|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
416-944 |
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: 593.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 416 ASENFMSAIFDLDVDNPAFKREESRFRASINDLATLIDApapgpNHAQDRSTETLIDaplvPFYNEPDTNPALIQNQQWA 495
Cdd:cd07125 1 ANSSFVNRIFDLEVPLEALADALKAFDEKEWEAIPIING-----EETETGEGAPVID----PADHERTIGEVSLADAEDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 496 TDALATAAED--GWldkQTKPtvldggdvekligdvraaaqawaarpAEERARILYKTAELLAVRRGHLVSVAAAEVGKS 573
Cdd:cd07125 72 DAALAIAAAAfaGW---SATP--------------------------VEERAEILEKAADLLEANRGELIALAAAEAGKT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 574 VEQTDPEISEAIDFARYYAQLALDL----------GDVDNAEFTPDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKP 643
Cdd:cd07125 123 LADADAEVREAIDFCRYYAAQARELfsdpelpgptGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 644 SKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVILTGSSETAAMFSSWRPE-----VEINAETSG 718
Cdd:cd07125 203 AEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgpiLPLIAETGG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 719 KNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPLTELPS 798
Cdd:cd07125 283 KNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAE--RFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 799 DKLQHALTTLEEGESWLLKPRQLDDS-GRLWSPGIKEGVkpGTFFHLTEVFGPVLGLM--KAADLEEAIEFQNGNDFGLT 875
Cdd:cd07125 361 GKLLRAHTELMRGEAWLIAPAPLDDGnGYFVAPGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLT 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027915378 876 GGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWKKSsvGLGSKAGGPNYVMLMGTWADAP 944
Cdd:cd07125 439 LGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLS--GTGPKAGGPNYLLRFGNEKTVS 505
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
8-933 |
7.32e-134 |
|
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: 431.78 E-value: 7.32e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 8 ATLSDQAVSKVRAWLEYSKKESvPNADAKRLAAVLQDPNGLDFTVGFVDRVVRTEDAEAAAHALHELGKIAPATMSFLDR 87
Cdd:COG0506 7 EALRARAVALARRLVEAIRAAP-EGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFLVNAST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 88 AQIQAGsLVGRALPKVVVPAARARIRQMVGHMIVDARDKQFGKAVADIQSDGHRLNINLLGEAVLGRKEAAKHLEDTVRL 167
Cdd:COG0506 86 WGLMLT-LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 168 LRRPDveyvsiKVSSVSSQIS-----------MWGFEDTVEYVVEQLTPLYTEAAQAPKgtkFINLDMEEYRDLRLTMEV 236
Cdd:COG0506 165 LEAIG------AAGVDRPGVSvklsalgprysPAQRERVVEELLERLRPLARAAREAGI---FVTIDMEEYDRLDLTLDV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 237 FKRLLSKPELADF-EAGIVLQAYLPDALGAIQDLAEFGRKrtanGGAGIKVRLVKGANLPMEHVHAQITGWPVATEPSKQ 315
Cdd:COG0506 236 FERLLADPELAGWpGVGIVLQAYLKRAEADLDRLAALARR----GGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 316 ATDANYKRVLYWTMrkENMEGLRLGVAGHNLFDIAFAHLLSVERGV-ADRVEFEMLQGMASDQARAV-SQDVGDLLLYVP 393
Cdd:COG0506 312 DTDANYLRCARKLL--EAGDAIYPQFATHNARTIAAALALAGERGRpPDRFEFQMLYGMGEDLQRALaAVDGGRLLLYCP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 394 AVSPQEFDVAISYLVRRLEENGASENFMSAIFDLDVDNPAFKREESRFRASINDLATLIDAPAPGPNHAQDRSTETLIDA 473
Cdd:COG0506 390 VVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 474 PLVPFYNEPDTNPALIQNQQWATDALATAAEDGWLDKQTKPTVLDGGDVEKLIGDV-------RAAAQAWAARPAEERAR 546
Cdd:COG0506 470 ALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAaaaaaaaAAAAAAAAAAAAAAAAA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 547 ILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGDVDNAEFTPDRVVVVTPPWNFPIAIPA 626
Cdd:COG0506 550 AAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAA 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 627 GSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVILTGSSETAAMFSSW 706
Cdd:COG0506 630 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAAT 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 707 RPEVEINAETSGKNAIVITP----------------SADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDSERFRKQ 770
Cdd:COG0506 710 AATAAAAAAAAALAAAAAAAaaaaaaaaggaaaaaaAAAAAAAVAAVAASAAASASASASLLSLLALLLLDADLVILLLA 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 771 LLDAASSLIVDWPTNPSATVGPLTELPSDKLQHALTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHLTEVFGP 850
Cdd:COG0506 790 LAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVL 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 851 VLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWKKSSVGLGSKAGG 930
Cdd:COG0506 870 VLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 949
|
...
gi 1027915378 931 PNY 933
Cdd:COG0506 950 GGA 952
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
542-930 |
4.25e-98 |
|
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: 320.15 E-value: 4.25e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAEFTPDR---------V 611
Cdd:COG1012 65 AERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLyGETIPSDAPGTRayvrreplgV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:COG1012 145 VGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSETAAMFSSWRPE--VEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRK 769
Cdd:COG1012 225 SFTGSTAVGRRIAAAAAEnlKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYD--EFVE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVDWPTNPSATVGPLTELPS-DKLQHALTT-LEEGESWLLKPRQLDDS-GRLWSPGIKEGVKPGTFFHLTE 846
Cdd:COG1012 303 RLVAAAKALKVGDPLDPGTDMGPLISEAQlERVLAYIEDaVAEGAELLTGGRRPDGEgGYFVEPTVLADVTPDMRIAREE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 847 VFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAiVQRQSFGGWKKSsvGLGS 926
Cdd:COG1012 383 IFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQS--GIGR 459
|
....
gi 1027915378 927 KAGG 930
Cdd:COG1012 460 EGGR 463
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
542-936 |
1.88e-94 |
|
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: 311.46 E-value: 1.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL--------GDVDNAEF-TPDRVV 612
Cdd:cd07124 91 EERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLrgfpvemvPGEDNRYVyRPLGVG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:cd07124 171 AVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSET-------AAMFSSWRPEVE-INAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDs 764
Cdd:cd07124 251 FTGSREVglriyerAAKVQPGQKWLKrVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYD- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 765 eRFRKQLLDAASSLIVDWPTNPSATVGPLTELPS-DKLQHALTTLEEGESWLL--KPRQLDDSGRLWSPGIKEGVKPGTF 841
Cdd:cd07124 330 -EFLERLVERTKALKVGDPEDPEVYMGPVIDKGArDRIRRYIEIGKSEGRLLLggEVLELAAEGYFVQPTIFADVPPDHR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWKKSs 921
Cdd:cd07124 409 LAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMS- 487
|
410
....*....|....*
gi 1027915378 922 vGLGSKAGGPNYVML 936
Cdd:cd07124 488 -GTGSKAGGPDYLLQ 501
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
542-937 |
4.42e-89 |
|
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: 294.82 E-value: 4.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGDvDNAEFTPDR----------V 611
Cdd:pfam00171 51 AERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDG-ETLPSDPGRlaytrreplgV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:pfam00171 130 VGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSETAA--MFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRK 769
Cdd:pfam00171 210 SFTGSTAVGRhiAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYD--EFVE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVDWPTNPSATVGPLTELPS-DKLQHAL-TTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHLTEV 847
Cdd:pfam00171 288 KLVEAAKKLKVGDPLDPDTDMGPLISKAQlERVLKYVeDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 848 FGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRqSFGGWKKSSVGlgsK 927
Cdd:pfam00171 368 FGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG---R 443
|
410
....*....|
gi 1027915378 928 AGGPNYVMLM 937
Cdd:pfam00171 444 EGGPYGLEEY 453
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
220-1127 |
1.70e-81 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 290.61 E-value: 1.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 220 INLDMEEYRDLRLTMEVFKRLLSKPELADFEA-GIVLQAYLPDA---LGAIQDLAE-FGRKrtanggagIKVRLVKGANL 294
Cdd:PRK11905 287 LNIDAEEADRLELSLDLLEALCSDPDLAGWNGiGFVVQAYQKRCpfvIDYLIDLARrSGRR--------LMVRLVKGAYW 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 295 PMEHVHAQI---TGWPVATepSKQATDANY----KRVLywtmrkenmeGLRLGV----AGHNlfdiafAHLLSVERGVAD 363
Cdd:PRK11905 359 DAEIKRAQVdglEGFPVFT--RKVHTDVSYiacaRKLL----------AARDVIypqfATHN------AQTLAAIYELAG 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 364 ---RVEFEMLQGMasdqaravsqdvGDLLlYVPAVSPQEFDVA-------------ISYLVRRLEENGASENFMSAIFDL 427
Cdd:PRK11905 421 gkgDFEFQCLHGM------------GEPL-YDQVVGKEKLGRPcriyapvgthetlLAYLVRRLLENGANSSFVNRIVDE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 428 DVD-------------------NPAF---------KREESR-FR-ASINDLATL---IDAPAPGPNHAQDRSTETLIDAP 474
Cdd:PRK11905 488 NVPveeliadpvekvaamgvapHPQIplprdlygpERRNSKgLDlSDEATLAALdeaLNAFAAKTWHAAPLLAGGDVDGG 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 475 LVPFYNEPDTNpALIQNQQWATDAlataaedgwldkqtkptvldggDVEKLIGDVRAAAQAWAARPAEERARILYKTAEL 554
Cdd:PRK11905 568 TRPVLNPADHD-DVVGTVTEASAE----------------------DVERALAAAQAAFPEWSATPAAERAAILERAADL 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 555 LAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLgdVDNAEFTPDRVVVVTPPWNFPIAIPAGSTFAALA 634
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRL--LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALV 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 635 AGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVyPAD-RDAGRALISNEHVDRVILTGSSETA-----AMFSSWRP 708
Cdd:PRK11905 703 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLL-PGDgRTVGAALVADPRIAGVMFTGSTEVArliqrTLAKRSGP 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 709 EVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAasLGILVgsVYD--SERFRKQLLDAASSLIVDWPTNP 786
Cdd:PRK11905 782 PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSA--LRVLC--LQEdvADRVLTMLKGAMDELRIGDPWRL 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 787 SATVGPLTelpSDKLQHALttleegESWLLKPRQLddsGR-LWSPGIKEGVKPGTFFHLT------------EVFGPVLG 853
Cdd:PRK11905 858 STDVGPVI---DAEAQANI------EAHIEAMRAA---GRlVHQLPLPAETEKGTFVAPTlieidsisdlerEVFGPVLH 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 854 LM--KAADLEEAIEFQNGNDFGLTGGLQSlDVDET-RTWLDRVDVGNAYVNRGITGAIVQRQSFGGWKKSsvGLGSKAGG 930
Cdd:PRK11905 926 VVrfKADELDRVIDDINATGYGLTFGLHS-RIDETiAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGG 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 931 PNYV--MLMGTWADAPSLHAPRKAHSLISSLDLPGEDLEWIEKANASDELAWSEEFGTPRDLSGLDVEANIFRYRPAHVV 1008
Cdd:PRK11905 1003 PLYLgrLVREAPTPIPPAHESVDTDAAARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRV 1082
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 1009 LRLddAASARDVARVLLAARRAGSDLRVLQSPGISEQVRE----ILVAAGVSAETVDESVFISNLLRGEyddnaSVRVRY 1084
Cdd:PRK11905 1083 LCV--ADTEEALLRQLAAALATGNVAVVAADSGLAAALADlpglVAARIDWTQDWEADDPFAGALLEGD-----AERARA 1155
|
970 980 990 1000
....*....|....*....|....*....|....*....|...
gi 1027915378 1085 lgkvsdtLRERLAVRPEVALLDDAVTSSGRVELRYWLKEQAIS 1127
Cdd:PRK11905 1156 -------VRQALAARPGAIVPLIAAEPTDAYDLARLVEERSVS 1191
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
480-936 |
5.22e-81 |
|
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: 274.44 E-value: 5.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 480 NEPDTNPALIQNQQWATDALATAAEdgWLDKqTKPTVLDGGDVE--------------KLIGDVRAAAQAWAARP----- 540
Cdd:TIGR01237 3 HEPFTDFADEENRQAFFKALATVKE--QLGK-TYPLVINGERVEtenkivsinpcdksEVVGTVSKASQEHAEHAlqaaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 541 ----------AEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL----------GD 600
Cdd:TIGR01237 80 kafeawkktdPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELakgkpvnsreGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 601 VDNAEFTPDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGR 680
Cdd:TIGR01237 160 TNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 681 ALISNEHVDRVILTGSSETAAMFSSWRPEVE--------INAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAA 752
Cdd:TIGR01237 240 YLVDHPKTSLITFTGSREVGTRIFERAAKVQpgqkhlkrVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 753 SLGILVGSVYDSerFRKQLLDAASSLIVDWPTNPSATVGPLTELPS-DKLQHALtTLEEGESWLLKPRQLDDS-GRLWSP 830
Cdd:TIGR01237 320 SRAVVHEKVYDE--VVERFVEITESLKVGPPDSADVYVGPVIDQKSfNKIMEYI-EIGKAEGRLVSGGCGDDSkGYFIGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 831 GIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQ 910
Cdd:TIGR01237 397 TIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVG 476
|
490 500
....*....|....*....|....*.
gi 1027915378 911 RQSFGGWKKSsvGLGSKAGGPNYVML 936
Cdd:TIGR01237 477 YQPFGGFKMS--GTDSKAGGPDYLAL 500
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
197-934 |
2.10e-77 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 276.69 E-value: 2.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 197 EYVVEQLTPLYTEAAQAPKgTKFINL--DMEEYRDLRLTMEVFKRLLSKPELADFEA-GIVLQAYLPDALGAIQDLAEFG 273
Cdd:PRK11904 264 ERVLAELVPRVLELARLAK-EANIGLtiDAEEADRLELSLDLFEALFRDPSLKGWGGfGLAVQAYQKRALPVLDWLADLA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 274 RKRtangGAGIKVRLVKGANLPMEHVHAQ---ITGWPVATEpsKQATDANY----KRVLywTMRkenmeglrlGV----- 341
Cdd:PRK11904 343 RRQ----GRRIPVRLVKGAYWDSEIKRAQelgLPGYPVFTR--KAATDVSYlacaRKLL--SAR---------GAiypqf 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 342 AGHNlfdiafAHLLSVERGVADRVEFEM--LQGMAS---DQARAVSQ-------DVG---DLLlyvpavspqefdvaiSY 406
Cdd:PRK11904 406 ATHN------AHTVAAILEMAGHRGFEFqrLHGMGEalyDALLDAPGipcriyaPVGshkDLL---------------PY 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 407 LVRRLEENGASENFMSAIFDLDVdnPAfkrEESrfrasINDLATLIDAPAPGPN---------HAQDRST----ETLIDA 473
Cdd:PRK11904 465 LVRRLLENGANSSFVHRLVDPDV--PI---EEL-----VADPVEKLRSFETLPNpkiplprdiFGPERKNskglNLNDRS 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 474 PLVPFYNEPDTnpalIQNQQWAtdalATAAEDGwlDKQTKPtVLDGGDVEKLIGDVRAAAQAWAARP------------- 540
Cdd:PRK11904 535 ELEPLAAAIAA----FLEKQWQ----AGPIING--EGEARP-VVSPADRRRVVGEVAFADAEQVEQAlaaaraafpawsr 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 541 --AEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLgdVDNAEFTPD--------- 609
Cdd:PRK11904 604 tpVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRL--FGAPEKLPGptgesnelr 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 610 ---R-VVVVTPPWNFPIAIPAGSTFAALAAGAGVIhkpSKPSQQCS---AAVVEALWDAGVPREVLHCVyPAD-RDAGRA 681
Cdd:PRK11904 682 lhgRgVFVCISPWNFPLAIFLGQVAAALAAGNTVI---AKPAEQTPliaAEAVKLLHEAGIPKDVLQLL-PGDgATVGAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 682 LISNEHVDRVILTGSSETAAMFS---SWR--PEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGI 756
Cdd:PRK11904 758 LTADPRIAGVAFTGSTETARIINrtlAARdgPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLF 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 757 LVGSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPLTElpsdklQHALTTLEEGEswllkpRQLDDSGRL-WSPGIKEG 835
Cdd:PRK11904 838 VQEDIAD--RVIEMLKGAMAELKVGDPRLLSTDVGPVID------AEAKANLDAHI------ERMKREARLlAQLPLPAG 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 836 VKPGTFF-----------HLT-EVFGPVLGLM--KAADLEEAIEFQNGNDFGLTGGLQSlDVDETRTWL-DRVDVGNAYV 900
Cdd:PRK11904 904 TENGHFVaptafeidsisQLErEVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHS-RIEETADRIaDRVRVGNVYV 982
|
810 820 830
....*....|....*....|....*....|....
gi 1027915378 901 NRGITGAIVQRQSFGGWKKSsvGLGSKAGGPNYV 934
Cdd:PRK11904 983 NRNQIGAVVGVQPFGGQGLS--GTGPKAGGPHYL 1014
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
542-936 |
1.24e-76 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 262.56 E-value: 1.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL----------GDVDNAEFTPDRV 611
Cdd:PRK03137 95 EDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLadgkpvesrpGEHNRYFYIPLGV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:PRK03137 175 GVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSET-------AAMFS---SWRPEVEinAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSV 761
Cdd:PRK03137 255 TFTGSREVglriyerAAKVQpgqIWLKRVI--AEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 762 YDseRFRKQLLDAASSLIVDWPTNPSAtVGPLTELPS-DKLQHALTT-LEEGEsWLLKPRQLDDSGRLWSPGIKEGVKPG 839
Cdd:PRK03137 333 YD--EVLEKVVELTKELTVGNPEDNAY-MGPVINQASfDKIMSYIEIgKEEGR-LVLGGEGDDSKGYFIQPTIFADVDPK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 840 TFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLD---VDETRTwldRVDVGNAYVNRGITGAIVQRQSFGG 916
Cdd:PRK03137 409 ARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNrehLEKARR---EFHVGNLYFNRGCTGAIVGYHPFGG 485
|
410 420
....*....|....*....|
gi 1027915378 917 WKKSsvGLGSKAGGPNYVML 936
Cdd:PRK03137 486 FNMS--GTDSKAGGPDYLLL 503
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
130-423 |
6.18e-74 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 247.02 E-value: 6.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 130 KAVADIQSDGHRLNINLLGEAVLGRKEAAKHLEDTVRLLRRpDVEYVSIKVSSVSSQIS-----------MWGFEDTVEY 198
Cdd:pfam01619 3 KTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDA-LGKAAGPWPLGPRPGISvklsalhpryePLERERVMAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 199 VVEQLTPLYTEAAQAPKgtkFINLDMEEYRDLRLTMEVFKRLLSKPELADFE-AGIVLQAYLPDALGAIQDLAEFGRKRt 277
Cdd:pfam01619 82 LLERLRPLCRLAKELGV---RLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLELARRR- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 278 angGAGIKVRLVKGANLPMEHVHAQITGWPVATEPSKQATDANYKRVLYWTMrkENMEGLRLGVAGHNLFDIAFAHLLSV 357
Cdd:pfam01619 158 ---GRPLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027915378 358 ERGVA-DRVEFEMLQGMASDQARAVSQDVGDLLLYVPAVSPQEFdvaISYLVRRLEENGASENFMSA 423
Cdd:pfam01619 233 ELGIPpRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEEL---LAYLVRRLLENTANSSFVRR 296
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
542-931 |
2.43e-70 |
|
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: 242.11 E-value: 2.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAEFTPDR---------V 611
Cdd:cd07078 20 AERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLhGEVIPSPDPGELaivrreplgV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:cd07078 100 VGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSETAA--MFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVYDseRFR 768
Cdd:cd07078 180 SFTGSTAVGKaiMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASR-LLVhESIYD--EFV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 769 KQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTTLEEGESWLLK--PRQLDDSGRLWSPGIKEGVKPGTFFHLT 845
Cdd:cd07078 257 ERLVERVKALKVGNPLDPDTDMGPLiSAAQLDRVLAYIEDAKAEGAKLLCggKRLEGGKGYFVPPTVLTDVDPDMPIAQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 846 EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQrQSFGGWKKSSVGlg 925
Cdd:cd07078 337 EIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPS-APFGGVKQSGIG-- 413
|
....*.
gi 1027915378 926 sKAGGP 931
Cdd:cd07078 414 -REGGP 418
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
542-936 |
4.43e-66 |
|
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: 232.08 E-value: 4.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-----------GDVDNAEFTPDR 610
Cdd:cd07083 77 EDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLrypavevvpypGEDNESFYVGLG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDR 690
Cdd:cd07083 157 AGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGSSETA----------AMFSSWRPevEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGS 760
Cdd:cd07083 237 INFTGSLETGkkiyeaaarlAPGQTWFK--RLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 761 VYDseRFRKQLLDAASSLIVDWPTNPSATVGPLTELPSDKLQHALTTLEEGESWLLKPRQLDDS-GRLWSPGIKEGVKPG 839
Cdd:cd07083 315 AYE--PVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGeGYFVAPTVVEEVPPK 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 840 TFFHLTEVFGPVLGLM--KAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGW 917
Cdd:cd07083 393 ARIAQEEIFGPVLSVIryKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGF 472
|
410
....*....|....*....
gi 1027915378 918 KKSsvGLGSKAGGPNYVML 936
Cdd:cd07083 473 KLS--GTNAKTGGPHYLRR 489
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
220-1100 |
1.25e-64 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 240.26 E-value: 1.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 220 INLDMEEYRDLRLTMEVFKRLLSKPELADFEA-GIVLQAYL---PDALGAIQDLAEFGRKRtanggagIKVRLVKGANLP 295
Cdd:PRK11809 367 INIDAEEADRLEISLDLLEKLCFEPELAGWNGiGFVIQAYQkrcPFVIDYLIDLARRSRRR-------LMIRLVKGAYWD 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 296 MEHVHAQITG---WPVATEpsKQATDANY---KRVLywtmrkenmeglrLGV--------AGHNlfdiafAHLLSVERGV 361
Cdd:PRK11809 440 SEIKRAQVDGlegYPVYTR--KVYTDVSYlacARKL-------------LAVpnliypqfATHN------AHTLAAIYHL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 362 AD------RVEFEMLQGMASDQARAVSQDVGDLLL------YVPaVSPQEFDVAisYLVRRLEENGASENFMSAIFD--- 426
Cdd:PRK11809 499 AGqnyypgQYEFQCLHGMGEPLYEQVVGKVADGKLnrpcriYAP-VGTHETLLA--YLVRRLLENGANTSFVNRIADtsl 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 427 -LD--VDNP-----AFKREESRFRAS---IndlatlidaPAPGPNHAQDRSTETLIDaplvpFYNE---PDTNPALIQN- 491
Cdd:PRK11809 576 pLDelVADPveaveKLAQQEGQLGLPhpkI---------PLPRDLYGKGRANSAGLD-----LANEhrlASLSSALLASa 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 492 -QQW-ATDALATAAEDGwldkqTKPTVLDGGDVEKLIGDVRAAAQAWAARPAE---------------ERARILYKTAEL 554
Cdd:PRK11809 642 hQKWqAAPMLEDPVAAG-----EMSPVINPADPRDIVGYVREATPAEVEQALEsavnaapiwfatppaERAAILERAADL 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 555 LAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDlgDVDNAEFTPDRVVVVTPPWNFPIAIPAGSTFAALA 634
Cdd:PRK11809 717 MEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRD--DFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALA 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 635 AGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVILTGSSETAAMF---------SS 705
Cdd:PRK11809 795 AGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqrnlagrldPQ 874
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 706 WRPEVEInAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVydSERFRKQLLDAASSLIVDWPTN 785
Cdd:PRK11809 875 GRPIPLI-AETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDV--ADRTLKMLRGAMAECRMGNPDR 951
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 786 PSATVGPL--TELPSDKLQHALTTLEEGeswllkpRQLDDSGRLWSPGIKEG--VKP-----GTFFHLT-EVFGPVLGLM 855
Cdd:PRK11809 952 LSTDIGPVidAEAKANIERHIQAMRAKG-------RPVFQAARENSEDWQSGtfVPPtlielDSFDELKrEVFGPVLHVV 1024
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 856 --KAADLEEAIEFQNGNDFGLTGGLQSlDVDETRTWL-DRVDVGNAYVNRGITGAIVQRQSFGGWKKSsvGLGSKAGGPN 932
Cdd:PRK11809 1025 ryNRNQLDELIEQINASGYGLTLGVHT-RIDETIAQVtGSAHVGNLYVNRNMVGAVVGVQPFGGEGLS--GTGPKAGGPL 1101
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 933 YV--MLMGTWADAPSLHAPRKA------HSLISSLDLPGEDL-EWIEK-----ANASDELAWSEEFGTPRDLSGLDVEAN 998
Cdd:PRK11809 1102 YLyrLLATRPEDALAVTLARQDaeypvdAQLRAALLAPLTALrEWAAErepelAALCDQYAELAQAGTTRLLPGPTGERN 1181
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 999 IFRYRPAHVVLRLddAASARDvARVLLAARRAGSDLRVLQSPGISEQVREILVAAG------VSAETVDESVFISNLLRG 1072
Cdd:PRK11809 1182 TYTLLPRERVLCL--ADTEQD-ALTQLAAVLAVGSQALWPDDALHRALVAALPAAVqariqlAKDWQLADQPFDAVLFHG 1258
|
970 980 990
....*....|....*....|....*....|.
gi 1027915378 1073 EyddnasvrvrylgkvSDTLR---ERLAVRP 1100
Cdd:PRK11809 1259 D---------------SDQLRalcEQVAQRD 1274
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
196-1040 |
2.77e-64 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 238.30 E-value: 2.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 196 VEYVVEQLTPLYTEAAQAPKGTK-FINLDMEEYRDLRLTMEVFKRLLSKPELADFEAGIVLQAYLPDALGAIQDLAefgR 274
Cdd:COG4230 267 EERLLLLLLPLLALLALAAININiDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVGQAVQAYAKALLLVLDLL---A 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 275 KRTANGGAGIKVRLVKGANLPMEHVHAQITGWPVATepskqATDANYKRVLYwtMRKENMEGLRLGVAGHNLFDIAFAHL 354
Cdd:COG4230 344 RRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYP-----VTTRKVLYDAA--ALALALLLLAAQPAFAPQFATHAAAT 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 355 LSVERGVADRVEFEMLQGMAsdqaravsqdvGDLLLYVpAVSPQEFDVA-------------ISYLVRRLEENGASENFM 421
Cdd:COG4230 417 AAAAAAAGGGGEFEFQCLHG-----------MGEYLYD-QVGRGKLGRPcriyapvgshedlLAYLVRRLLENGANSSFV 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 422 SAIFDLDVD-------------------NPA-------F--KREESRF-----RASINDLATLIDAPAPGPNHAQdrste 468
Cdd:COG4230 485 NRIADEDVPveeliadpvekaralggapHPRiplprdlYgpERRNSAGldlsdEAVLAALSAALAAAAEKQWQAA----- 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 469 TLIDAPLVPFYNEPDTNPALIQNQ----QWATDA-------LATAAEDGWldKQTKPtvldggdvekligdvraaaqawa 537
Cdd:COG4230 560 PLIAGEAASGEARPVRNPADHSDVvgtvVEATAAdveaalaAAQAAFPAW--SATPV----------------------- 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 538 arpaEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGDVDnAEFTPDRVVVVTPP 617
Cdd:COG4230 615 ----EERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAP-TVLRGRGVFVCISP 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 618 WNFPIAIPAGSTFAALAAGAGVIhkpSKPSQQCS---AAVVEALWDAGVPREVLHCVyPAD-RDAGRALISNEHVDRVIL 693
Cdd:COG4230 690 WNFPLAIFTGQVAAALAAGNTVL---AKPAEQTPliaARAVRLLHEAGVPADVLQLL-PGDgETVGAALVADPRIAGVAF 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 694 TGSSETA-----AMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFR 768
Cdd:COG4230 766 TGSTETArlinrTLAARDGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIAD--RVL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 769 KQLLDAASSLIVDWPTNPSATVGP------LTELpsdkLQHAlttleegeswllkpRQLDDSGRL-WSPGIKEGVKPGTF 841
Cdd:COG4230 844 EMLKGAMAELRVGDPADLSTDVGPvidaeaRANL----EAHI--------------ERMRAEGRLvHQLPLPEECANGTF 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 F-----------HLT-EVFGPVLGLM--KAADLEEAIEFQNGNDFGLTGGLQSlDVDET-RTWLDRVDVGNAYVNRGITG 906
Cdd:COG4230 906 VaptlieidsisDLErEVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHS-RIDETiDRVAARARVGNVYVNRNIIG 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 907 AIVQRQSFGGWKKSsvGLGSKAGGPNYV--MLMGTWADAPSLHAPRKAhSLISSLDlpgedleWIEKANASdelawseef 984
Cdd:COG4230 985 AVVGVQPFGGEGLS--GTGPKAGGPHYLlrFATERTVTVNTTAAGGNA-SLLALGD-------WLASLLGA--------- 1045
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 1027915378 985 gtpRDLSGLDVEANIFRYRPAHVVLRLddAASARDVARVLLAARRAGSDLRVLQSP 1040
Cdd:COG4230 1046 ---LTLPGPTGERNTLTLRPRGRVLCL--ADSLEALLAQLAAALATGNRAVVAADL 1096
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
544-931 |
8.55e-64 |
|
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: 224.92 E-value: 8.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 544 RARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAE------FT---PDRVVV 613
Cdd:cd07131 61 RAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLfGETVPSElpnkdaMTrrqPIGVVA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 614 VTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVIL 693
Cdd:cd07131 141 LITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 694 TGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQL 771
Cdd:cd07131 221 TGSTEVgeRIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYD--EFLKRF 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 772 LDAASSLIVDWPTNPSATVGPLTElpSDKLQHALTTLE----EGESWLLKPRQLD----DSGRLWSPGIKEGVKPGTFFH 843
Cdd:cd07131 299 VERAKRLRVGDGLDEETDMGPLIN--EAQLEKVLNYNEigkeEGATLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIA 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 844 LTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQrQSFGGWKKSsvG 923
Cdd:cd07131 377 QEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVH-LPFGGVKKS--G 453
|
....*...
gi 1027915378 924 LGSKAGGP 931
Cdd:cd07131 454 NGHREAGT 461
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
542-923 |
7.51e-61 |
|
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: 216.35 E-value: 7.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDV-----DNAEFTPDR----V 611
Cdd:cd07097 59 EARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLsGETlpstrPGVEVETTReplgV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:cd07097 139 VGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSETAAMF--SSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRK 769
Cdd:cd07097 219 SFTGSTAVGRRIaaAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHD--RFVE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVDWPTNPSATVGPL---TELPSDKLQHALTTLEEGEswLL---KPRQLDDSGRLWSPGIKEGVKPGTFFH 843
Cdd:cd07097 297 ALVERTKALKVGDALDEGVDIGPVvseRQLEKDLRYIEIARSEGAK--LVyggERLKRPDEGYYLAPALFAGVTNDMRIA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 844 LTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQrQSFGGWKKSSVG 923
Cdd:cd07097 375 REEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYH-VPFGGRKGSSYG 453
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
542-931 |
7.06e-58 |
|
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: 204.39 E-value: 7.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGDVDNAEFTPDR----------V 611
Cdd:cd06534 16 AERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGeayvrreplgV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:cd06534 96 VGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPRVDKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRK 769
Cdd:cd06534 176 SFTGSTAVgkAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYD--EFVE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLdaasslivdwptnpsatvgpltelpsdklqhalttleegeswllkprqlddsgrlwspGIKEGVKPGTFFHLTEVFG 849
Cdd:cd06534 254 KLV----------------------------------------------------------TVLVDVDPDMPIAQEEIFG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 850 PVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQrQSFGGWKKSSVGlgsKAG 929
Cdd:cd06534 276 PVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGGVKNSGIG---REG 351
|
..
gi 1027915378 930 GP 931
Cdd:cd06534 352 GP 353
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
542-934 |
1.45e-55 |
|
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: 201.68 E-value: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDlgDVDNAEFTPDRVVVVTPPWNFP 621
Cdd:TIGR01238 96 KERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRD--VLGEFSVESRGVFVCISPWNFP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 622 IAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVILTGSSETA- 700
Cdd:TIGR01238 174 LAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAq 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 701 ----AMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQLLDAAS 776
Cdd:TIGR01238 254 linqTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVAD--RVLTMIQGAMQ 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 777 SLIVDWPTNPSATVGPLTElpSDKLQHALTTLEEGESWLLKPRQLD-DSGRLWSPGikEGVKPgTFFHLT-------EVF 848
Cdd:TIGR01238 332 ELKVGVPHLLTTDVGPVID--AEAKQNLLAHIEHMSQTQKKIAQLTlDDSRACQHG--TFVAP-TLFELDdiaelseEVF 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 849 GPVLGLM--KAADLEEAIEFQNGNDFGLTGGLQSlDVDETRTWLD-RVDVGNAYVNRGITGAIVQRQSFGGWKKSsvGLG 925
Cdd:TIGR01238 407 GPVLHVVryKARELDQIVDQINQTGYGLTMGVHS-RIETTYRWIEkHARVGNCYVNRNQVGAVVGVQPFGGQGLS--GTG 483
|
....*....
gi 1027915378 926 SKAGGPNYV 934
Cdd:TIGR01238 484 PKAGGPHYL 492
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
542-920 |
3.43e-53 |
|
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: 192.87 E-value: 3.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAI--------DFARYYAQLALDLGDVDNA-EFTPDRVV 612
Cdd:cd07095 22 EERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAgkidisikAYHERTGERATPMAQGRAVlRHRPHGVM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPAdRDAGRALISNEHVDRVI 692
Cdd:cd07095 102 AVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGG-RETGEALAAHEGIDGLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSETAAMFS---SWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSvYDSERFRK 769
Cdd:cd07095 181 FTGSAATGLLLHrqfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDG-AVGDAFLE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVDWPTNPSATVGPL--TELPSDKLQHALTTLEEGESWLLKPRQLDDSGRLWSPGI----KEGVKPGTffh 843
Cdd:cd07095 260 RLVEAAKRLRIGAPDAEPPFMGPLiiAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGIidvtDAADVPDE--- 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027915378 844 ltEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAiVQRQSFGGWKKS 920
Cdd:cd07095 337 --EIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA-SSTAPFGGVGLS 410
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
544-929 |
7.25e-52 |
|
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: 190.08 E-value: 7.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 544 RARILYKTAELLAVRR---GHLVSVaaaEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAEfTPDR--------- 610
Cdd:cd07086 59 RGEIVRQIGEALRKKKealGRLVSL---EMGKILPEGLGEVQEMIDICDYAVGLSRMLyGLTIPSE-RPGHrlmeqwnpl 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 -VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVV----EALWDAGVPREVLHCVYpADRDAGRALISN 685
Cdd:cd07086 135 gVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTkilaEVLEKNGLPPGVVNLVT-GGGDGGELLVHD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 686 EHVDRVILTGSSET--------AAMFSSwrpeveINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGIL 757
Cdd:cd07086 214 PRVPLVSFTGSTEVgrrvgetvARRFGR------VLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 758 VGSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTTL-EEGESWLLKPRQLD--DSGRLWSPGIK 833
Cdd:cd07086 288 HESVYD--EFLERLVKAYKQVRIGDPLDEGTLVGPLiNQAAVEKYLNAIEIAkSQGGTVLTGGKRIDggEPGNYVEPTIV 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 834 EGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDR--VDVGNAYVNRGITGAIVQr 911
Cdd:cd07086 366 TGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIG- 444
|
410
....*....|....*...
gi 1027915378 912 QSFGGWKKSsvGLGSKAG 929
Cdd:cd07086 445 GAFGGEKET--GGGRESG 460
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
517-923 |
1.85e-48 |
|
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: 179.55 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 517 LDGGDVEKLIGDVRAAAQAWAARPAEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLAL 596
Cdd:cd07094 18 DDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 597 DLGDV----DNAEFTPDRVVVVTP----------PWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAG 662
Cdd:cd07094 98 RIRGEeiplDATQGSDNRLAWTIRepvgvvlaitPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 663 VPREVLHCVYPADRDAGRALISNEHVDRVILTGSSETAAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAF 742
Cdd:cd07094 178 VPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGGF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 743 GHAGQKCSAASLGILVGSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALT-TLEEGESWLLKPRQ 820
Cdd:cd07094 258 YHAGQVCISVQRIYVHEELYD--EFIEAFVAAVKKLKVGDPLDEDTDVGPLiSEEAAERVERWVEeAVEAGARLLCGGER 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 821 lddSGRLWSPGIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYV 900
Cdd:cd07094 336 ---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMV 412
|
410 420
....*....|....*....|...
gi 1027915378 901 NRGiTGAIVQRQSFGGWKKSSVG 923
Cdd:cd07094 413 NDS-SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
542-923 |
2.51e-47 |
|
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: 175.73 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQ-----LALDLGDVDNAE----FTPDRVV 612
Cdd:cd07100 21 AERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEnaeafLADEPIETDAGKayvrYEPLGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFP------IAIPagstfaALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYpADRDAGRALISNE 686
Cdd:cd07100 101 LGIMPWNFPfwqvfrFAAP------NLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL-IDSDQVEAIIADP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 687 HVDRVILTGSSETAAmfsswrpEVeinAETSGKN------------AIVITPSADRDLAVADLVKSAFGHAGQKCSAASL 754
Cdd:cd07100 174 RVRGVTLTGSERAGR-------AV---AAEAGKNlkksvlelggsdPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 755 GILVGSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHAL-TTLEEGESWLLKPRQLDDSGRLWSPGI 832
Cdd:cd07100 244 FIVHEDVYD--EFLEKFVEAMAALKVGDPMDEDTDLGPLaRKDLRDELHEQVeEAVAAGATLLLGGKRPDGPGAFYPPTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 833 KEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrGITGAiVQRQ 912
Cdd:cd07100 322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN-GMVKS-DPRL 399
|
410
....*....|.
gi 1027915378 913 SFGGWKKSSVG 923
Cdd:cd07100 400 PFGGVKRSGYG 410
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
543-929 |
3.87e-47 |
|
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: 175.62 E-value: 3.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLAL-DLG---DVDNAE-------FT---P 608
Cdd:cd07146 41 QRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALrDDGesfSCDLTAngkarkiFTlreP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 609 DRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHV 688
Cdd:cd07146 121 LGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSETAAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFR 768
Cdd:cd07146 201 DLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVAD--EFV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 769 KQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHA-LTTLEEGESWLLKPRQlddSGRLWSPGIKEGVKPGTFFHLTE 846
Cdd:cd07146 279 DLLVEKSAALVVGDPMDPATDMGTViDEEAAIQIENRvEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 847 VFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrGITGAIVQRQSFGGWKKSsvGLGS 926
Cdd:cd07146 356 TFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDS--GLGG 432
|
...
gi 1027915378 927 KAG 929
Cdd:cd07146 433 KEG 435
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
541-923 |
6.44e-46 |
|
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: 172.45 E-value: 6.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 541 AEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDV---DNAEFT------PDR 610
Cdd:cd07088 56 AIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIeGEIipsDRPNENififkvPIG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDR 690
Cdd:cd07088 136 VVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGM 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFR 768
Cdd:cd07088 216 ISLTGSTEAgqKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYD--EFM 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 769 KQLLDAASSLIVDWPTNPSATVGPLTELPSDKLQHALTT--LEEGESWLLKPRQLD-DSGRLWSPGIKEGVKPGTFFHLT 845
Cdd:cd07088 294 EKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVEraVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQE 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027915378 846 EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIvqrQSF-GGWKKSSVG 923
Cdd:cd07088 374 EIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAM---QGFhAGWKKSGLG 449
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
542-929 |
6.64e-46 |
|
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: 172.14 E-value: 6.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAeFTPDR---------- 610
Cdd:cd07118 43 AERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLhGDSYNN-LGDDMlglvlrepig 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDR 690
Cdd:cd07118 122 VVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDM 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGSSE--TAAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDSerFR 768
Cdd:cd07118 202 VSFTGSTRvgKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA--FV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 769 KQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTT-LEEGESWLLKPRQLDD-SGRLWSPGIKEGVKPGTFFHLT 845
Cdd:cd07118 280 AAVVARSRKVRVGDPLDPETKVGAIiNEAQLAKITDYVDAgRAEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIARE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 846 EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAivQRQSFGGWKKSsvGLG 925
Cdd:cd07118 360 EIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGS--PELPFGGFKQS--GIG 435
|
....
gi 1027915378 926 SKAG 929
Cdd:cd07118 436 RELG 439
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
543-929 |
1.12e-44 |
|
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: 168.50 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLA---------LDLGDVDNaeFT---PDR 610
Cdd:cd07114 44 ERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLAdkiegavipVDKGDYLN--FTrrePLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIhkpSKPSQQCSAAVVEA---LWDAGVPREVLHCVYPADRDAGRALISNEH 687
Cdd:cd07114 122 VVAAITPWNSPLLLLAKKLAPALAAGNTVV---LKPSEHTPASTLELaklAEEAGFPPGVVNVVTGFGPETGEALVEHPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 688 VDRVILTGSSETAAMFSSWRPE--VEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDse 765
Cdd:cd07114 199 VAKIAFTGGTETGRHIARAAAEnlAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYD-- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 766 RFRKQLLDAASSLIVDWPTNPSATVGPLTELPS-DKLQHAL-TTLEEGESWLLKPRQLD----DSGRLWSPGIKEGVKPG 839
Cdd:cd07114 277 EFVERLVARARAIRVGDPLDPETQMGPLATERQlEKVERYVaRAREEGARVLTGGERPSgadlGAGYFFEPTILADVTND 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 840 TFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVN--RgitgAIVQRQSFGGW 917
Cdd:cd07114 357 MRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNtyR----ALSPSSPFGGF 432
|
410
....*....|..
gi 1027915378 918 KKSsvGLGSKAG 929
Cdd:cd07114 433 KDS--GIGRENG 442
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
541-931 |
2.60e-44 |
|
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: 166.94 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 541 AEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL----------GDVDNAEFTPDR 610
Cdd:cd07104 21 PQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPegeilpsdvpGKESMVRRVPLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVV-EALWDAGVPREVLHCVYPADRDAGRALISNEHVD 689
Cdd:cd07104 101 VVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 690 RVILTGSS-------ETAAmfsswRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVY 762
Cdd:cd07104 181 MISFTGSTavgrhigELAG-----RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 763 DSerFRKQLLDAASSLIVDWPTNPSATVGPL-----TELPSDKLQHALT---TLEEGESWllkprqlddSGRLWSPGIKE 834
Cdd:cd07104 256 DE--FVEKLVAKAKALPVGDPRDPDTVIGPLinerqVDRVHAIVEDAVAagaRLLTGGTY---------EGLFYQPTVLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 835 GVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrGIT---GAIVqr 911
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN-DQTvndEPHV-- 401
|
410 420
....*....|....*....|
gi 1027915378 912 qSFGGWKKSsvGLGSkAGGP 931
Cdd:cd07104 402 -PFGGVKAS--GGGR-FGGP 417
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
542-923 |
2.71e-43 |
|
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: 164.32 E-value: 2.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLA---LDLGDVDNAEFTPDR-------- 610
Cdd:cd07099 40 EGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAprvLAPRKVPTGLLMPNKkatveyrp 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 --VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYpADRDAGRALISNEhV 688
Cdd:cd07099 120 ygVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVT-GDGATGAALIDAG-V 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSET-----AAMFSSWRPEVeinAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYD 763
Cdd:cd07099 198 DKVAFTGSVATgrkvmAAAAERLIPVV---LELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 seRFRKQLLDAASSLIVDWPTNPSATVGPLT-----ELPSDKLQHAlttLEEGESWLLKPRQLDDSGRLWSPGIKEGVKP 838
Cdd:cd07099 275 --EFVARLVAKARALRPGADDIGDADIGPMTtarqlDIVRRHVDDA---VAKGAKALTGGARSNGGGPFYEPTVLTDVPH 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 839 GTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWK 918
Cdd:cd07099 350 DMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVK 429
|
....*
gi 1027915378 919 KSSVG 923
Cdd:cd07099 430 DSGGG 434
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
542-925 |
6.43e-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: 163.19 E-value: 6.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALD-LGDVDNAE---FT------PDRV 611
Cdd:cd07102 40 EERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEaLADIRVPEkdgFEryirrePLGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRaLISNEHVDRV 691
Cdd:cd07102 120 VLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAA-LIADPRIDHV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSETAAMF--SSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVYDseRFR 768
Cdd:cd07102 199 SFTGSVAGGRAIqrAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIER-IYVhESIYD--AFV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 769 KQLLDAASSLIVDWPTNPSATVGPLTELPSDK--LQHALTTLEEGESWLLKP---RQLDDSGRLWSPGIKEGVKPGTFFH 843
Cdd:cd07102 276 EAFVAVVKGYKLGDPLDPSTTLGPVVSARAADfvRAQIADAIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVM 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 844 LTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGItgAIVQRQSFGGWKKSSVG 923
Cdd:cd07102 356 REETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCD--YLDPALAWTGVKDSGRG 433
|
..
gi 1027915378 924 LG 925
Cdd:cd07102 434 VT 435
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
543-923 |
3.56e-42 |
|
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: 161.53 E-value: 3.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEIS---EAIDFA---------RYYAQLAldlGDVDNAEF-TPD 609
Cdd:cd07085 61 KRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLrglEVVEFAcsiphllkgEYLENVA---RGIDTYSYrQPL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 610 RVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYpADRDAGRALISNEHVD 689
Cdd:cd07085 138 GVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVH-GGKEAVNALLDHPDIK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 690 RVILTGSS-------ETAAMFSSwrpevEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVY 762
Cdd:cd07085 217 AVSFVGSTpvgeyiyERAAANGK-----RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 763 DseRFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTT-LEEGESWLLKPRQLD----DSGRLWSPGIKEGV 836
Cdd:cd07085 292 D--EWIPKLVERAKKLKVGAGDDPGADMGPViSPAAKERIEGLIESgVEEGAKLVLDGRGVKvpgyENGNFVGPTILDNV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 837 KPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITgAIVQRQSFGG 916
Cdd:cd07085 370 TPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGG 448
|
....*..
gi 1027915378 917 WKKSSVG 923
Cdd:cd07085 449 WKGSFFG 455
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
543-929 |
6.71e-42 |
|
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: 160.29 E-value: 6.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAEFTPDRVVVVT-P---- 616
Cdd:cd07103 42 ERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARRIyGRTIPSPAPGKRILVIKqPvgvv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 617 ----PWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:cd07103 122 aaitPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKIS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSETAAMFSswrpevEINAETS-------GKNAIVI-TPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVYD 763
Cdd:cd07103 202 FTGSTAVGKLLM------AQAADTVkrvslelGGNAPFIvFDDADLDKAVDGAIASKFRNAGQTCVCANR-IYVhESIYD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 seRFRKQLLDAASSLIVDWPTNPSATVGPLTELPS-DKLQ-HALTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTF 841
Cdd:cd07103 275 --EFVEKLVERVKKLKVGNGLDEGTDMGPLINERAvEKVEaLVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDML 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVqrQSFGGWKKSs 921
Cdd:cd07103 353 IMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKES- 429
|
....*...
gi 1027915378 922 vGLGSKAG 929
Cdd:cd07103 430 -GLGREGG 436
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
542-923 |
7.13e-42 |
|
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: 160.09 E-value: 7.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLA-------LDLGDvDNAEFT---PDRV 611
Cdd:cd07109 42 AERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAAdklhgetIPLGP-GYFVYTvrePHGV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:cd07109 121 TGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDS----- 764
Cdd:cd07109 201 SFTGSVETgiAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEvlerl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 765 -ERFRKQLLDAASSlivdwptNPSatVGPL-TELPSDKLQHALTTLEEGESWLL----KPRQLDDSGRLWSPGIKEGVKP 838
Cdd:cd07109 281 vERFRALRVGPGLE-------DPD--LGPLiSAKQLDRVEGFVARARARGARIVaggrIAEGAPAGGYFVAPTLLDDVPP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 839 GTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRqSFGGWK 918
Cdd:cd07109 352 DSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIEL-PFGGVK 430
|
....*
gi 1027915378 919 KSSVG 923
Cdd:cd07109 431 KSGHG 435
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
542-923 |
9.41e-42 |
|
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: 160.10 E-value: 9.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDP-EISEAIDFARYYAQLALDLGDVDNAEFTPDR---------- 610
Cdd:cd07089 42 EERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAmQVDGPIGHLRYFADLADSFPWEFDLPVPALRggpgrrvvrr 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 ----VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNE 686
Cdd:cd07089 122 epvgVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 687 HVDRVILTGSSETAAMFsswrpeVEINAET--------SGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILV 758
Cdd:cd07089 202 RVDMVSFTGSTAVGRRI------MAQAAATlkrvllelGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 759 GSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTT-LEEGESWLL---KPRQLdDSGRLWSPGIK 833
Cdd:cd07089 276 RSRYD--EVVEALAAAFEALPVGDPADPGTVMGPLiSAAQRDRVEGYIARgRDEGARLVTgggRPAGL-DKGFYVEPTLF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 834 EGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIvqRQS 913
Cdd:cd07089 353 ADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGP--DAP 430
|
410
....*....|
gi 1027915378 914 FGGWKKSSVG 923
Cdd:cd07089 431 FGGYKQSGLG 440
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
543-923 |
2.19e-41 |
|
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: 158.76 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQT-DPEISEAIDFARYYAQLALDL-GDV-----DNAEFT---PDRVV 612
Cdd:cd07115 42 ERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPRAADTFRYYAGWADKIeGEVipvrgPFLNYTvrePVGVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:cd07115 122 GAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKIT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSETAA--MFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQ 770
Cdd:cd07115 202 FTGSTAVGRkiMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYD--EFLER 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 771 LLDAASSLIVDWPTNPSATVGPLT-ELPSDKLQHALTT-LEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHLTEVF 848
Cdd:cd07115 280 FTSLARSLRPGDPLDPKTQMGPLVsQAQFDRVLDYVDVgREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIF 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027915378 849 GPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgITGAIVQRQSFGGWKKSSVG 923
Cdd:cd07115 360 GPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFG 432
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
541-932 |
2.60e-41 |
|
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: 158.23 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 541 AEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLAL---------DLGDVDNAEFTPDRV 611
Cdd:cd07152 34 PRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTqpqgeilpsAPGRLSLARRVPLGV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVV-EALWDAGVPREVLHcVYPADRDAGRALISNEHVDR 690
Cdd:cd07152 114 VGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLFEEAGLPAGVLH-VLPGGADAGEALVEDPNVAM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGSS-------ETAAmfsswRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYD 763
Cdd:cd07152 193 ISFTGSTavgrkvgEAAG-----RHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVAD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 seRFRKQLLDAASSLIVDWPTNPSATVGPLteLPSDKLQHAL----------TTLEEGESWllkprqlddSGRLWSPGIK 833
Cdd:cd07152 268 --AYTAKLAAKAKHLPVGDPATGQVALGPL--INARQLDRVHaivddsvaagARLEAGGTY---------DGLFYRPTVL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 834 EGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQrQS 913
Cdd:cd07152 335 SGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPH-NP 413
|
410
....*....|....*....
gi 1027915378 914 FGGWKKSsvGLGSKAGGPN 932
Cdd:cd07152 414 FGGMGAS--GNGSRFGGPA 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
542-923 |
5.13e-41 |
|
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: 158.12 E-value: 5.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYyaqLALDLGDVDNAEFTPDR----------- 610
Cdd:cd07082 61 EERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRD---TIEELKRLDGDSLPGDWfpgtkgkiaqv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 ------VVVVTPPWNFPIAIPAgSTFA-ALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALI 683
Cdd:cd07082 138 rreplgVVLAIGPFNYPLNLTV-SKLIpALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 684 SNEHVDRVILTGSSETAAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVY 762
Cdd:cd07082 217 THGRIDVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR-VLVhESVA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 763 DseRFRKQLLDAASSLIVDWPTNPSATVGPL---------TELPSDKLQHALTTLEEGESwllkprqldDSGRLWSPGIK 833
Cdd:cd07082 296 D--ELVELLKEEVAKLKVGMPWDNGVDITPLidpksadfvEGLIDDAVAKGATVLNGGGR---------EGGNLIYPTLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 834 EGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGitgaiVQRQ- 912
Cdd:cd07082 365 DPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK-----CQRGp 439
|
410
....*....|....
gi 1027915378 913 ---SFGGWKKSSVG 923
Cdd:cd07082 440 dhfPFLGRKDSGIG 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
516-923 |
1.39e-40 |
|
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: 156.22 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 516 VLDGGDVEKLIGDVRAAAQAWAARPAEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLA 595
Cdd:cd07149 17 VASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 596 LDLG----DVDNAEFTPDR----------VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDA 661
Cdd:cd07149 97 KRLAgetiPFDASPGGEGRigftirepigVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 662 GVPREVLHCVYPADRDAGRALISNEHVDRVILTGSSETAAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSA 741
Cdd:cd07149 177 GLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 742 FGHAGQKCSAASLgILV-GSVYDSerFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALT-TLEEGESWLLKP 818
Cdd:cd07149 257 FANAGQVCISVQR-IFVhEDIYDE--FLERFVAATKKLVVGDPLDEDTDVGPMiSEAEAERIEEWVEeAVEGGARLLTGG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 819 RQlddSGRLWSPGIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNA 898
Cdd:cd07149 334 KR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGV 410
|
410 420
....*....|....*....|....*
gi 1027915378 899 YVNrGITGAIVQRQSFGGWKKSSVG 923
Cdd:cd07149 411 MIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
543-929 |
1.54e-40 |
|
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: 155.81 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLG------DVDN----AEFTPDRVV 612
Cdd:cd07105 23 ERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIggsipsDKPGtlamVVKEPVGVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGR---ALISNEHVD 689
Cdd:cd07105 103 LGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEDAPEvveALIAHPAVR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 690 RVILTGSS-------ETAAMFssWRPEVeinAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVY 762
Cdd:cd07105 183 KVNFTGSTrvgriiaETAAKH--LKPVL---LELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 763 DseRFRKQLLDAASSLivdwpTNPSATVGPL-TELPSDKLQHALT-TLEEGESWLL-KPRQLDDSGRLWSPGIKEGVKPG 839
Cdd:cd07105 258 D--EFVEKLKAAAEKL-----FAGPVVLGSLvSAAAADRVKELVDdALSKGAKLVVgGLADESPSGTSMPPTILDNVTPD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 840 TFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgitGAIVQRQS---FGG 916
Cdd:cd07105 331 MDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN----GMTVHDEPtlpHGG 406
|
410
....*....|....
gi 1027915378 917 WKKSSVG-LGSKAG 929
Cdd:cd07105 407 VKSSGYGrFNGKWG 420
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
542-907 |
4.51e-40 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 155.50 E-value: 4.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISE-----AIDFARYYAQLALDLGDVDNA----EFTPDRVV 612
Cdd:PRK09457 59 EERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiAISIQAYHERTGEKRSEMADGaavlRHRPHGVV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVyPADRDAGRALISNEHVDRVI 692
Cdd:PRK09457 139 AVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLV-QGGRETGKALAAHPDIDGLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSETAAMFS---SWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILVGSVYDSERFRK 769
Cdd:PRK09457 218 FTGSANTGYLLHrqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARR-LLVPQGAQGDAFLA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVD-WPTNPSATVGPL-TELPSDKLQHALTTLEE--GESwLLKPRQLDDSGRLWSPGIKE--GVK--PGtf 841
Cdd:PRK09457 297 RLVAVAKRLTVGrWDAEPQPFMGAViSEQAAQGLVAAQAQLLAlgGKS-LLEMTQLQAGTGLLTPGIIDvtGVAelPD-- 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027915378 842 fhlTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGA 907
Cdd:PRK09457 374 ---EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA 436
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
520-923 |
6.10e-40 |
|
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: 154.39 E-value: 6.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 520 GDVEKLIGDVRAAAQAWAARPAEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALD-L 598
Cdd:cd07101 18 ADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERlL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 599 GDVDNA-----------EFTPDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREV 667
Cdd:cd07101 98 KPRRRRgaipvltrttvNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 668 LHCVYPADRDAGRALIsnEHVDRVILTGSSETAAMFSSW--RPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHA 745
Cdd:cd07101 178 WQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERagRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 746 GQKCSAASLGILVGSVYDseRFRKQLLDAASSLIV----DWptnpSATVGPLTElpSDKL----QHALTTLEEGESWLLK 817
Cdd:cd07101 256 GQLCVSIERIYVHESVYD--EFVRRFVARTRALRLgaalDY----GPDMGSLIS--QAQLdrvtAHVDDAVAKGATVLAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 818 PRQLDDSGRL-WSPGIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVG 896
Cdd:cd07101 328 GRARPDLGPYfYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAG 407
|
410 420
....*....|....*....|....*...
gi 1027915378 897 NAYVNRGITGAIVQRQS-FGGWKKSSVG 923
Cdd:cd07101 408 TVNVNEGYAAAWASIDApMGGMKDSGLG 435
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
543-931 |
4.81e-39 |
|
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: 151.71 E-value: 4.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAEFT---------PDRVV 612
Cdd:cd07150 44 ERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVrGETLPSDSPgtvsmsvrrPLGVV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:cd07150 124 AGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSETAAMFSS--WRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDSerFRKQ 770
Cdd:cd07150 204 FTGSTAVGREIAEkaGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE--FVKK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 771 LLDAASSLIVDWPTNPSATVGPL-----TELPSDKLQHALT---TLEEGESWllkprqlddSGRLWSPGIKEGVKPG-TF 841
Cdd:cd07150 282 FVARASKLKVGDPRDPDTVIGPLisprqVERIKRQVEDAVAkgaKLLTGGKY---------DGNFYQPTVLTDVTPDmRI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHlTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgitGAIVQRQS---FGGWK 918
Cdd:cd07150 353 FR-EETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHIN----DPTILDEAhvpFGGVK 427
|
410
....*....|...
gi 1027915378 919 KSSVGlgsKAGGP 931
Cdd:cd07150 428 ASGFG---REGGE 437
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
542-923 |
8.26e-39 |
|
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: 151.18 E-value: 8.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDP-EISEAIDFARYYAQLALdlgDVDNAEFTPDR---------- 610
Cdd:cd07093 41 AERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFADYIL---QLDGESYPQDGgalnyvlrqp 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 --VVVVTPPWNFPIAIpagSTF---AALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISN 685
Cdd:cd07093 118 vgVAGLITPWNLPLML---LTWkiaPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 686 EHVDRVILTGSSETAA--MFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVY 762
Cdd:cd07093 195 PDVDLISFTGETATGRtiMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSR-ILVqRSIY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 763 DseRFRKQLLDAASSLIVDWPTNPSATVGPLTElpsdkLQHalttLEEGESWLLKPRQ-----LDDSGRLWSPGIKEG-- 835
Cdd:cd07093 274 D--EFLERFVERAKALKVGDPLDPDTEVGPLIS-----KEH----LEKVLGYVELARAegatiLTGGGRPELPDLEGGyf 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 836 VKPGTFFHLT--------EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVN----RG 903
Cdd:cd07093 343 VEPTVITGLDndsrvaqeEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNcwlvRD 422
|
410 420
....*....|....*....|
gi 1027915378 904 ItgaivqRQSFGGWKKSSVG 923
Cdd:cd07093 423 L------RTPFGGVKASGIG 436
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
542-933 |
1.42e-38 |
|
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: 150.58 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLG-------DVDNAEFT------P 608
Cdd:cd07110 41 AERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQLDakaeravPLPSEDFKarvrreP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 609 DRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHV 688
Cdd:cd07110 121 VGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseR 766
Cdd:cd07110 201 DKISFTGSTATgsQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIAD--A 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 767 FRKQLLDAASSLIVDWPTNPSATVGPLT-ELPSDKLQHALTT-LEEGESWLLKPRQLDDSGRLW--SPGIKEGVKPGTFF 842
Cdd:cd07110 279 FLERLATAAEAIRVGDPLEEGVRLGPLVsQAQYEKVLSFIARgKEEGARLLCGGRRPAHLEKGYfiAPTVFADVPTDSRI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 843 HLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgITGAIVQRQSFGGWKKSSV 922
Cdd:cd07110 359 WREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGI 436
|
410
....*....|...
gi 1027915378 923 G--LGsKAGGPNY 933
Cdd:cd07110 437 GreLG-EWGLDNY 448
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
542-923 |
3.71e-38 |
|
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: 149.38 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLG------DVDNAEF----TPDRV 611
Cdd:cd07151 54 QERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLRMEgrilpsDVPGKENrvyrEPLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVV-EALWDAGVPREVLHCVYPADRDAGRALISNeHVDR 690
Cdd:cd07151 134 VGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEH-PVPR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VI-LTGSSE------TAAMFSSWRPEVEInaetSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYD 763
Cdd:cd07151 213 LIsFTGSTPvgrhigELAGRHLKKVALEL----GGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 SerFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHAL-TTLEEGESWLLKPrqlDDSGRLWSPGIKEGVKPGTF 841
Cdd:cd07151 289 E--FVEKFVERVKALPYGDPSDPDTVVGPLiNESQVDGLLDKIeQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDME 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGitgaIVQRQ---SFGGWK 918
Cdd:cd07151 364 IAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQ----PVNDEphvPFGGEK 439
|
....*
gi 1027915378 919 KSSVG 923
Cdd:cd07151 440 NSGLG 444
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
543-928 |
3.85e-37 |
|
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: 146.35 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVE-QTDPEISEAIDFARYYAQLA-------LDLGDvDNAEFT---PDRV 611
Cdd:cd07108 42 ERGKLLARIADALEARSEELARLLALETGNALRtQARPEAAVLADLFRYFGGLAgelkgetLPFGP-DVLTYTvrePLGV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAgVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:cd07108 121 VGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSA-FGHAGQKCSAASLGILVGSVYDSerFR 768
Cdd:cd07108 200 TFTGSTEVgkIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDA--FL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 769 KQLLDAASSLIVDWPTNPSATVGPLTelpSDKlQHALTT--LEEGESW---------LLKPRQLDDSGRLWSPGIKEGVK 837
Cdd:cd07108 278 EKLVAKLSKLKIGDPLDEATDIGAII---SEK-QFAKVCgyIDLGLSTsgatvlrggPLPGEGPLADGFFVQPTIFSGVD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 838 PGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGitGAIVQRQSFGGW 917
Cdd:cd07108 354 NEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGF 431
|
410
....*....|.
gi 1027915378 918 KKSsvGLGSKA 928
Cdd:cd07108 432 KQS--GLGREA 440
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
543-923 |
4.00e-37 |
|
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: 146.34 E-value: 4.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGD----VDNAEFTPDR-------- 610
Cdd:cd07145 44 KRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRGetipVDAYEYNERRiaftvrep 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 --VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHV 688
Cdd:cd07145 124 igVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSETAAMFSS--WRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseR 766
Cdd:cd07145 204 NMISFTGSTAVGLLIASkaGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYD--K 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 767 FRKQLLDAASSLIVDWPTNPSATVGPLTELPSDKLQHALT--TLEEGESWLLKPRQldDSGRLWSPGIKEGVKPGTFFHL 844
Cdd:cd07145 282 FLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVndAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 845 TEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITgaivQRQS---FGGWKKSS 921
Cdd:cd07145 360 EEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR----FRWDnlpFGGFKKSG 435
|
..
gi 1027915378 922 VG 923
Cdd:cd07145 436 IG 437
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
541-923 |
1.09e-36 |
|
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: 144.59 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 541 AEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGDV-DNAE------FTPDRVVV 613
Cdd:cd07106 40 LEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTASLDLPDEVIeDDDTrrvelrRKPLGVVA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 614 VTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAgVPREVLHCVyPADRDAGRALISNEHVDRVIL 693
Cdd:cd07106 120 AIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVV-SGGDELGPALTSHPDIRKISF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 694 TGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVYDseRFRKQ 770
Cdd:cd07106 198 TGSTATgkKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKR-LYVhESIYD--EFCEA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 771 LLDAASSLIVDWPTNPSATVGPL---------TELPSDKLQHALTTLEEGESwllkprqLDDSGRLWSPGIKEGVKPGTF 841
Cdd:cd07106 275 LVALAKAAVVGDGLDPGTTLGPVqnkmqydkvKELVEDAKAKGAKVLAGGEP-------LDGPGYFIPPTIVDDPPEGSR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRgiTGAIVQRQSFGGWKKSS 921
Cdd:cd07106 348 IVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSG 425
|
..
gi 1027915378 922 VG 923
Cdd:cd07106 426 IG 427
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
542-923 |
1.30e-36 |
|
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: 144.95 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQ-TDPEISEAIDFARYYAQLAldlgdvDNAEFTPDR---------- 610
Cdd:cd07138 58 EERAALLERIAEAYEARADELAQAITLEMGAPITLaRAAQVGLGIGHLRAAADAL------KDFEFEERRgnslvvrepi 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 -VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVD 689
Cdd:cd07138 132 gVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 690 RVILTGSSETAAmfsswrpEVEINA---------ETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-G 759
Cdd:cd07138 212 MVSFTGSTRAGK-------RVAEAAadtvkrvalELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTR-MLVpR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 760 SVYdsERFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTT-LEEGeswllkprqlddsGRLWS--PGIKEG 835
Cdd:cd07138 284 SRY--AEAEEIAAAAAEAYVVGDPRDPATTLGPLaSAAQFDRVQGYIQKgIEEG-------------ARLVAggPGRPEG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 836 ------VKPGTFFHLT--------EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVN 901
Cdd:cd07138 349 lergyfVKPTVFADVTpdmtiareEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN 428
|
410 420
....*....|....*....|..
gi 1027915378 902 RGITGAivqRQSFGGWKKSSVG 923
Cdd:cd07138 429 GAAFNP---GAPFGGYKQSGNG 447
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
543-923 |
2.06e-36 |
|
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: 144.51 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDP-EISEAIDFARYYA---------QLALDLGDVDNAEFT----- 607
Cdd:cd07113 61 ERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQSANFLRYFAgwatkingeTLAPSIPSMQGERYTaftrr 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 608 -PDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVyPADRDAGRALISNE 686
Cdd:cd07113 141 ePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVV-NGKGAVGAQLISHP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 687 HVDRVILTGSSET------AAMFSSWRPEVEInaetSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGS 760
Cdd:cd07113 220 DVAKVSFTGSVATgkkigrQAASDLTRVTLEL----GGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 761 VYDS--ERFRKQLldaaSSLIVDWPTNPSATVGPLTELPS-DKLQHALT-TLEEGESWLLKPRQLDDSGRLWSPGIkegV 836
Cdd:cd07113 296 KFDElvTKLKQAL----SSFQVGSPMDESVMFGPLANQPHfDKVCSYLDdARAEGDEIVRGGEALAGEGYFVQPTL---V 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 837 KP----GTFFHlTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVN-RGITGAIVqr 911
Cdd:cd07113 369 LArsadSRLMR-EETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV-- 445
|
410
....*....|..
gi 1027915378 912 qSFGGWKKSSVG 923
Cdd:cd07113 446 -PFGGMKQSGIG 456
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
542-923 |
3.36e-36 |
|
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: 143.89 E-value: 3.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQT-DPEISEAIDFARYYAQLA-------LDLGDvDNAEFT---PDR 610
Cdd:cd07091 65 RERGRLLNKLADLIERDRDELAALESLDNGKPLEESaKGDVALSIKCLRYYAGWAdkiqgktIPIDG-NFLAYTrrePIG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDR 690
Cdd:cd07091 144 VCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGSSET------AAMFSSWRPeveINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVYD 763
Cdd:cd07091 224 IAFTGSTAVgrtimeAAAKSNLKK---VTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSR-IFVqESIYD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 seRFRKQLLDAASSLIVDWPTNPSATVGPLT-ELPSDKLQHALTT-LEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTF 841
Cdd:cd07091 300 --EFVEKFKARAEKRVVGDPFDPDTFQGPQVsKAQFDKILSYIESgKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgiTGAIVQRQS-FGGWKKS 920
Cdd:cd07091 378 IAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYNVFDAAVpFGGFKQS 454
|
...
gi 1027915378 921 SVG 923
Cdd:cd07091 455 GFG 457
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
521-923 |
6.20e-36 |
|
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: 142.51 E-value: 6.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 521 DVEKLIGDVRAAAQAWAARPAEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLG- 599
Cdd:cd07107 20 DVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTELKg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 600 -----DVDNAEFT---PDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPskPSQqcsaAVVEALWDAGVPREVL--- 668
Cdd:cd07107 100 etipvGGRNLHYTlrePYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKP--PEQ----APLSALRLAELAREVLppg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 669 -HCVYPADRD-AGRALISNEHVDRVILTGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSA-FG 743
Cdd:cd07107 174 vFNILPGDGAtAGAALVRHPDVKRIALIGSVPTgrAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGMnFT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 744 HAGQKCSAASLGILVGSVYDSerFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTTLEEGESWLL----KP 818
Cdd:cd07107 254 WCGQSCGSTSRLFVHESIYDE--VLARVVERVAAIKVGDPTDPATTMGPLvSRQQYDRVMHYIDSAKREGARLVtgggRP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 819 RQLDDSGRLW-SPGIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGN 897
Cdd:cd07107 332 EGPALEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGY 411
|
410 420
....*....|....*....|....*....
gi 1027915378 898 AYVN---RGITGAivqrqSFGGWKKSSVG 923
Cdd:cd07107 412 VWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
543-923 |
8.95e-36 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 142.63 E-value: 8.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTD-PEISEAIDFARYYAQLALDL------GDVDNAEFT---PDRVV 612
Cdd:cd07142 66 ERSRILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIhgmtlpADGPHHVYTlhePIGVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:cd07142 146 GQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSET------AAMFSSWRPeveINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseR 766
Cdd:cd07142 226 FTGSTEVgkiimqLAAKSNLKP---VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYD--E 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 767 FRKQLLDAASSLIVDWPTNPSATVGPLTELP--SDKLQHALTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHL 844
Cdd:cd07142 301 FVEKAKARALKRVVGDPFRKGVEQGPQVDKEqfEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIAR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 845 TEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVN--RGITGAIvqrqSFGGWKKSSV 922
Cdd:cd07142 381 DEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFDASI----PFGGYKMSGI 456
|
.
gi 1027915378 923 G 923
Cdd:cd07142 457 G 457
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
544-925 |
1.17e-35 |
|
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: 141.71 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 544 RARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL----GDVDNAEFT-----PDRVVVV 614
Cdd:cd07120 44 RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEagrmIEPEPGSFSlvlrePMGVAGI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 615 TPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDA-GVPREVLHCVYPADRDAGRALISNEHVDRVIL 693
Cdd:cd07120 124 IVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 694 TGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQL 771
Cdd:cd07120 204 TGSTATgrAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIAD--EVRDRL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 772 LDAASSLIVDWPTNPSATVGPLTELPS-DKLQHALT-TLEEGESWLLKPRQLDDS---GRLWSPGIKEGVKPGTFFHLTE 846
Cdd:cd07120 282 AARLAAVKVGPGLDPASDMGPLIDRANvDRVDRMVErAIAAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEE 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027915378 847 VFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRgiTGAIVQRQSFGGWKKSsvGLG 925
Cdd:cd07120 362 IFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND--WNKLFAEAEEGGYRQS--GLG 436
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
542-934 |
1.87e-35 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 142.14 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAEFTPDRVVVV------ 614
Cdd:PLN02278 84 SERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVyGDIIPSPFPDRRLLVLkqpvgv 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 615 ---TPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:PLN02278 164 vgaITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSETAAMFSSWRPEV--EINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRK 769
Cdd:PLN02278 244 TFTGSTAVGKKLMAGAAATvkRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYD--KFAE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVDWPTNPSATVGPL-TELPSDKL-QHALTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHLTEV 847
Cdd:PLN02278 322 AFSKAVQKLVVGDGFEEGVTQGPLiNEAAVQKVeSHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEV 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 848 FGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVdeTRTW--LDRVDVGNAYVNRGITGAIVqrQSFGGWKKSSVGL- 924
Cdd:PLN02278 402 FGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDL--QRAWrvSEALEYGIVGVNEGLISTEV--APFGGVKQSGLGRe 477
|
410
....*....|
gi 1027915378 925 GSKAGGPNYV 934
Cdd:PLN02278 478 GSKYGIDEYL 487
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
520-923 |
2.86e-35 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 141.94 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 520 GDVEKLIGDVRAAAQAWAARPAEERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLg 599
Cdd:PRK09407 54 ADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKL- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 600 dvdnaeFTPDR-------------------VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWD 660
Cdd:PRK09407 133 ------LAPRRragalpvltkttelrqpkgVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 661 AGVPREVLHCVYPADRDAGRALIsnEHVDRVILTGSSET-------AAmfsswRPEVEINAETSGKNAIVITPSADRDLA 733
Cdd:PRK09407 207 AGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATgrvlaeqAG-----RRLIGFSLELGGKNPMIVLDDADLDKA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 734 VADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQLLDAASSLIV----DWptnpSATVGPLTElpSDKL----QHAL 805
Cdd:PRK09407 280 AAGAVRACFSNAGQLCISIERIYVHESIYD--EFVRAFVAAVRAMRLgagyDY----SADMGSLIS--EAQLetvsAHVD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 806 TTLEEGESWLLKPRQLDDSGRL-WSPGIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVD 884
Cdd:PRK09407 352 DAVAKGATVLAGGKARPDLGPLfYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTA 431
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1027915378 885 ETRTWLDRVDVGNAYVNRGITGAIVQRQS-FGGWKKSSVG 923
Cdd:PRK09407 432 RGRAIAARIRAGTVNVNEGYAAAWGSVDApMGGMKDSGLG 471
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
542-935 |
2.99e-35 |
|
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: 141.96 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVsVAAAEVG--KSVEQTdpEI---SEAIDFARYYAQLALDLGD---VDNAEFTPDRV-- 611
Cdd:cd07123 91 EDRAAIFLKAADLLSGKYRYEL-NAATMLGqgKNVWQA--EIdaaCELIDFLRFNVKYAEELYAqqpLSSPAGVWNRLey 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 ------VVVTPPWNFpIAIpaGSTFAALAA--GAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALI 683
Cdd:cd07123 168 rplegfVYAVSPFNF-TAI--GGNLAGAPAlmGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 684 SNEHVDRVILTGSSETaamFSS-WRPEVE----------INAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAA 752
Cdd:cd07123 245 ASPHLAGLHFTGSTPT---FKSlWKQIGEnldryrtyprIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 753 SLGILVGSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPLTELPS-DKLQ----HA-----LTTLEEGESwllkprqlD 822
Cdd:cd07123 322 SRAYVPESLWP--EVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAfDRIKgyidHAksdpeAEIIAGGKC--------D 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 823 DS-GRLWSPGIKEGVKPGTFFHLTEVFGPVLGLM--KAADLEEAIEF-QNGNDFGLTGGLQSLDVDETRTWLD--RVDVG 896
Cdd:cd07123 392 DSvGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYvyPDSDFEETLELvDTTSPYALTGAIFAQDRKAIREATDalRNAAG 471
|
410 420 430
....*....|....*....|....*....|....*....
gi 1027915378 897 NAYVNRGITGAIVQRQSFGGWKKSsvGLGSKAGGPNYVM 935
Cdd:cd07123 472 NFYINDKPTGAVVGQQPFGGARAS--GTNDKAGSPLNLL 508
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
543-923 |
3.46e-35 |
|
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: 140.15 E-value: 3.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGK-SVEQTDPEISEAIDFARYYAQLALDLGDVDNAEFTPDR----------V 611
Cdd:cd07092 42 ERSKALLKLADAIEENAEELAALESRNTGKpLHLVRDDELPGAVDNFRFFAGAARTLEGPAAGEYLPGHtsmirrepigV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQqCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:cd07092 122 VAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP-LTTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRK 769
Cdd:cd07092 201 SLTGSVRTgkKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYD--EFVA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHLTEVF 848
Cdd:cd07092 279 ALVEAVSAIRVGDPDDEDTEMGPLnSAAQRERVAGFVERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIF 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027915378 849 GPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITgaIVQRQSFGGWKKSSVG 923
Cdd:cd07092 359 GPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
542-931 |
3.18e-34 |
|
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: 137.71 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVE-QTDPEISEAIDFARYYAQLALDLgdvdNAEFT------------- 607
Cdd:cd07139 60 AERAAVLRRLADALEARADELARLWTAENGMPISwSRRAQGPGPAALLRYYAALARDF----PFEERrpgsggghvlvrr 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 608 -PDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSkPSQQCSAAVV-EALWDAGVPREVLHcVYPADRDAGRALISN 685
Cdd:cd07139 136 ePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPS-PETPLDAYLLaEAAEEAGLPPGVVN-VVPADREVGEYLVRH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 686 EHVDRVILTGSSET-----AAMFSSWRPeveINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-G 759
Cdd:cd07139 214 PGVDKVSFTGSTAAgrriaAVCGERLAR---VTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTR-ILVpR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 760 SVYDseRFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTT-LEEGESWLLKPRQLDDSGRLW--SPGIKEG 835
Cdd:cd07139 290 SRYD--EVVEALAAAVAALKVGDPLDPATQIGPLaSARQRERVEGYIAKgRAEGARLVTGGGRPAGLDRGWfvEPTLFAD 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 836 VKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgitGAIVQRQS-F 914
Cdd:cd07139 368 VDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGApF 443
|
410
....*....|....*..
gi 1027915378 915 GGWKKSSVGlgsKAGGP 931
Cdd:cd07139 444 GGFKQSGIG---REGGP 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
542-923 |
5.15e-34 |
|
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: 137.44 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGD--VDNAEFTPDRVV------- 612
Cdd:cd07119 59 QERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGevYDVPPHVISRTVrepvgvc 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:cd07119 139 GLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSETAA--MFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQ 770
Cdd:cd07119 219 FTGGTATGRsiMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHD--KFVAA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 771 LLDAASSLIVDWPTNPSATVGPLT-ELPSDKLQHALTT-LEEGESWLLKPRQLDDsgrlwsPGIKEG--VKPGTFFHLT- 845
Cdd:cd07119 297 LAERAKKIKLGNGLDADTEMGPLVsAEHREKVLSYIQLgKEEGARLVCGGKRPTG------DELAKGyfVEPTIFDDVDr 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 846 -------EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRgiTGAIVQRQSFGGWK 918
Cdd:cd07119 371 tmrivqeEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYK 448
|
....*
gi 1027915378 919 KSSVG 923
Cdd:cd07119 449 QSGIG 453
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
543-923 |
2.91e-33 |
|
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: 134.74 E-value: 2.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLG----DVDNAEFTPDR-----VVV 613
Cdd:cd07090 42 ERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTLSgehvPLPGGSFAYTRreplgVCA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 614 VTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYpADRDAGRALISNEHVDRVIL 693
Cdd:cd07090 122 GIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQ-GGGETGQLLCEHPDVAKVSF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 694 TGSSET----AAMFSSWRPEVEInaETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRK 769
Cdd:cd07090 201 TGSVPTgkkvMSAAAKGIKHVTL--ELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKD--EFTE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVDWPTNPSATVGPLteLPSDKLQHALTTLE----EGESWL-----LKPRQLDDSGRLWSPGIKEGVKPGT 840
Cdd:cd07090 277 RLVERTKKIRIGDPLDEDTQMGAL--ISEEHLEKVLGYIEsakqEGAKVLcggerVVPEDGLENGFYVSPCVLTDCTDDM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 841 FFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNR-GITGAIVqrqSFGGWKK 919
Cdd:cd07090 355 TIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQ 431
|
....
gi 1027915378 920 SSVG 923
Cdd:cd07090 432 SGFG 435
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
560-918 |
3.72e-33 |
|
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: 134.64 E-value: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 560 GHLVSVaaaEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAE---------FTPDRVVVVTPPWNFPIAIPAGST 629
Cdd:cd07130 77 GKLVSL---EMGKILPEGLGEVQEMIDICDFAVGLSRQLyGLTIPSErpghrmmeqWNPLGVVGVITAFNFPVAVWGWNA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 630 FAALAAGAGVIHKPSKPSQQCSAAV----VEALWDAGVPREVLHCVYpADRDAGRALISNEHVDRVILTGSSETAAMFSs 705
Cdd:cd07130 154 AIALVCGNVVVWKPSPTTPLTAIAVtkivARVLEKNGLPGAIASLVC-GGADVGEALVKDPRVPLVSFTGSTAVGRQVG- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 706 wrpeVEINA-------ETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDSerFRKQLLDAASSL 778
Cdd:cd07130 232 ----QAVAArfgrsllELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDE--VLERLKKAYKQV 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 779 IVDWPTNPSATVGPL-TELPSDKLQHALTTL-EEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHlTEVFGPVLGLMK 856
Cdd:cd07130 306 RIGDPLDDGTLVGPLhTKAAVDNYLAAIEEAkSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDAPIVK-EETFAPILYVLK 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027915378 857 AADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRV--DVGNAYVNRGITGAIVQrQSFGGWK 918
Cdd:cd07130 385 FDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIG-GAFGGEK 447
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
542-923 |
7.63e-33 |
|
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: 133.50 E-value: 7.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSV-EQTDPEISEAIDFARYYAQlALD--LGDVdnAEFTPDRVVVVT--P 616
Cdd:cd07112 48 AERKAVLLRLADLIEAHRDELALLETLDMGKPIsDALAVDVPSAANTFRWYAE-AIDkvYGEV--APTGPDALALITreP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 617 --------PWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHV 688
Cdd:cd07112 125 lgvvgavvPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSETAAMFSSWRPEV---EINAETSGKNAIVITPSA-DRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDs 764
Cdd:cd07112 205 DALAFTGSTEVGRRFLEYSGQSnlkRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKD- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 765 eRFRKQLLDAASSLIVDWPTNPSATVGPLTElpSDKLQHALTTLEEGES---WLL---KPRQLDDSGRLWSPGIKEGVKP 838
Cdd:cd07112 284 -EFLEKVVAAAREWKPGDPLDPATRMGALVS--EAHFDKVLGYIESGKAegaRLVaggKRVLTETGGFFVEPTVFDGVTP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 839 GTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgITGAIVQRQSFGGWK 918
Cdd:cd07112 361 DMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN--CFDEGDITTPFGGFK 438
|
....*
gi 1027915378 919 KSSVG 923
Cdd:cd07112 439 QSGNG 443
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
543-923 |
4.88e-32 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 131.87 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDP-EISEAIDFARYYAQLALDL-GDV--DNAEF------TPDRVV 612
Cdd:PLN02766 83 ERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIhGETlkMSRQLqgytlkEPIGVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:PLN02766 163 GHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSET------AAMFSSWRPeveINAETSGKNAIVITPSADRDLAVaDLVKSA-FGHAGQKCSAASLGILVGSVYDse 765
Cdd:PLN02766 243 FTGSTEVgrkimqAAATSNLKQ---VSLELGGKSPLLIFDDADVDMAV-DLALLGiFYNKGEICVASSRVYVQEGIYD-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 766 RFRKQLLDAASSLIVDWPTNPSATVGPltELPSDKLQHALTTLE----EGESWLLKPRQLDDSGRLWSPGIKEGVKPGTF 841
Cdd:PLN02766 317 EFVKKLVEKAKDWVVGDPFDPRARQGP--QVDKQQFEKILSYIEhgkrEGATLLTGGKPCGDKGYYIEPTIFTDVTEDMK 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgITGAIVQRQSFGGWKKSS 921
Cdd:PLN02766 395 IAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSG 472
|
..
gi 1027915378 922 VG 923
Cdd:PLN02766 473 FG 474
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
543-935 |
6.09e-32 |
|
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: 130.83 E-value: 6.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLA-------LDLGDVDNAE--------Ft 607
Cdd:cd07147 44 RRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEAtriygevLPLDISARGEgrqglvrrF- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 608 PDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHcVYPADRDAGRALISNEH 687
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFS-VLPCSRDDADLLVTDER 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 688 VDRVILTGSSETAAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRF 767
Cdd:cd07147 202 IKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYD--EF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 768 RKQLLDAASSLIVDWPTNPSATVGPLTElPSDklqhalttLEEGESW----------LLKPRQLDdsGRLWSPGIKEGVK 837
Cdd:cd07147 280 KSRLVARVKALKTGDPKDDATDVGPMIS-ESE--------AERVEGWvneavdagakLLTGGKRD--GALLEPTILEDVP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 838 PGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRgITGAIVQRQSFGGW 917
Cdd:cd07147 349 PDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND-VPTFRVDHMPYGGV 427
|
410
....*....|....*...
gi 1027915378 918 KKSsvGLGSKagGPNYVM 935
Cdd:cd07147 428 KDS--GIGRE--GVRYAI 441
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
542-923 |
6.17e-32 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 130.63 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLA--------LDLGDVDNAE----FTPD 609
Cdd:PRK09406 45 AQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAealladepADAAAVGASRayvrYQPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 610 RVVVVTPPWNFPI--AIpagsTFAALAAGAGVI----HKPSKPsqQCSAAVVEALWDAGVPREVLHCVYpADRDAGRALI 683
Cdd:PRK09406 125 GVVLAVMPWNFPLwqVV----RFAAPALMAGNVgllkHASNVP--QTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAIL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 684 SNEHVDRVILTGSSETA-AMFSSWRPEVEINA-ETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSV 761
Cdd:PRK09406 198 RDPRVAAATLTGSEPAGrAVAAIAGDEIKKTVlELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 762 YDSerFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALT-TLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPG 839
Cdd:PRK09406 278 YDA--FAEKFVARMAALRVGDPTDPDTDVGPLaTEQGRDEVEKQVDdAVAAGATILCGGKRPDGPGWFYPPTVITDITPD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 840 TFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrGITgAIVQRQSFGGWKK 919
Cdd:PRK09406 356 MRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMT-VSYPELPFGGVKR 433
|
....
gi 1027915378 920 SSVG 923
Cdd:PRK09406 434 SGYG 437
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
543-923 |
9.99e-31 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 127.28 E-value: 9.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQ-----LALDLGDVDNA----EFTPDRVVV 613
Cdd:PRK13968 52 YRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEhgpamLKAEPTLVENQqaviEYRPLGTIL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 614 VTPPWNFPI------AIPAgstfaaLAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVyPADRDAGRALISNEH 687
Cdd:PRK13968 132 AIMPWNFPLwqvmrgAVPI------LLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWL-NADNDGVSQMINDSR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 688 VDRVILTGSSETAAMFSSWRPEV--EINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVydSE 765
Cdd:PRK13968 205 IAAVTVTGSVRAGAAIGAQAGAAlkKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGI--AS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 766 RFRKQLLDAASSLIVDWPTNPSATVGPLTELP-SDKLQHALT-TLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFH 843
Cdd:PRK13968 283 AFTERFVAAAAALKMGDPRDEENALGPMARFDlRDELHHQVEaTLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 844 LTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrGITgAIVQRQSFGGWKKSSVG 923
Cdd:PRK13968 363 REELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN-GYC-ASDARVAFGGVKKSGFG 440
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
543-923 |
3.20e-30 |
|
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: 125.92 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSV-EQTDPEISEAIDFARYYAQLAldlgD--------VDNAEFTPDR--- 610
Cdd:cd07141 70 ERGRLLNKLADLIERDRAYLASLETLDNGKPFsKSYLVDLPGAIKVLRYYAGWA----DkihgktipMDGDFFTYTRhep 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 --VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHV 688
Cdd:cd07141 146 vgVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSET------AAMFSSWRpevEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVY 762
Cdd:cd07141 226 DKVAFTGSTEVgkliqqAAGKSNLK---RVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIY 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 763 DseRFRKQLLDAASSLIVDWPTNPSATVGP-LTELPSDKLQHALTT-LEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGT 840
Cdd:cd07141 303 D--EFVKRSVERAKKRVVGNPFDPKTEQGPqIDEEQFKKILELIESgKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDM 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 841 FFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgiTGAIVQRQS-FGGWKK 919
Cdd:cd07141 381 RIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQApFGGYKM 457
|
....
gi 1027915378 920 SSVG 923
Cdd:cd07141 458 SGNG 461
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
548-923 |
9.77e-30 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 123.31 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 548 LYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAEFTPDRVVV------VTP---P 617
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYeGEIIQSDRPGENILLfkralgVTTgilP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 618 WNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVILTGSS 697
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 698 ETAA--MFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQLLDAA 775
Cdd:PRK10090 161 SAGEkiMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD--QFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 776 SSLIVDWP-TNPSATVGPLTElpSDKLQHALTTL----EEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHLTEVFGP 850
Cdd:PRK10090 239 QAVQFGNPaERNDIAMGPLIN--AAALERVEQKVaravEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGP 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027915378 851 VLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIvqrQSF-GGWKKSSVG 923
Cdd:PRK10090 317 VLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSGIG 387
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
605-929 |
1.55e-29 |
|
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: 123.56 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 605 EFTPDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSK----PSQQCSAAVVEALWDAGVPREVLHCV--YPadrDA 678
Cdd:cd07098 117 EYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEqvawSSGFFLSIIRECLAACGHDPDLVQLVtcLP---ET 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 679 GRALISNEHVDRVILTGSSETA--AMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGI 756
Cdd:cd07098 194 AEALTSHPVIDHITFIGSPPVGkkVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 757 LVGSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPLT-ELPSDKLQHALTT-LEEGESWL----LKPRQLDDSGRLWSP 830
Cdd:cd07098 274 VHEKIYD--KLLEILTDRVQALRQGPPLDGDVDVGAMIsPARFDRLEELVADaVEKGARLLaggkRYPHPEYPQGHYFPP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 831 GIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQ 910
Cdd:cd07098 352 TLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQ 431
|
330
....*....|....*....
gi 1027915378 911 RQSFGGWKKSsvGLGSKAG 929
Cdd:cd07098 432 QLPFGGVKGS--GFGRFAG 448
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
543-928 |
2.36e-29 |
|
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: 123.41 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDP-EISEAIDFARYYAQLA-LDLG---DVDNAEFT-----PDRVV 612
Cdd:cd07143 69 KRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWAdKIHGqviETDIKKLTytrhePIGVC 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSK--P-SQQCSAAVVEalwDAGVPREVLHCVYPADRDAGRALISNEHVD 689
Cdd:cd07143 149 GQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSEltPlSALYMTKLIP---EAGFPPGVINVVSGYGRTCGNAISSHMDID 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 690 RVILTGSSET------AAMFSSWRpevEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYD 763
Cdd:cd07143 226 KVAFTGSTLVgrkvmeAAAKSNLK---KVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 seRFRKQLLDAASSLIVDWPTNPSATVGP-LTELPSDKLQHALTT-LEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTF 841
Cdd:cd07143 303 --KFVKRFKEKAKKLKVGDPFAEDTFQGPqVSQIQYERIMSYIESgKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgITGAIVQRQSFGGWKKSS 921
Cdd:cd07143 381 IVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSG 458
|
....*....
gi 1027915378 922 VG--LGSKA 928
Cdd:cd07143 459 IGreLGEYA 467
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
542-926 |
4.22e-29 |
|
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: 122.90 E-value: 4.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQT-DPEISEAIDFARYYAQLALDL-GDV---DNAEF-----TPDRV 611
Cdd:cd07144 68 EERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSNaLGDLDEIIAVIRYYAGWADKIqGKTiptSPNKLaytlhEPYGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:cd07144 148 CGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSET--AAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVYDS--ER 766
Cdd:cd07144 228 AFTGSTATgrLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSR-IYVqESIYDKfvEK 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 767 FRKQlldAASSLIVDWPTNPSATVGPLTelpsDKLQH--ALTTLEEGESWLLKprqLDDSGRLWSPGIKEG--VKPGTFF 842
Cdd:cd07144 307 FVEH---VKQNYKVGSPFDDDTVVGPQV----SKTQYdrVLSYIEKGKKEGAK---LVYGGEKAPEGLGKGyfIPPTIFT 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 843 HLT--------EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIvqRQSF 914
Cdd:cd07144 377 DVPqdmrivkeEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GVPF 454
|
410
....*....|....
gi 1027915378 915 GGWKKSSVG--LGS 926
Cdd:cd07144 455 GGFKMSGIGreLGE 468
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
543-923 |
7.52e-29 |
|
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: 121.79 E-value: 7.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSV-EQTDPEISEAIDFARYYAQLAL----DLGDVDNAEFT-----PDRVV 612
Cdd:cd07117 61 ERANILNKIADIIDENKELLAMVETLDNGKPIrETRAVDIPLAADHFRYFAGVIRaeegSANMIDEDTLSivlrePIGVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKpSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:cd07117 141 GQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSS-TTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSETAAMFSSWRPEVEINA--ETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRKQ 770
Cdd:cd07117 220 FTGSTEVGRDVAIAAAKKLIPAtlELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYD--EFVAK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 771 LLDAASSLIVDWPTNPSATVGP-LTELPSDKLQHAL-TTLEEGESWLLKPRQLD----DSGRLWSPGIKEGVKPGTFFHL 844
Cdd:cd07117 298 LKEKFENVKVGNPLDPDTQMGAqVNKDQLDKILSYVdIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQ 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027915378 845 TEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgITGAIVQRQSFGGWKKSSVG 923
Cdd:cd07117 378 EEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYKKSGIG 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
543-901 |
1.97e-28 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 120.99 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLG-------DVDNAEFT------PD 609
Cdd:PLN02467 73 VRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDakqkapvSLPMETFKgyvlkePL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 610 RVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVD 689
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 690 RVILTGSSETAA-MFSSWRPEVE-INAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVydSERF 767
Cdd:PLN02467 233 KIAFTGSTATGRkIMTAAAQMVKpVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERI--ASEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 768 RKQLLDAASSLIVDWPTNPSATVGPL-TELPSDK-LQHALTTLEEGESWLL---KPRQLDdSGRLWSPGIKEGVKPGTFF 842
Cdd:PLN02467 311 LEKLVKWAKNIKISDPLEEGCRLGPVvSEGQYEKvLKFISTAKSEGATILCggkRPEHLK-KGFFIEPTIITDVTTSMQI 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1027915378 843 HLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVN 901
Cdd:PLN02467 390 WREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
542-934 |
2.84e-28 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 120.01 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAEFTPDRVVVVT----- 615
Cdd:PRK11241 70 KERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIyGDTIPGHQADKRLIVIKqpigv 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 616 ----PPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:PRK11241 150 taaiTPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSETAA--MFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDseRFRK 769
Cdd:PRK11241 230 SFTGSTEIGRqlMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYD--RFAE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 770 QLLDAASSLIVDWPTNPSATVGPLT-ELPSDKLQ-HALTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFHLTEV 847
Cdd:PRK11241 308 KLQQAVSKLHIGDGLEKGVTIGPLIdEKAVAKVEeHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEET 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 848 FGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVqrQSFGGWKKSSVGL-GS 926
Cdd:PRK11241 388 FGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIKASGLGReGS 465
|
....*...
gi 1027915378 927 KAGGPNYV 934
Cdd:PRK11241 466 KYGIEDYL 473
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
544-945 |
4.33e-27 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 117.93 E-value: 4.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 544 RARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLA-LDLGD-VDNAEFTPDRVVVVTP----- 616
Cdd:PLN02419 175 RQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMAtLQMGEyLPNVSNGVDTYSIREPlgvca 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 617 ---PWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADrDAGRALISNEHVDRVIL 693
Cdd:PLN02419 255 gicPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTN-DTVNAICDDEDIRAVSF 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 694 TGSSeTAAMFSSWRPEVE---INAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGsvyDSERFRKQ 770
Cdd:PLN02419 334 VGSN-TAGMHIYARAAAKgkrIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVG---DAKSWEDK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 771 LLDAASSLIVDWPTNPSATVGP-LTELPSDKLQHALTT-LEEGESWLLKPRQL----DDSGRLWSPGIKEGVKPGTFFHL 844
Cdd:PLN02419 410 LVERAKALKVTCGSEPDADLGPvISKQAKERICRLIQSgVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 845 TEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITgAIVQRQSFGGWKKSSVG- 923
Cdd:PLN02419 490 EEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIP-VPLPFFSFTGNKASFAGd 568
|
410 420
....*....|....*....|....*..
gi 1027915378 924 --LGSKAGGPNYVMLMGT---WADAPS 945
Cdd:PLN02419 569 lnFYGKAGVDFFTQIKLVtqkQKDIHS 595
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
543-923 |
1.95e-26 |
|
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: 114.75 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSV-EQTDPEISEAIDFARYYAQLAL----DLGDVDNAEFT-----PDRVV 612
Cdd:cd07559 61 ERANILNKIADRIEENLELLAVAETLDNGKPIrETLAADIPLAIDHFRYFAGVIRaqegSLSEIDEDTLSyhfhePLGVV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIhkpSKPSQQCSAAVVE--ALWDAGVPREVLHCVYPADRDAGRALISNEHVDR 690
Cdd:cd07559 141 GQIIPWNFPLLMAAWKLAPALAAGNTVV---LKPASQTPLSILVlmELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGSSETAAMFSSWRPEVEINA--ETSGKNAIVITPSA-DRDLAVADLVKSAF-GHA---GQKCSAASLGILVGSVYD 763
Cdd:cd07559 218 LAFTGSTTVGRLIMQYAAENLIPVtlELGGKSPNIFFDDAmDADDDFDDKAEEGQlGFAfnqGEVCTCPSRALVQESIYD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 seRFRKQLLDAASSLIVDWPTNPSATVGplTELPSDKLQHALTTL----EEGeswllkPRQLDDSGRLWSPGIKEG--VK 837
Cdd:cd07559 298 --EFIERAVERFEAIKVGNPLDPETMMG--AQVSKDQLEKILSYVdigkEEG------AEVLTGGERLTLGGLDKGyfYE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 838 PGTFFHLT--------EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDEtrtwldrvdvgnAY-VNRGI-TG- 906
Cdd:cd07559 368 PTLIKGGNndmrifqeEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINR------------ALrVARGIqTGr 435
|
410 420
....*....|....*....|....
gi 1027915378 907 -------AIVQRQSFGGWKKSSVG 923
Cdd:cd07559 436 vwvncyhQYPAHAPFGGYKKSGIG 459
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
543-923 |
1.54e-25 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 112.59 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQT-DPEISEAIDFARYYAQLALDL------GDVDNAEFT---PDRVV 612
Cdd:PLN02466 120 ERSRILLRFADLLEKHNDELAALETWDNGKPYEQSaKAELPMFARLFRYYAGWADKIhgltvpADGPHHVQTlhePIGVA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRVI 692
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 693 LTGSSET------AAMFSSWRPeveINAETSGKNAIVITPSADRDLAVaDLVKSA-FGHAGQKCSAASLGILVGSVYDse 765
Cdd:PLN02466 280 FTGSTDTgkivleLAAKSNLKP---VTLELGGKSPFIVCEDADVDKAV-ELAHFAlFFNQGQCCCAGSRTFVHERVYD-- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 766 RFRKQLLDAASSLIVDWPTNPSATVGPltELPSDKLQHAL----TTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTF 841
Cdd:PLN02466 354 EFVEKAKARALKRVVGDPFKKGVEQGP--QIDSEQFEKILryikSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDML 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVN--RGITGAIvqrqSFGGWKK 919
Cdd:PLN02466 432 IAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFDAAI----PFGGYKM 507
|
....
gi 1027915378 920 SSVG 923
Cdd:PLN02466 508 SGIG 511
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
543-923 |
3.96e-25 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 110.38 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQT-DPEISEAIDFARYYAQLALDLGDVDNAEFTPDR----------V 611
Cdd:PRK13473 62 ERAEALLKLADAIEENADEFARLESLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHtsmirrdpvgV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAgVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:PRK13473 142 VASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSET------AAMFSSWRPEVEInaetSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDse 765
Cdd:PRK13473 221 SLTGSIATgkhvlsAAADSVKRTHLEL----GGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYD-- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 766 RFRKQLLDAASSLIVDWPTNPSATVGPLTELP-----------SDKLQHAlTTLEEGeswllkpRQLDDSGRLWSPGIKE 834
Cdd:PRK13473 295 DLVAKLAAAVATLKVGDPDDEDTELGPLISAAhrdrvagfverAKALGHI-RVVTGG-------EAPDGKGYYYEPTLLA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 835 GVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITgaIVQRQSF 914
Cdd:PRK13473 367 GARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPH 444
|
....*....
gi 1027915378 915 GGWKKSSVG 923
Cdd:PRK13473 445 GGQKQSGYG 453
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
543-935 |
5.34e-25 |
|
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: 110.18 E-value: 5.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQT-DPEISEAIDFARYYAQLAlDLGDVDNAEFTPDRVVVVTPPWNFP 621
Cdd:cd07111 82 VRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWA-QLLDTELAGWKPVGVVGQIVPWNFP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 622 IAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVyPADRDAGRALISNEHVDRVILTGSSETAA 701
Cdd:cd07111 161 LLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIV-TGNGSFGSALANHPGVDKVAFTGSTEVGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 702 MF----SSWRPEVEInaETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVydSERFRKQLLDAASS 777
Cdd:cd07111 240 ALrratAGTGKKLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESV--AEELIRKLKERMSH 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 778 LIVDWPTNPSATVGPLTELPSDKLQHALTtlEEGES-----WLlKPRQLDDSGRLWSPGIKEGVKPGTFFHLTEVFGPVL 852
Cdd:cd07111 316 LRVGDPLDKAIDMGAIVDPAQLKRIRELV--EEGRAegadvFQ-PGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 853 GLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRgiTGAIVQRQSFGGWKKSSVGL-GSKAGGP 931
Cdd:cd07111 393 VVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING--HNLFDAAAGFGGYRESGFGReGGKEGLY 470
|
....
gi 1027915378 932 NYVM 935
Cdd:cd07111 471 EYLR 474
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
543-928 |
3.25e-24 |
|
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: 107.97 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVE-QTDPEISEAIDFARYYA----QLALDLGDVDNAE------FT---P 608
Cdd:cd07140 68 DRGRLMYRLADLMEEHQEELATIESLDSGAVYTlALKTHVGMSIQTFRYFAgwcdKIQGKTIPINQARpnrnltLTkreP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 609 DRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHV 688
Cdd:cd07140 148 IGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSETAA--MFSSWRPEV-EINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDse 765
Cdd:cd07140 228 RKLGFTGSTPIGKhiMKSCAVSNLkKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHD-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 766 RFRKQLLDAASSLIVDWPTNPSATVGPLTELPS-DKL-QHALTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFFH 843
Cdd:cd07140 306 EFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHlDKLvEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 844 LTEVFGPVLGLMK--AADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVqrQSFGGWKKSS 921
Cdd:cd07140 386 KEESFGPIMIISKfdDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVA--APFGGFKQSG 463
|
....*....
gi 1027915378 922 VG--LGSKA 928
Cdd:cd07140 464 FGkdLGEEA 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
543-923 |
8.22e-24 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 106.90 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQT-DPEISEAIDFARYYAQlALD--LGDV---DNAEFT-----PDRV 611
Cdd:PRK09847 82 KRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAE-AIDkvYGEVattSSHELAmivrePVGV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVDRV 691
Cdd:PRK09847 161 IAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 692 ILTGSSETAAMFSSWRPEVEINA---ETSGKNA-IVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDSerF 767
Cdd:PRK09847 241 AFTGSTRTGKQLLKDAGDSNMKRvwlEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADE--F 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 768 RKQLLDAASSLIVDWPTNPSATVGPLTElpSDKLQHALTTLEEGES---WLLKPRQLDDSGRLwSPGIKEGVKPGTFFHL 844
Cdd:PRK09847 319 LALLKQQAQNWQPGHPLDPATTMGTLID--CAHADSVHSFIREGESkgqLLLDGRNAGLAAAI-GPTIFVDVDPNASLSR 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027915378 845 TEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVqrQSFGGWKKSSVG 923
Cdd:PRK09847 396 EEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSGNG 472
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
543-901 |
1.40e-22 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 102.91 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQ---LALDLGDVDNAEFTP--DR------- 610
Cdd:PLN00412 76 KRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEegvRILGEGKFLVSDSFPgnERnkyclts 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 -----VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPskPSQQCSAAV--VEALWDAGVPREVLHCVYPADRDAGRALI 683
Cdd:PLN00412 156 kiplgVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP--PTQGAVAALhmVHCFHLAGFPKGLISCVTGKGSEIGDFLT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 684 SNEHVDRVILTGSsETAAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYD 763
Cdd:PLN00412 234 MHPGVNCISFTGG-DTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVAD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 seRFRKQLLDAASSLIVDWPTNPSATVGPLTELPSDKLQHALTTLEEGESWLLKPRQLDdsGRLWSPGIKEGVKPGTFFH 843
Cdd:PLN00412 313 --ALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRE--GNLIWPLLLDNVRPDMRIA 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1027915378 844 LTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVN 901
Cdd:PLN00412 389 WEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN 446
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
543-925 |
2.12e-22 |
|
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: 101.73 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGDVDNA-----------EFT---P 608
Cdd:cd07148 45 ERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPmgltpasagriAFTtreP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 609 DRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVyPADRDAGRALISNEHV 688
Cdd:cd07148 125 IGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAV-PCENAVAEKLVTDPRV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSETAAMF-SSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCsaaslgILVGSVY----D 763
Cdd:cd07148 204 AFFSFIGSARVGWMLrSKLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVC------VSVQRVFvpaeI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 SERFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALT-TLEEGESWLLKPRQLDDSgrLWSPGIKEGVKPGTF 841
Cdd:cd07148 278 ADDFAQRLAAAAEKLVVGDPTDPDTEVGPLiRPREVDRVEEWVNeAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGiTGAIVQRQSFGGWKKSS 921
Cdd:cd07148 356 VSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSG 434
|
....
gi 1027915378 922 VGLG 925
Cdd:cd07148 435 YGTG 438
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
542-923 |
5.00e-22 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 101.11 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTD-PEISEAIDFARYYAQLA-------LDLGDVDNAeFT---PDR 610
Cdd:PRK13252 66 MERSRILRRAVDILRERNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLApalegeqIPLRGGSFV-YTrrePLG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHcVYPADRDAGRALISNEHVDR 690
Cdd:PRK13252 145 VCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFN-VVQGDGRVGAWLTEHPDIAK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGSSET-----AAMFSSWRpevEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDse 765
Cdd:PRK13252 224 VSFTGGVPTgkkvmAAAAASLK---EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKA-- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 766 RFRKQLLDAASSLIVDWPTNPSATVGPLTELPsdKLQHALTTLEEGESwlLKPRQLDDSGRLWSPGIKEG--VKPGTFFH 843
Cdd:PRK13252 299 AFEARLLERVERIRIGDPMDPATNFGPLVSFA--HRDKVLGYIEKGKA--EGARLLCGGERLTEGGFANGafVAPTVFTD 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 844 LT--------EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNR-GITGAivqRQSF 914
Cdd:PRK13252 375 CTddmtivreEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTwGESPA---EMPV 451
|
....*....
gi 1027915378 915 GGWKKSSVG 923
Cdd:PRK13252 452 GGYKQSGIG 460
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
543-937 |
8.51e-22 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 100.68 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDL-GDVDNAE---------FTPDRVV 612
Cdd:PLN02315 79 KRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLnGSIIPSErpnhmmmevWNPLGIV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 VVTPPWNFPIAIPAGSTFAALAAGAGVIHK--PSKP--SQQCSAAVVEALWDAGVPREVLHCVYpADRDAGRALISNEHV 688
Cdd:PLN02315 159 GVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTPliTIAMTKLVAEVLEKNNLPGAIFTSFC-GGAEIGEAIAKDTRI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 689 DRVILTGSSETAAMFSSwrpevEINA-------ETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSV 761
Cdd:PLN02315 238 PLVSFTGSSKVGLMVQQ-----TVNArfgkcllELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 762 YDseRFRKQLLDAASSLIVDWPTNPSATVGPL-TELPSDKLQHALTTLE-EGESWLLKPRQLDDSGRLWSPGIKEgVKPG 839
Cdd:PLN02315 313 YD--DVLEQLLTVYKQVKIGDPLEKGTLLGPLhTPESKKNFEKGIEIIKsQGGKILTGGSAIESEGNFVQPTIVE-ISPD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 840 TFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRV--DVGNAYVNRGITGAIVQrQSFGGW 917
Cdd:PLN02315 390 ADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVNIPTNGAEIG-GAFGGE 468
|
410 420
....*....|....*....|
gi 1027915378 918 KksSVGLGSKAGGPNYVMLM 937
Cdd:PLN02315 469 K--ATGGGREAGSDSWKQYM 486
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
543-923 |
1.26e-21 |
|
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: 99.83 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLavrRGHLVSVAAAEV---GKSV-EQTDPEISEAIDFARYYAQL---------ALDLGDVDNAEFTPD 609
Cdd:cd07116 61 ERANILNKIADRM---EANLEMLAVAETwdnGKPVrETLAADIPLAIDHFRYFAGCiraqegsisEIDENTVAYHFHEPL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 610 RVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAgVPREVLHCVYPADRDAGRALISNEHVD 689
Cdd:cd07116 138 GVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 690 RVILTGSSETAAMFSSWRPE--VEINAETSGKNAIVITPS---ADRDL---AVADLVKSAFgHAGQKCSAASLGILVGSV 761
Cdd:cd07116 217 KVAFTGETTTGRLIMQYASEniIPVTLELGGKSPNIFFADvmdADDAFfdkALEGFVMFAL-NQGEVCTCPSRALIQESI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 762 YDseRFRKQLLDAASSLIVDWPTNPSATVGPLTELpsDKLQHALTTL----EEGESWLLKPRqlddsgRLWSPGIKEG-- 835
Cdd:cd07116 296 YD--RFMERALERVKAIKQGNPLDTETMIGAQASL--EQLEKILSYIdigkEEGAEVLTGGE------RNELGGLLGGgy 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 836 VKPGTFFHLT-------EVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNrgITGAI 908
Cdd:cd07116 366 YVPTTFKGGNkmrifqeEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLY 443
|
410
....*....|....*
gi 1027915378 909 VQRQSFGGWKKSSVG 923
Cdd:cd07116 444 PAHAAFGGYKQSGIG 458
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
611-916 |
4.53e-18 |
|
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: 88.43 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSqQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALisNEHVDR 690
Cdd:cd07135 111 VVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELT-PHTAALLAELVPKYLDPDAFQVVQGGVPETTALL--EQKFDK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGS-------SETAAmfSSWRPEVeinAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYD 763
Cdd:cd07135 188 IFYTGSgrvgriiAEAAA--KHLTPVT---LELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 764 S--ERFRKQLLDAasslivdWPTNPSATVGpLTELPSDK-LQHALTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGT 840
Cdd:cd07135 263 EfvEELKKVLDEF-------YPGGANASPD-YTRIVNPRhFNRLKSLLDTTKGKVVIGGEMDEATRFIPPTIVSDVSWDD 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027915378 841 FFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGG 916
Cdd:cd07135 335 SLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGG 410
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
544-931 |
9.87e-17 |
|
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: 84.21 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 544 RARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDpEISEAIDFARYYAQLALDLGDVDNAEFTPDR------------- 610
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAE-NICGDQVQLRARAFVIYSYRIPHEPGNHLGQglkqqshgyrwpy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 -VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNEHVD 689
Cdd:cd07084 102 gPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLINGDGKTMQALLLHPNPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 690 RVILTGSSETAAMFSSWRPEVEINAETSGKNAIVITPSADRDLAVAD-LVKSAFGHAGQKCSAASLgILVGSVYDSERFr 768
Cdd:cd07084 182 MVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTACSGQKCTAQSM-LFVPENWSKTPL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 769 kqlLDAASSLIVDwPTNPSATVGPltELPSDKLQHALTTLEEGESWLL---KPRQLDDSGRLWSPGIK-------EGVKP 838
Cdd:cd07084 260 ---VEKLKALLAR-RKLEDLLLGP--VQTFTTLAMIAHMENLLGSVLLfsgKELKNHSIPSIYGACVAsalfvpiDEILK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 839 GTFFHLTEVFGPVLGLMK-----AADLEEAIEFQNGNdfgLTGGLQSLD---VDET--RTWLDRVDVGNayvNRGITGAI 908
Cdd:cd07084 334 TYELVTEEIFGPFAIVVEykkdqLALVLELLERMHGS---LTAAIYSNDpifLQELigNLWVAGRTYAI---LRGRTGVA 407
|
410 420
....*....|....*....|...
gi 1027915378 909 VQRQSFGGWKKSSVGLGSkaGGP 931
Cdd:cd07084 408 PNQNHGGGPAADPRGAGI--GGP 428
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
542-892 |
2.43e-14 |
|
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: 76.81 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAID----FAR-----YYAQLALDLGDVDNAE------- 605
Cdd:cd07129 21 ARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGqlrlFADlvregSWLDARIDPADPDRQPlprpdlr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 606 --FTPDRVVVVTPPWNFPIA--IPAGSTFAALAAGAGVIHK--PSKP--SQQCSAAVVEALWDAGVPREVLHCVYPADRD 677
Cdd:cd07129 101 rmLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAHPgtSELVARAIRAALRATGLPAGVFSLLQGGGRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 678 AGRALISNEHVDRVILTGS-------SETAAMfsswRPE-VEINAETSGKNAIVITPSA--DRDLAVAD-LVKSAFGHAG 746
Cdd:cd07129 181 VGVALVKHPAIKAVGFTGSrrggralFDAAAA----RPEpIPFYAELGSVNPVFILPGAlaERGEAIAQgFVGSLTLGAG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 747 QKCSAASLGILVGSVyDSERFRKQLLDAASSLivdwptnPSATVgpLTELPSDKLQHALTTLEEGESWLLKPRQLDDSGR 826
Cdd:cd07129 257 QFCTNPGLVLVPAGP-AGDAFIAALAEALAAA-------PAQTM--LTPGIAEAYRQGVEALAAAPGVRVLAGGAAAEGG 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027915378 827 LWSPGIKEGVKPGTFFH----LTEVFGPVLGLMKAADLEEAIEFQN---GNdfgLTGGLQSL--DVDETRTWLDR 892
Cdd:cd07129 327 NQAAPTLFKVDAAAFLAdpalQEEVFGPASLVVRYDDAAELLAVAEaleGQ---LTATIHGEedDLALARELLPV 398
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
542-865 |
5.11e-14 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 76.28 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 542 EERARILYKTAELLAVRRGHLVSVAAAEVGKSVEQTDPEISEAIDFARYYAQLALDLGDV-------------DNAEF-- 606
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDArllrdgeavqlgkDPAFQgq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 607 ---TPDR-VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGV-PREVLHCVYPADRDAGRA 681
Cdd:PRK11903 143 hvlVPTRgVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 682 LisnEHVDRVILTGSSETAAMFSSW----RPEVEINAETSGKNAIVITP-----SADRDLAVADLVKSAFGHAGQKCSAA 752
Cdd:PRK11903 223 L---QPFDVVSFTGSAETAAVLRSHpavvQRSVRVNVEADSLNSALLGPdaapgSEAFDLFVKEVVREMTVKSGQKCTAI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 753 SLGILVGSVYDseRFRKQLLDAASSLIVDWPTNPSATVGPLTELPS-DKLQHALTTLEEGESWLLKPRQLDDSGRlwSPG 831
Cdd:PRK11903 300 RRIFVPEALYD--AVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQlAAVRAGLAALRAQAEVLFDGGGFALVDA--DPA 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1027915378 832 IKEGVKPGTFF----------HLTEVFGPVLGLMKAADLEEAIE 865
Cdd:PRK11903 376 VAACVGPTLLGasdpdaatavHDVEVFGPVATLLPYRDAAHALA 419
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
611-929 |
4.34e-13 |
|
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: 72.64 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVlhCVYPADRDAGRALIS------ 684
Cdd:cd07134 103 VCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFEGDAEVAQALLElpfdhi 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 685 ----NEHVDRVILTGSSETaamFSSwrpeveINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSA--------- 751
Cdd:cd07134 181 fftgSPAVGKIVMAAAAKH---LAS------VTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIApdyvfvhes 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 752 ------ASLGILVGSVYDSERFRKQLLDAASslIVDwptnpSATVGPLTELPSDKLQHALTTLEEGeswllkprQLDDSG 825
Cdd:cd07134 252 vkdafvEHLKAEIEKFYGKDAARKASPDLAR--IVN-----DRHFDRLKGLLDDAVAKGAKVEFGG--------QFDAAQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 826 RLWSPGIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGIT 905
Cdd:cd07134 317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVL 396
|
330 340
....*....|....*....|....
gi 1027915378 906 GAIVQRQSFGGWKKSsvGLGSKAG 929
Cdd:cd07134 397 HFLNPNLPFGGVNNS--GIGSYHG 418
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
611-868 |
5.80e-13 |
|
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: 72.17 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIA---IPAgstFAALAAGAGVIHKPSKPSQQCSAAVVEALwDAGVPREVLHCVYpADRDAGRALISnEH 687
Cdd:cd07087 103 VVLIIGPWNYPLQlalAPL---IGAIAAGNTVVLKPSELAPATSALLAKLI-PKYFDPEAVAVVE-GGVEVATALLA-EP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 688 VDRVILTGSSETAAmfsswrpevEINA-----------ETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCsaaslgI 756
Cdd:cd07087 177 FDHIFFTGSPAVGK---------IVMEaaakhltpvtlELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC------I 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 757 LVGSVYDSERFRKQLLDAASSLIVD-WPTNPSAtvgpltelpSDKL-----QHALTTLEEgeswLLKPRQL------DDS 824
Cdd:cd07087 242 APDYVLVHESIKDELIEELKKAIKEfYGEDPKE---------SPDYgriinERHFDRLAS----LLDDGKVviggqvDKE 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1027915378 825 GRLWSPGIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQN 868
Cdd:cd07087 309 ERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFIN 352
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
605-871 |
8.40e-12 |
|
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: 68.67 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 605 EFTPDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGVPREVlhCVYPADRDAGRAlIS 684
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV--AVVTGGADVAAA-FS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 685 NEHVDRVILTGSSETAAMfsswrpeVEINA---------ETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLg 755
Cdd:cd07133 175 SLPFDHLLFTGSTAVGRH-------VMRAAaenltpvtlELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 756 ILV--GSVydsERFRKQLLDAASSLIVDWPTNPSATvGPLTELPSDKLQHALTTLEEGESWLL---KPRQLDDSGRLWSP 830
Cdd:cd07133 247 VLVpeDKL---EEFVAAAKAAVAKMYPTLADNPDYT-SIINERHYARLQGLLEDARAKGARVIelnPAGEDFAATRKLPP 322
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1027915378 831 GIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQNGND 871
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARP 363
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
611-923 |
1.94e-11 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 67.75 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPI---AIPAGstfAALAAGAGVIHKPSKPSQQCSAAVVEaLWDAGVPREVLHCVypadrDAGRALISN-- 685
Cdd:PTZ00381 112 VVLVIGAWNYPLnltLIPLA---GAIAAGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSYVRVI-----EGGVEVTTEll 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 686 -EHVDRVILTGSSETAAMFSSWRPE--VEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVY 762
Cdd:PTZ00381 183 kEPFDHIFFTGSPRVGKLVMQAAAEnlTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 763 DseRFRKQLLDAASSLIVDWPTNPSATVGPLTELPSDKLQhalTTLEEGESWLLKPRQLDDSGRLWSPGIKEGVKPGTFF 842
Cdd:PTZ00381 263 D--KFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLA---ELIKDHGGKVVYGGEVDIENKYVAPTIIVNPDLDSPL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 843 HLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWKKSSV 922
Cdd:PTZ00381 338 MQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGM 417
|
.
gi 1027915378 923 G 923
Cdd:PTZ00381 418 G 418
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
611-923 |
2.67e-10 |
|
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: 64.16 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALwdagvPR----EVLHCVYPADRDAGRALisNE 686
Cdd:cd07132 103 VVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-----PKyldkECYPVVLGGVEETTELL--KQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 687 HVDRVILTGSSETA--AMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILVgsvydS 764
Cdd:cd07132 176 RFDYIFYTGSTSVGkiVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY-VLC-----T 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 765 ERFRKQLLDAASSLIVDWPTNPSATVGPLTELPSDK-LQHALTTLEEGEswLLKPRQLDDSGRLWSPGIKEGVKPGTFFH 843
Cdd:cd07132 250 PEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRhFQRLKKLLSGGK--VAIGGQTDEKERYIAPTVLTDVKPSDPVM 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 844 LTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWKKSSVG 923
Cdd:cd07132 328 QEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
543-906 |
8.76e-09 |
|
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: 59.59 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 543 ERARILYKTAELLAVRRGHLVSVAAAEVGKsveQTDP--EISEAIDFARYYAQLALDLGDvdNAEFTPDRVV-------- 612
Cdd:cd07128 60 ERAAMLKALAKYLMERKEDLYALSAATGAT---RRDSwiDIDGGIGTLFAYASLGRRELP--NAHFLVEGDVeplskdgt 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 613 -----VVTP---------PWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDAGV-PREVLHCVYPADRD 677
Cdd:cd07128 135 fvgqhILTPrrgvavhinAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 678 AGRALisnEHVDRVILTGSSETAAMFSSW----RPEVEINAETSGKNAIVITPSADR-----DLAVADLVKSAFGHAGQK 748
Cdd:cd07128 215 LLDHL---GEQDVVAFTGSAATAAKLRAHpnivARSIRFNAEADSLNAAILGPDATPgtpefDLFVKEVAREMTVKAGQK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 749 CSAASLGILVGSVYDS--ERFRKQLldaASSLIVDwPTNPSATVGPLTELpsDKLQHALTTLEEgeswLLKPRQLDDSGR 826
Cdd:cd07128 292 CTAIRRAFVPEARVDAviEALKARL---AKVVVGD-PRLEGVRMGPLVSR--EQREDVRAAVAT----LLAEAEVVFGGP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 827 LWSPGIKEGVKPGTFF----------------HLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETR--- 887
Cdd:cd07128 362 DRFEVVGADAEKGAFFpptlllcddpdaatavHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARelv 441
|
410 420
....*....|....*....|...
gi 1027915378 888 ----TWLDRVDVGNAYVNRGITG 906
Cdd:cd07128 442 lgaaPYHGRLLVLNRDSAKESTG 464
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
611-951 |
1.53e-08 |
|
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: 58.28 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSaAVVEALWDAGVPREVLHCVyPADRDAGRALIsNEHVDR 690
Cdd:cd07136 103 VVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTS-KVIAKIIEETFDEEYVAVV-EGGVEENQELL-DQKFDY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 691 VILTGSS-------ETAAmfsswRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLgILV-GSVY 762
Cdd:cd07136 180 IFFTGSVrvgkivmEAAA-----KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDY-VLVhESVK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 763 DseRFRKQLLDAASSLIVDWP-TNPSatvgpLTELPSDKLQHALTTLEEGESwLLKPRQLDDSGRLWSPGIKEGVKPGTF 841
Cdd:cd07136 254 E--KFIKELKEEIKKFYGEDPlESPD-----YGRIINEKHFDRLAGLLDNGK-IVFGGNTDRETLYIEPTILDNVTWDDP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 842 FHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWKKSs 921
Cdd:cd07136 326 VMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGNS- 404
|
330 340 350
....*....|....*....|....*....|....*...
gi 1027915378 922 vGLGS---KAGGPNY-----VMLMGTWADAPSLHAPRK 951
Cdd:cd07136 405 -GMGSyhgKYSFDTFshkksILKKSTWFDLPLRYPPYK 441
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
608-923 |
3.08e-07 |
|
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: 54.34 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 608 PDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCS---AAVVEALWDAGVPRevlhcVYPADRDAGRALIS 684
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSallAKLIPEYLDTKAIK-----VIEGGVPETTALLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 685 NEHvDRVILTGSSETA--AMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFG-HAGQKCsaaslgILVGSV 761
Cdd:cd07137 176 QKW-DKIFFTGSPRVGriIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGcNNGQAC------IAPDYV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 762 YDSERFRKQLLDAASSLIVDWPTNPSATVGPLTELPSDKLQHALTTL---EEGESWLLKPRQLDDSGRLWSPGIKEGVKP 838
Cdd:cd07137 249 LVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLlddPSVADKIVHGGERDEKNLYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 839 GTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWK 918
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVG 408
|
....*
gi 1027915378 919 KSSVG 923
Cdd:cd07137 409 ESGFG 413
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
256-414 |
1.72e-06 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 52.01 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 256 QAYLPDALGAIQDLAEFGRKRtangGAGIKVRLVKGANLPMEHVHAQITGWPVATEPSKQATDANYKRVLYWTMRKENME 335
Cdd:PLN02681 274 QAYLKDARERLRLDLERSERE----GVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 336 GLRLGVAGHNLFDIAFAHLLSVERGVA---DRVEFEMLQGMASDQARAVSQDVGDLLLYVPAvspQEFDVAISYLVRRLE 412
Cdd:PLN02681 350 DGEVMLATHNVESGELAAAKMNELGLHkgdPRVQFAQLLGMSDNLSFGLGNAGFRVSKYLPY---GPVEEVIPYLLRRAE 426
|
..
gi 1027915378 413 EN 414
Cdd:PLN02681 427 EN 428
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
611-770 |
3.78e-06 |
|
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: 50.73 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNfPIAIPAGSTFAALAAGAGVIHKP----SKPSQQCSAAVVEALWDAGVPREVLHCVYPADRDAGRALISNE 686
Cdd:cd07081 99 VASITPSTN-PTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 687 HVDRVILTGS-SETAAMFSSWRPEVEINAetsGKNAIVITPSADRDLAVADLVKSAFGHAGQKCSAASLGILVGSVYDS- 764
Cdd:cd07081 178 GIGLLLATGGpAVVKAAYSSGKPAIGVGA---GNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEv 254
|
....*..
gi 1027915378 765 -ERFRKQ 770
Cdd:cd07081 255 mRLFEGQ 261
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
611-771 |
9.30e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 49.41 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 611 VVVVTPPWNfPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSAAVVEALWDA----GVPREVLHCVYPADRDAGRALISNE 686
Cdd:cd07122 99 IAALIPSTN-PTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEPSIELTQELMKHP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 687 HVDRVILTGSsetAAMFSSwrpeveinAETSGKNAI---------VITPSADRDLAVADLVKS-AFGHaGQKCSAASLGI 756
Cdd:cd07122 178 DVDLILATGG---PGMVKA--------AYSSGKPAIgvgpgnvpaYIDETADIKRAVKDIILSkTFDN-GTICASEQSVI 245
|
170
....*....|....*
gi 1027915378 757 LVGSVYDseRFRKQL 771
Cdd:cd07122 246 VDDEIYD--EVRAEL 258
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
608-923 |
5.56e-04 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 43.88 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 608 PDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCSA---AVVEALWDAGVPREVLHCVYPADrdagrALIS 684
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAllaKLLEQYLDSSAVRVVEGAVTETT-----ALLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 685 NEHvDRVILTGSSETA--AMFSSWRPEVEINAETSGKNAIVITPSADRDLAVADLVKSAFG-HAGQKCSAASLgilvgsV 761
Cdd:PLN02174 187 QKW-DKIFYTGSSKIGrvIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDY------I 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 762 YDSERFRKQLLDAAS-SLIVDWPTNPSATVGPLTELPSDKLQHALTTLEEGE--SWLLKPRQLDDSGRLWSPGIKEGVKP 838
Cdd:PLN02174 260 LTTKEYAPKVIDAMKkELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEvsDKIVYGGEKDRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 839 GTFFHLTEVFGPVLGLMKAADLEEAIEFQNGNDFGLTGGLQSLDVDETRTWLDRVDVGNAYVNRGITGAIVQRQSFGGWK 918
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVG 419
|
....*
gi 1027915378 919 KSSVG 923
Cdd:PLN02174 420 ESGMG 424
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
608-868 |
7.25e-04 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 43.56 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 608 PDRVVVVTPPWNFPIAIPAGSTFAALAAGAGVIHKPSKPSQQCS---AAVVEALWDAGVPRevlhcVYPADRDAGRALIs 684
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSaflAANIPKYLDSKAVK-----VIEGGPAVGEQLL- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 685 nEHV-DRVILTGSSETA--AMFSSWRPEVEINAETSGK-NAIV--ITPSADRDLAVADLVKSAFGH-AGQKCSAASLgIL 757
Cdd:PLN02203 182 -QHKwDKIFFTGSPRVGriIMTAAAKHLTPVALELGGKcPCIVdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDY-VL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 758 VgsvydSERFRKQLLDAASSLIVDWPTNPSATVGPLTELPSDKLQHALTTleegeswLLKPRQLD---------DSGRLW 828
Cdd:PLN02203 260 V-----EERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSN-------LLKDPRVAasivhggsiDEKKLF 327
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1027915378 829 -SPGIKEGVKPGTFFHLTEVFGPVLGLMKAADLEEAIEFQN 868
Cdd:PLN02203 328 iEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFIN 368
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
612-754 |
1.47e-03 |
|
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: 42.48 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027915378 612 VVVTPPWNFPIAIPAGSTFAALAAGagviHKPSKPSQQCSAAVVEA----LWDAGVPRE---VLHCvypaDRDAGRALIS 684
Cdd:cd07126 146 VAIITPFNFPLEIPALQLMGALFMG----NKPLLKVDSKVSVVMEQflrlLHLCGMPATdvdLIHS----DGPTMNKILL 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027915378 685 NEHVDRVILTGSSETAAMFSSwRPEVEINAETSGKNAIVITPsadrDLAVADLV-----KSAFGHAGQKCSAASL 754
Cdd:cd07126 218 EANPRMTLFTGSSKVAERLAL-ELHGKVKLEDAGFDWKILGP----DVSDVDYVawqcdQDAYACSGQKCSAQSI 287
|
|
| |
