPDAD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 843 MGPLIAPPGKT-LTRGMKTLEDDETWL-------VAPEHIVGqpNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLE 914
Cdd:PLN02419 429 LGPVISKQAKErICRLIQSGVDDGAKLlldgrdiVVPGYEKG--NFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFD 506
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1712455972 915 EAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYIN 954
Cdd:PLN02419 507 EAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
593-976 |
1.22e-26 |
|
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: 114.55 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 593 SLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEAD-PEIS---EAIDFcefyplTVNH---WAQQAGVDI------ 659
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYlTEIAvvlGEIDH------ALKHlkkWMKPRRVSVplllqp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 660 --CSR-----GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFwDAGVPRDALQMlpCEDEVAE 732
Cdd:cd07087 92 akAYVipeplGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI-PKYFDPEAVAV--VEGGVEV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 733 SGLVKDGRVETVILTGGTSTAKR-MLAVRPdlHL----LaETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSL 807
Cdd:cd07087 169 ATALLAEPFDHIFFTGSPAVGKIvMEAAAK--HLtpvtL-ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 808 LLLEQEVFDdpKFQSLLADAVESLpVGSAWDLETKMGPLI-----------APPGKTLTRGmktLEDDETWLVAPEHIVg 876
Cdd:cd07087 246 VLVHESIKD--ELIEELKKAIKEF-YGEDPKESPDYGRIInerhfdrlaslLDDGKVVIGG---QVDKEERYIAPTILD- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 877 qpnlyrpgvkwNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRS 956
Cdd:cd07087 319 -----------DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDV 387
|
410 420
....*....|....*....|
gi 1712455972 957 TTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07087 388 LLHAAIPNLPFGGVGNSGMG 407
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
661-976 |
1.52e-26 |
|
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: 114.24 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 661 SRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPaSETVWVAAMVCDAFWDAGVPRDALQMLpcEDEVAESGLVKDGR 740
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKP-SELTPHTAALLAELVPKYLDPDAFQVV--QGGVPETTALLEQK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 741 VETVILTGGTSTAkRMLAVRPDLHL---LAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDd 817
Cdd:cd07135 185 FDKIFYTGSGRVG-RIIAEAAAKHLtpvTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYD- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 818 pKFQSLLADAVESLpVGSAWDLETKMGPLIAPP-------------GKTLTRGmktLEDDETWLVAPEHIVgqpnlyrpG 884
Cdd:cd07135 263 -EFVEELKKVLDEF-YPGGANASPDYTRIVNPRhfnrlkslldttkGKVVIGG---EMDEATRFIPPTIVS--------D 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 885 VKWNVapgsfSHLT-ELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVL 963
Cdd:cd07135 330 VSWDD-----SLMSeELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVD 404
|
330
....*....|...
gi 1712455972 964 RQPFGGVGLSAYG 976
Cdd:cd07135 405 NAPFGGVGDSGYG 417
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
556-976 |
6.27e-26 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 113.75 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 556 DPsRPGCVVCRYPMASLDQVQQAVSIA--ASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPE-ADP 632
Cdd:PLN02466 79 DP-RTGEVIAHVAEGDAEDVNRAVAAArkAFDEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQsAKA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 633 EISEAIDFCEFYP--------LTV----NHWAQQAGVDIcsrGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASET 700
Cdd:PLN02466 158 ELPMFARLFRYYAgwadkihgLTVpadgPHHVQTLHEPI---GVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 701 VWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRM--LAVRPDLHLLA-ETGGKNATIV 777
Cdd:PLN02466 235 PLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVleLAAKSNLKPVTlELGGKSPFIV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 778 TAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkF-QSLLADAVESLpVGSAWDLETKMGPLIAPPG-KTLT 855
Cdd:PLN02466 315 CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDE--FvEKAKARALKRV-VGDPFKKGVEQGPQIDSEQfEKIL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 856 RGMKTLEDDETWLVAPEHIVGQPNLY-RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESL 934
Cdd:PLN02466 392 RYIKSGVESGATLECGGDRFGSKGYYiQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQ 471
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1712455972 935 DDREIELWKQSIHAGNLYIN--RSTTGAIvlrqPFGGVGLSAYG 976
Cdd:PLN02466 472 NLDTANTLSRALRVGTVWVNcfDVFDAAI----PFGGYKMSGIG 511
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
553-976 |
7.62e-26 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 113.05 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 553 ESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEAD- 631
Cdd:PRK13252 25 EVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 632 PEISEAIDFCEFY------------PLTVNHWAQqagvdicSR----GVVAVITPWNFPLAIPAGGIAAALACGNTVILK 695
Cdd:PRK13252 104 VDIVTGADVLEYYaglapalegeqiPLRGGSFVY-------TRreplGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 696 PASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAEsGLVKDGRVETVILTGGTSTAKR-MLAVRPDL-HLLAETGGKN 773
Cdd:PRK13252 177 PSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGA-WLTEHPDIAKVSFTGGVPTGKKvMAAAAASLkEVTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 774 ATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIAPP--G 851
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAA--FEARLLERVERIRIGDPMDPATNFGPLVSFAhrD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 852 KTLTRGMKTLEDDETWLVAPEHIvgQPNLYRPGvkWNVAPGSFSHLT--------ELFGPVLGVMPFSRLEEAIEIVRST 923
Cdd:PRK13252 334 KVLGYIEKGKAEGARLLCGGERL--TEGGFANG--AFVAPTVFTDCTddmtivreEIFGPVMSVLTFDDEDEVIARANDT 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1712455972 924 GYGLTSGLESlddREIELWKQSIH---AGNLYINrsTTGAIVLRQPFGGVGLSAYG 976
Cdd:PRK13252 410 EYGLAAGVFT---ADLSRAHRVIHqleAGICWIN--TWGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
538-954 |
1.96e-24 |
|
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: 108.69 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 538 WVGDQQVTPEPDQMRESTDPSRpGCVVCRYPMASLDQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIG 617
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 618 AMVAEGGKTIPEAdpeisEAIDFcefyPLTVNHW--------AQQAGV-DICSR----------GVVAVITPWNFPLAIP 678
Cdd:cd07116 83 AETWDNGKPVRET-----LAADI----PLAIDHFryfagcirAQEGSIsEIDENtvayhfheplGVVGQIIPWNFPLLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 679 AGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAgVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTSTAKRML- 757
Cdd:cd07116 154 TWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMq 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 758 -AVRPDLHLLAETGGKNATIV---TAMADRDL---AVKHVVQSAFgHAGQKCSATSLLLLEQEVFDdpKFQSLLADAVES 830
Cdd:cd07116 233 yASENIIPVTLELGGKSPNIFfadVMDADDAFfdkALEGFVMFAL-NQGEVCTCPSRALIQESIYD--RFMERALERVKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 831 LPVGSAWDLETKMGPLIAPP-----------GK-----TLTRGMKTLEDDEtwlvaPEHIVGQPNLYRPGVKWNVapgsF 894
Cdd:cd07116 310 IKQGNPLDTETMIGAQASLEqlekilsyidiGKeegaeVLTGGERNELGGL-----LGGGYYVPTTFKGGNKMRI----F 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 895 SHltELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYIN 954
Cdd:cd07116 381 QE--EIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN 438
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
589-976 |
3.69e-23 |
|
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: 103.85 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 589 WKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKtiPEADPEISE------AIDFcefyplTVNH---WAQ------ 653
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRK--PAAEVDLTEilpvlsEINH------AIKHlkkWMKpkrvrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 654 -------QAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASET----VWVAAMVCDAFwdagvprdalq 722
Cdd:cd07134 86 plllfgtKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTphtsAVIAKIIREAF----------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 723 mlpCEDEVAesglVKDGRVET-----------VILTGGTSTAKRMLAVRPDlHLLA---ETGGKNATIVTAMADRDLAVK 788
Cdd:cd07134 155 ---DEDEVA----VFEGDAEVaqallelpfdhIFFTGSPAVGKIVMAAAAK-HLASvtlELGGKSPTIVDETADLKKAAK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 789 HVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLET-KMGPLIAPpgKTLTRGMKTLED---D 864
Cdd:cd07134 227 KIAWGKFLNAGQTCIAPDYVFVHESVKDA--FVEHLKAEIEKFYGKDAARKASpDLARIVND--RHFDRLKGLLDDavaK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 865 ETWLVAPEHIVGQPNLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQ 944
Cdd:cd07134 303 GAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLA 382
|
410 420 430
....*....|....*....|....*....|..
gi 1712455972 945 SIHAGNLYINRSTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07134 383 RTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIG 414
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
663-976 |
4.10e-23 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 104.73 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPaSETVWVAAMVCDAFWDAGVPRDALQMlpCEDEVAESGLVKDGRVE 742
Cdd:PTZ00381 111 GVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKP-SELSPHTSKLMAKLLTKYLDPSYVRV--IEGGVEVTTELLKEPFD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 743 TVILTGGTSTAKrMLAVRPDLHLLA---ETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDdpK 819
Cdd:PTZ00381 188 HIFFTGSPRVGK-LVMQAAAENLTPctlELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKD--K 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 820 FQSLLADAV-----------ESLP--VGSawDLETKMGPLIAPPGKTLTRGMKTleDDETWLVAPEHIVgqpnlyrpgvk 886
Cdd:PTZ00381 265 FIEALKEAIkeffgedpkksEDYSriVNE--FHTKRLAELIKDHGGKVVYGGEV--DIENKYVAPTIIV----------- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 887 wNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQP 966
Cdd:PTZ00381 330 -NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLP 408
|
330
....*....|
gi 1712455972 967 FGGVGLSAYG 976
Cdd:PTZ00381 409 FGGVGNSGMG 418
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
573-927 |
2.49e-20 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 95.98 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 573 DQVQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEISEAIDFCEFypltvnhwA 652
Cdd:PLN00412 53 EEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISY--------T 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 653 QQAGVDICSRG-------------------------VVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMV 707
Cdd:PLN00412 125 AEEGVRILGEGkflvsdsfpgnernkycltskiplgVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 708 CDAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGG-----TSTAKRMLAVRPDLhllaetGGKNATIVTAMAD 782
Cdd:PLN00412 205 VHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGdtgiaISKKAGMVPLQMEL------GGKDACIVLEDAD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 783 RDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDlETKMGPLIAPPGKTLTRGmktLE 862
Cdd:PLN00412 279 LDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADA--LVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEG---LV 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 863 DDETWLVAPEHivgQP-----NLYRPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGL 927
Cdd:PLN00412 353 MDAKEKGATFC---QEwkregNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGL 419
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
663-976 |
2.47e-16 |
|
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: 82.92 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPaSE----TVWVAAMVCDAFWDagvprdalqmlpcEDEVAesglVKD 738
Cdd:cd07133 103 GVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKP-SEftprTSALLAELLAEYFD-------------EDEVA----VVT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 739 GRVET-----------VILTGGTSTAKR-MLAVRPDL---HLlaETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCS 803
Cdd:cd07133 165 GGADVaaafsslpfdhLLFTGSTAVGRHvMRAAAENLtpvTL--ELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 804 ATSLLLLEQE-------------------VFDDPKF------------QSLLADA-------VESLPVGSAWDLETKMGP 845
Cdd:cd07133 243 APDYVLVPEDkleefvaaakaavakmyptLADNPDYtsiinerhyarlQGLLEDArakgarvIELNPAGEDFAATRKLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 846 liappgktltrgmktleddetwlvapeHIVgqpnlyrpgvkWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGY 925
Cdd:cd07133 323 ---------------------------TLV-----------LNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPR 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1712455972 926 GLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07133 365 PLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
663-976 |
5.69e-15 |
|
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: 79.09 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAA----MVCDAFwdagvPRDALQMLPCEDEVAESGLvkD 738
Cdd:cd07136 102 GVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKviakIIEETF-----DEEYVAVVEGGVEENQELL--D 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 739 GRVETVILTGGTSTAKR-MLAVRPdlHL----LaETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQE 813
Cdd:cd07136 175 QKFDYIFFTGSVRVGKIvMEAAAK--HLtpvtL-ELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 814 VFDdpKFQSLLADAVESL----PVGSAwdletKMGPLIAPpgKTLTRGMKTLEDDEtwlvapehIV--GQPN---LY-RP 883
Cdd:cd07136 252 VKE--KFIKELKEEIKKFygedPLESP-----DYGRIINE--KHFDRLAGLLDNGK--------IVfgGNTDretLYiEP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 884 GVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVL 963
Cdd:cd07136 315 TILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANP 394
|
330
....*....|...
gi 1712455972 964 RQPFGGVGLSAYG 976
Cdd:cd07136 395 YLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
663-976 |
4.41e-14 |
|
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: 75.91 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPaSETVWVAAmvcdAFWDAGVPR--DALQMLPCEDEVAESGLVKDGR 740
Cdd:cd07137 103 GVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKP-SELAPATS----ALLAKLIPEylDTKAIKVIEGGVPETTALLEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 741 VETVILTGGTSTAKRMLAVRPDlHLLA---ETGGKNATIVTAMADRDLAVKHVVQSAFG-HAGQKCSATSLLLLEQEvfd 816
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAK-HLTPvtlELGGKCPVIVDSTVDLKVAVRRIAGGKWGcNNGQACIAPDYVLVEES--- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 817 dpkFQSLLADAVESLpvgsawdLETKMGPlIAPPGKTLTRGMKT--------LEDDETwlVAPEHIVG----QPNLY-RP 883
Cdd:cd07137 254 ---FAPTLIDALKNT-------LEKFFGE-NPKESKDLSRIVNShhfqrlsrLLDDPS--VADKIVHGgerdEKNLYiEP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 884 GVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRS-----TGYGLTSGlESLDDREIelwkQSIHAGNLYINRSTT 958
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSrpkplAAYVFTKN-KELKRRIV----AETSSGGVTFNDTVV 395
|
330
....*....|....*...
gi 1712455972 959 GAIVLRQPFGGVGLSAYG 976
Cdd:cd07137 396 QYAIDTLPFGGVGESGFG 413
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
662-983 |
6.62e-13 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 72.81 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 662 RGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAA-MVCDaFWDAGV-PRDALQMLpCEdevAESGLVKD- 738
Cdd:PRK11903 149 RGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQrMVKD-VVAAGIlPAGALSVV-CG---SSAGLLDHl 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 739 GRVETVILTGGTSTAKRMLA----VRPDLHLLAETGGKNATIVTAMADR-----DLAVKHVVQSAFGHAGQKCSATSLLL 809
Cdd:PRK11903 224 QPFDVVSFTGSAETAAVLRShpavVQRSVRVNVEADSLNSALLGPDAAPgseafDLFVKEVVREMTVKSGQKCTAIRRIF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 810 LEQEVFDDpkfqslLADAVES----LPVGSAWDLETKMGPLIAPPGKTLTR-GMKTLEDDETWL-----VAPehiVGQPn 879
Cdd:PRK11903 304 VPEALYDA------VAEALAArlakTTVGNPRNDGVRMGPLVSRAQLAAVRaGLAALRAQAEVLfdgggFAL---VDAD- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 880 lyrPGVKWNVAPGSFS----------HLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDR-------EIELW 942
Cdd:PRK11903 374 ---PAVAACVGPTLLGasdpdaatavHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAflaaaalELADS 450
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1712455972 943 KQSIHAGNLYINRSTTG-AIVLRQPFGGvglsayGPGvKAGG 983
Cdd:PRK11903 451 HGRVHVISPDVAALHTGhGNVMPQSLHG------GPG-RAGG 485
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
663-976 |
1.61e-12 |
|
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: 71.10 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPaSETVWVAAMV------------CDAFWDAGVPrdalqmlpcedev 730
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKP-SEVSPATAKLlaelipkyldkeCYPVVLGGVE------------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 731 aESGLVKDGRVETVILTGGTSTAKR-MLAVRPdlHL---LAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATS 806
Cdd:cd07132 168 -ETTELLKQRFDYIFYTGSTSVGKIvMQAAAK--HLtpvTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 807 LLLLEQEVFDD--PKFQSLLADAVESLPVGSAwDLetkmGPLIAppGKTLTRGMKTLE----------DDETWLVAPEHI 874
Cdd:cd07132 245 YVLCTPEVQEKfvEALKKTLKEFYGEDPKESP-DY----GRIIN--DRHFQRLKKLLSggkvaiggqtDEKERYIAPTVL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 875 VgqpnlyrpgvkwNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYIN 954
Cdd:cd07132 318 T------------DVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN 385
|
330 340
....*....|....*....|..
gi 1712455972 955 RSTTGAIVLRQPFGGVGLSAYG 976
Cdd:cd07132 386 DTIMHYTLDSLPFGGVGNSGMG 407
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
663-976 |
1.73e-12 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 71.30 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKPaSETvwvaAMVCDAFWDAGVPR----DALQMLPCEDEVAESGLvkD 738
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKP-SEL----APATSAFLAANIPKyldsKAVKVIEGGPAVGEQLL--Q 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 739 GRVETVILTGGTSTAkRMLAVRPDLHLLA---ETGGKNATIV---TAMADRDLAVKHVVQSAFGH-AGQKCSATSLLLLE 811
Cdd:PLN02203 183 HKWDKIFFTGSPRVG-RIIMTAAAKHLTPvalELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 812 QevfddpKFQSLLADAVESLpvgsawdLETKMGPLIAPPG--------KTLTRGMKTLEDDetwLVAPEHIVG----QPN 879
Cdd:PLN02203 262 E------RFAPILIELLKST-------IKKFFGENPRESKsmarilnkKHFQRLSNLLKDP---RVAASIVHGgsidEKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 880 LY-RPGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTG-----YGLTSGlESLDDREIElwkqSIHAGNLYI 953
Cdd:PLN02203 326 LFiEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPkplaiYAFTNN-EKLKRRILS----ETSSGSVTF 400
|
330 340
....*....|....*....|...
gi 1712455972 954 NRSTTGAIVLRQPFGGVGLSAYG 976
Cdd:PLN02203 401 NDAIIQYACDSLPFGGVGESGFG 423
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
663-976 |
2.51e-12 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 70.85 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKP---ASETVWVAAMVCDAFWDAGVPRdalqmlPCEDEVAESGLVKDG 739
Cdd:PLN02174 114 GVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPselAPASSALLAKLLEQYLDSSAVR------VVEGAVTETTALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 740 RVETVILTGGTSTAKRMLAVRPDlHL---LAETGGKNATIVTAMADRDLAVKHVVQSAFG-HAGQKCSATSLLLLEQEVf 815
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAK-HLtpvVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEY- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 816 dDPKfqslLADAVESlpvgsawDLETKMG--PLiapPGKTLTRGMKTLEDDETWLVAPEHIVGQPNLY-----------R 882
Cdd:PLN02174 266 -APK----VIDAMKK-------ELETFYGknPM---ESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYggekdrenlkiA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 883 PGVKWNVAPGSFSHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIV 962
Cdd:PLN02174 331 PTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAL 410
|
330
....*....|....
gi 1712455972 963 LRQPFGGVGLSAYG 976
Cdd:PLN02174 411 HTLPFGGVGESGMG 424
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
661-983 |
2.86e-12 |
|
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: 70.76 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 661 SRGVVAV-ITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGV-PRDALQMLpcedevaeSGLVKD 738
Cdd:cd07128 143 PRRGVAVhINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLI--------CGSVGD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 739 -----GRVETVILTGGTSTAKRMLA----VRPDLHLLAETGGKNATI-----VTAMADRDLAVKHVVQSAFGHAGQKCSA 804
Cdd:cd07128 215 lldhlGEQDVVAFTGSAATAAKLRAhpniVARSIRFNAEADSLNAAIlgpdaTPGTPEFDLFVKEVAREMTVKAGQKCTA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 805 TSLLLLEQEVFDDpkFQSLLADAVESLPVGSAWDLETKMGPLIappgkTLTRGMKTLEDDETWLVAPEHIVGQPNLYRPg 884
Cdd:cd07128 295 IRRAFVPEARVDA--VIEALKARLAKVVVGDPRLEGVRMGPLV-----SREQREDVRAAVATLLAEAEVVFGGPDRFEV- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 885 VKWNVAPGSF----------------SHLTELFGPVLGVMPFSRLEEAIEIVRSTGYGLTSGLESLDD-------REIEL 941
Cdd:cd07128 367 VGADAEKGAFfpptlllcddpdaataVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPafarelvLGAAP 446
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1712455972 942 WKQSIHAGNLYINRSTTG-AIVLRQPFGGvglsayGPGvKAGG 983
Cdd:cd07128 447 YHGRLLVLNRDSAKESTGhGSPLPQLVHG------GPG-RAGG 482
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
649-960 |
2.85e-10 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 64.05 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 649 NHWAQQAGVDICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVAAMVCDAFWDAGVPRDALQMLPCED 728
Cdd:cd07126 130 DHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 729 EVAESgLVKDGRVETVILTGGTSTAKRmLAVRPDLHLLAETGGKNATIVTA-MADRDLAVKHVVQSAFGHAGQKCSATSL 807
Cdd:cd07126 210 PTMNK-ILLEANPRMTLFTGSSKVAER-LALELHGKVKLEDAGFDWKILGPdVSDVDYVAWQCDQDAYACSGQKCSAQSI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 808 LLLEQEVFDDP---KFQSLLAD-AVESLPVGS--AWDLE---TKMGPLIAPPGKTLTRGMKTLEDdetwlvapEHIVGQP 878
Cdd:cd07126 288 LFAHENWVQAGildKLKALAEQrKLEDLTIGPvlTWTTErilDHVDKLLAIPGAKVLFGGKPLTN--------HSIPSIY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 879 NLYRPG-----VKWNVAPGSFSHLT-ELFGPVLGVMPF--SRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGN 950
Cdd:cd07126 360 GAYEPTavfvpLEEIAIEENFELVTtEVFGPFQVVTEYkdEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGT 439
|
330
....*....|..
gi 1712455972 951 LY--INRSTTGA 960
Cdd:cd07126 440 TYagIRARTTGA 451
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
279-439 |
2.28e-08 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 58.17 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 279 QAYVPDSYPVMQRLIEWSTKRvadgctGLTI--RLVKGANLEMER-------VESSIGGHRQspymskvETDANYKRMLR 349
Cdd:PLN02681 274 QAYLKDARERLRLDLERSERE------GVPLgaKLVRGAYLSLERrlaaslgVPSPVHDTIQ-------DTHACYNRCAE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 350 DLVAAARSGIVHIGLASHNLFDVALGLIWAGDL-VH--TDAIQIEMLEGMANHQRRAIGDHVENLLLYAPACRQDEflnA 426
Cdd:PLN02681 341 FLLEKASNGDGEVMLATHNVESGELAAAKMNELgLHkgDPRVQFAQLLGMSDNLSFGLGNAGFRVSKYLPYGPVEE---V 417
|
170
....*....|...
gi 1712455972 427 IGYLIRRLDENTG 439
Cdd:PLN02681 418 IPYLLRRAEENRG 430
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
663-985 |
1.41e-05 |
|
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: 48.76 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLaIPAGGIAAALACGNTVILKP---ASETVWVAAMVCDAFWDAGVPRDALQMLP-CEDEVAESgLVKD 738
Cdd:cd07077 102 GVTMHILPSTNPL-SGITSALRGIATRNQCIFRPhpsAPFTNRALALLFQAADAAHGPKILVLYVPhPSDELAEE-LLSH 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 739 GRVETVILTGGTSTAKRMLAVRPDLHLLAETGGKNATIVTAMADRDLAVKHVVQSAFgHAGQKCSATSLLLLEQEVFDDP 818
Cdd:cd07077 180 PKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYVVDDVLDPL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 819 KFQSLLADAVESLPVgsawdletKMGPLIAppgktltrgmktleddeTWLVAPEHIvgqpnlyrpgvkwnvapgsfSHLT 898
Cdd:cd07077 259 YEEFKLKLVVEGLKV--------PQETKPL-----------------SKETTPSFD--------------------DEAL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 899 ELFGPVL----GVMPFSRLEEAIEIVRSTGYGLTSGLESLDDREIELWKQSIHAGNLYINRSTTGAIVLRQPFGGvglsa 974
Cdd:cd07077 294 ESMTPLEcqfrVLDVISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGKGV----- 368
|
330
....*....|.
gi 1712455972 975 yGPGVKAGGPH 985
Cdd:cd07077 369 -ERIVTSGMNN 378
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
575-904 |
1.77e-05 |
|
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: 48.69 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 575 VQQAVSIAASDSNPWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTIPEADPEIS----------EAIDFCEFY 644
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGrttgqlrlfaDLVREGSWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 645 PLTVNH----WAQQAGVDICSR----GVVAVITPWNFPLAIPAG--GIAAALACGNTVILK--PA----SETvwVAAMVC 708
Cdd:cd07129 81 DARIDPadpdRQPLPRPDLRRMlvplGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKahPAhpgtSEL--VARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 709 DAFWDAGVPRDALQMLPCEDEVAESGLVKDGRVETVILTGGTStAKRML----AVRPD-LHLLAETGGKNATIVT--AMA 781
Cdd:cd07129 159 AALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRR-GGRALfdaaAARPEpIPFYAELGSVNPVFILpgALA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 782 DR--DLAvKHVVQSAFGHAGQKCSATSLLLLEQEVFDDpKFQSLLADAVESLPVGsawdleTKMGPLIAppgKTLTRGMK 859
Cdd:cd07129 238 ERgeAIA-QGFVGSLTLGAGQFCTNPGLVLVPAGPAGD-AFIAALAEALAAAPAQ------TMLTPGIA---EAYRQGVE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1712455972 860 TLED-DETWLVAPEHIVGQPNLYRP------GVKWnVAPGSFSHltELFGPV 904
Cdd:cd07129 307 ALAAaPGVRVLAGGAAAEGGNQAAPtlfkvdAAAF-LADPALQE--EVFGPA 355
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
566-972 |
6.32e-05 |
|
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: 47.09 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 566 RYPMASLDQVQQAVSIAASDsnpWKDTSLEHRHEVLRGAAQRMRQRRGDMIGAMVAEGGKTI--------PEADPEISEA 637
Cdd:cd07127 80 TYPQCDPDALLAAARAAMPG---WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFmmafqaggPHAQDRGLEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 638 IDFC----EFYPLTVNHWAQQAGVD---------ICSRGVVAVITPWNFPLAIPAGGIAAALACGNTVILKPASETVWVA 704
Cdd:cd07127 157 VAYAwremSRIPPTAEWEKPQGKHDplamektftVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 705 AM---VCDA-FWDAGVPRD--ALQMLPCEDEVAESgLVKDGRVETVILTGGTSTAKRMLAVRPDLHLLAETGGKNATIVT 778
Cdd:cd07127 237 AItvqVAREvLAEAGFDPNlvTLAADTPEEPIAQT-LATRPEVRIIDFTGSNAFGDWLEANARQAQVYTEKAGVNTVVVD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 779 AMADRDLAVKHVVQSAFGHAGQKCSATSLLLL-------EQEVFDDPKFQSLLADAVESLPVGSAWDLETkMGPLIAPpg 851
Cdd:cd07127 316 STDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtDDGRKSFDEVAADLAAAIDGLLADPARAAAL-LGAIQSP-- 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 852 KTLTRGMKTLEDDEtwLVAPEHIVGQPNLYRPGVKWNV-----APGSFSHLTELFGPVLGVMPF----SRLEEAIEIVRS 922
Cdd:cd07127 393 DTLARIAEARQLGE--VLLASEAVAHPEFPDARVRTPLllkldASDEAAYAEERFGPIAFVVATdstdHSIELARESVRE 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1712455972 923 TGyGLTSGLESLDDREIELWKQ-SIHAG-NLYINrsTTGAIVLRQP-----FGGVGL 972
Cdd:cd07127 471 HG-AMTVGVYSTDPEVVERVQEaALDAGvALSIN--LTGGVFVNQSaafsdFHGTGA 524
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
663-816 |
4.00e-03 |
|
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: 41.10 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712455972 663 GVVAVITPWNFPLAIPAGGIAAALACGNTVILKP----ASETVWVAAMVCDAFWDAGVPRDALQMLPCEDEVAESGLVKD 738
Cdd:cd07081 97 GVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712455972 739 GRVETVILTGGTSTAKRmlAVRPDLHLLAETGGKNATIVTAMADRDLAVKHVVQSAFGHAGQKCSATSLLLLEQEVFD 816
Cdd:cd07081 177 PGIGLLLATGGPAVVKA--AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYD 252
|
|
| |
