|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
438-959 |
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: 542.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 438 ASENFMSAVFELSSSEQLFARERDRFLASLAEVDDTVPAPHRVQDRTLPPapapgtgegfhnapdTDPAVaanrawaraa 517
Cdd:cd07125 1 ANSSFVNRIFDLEVPLEALADALKAFDEKEWEAIPIINGEETETGEGAPV---------------IDPAD---------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 518 lersrttrlGEETVAASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQS 597
Cdd:cd07125 56 ---------HERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 598 DPEVSEVVDFAHYYAEQSLGL----------ERLDGARFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRT 667
Cdd:cd07125 127 DAEVREAIDFCRYYAAQARELfsdpelpgptGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 668 ARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELFRSFRPG-----LTLLAETSGKNAI 742
Cdd:cd07125 207 PLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAErdgpiLPLIAETGGKNAM 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 743 VVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLL 822
Cdd:cd07125 287 IVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIA--ERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 823 DALTRLAPGESWLLEPRQLDEE-GRVWSPGIKTGVapGSEFHRTEYFGPVLGIMHAA--TLDEAIELQNAVDYGLTAGLH 899
Cdd:cd07125 365 RAHTELMRGEAWLIAPAPLDDGnGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIH 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 900 SLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSvvGAGAKAGGPNYLLGLGR 959
Cdd:cd07125 443 SRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLS--GTGPKAGGPNYLLRFGN 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
29-1003 |
4.81e-129 |
|
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: 419.45 E-value: 4.81e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 29 ADEEHVADAVVAQVRRWLAEAERLPVDPSARRLAGLLRDPDGLAFAVGFVDGVIRPEDPRVAARALTRLSRRPPRFLAWP 108
Cdd:COG0506 4 ALDEALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFLVNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 109 LRAALRVGgMVAPILPGVVVPVARAVLRRMVAHLVIDADDPRLGRALRRIRDRGARPNVNLLGEAVLGAREAARRLEGTR 188
Cdd:COG0506 84 STWGLMLT-LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 189 RLLARD-----DVDYVSIKVSATVAPHSPWAFDEAVDDIVQALTPLYAdaAAASPPKFVNLDMEEYKDLDLTIAVFQRIL 263
Cdd:COG0506 163 EALEAIgaagvDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLAR--AAREAGIFVTIDMEEYDRLDLTLDVFERLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 264 DGPELRG-LEAGIVLQAYLPDALGAYLRLRDWARErraaGGAGIKVRLVKGANLPMERVDASLHDWPLATWHTKQETDTN 342
Cdd:COG0506 241 ADPELAGwPGVGIVLQAYLKRAEADLDRLAALARR----GGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDAN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 343 YKRVLDVALrpENTAHVRLGVAGHNLFDLAYARHLAAERGV-ADAMEIEMLLGMAPAQAEAVRR-DTGGLLLYTPVVAAS 420
Cdd:COG0506 317 YLRCARKLL--EAGDAIYPQFATHNARTIAAALALAGERGRpPDRFEFQMLYGMGEDLQRALAAvDGGRLLLYCPVVAPV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 421 DFDAAIAYLIRRLEEGAASENFMSAVFELSSSEQLFARERDRFLASLAEVDDTVPAPHRVQDRtlPPAPAPGTGEGFHNA 500
Cdd:COG0506 395 GGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRR--RRRRARGGALAAALA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 501 PDTDPAVAANRAWARAALERSRTTRLGEETVAASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRG 580
Cdd:COG0506 473 AAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 581 ELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLERLDGARFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVV 660
Cdd:COG0506 553 AAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAA 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 661 FKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELFRSFRPGLTLLAETSGKN 740
Cdd:COG0506 633 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAAT 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 741 AIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARSRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGK 820
Cdd:COG0506 713 AAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDADLVILLLALAA 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 821 LLDALTRLAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHS 900
Cdd:COG0506 793 AAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLA 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 901 LDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSVVGAGAKAGGPNYLLGLGRVEPVAATVEPAAVDPGAERLI 980
Cdd:COG0506 873 LVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGA 952
|
970 980
....*....|....*....|...
gi 1899179363 981 AVFGARGDEARRMLLRAAASDRR 1003
Cdd:COG0506 953 GTLALAAAAAAATALAAAAAAAA 975
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
567-955 |
2.11e-102 |
|
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: 333.42 E-value: 2.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQslgLERLDGARFVPAR------------VTLV 634
Cdd:cd07124 96 LLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYARE---MLRLRGFPVEMVPgednryvyrplgVGAV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 635 VPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILT 714
Cdd:cd07124 173 ISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFT 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 715 GGYETA----ELFRSFRPGLT----LLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVarSRR 786
Cdd:cd07124 253 GSREVGlriyERAAKVQPGQKwlkrVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESV--YDE 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 787 FHEQLLDAVRSMPVGEAWDPSSRMGPLI-APADGKLLDALtRLAPGESWLL---EPRQLDEEGRVWSPGIKTGVAPGSEF 862
Cdd:cd07124 331 FLERLVERTKALKVGDPEDPEVYMGPVIdKGARDRIRRYI-EIGKSEGRLLlggEVLELAAEGYFVQPTIFADVPPDHRL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 863 HRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSvv 942
Cdd:cd07124 410 AQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMS-- 487
|
410
....*....|...
gi 1899179363 943 GAGAKAGGPNYLL 955
Cdd:cd07124 488 GTGSKAGGPDYLL 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
567-950 |
5.15e-101 |
|
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: 328.24 E-value: 5.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQslgLERLDG-------------ARFVPARVTL 633
Cdd:COG1012 70 ILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGE---ARRLYGetipsdapgtrayVRREPLGVVG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVIL 713
Cdd:COG1012 147 AITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGGYETAELF-RSFRPGLT-LLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARsrRFHEQL 791
Cdd:COG1012 227 TGSTAVGRRIaAAAAENLKrVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYD--EFVERL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLI-APADGKLLDALTR-LAPGESWLLEPRQLD-EEGRVWSPGIKTGVAPGSEFHRTEYF 868
Cdd:COG1012 305 VAAAKALKVGDPLDPGTDMGPLIsEAQLERVLAYIEDaVAEGAELLTGGRRPDgEGGYFVEPTVLADVTPDMRIAREEIF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 869 GPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAiVQRQPFGGWKRSvvGAGAKA 948
Cdd:COG1012 385 GPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQS--GIGREG 461
|
..
gi 1899179363 949 GG 950
Cdd:COG1012 462 GR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
567-954 |
3.73e-92 |
|
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: 303.68 E-value: 3.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQslgLERLDG------------ARFVPARVTLV 634
Cdd:pfam00171 56 ILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGL---ARRLDGetlpsdpgrlayTRREPLGVVGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 635 VPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILT 714
Cdd:pfam00171 133 ITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 715 GGYETAELF--RSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLL 792
Cdd:pfam00171 213 GSTAVGRHIaeAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIY--DEFVEKLV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 793 DAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLEP--RQLDEEGRVWSPGIKTGVAPGSEFHRTEYFGP 870
Cdd:pfam00171 291 EAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTggEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 871 VLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRqPFGGWKRSVVGagaKAGG 950
Cdd:pfam00171 371 VLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG---REGG 446
|
....
gi 1899179363 951 PNYL 954
Cdd:pfam00171 447 PYGL 450
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
154-1148 |
8.52e-83 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 294.85 E-value: 8.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 154 ALRRIRD---RGARPNVNLLGEAVLGAREAARRLEGTRRLLA--------RD--DVDYVSIKVSAtVAPHSPWAFDEAV- 219
Cdd:PRK11905 188 ALKRAREleaRGYRYSYDMLGEAARTAADAERYYRDYERAIHaigkaatgRGvyDGPGISVKLSA-LHPRYERAQRERVm 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 220 DDIVQALTPLYADAAAASPPkfVNLDMEEYKDLDLTIAVFQRILDGPELRGLEA-GIVLQAYLPDALGAYLRLRDWAR-- 296
Cdd:PRK11905 267 AELLPRLKALALLAKAYDIG--LNIDAEEADRLELSLDLLEALCSDPDLAGWNGiGFVVQAYQKRCPFVIDYLIDLARrs 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 297 ERRaaggagIKVRLVKGANLPME----RVDAsLHDWPLATwhTKQETDTNY----KRVLdvalrpENTAHVRLGVAGHNL 368
Cdd:PRK11905 345 GRR------LMVRLVKGAYWDAEikraQVDG-LEGFPVFT--RKVHTDVSYiacaRKLL------AARDVIYPQFATHNA 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 369 FDLAYARHLAAERgvaDAMEIEMLLGMAPAQAEAVRRDTG---GLLLYTPVVAASDFdaaIAYLIRRLEEGAASENFMSA 445
Cdd:PRK11905 410 QTLAAIYELAGGK---GDFEFQCLHGMGEPLYDQVVGKEKlgrPCRIYAPVGTHETL---LAYLVRRLLENGANSSFVNR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 446 VfelssseqlfarerdrflaslaeVDDTVPAPHRVQD-----RTLPPAPAPGT-------GEGFHNAPDTDPAVAANRAW 513
Cdd:PRK11905 484 I-----------------------VDENVPVEELIADpvekvAAMGVAPHPQIplprdlyGPERRNSKGLDLSDEATLAA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 514 ARAALERSRTTR------LGEETVAASRIP-----------------DAAGVDRVLATAAAASGSWAARGAAERAAILHR 570
Cdd:PRK11905 541 LDEALNAFAAKTwhaaplLAGGDVDGGTRPvlnpadhddvvgtvteaSAEDVERALAAAQAAFPEWSATPAAERAAILER 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 571 AGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQslGLERLDGARFVPARVTLVVPPWNFPLAIPGGSTL 650
Cdd:PRK11905 621 AADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQ--ARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIA 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 651 AALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELFRS----- 725
Cdd:PRK11905 699 AALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRtlakr 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 726 FRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVGEAWD 805
Cdd:PRK11905 779 SGPPVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVA--DRVLTMLKGAMDELRIGDPWR 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 806 PSSRMGPLI-APADGKLLDALTRL-APGES-WLLEPRQLDEEGrvwspgikTGVAPG-------SEFHRtEYFGPVLGIM 875
Cdd:PRK11905 857 LSTDVGPVIdAEAQANIEAHIEAMrAAGRLvHQLPLPAETEKG--------TFVAPTlieidsiSDLER-EVFGPVLHVV 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 876 --HAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSvvGAGAKAGGPNY 953
Cdd:PRK11905 928 rfKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGGPLY 1005
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 954 LLGLGRVEP--VAATVEPAAVDPGAERLIAVFGARGDEARRMLLRAAASdrrawETEFGVVRDVTALAAERNafRYRALP 1031
Cdd:PRK11905 1006 LGRLVREAPtpIPPAHESVDTDAAARDFLAWLDKEGKAALAAAARDARA-----RSALGLEQELPGPTGESN--LLSLHP 1078
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 1032 VVVRAEAAADPVELARVVLAGLRAGAALTLSTDAEL--APADLDALREAGVGIRSESAEE-------WLRSASALRDARI 1102
Cdd:PRK11905 1079 RGRVLCVADTEEALLRQLAAALATGNVAVVAADSGLaaALADLPGLVAARIDWTQDWEADdpfagalLEGDAERARAVRQ 1158
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 1899179363 1103 RLVGGSGAeLLTALGGRPDIAVYdgavtesgrveLLAFLREQAVSI 1148
Cdd:PRK11905 1159 ALAARPGA-IVPLIAAEPTDAYD-----------LARLVEERSVSI 1192
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
567-955 |
5.33e-82 |
|
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: 277.52 E-value: 5.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQslgLERLDGAR-------------FVPARVTL 633
Cdd:TIGR01237 96 ILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQ---MIELAKGKpvnsregetnqyvYTPTGVTV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVIL 713
Cdd:TIGR01237 173 VISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGGYETA----ELFRSFRPGLT----LLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARSr 785
Cdd:TIGR01237 253 TGSREVGtrifERAAKVQPGQKhlkrVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDE- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 786 rFHEQLLDAVRSMPVGEAWDPSSRMGPLI-APADGKLLDALtRLAPGESWLLE-PRQLDEEGRVWSPGIKTGVAPGSEFH 863
Cdd:TIGR01237 332 -VVERFVEITESLKVGPPDSADVYVGPVIdQKSFNKIMEYI-EIGKAEGRLVSgGCGDDSKGYFIGPTIFADVDRKARLA 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSvvG 943
Cdd:TIGR01237 410 QEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMS--G 487
|
410
....*....|..
gi 1899179363 944 AGAKAGGPNYLL 955
Cdd:TIGR01237 488 TDSKAGGPDYLA 499
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
567-955 |
8.49e-81 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 274.12 E-value: 8.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLER----------LDGARFVPARVTLVVP 636
Cdd:PRK03137 100 ILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADgkpvesrpgeHNRYFYIPLGVGVVIS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:PRK03137 180 PWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETA----ELFRSFRPGLTLL----AETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVarsrrfH 788
Cdd:PRK03137 260 REVGlriyERAAKVQPGQIWLkrviAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDV------Y 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 789 EQLLDAV----RSMPVGEAWDPSSrMGPLIAPADGKLLDALTRLAPGESWL-LEPRQLDEEGRVWSPGIKTGVAPGSEFH 863
Cdd:PRK03137 334 DEVLEKVveltKELTVGNPEDNAY-MGPVINQASFDKIMSYIEIGKEEGRLvLGGEGDDSKGYFIQPTIFADVDPKARIM 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSvvG 943
Cdd:PRK03137 413 QEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMS--G 490
|
410
....*....|..
gi 1899179363 944 AGAKAGGPNYLL 955
Cdd:PRK03137 491 TDSKAGGPDYLL 502
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
129-955 |
1.90e-77 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 277.08 E-value: 1.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 129 PVARAVLRR----MVAHLVidaddprLGR----ALRRI---RDRGARPNVNLLGEAVLGAREAAR-------------RL 184
Cdd:PRK11904 163 PVIRKAMRQamkiMGKQFV-------LGRtieeALKRArsaRNKGYRYSFDMLGEAALTAADAERyfkayaraieaigRA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 185 EGTRRLLARDDVdyvSIKVSATVAPHSPWAFDEAVDDIVQALTPLYADAAAAsppkFVNL--DMEEYKDLDLTIAVFQRI 262
Cdd:PRK11904 236 AGGADLPARPGI---SIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEA----NIGLtiDAEEADRLELSLDLFEAL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 263 LDGPELRGLEA-GIVLQAYLPDALGAYLRLRDWARE--RRaaggagIKVRLVKGANLPMERVDAS---LHDWPLATwhTK 336
Cdd:PRK11904 309 FRDPSLKGWGGfGLAVQAYQKRALPVLDWLADLARRqgRR------IPVRLVKGAYWDSEIKRAQelgLPGYPVFT--RK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 337 QETDTNY----KRVLdvALRPentaHVRLGVAGHNLFDLAYARHLAAERGvadaMEIEMLLGMAPAQAEAVRRDTG-GLL 411
Cdd:PRK11904 381 AATDVSYlacaRKLL--SARG----AIYPQFATHNAHTVAAILEMAGHRG----FEFQRLHGMGEALYDALLDAPGiPCR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 412 LYTPVVAASDFdaaIAYLIRRLEEGAASENFMSA-------VFELSSS-------------------EQLFARER----- 460
Cdd:PRK11904 451 IYAPVGSHKDL---LPYLVRRLLENGANSSFVHRlvdpdvpIEELVADpveklrsfetlpnpkiplpRDIFGPERknskg 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 461 ---------DRFLASLAEVDDTvpaphrvqDRTLPPAPApGTGEGfhnAPDTDPAvaanrawaraalerSRTTRLGEETV 531
Cdd:PRK11904 528 lnlndrselEPLAAAIAAFLEK--------QWQAGPIIN-GEGEA---RPVVSPA--------------DRRRVVGEVAF 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 532 AasripDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYY 611
Cdd:PRK11904 582 A-----DAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYY 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 612 AEQSlglERLDGA--------------RFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTET 677
Cdd:PRK11904 657 AAQA---RRLFGApeklpgptgesnelRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKL 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 678 LWEAGVPREALQFvVLGD-SSLGETLIADERVDQVILTGGYETAELF-RSF--RPG--LTLLAETSGKNAIVVTPSADLD 751
Cdd:PRK11904 734 LHEAGIPKDVLQL-LPGDgATVGAALTADPRIAGVAFTGSTETARIInRTLaaRDGpiVPLIAETGGQNAMIVDSTALPE 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 752 LAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPG 831
Cdd:PRK11904 813 QVVDDVVTSAFRSAGQRCSALRVLFVQEDIA--DRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKR 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 832 ESWLLEPRQLDEEGRVwspgiKTGVAP------GSEFHRTEYFGPVLGIMH--AATLDEAIELQNAVDYGLTAGLHSlDA 903
Cdd:PRK11904 891 EARLLAQLPLPAGTEN-----GHFVAPtafeidSISQLEREVFGPILHVIRykASDLDKVIDAINATGYGLTLGIHS-RI 964
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1899179363 904 DEVARWI-DGVEAGNLYVNRGTTGAIVQRQPFGGWKRSvvGAGAKAGGPNYLL 955
Cdd:PRK11904 965 EETADRIaDRVRVGNVYVNRNQIGAVVGVQPFGGQGLS--GTGPKAGGPHYLL 1015
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
567-954 |
5.52e-75 |
|
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: 255.21 E-value: 5.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLE-------RLDGA---RFVPARVTLVVP 636
Cdd:cd07078 25 ILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHgevipspDPGELaivRREPLGVVGAIT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd07078 105 PWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAELF-----RSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQL 791
Cdd:cd07078 185 TAVGKAImraaaENLKR-VTL--ELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIY--DEFVERL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLI-APADGKLLDAL--------TRLAPGEswllepRQLDEEGRVWSPGIKTGVAPGSEF 862
Cdd:cd07078 260 VERVKALKVGNPLDPDTDMGPLIsAAQLDRVLAYIedakaegaKLLCGGK------RLEGGKGYFVPPTVLTDVDPDMPI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 863 HRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQrQPFGGWKRSvv 942
Cdd:cd07078 334 AQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPS-APFGGVKQS-- 410
|
410
....*....|..
gi 1899179363 943 gAGAKAGGPNYL 954
Cdd:cd07078 411 -GIGREGGPYGL 421
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
153-445 |
2.41e-74 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 248.56 E-value: 2.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 153 RALRRIRDRGARPNVNLLGEAVLGAREAARRLEGTRRLLA----------RDDVDYVSIKVSATVAPHSPWAFDEAVDDI 222
Cdd:pfam01619 3 KTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDalgkaagpwpLGPRPGISVKLSALHPRYEPLERERVMAEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 223 VQALTPLYADAAAAspPKFVNLDMEEYKDLDLTIAVFQRILDGPELRGLE-AGIVLQAYLPDALGAYLRLRDWARERraa 301
Cdd:pfam01619 83 LERLRPLCRLAKEL--GVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLELARRR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 302 gGAGIKVRLVKGANLPMERVDASLHDWPLATWHTKQETDTNYKRVLDVALrpENTAHVRLGVAGHNLFDLAYARHLAAER 381
Cdd:pfam01619 158 -GRPLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAEEL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899179363 382 GVA-DAMEIEMLLGMAPAQAEAVRRDTGGLLLYTPVVAASDFdaaIAYLIRRLEEGAASENFMSA 445
Cdd:pfam01619 235 GIPpRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEEL---LAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
527-951 |
7.79e-69 |
|
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: 239.56 E-value: 7.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 527 GEETVAASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVD 606
Cdd:cd07131 24 LEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 607 FAHYYAEQSlglERLDG-------------ARFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAV 673
Cdd:cd07131 104 MAQYAAGEG---RRLFGetvpselpnkdamTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 674 LTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELFR--SFRPGLTLLAETSGKNAIVVTPSADLD 751
Cdd:cd07131 181 LVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGetCARPNKRVALEMGGKNPIIVMDDADLD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 752 LAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPG 831
Cdd:cd07131 261 LALEGALWSAFGTTGQRCTATSRLIVHESVY--DEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 832 E--SWLLEPRQLD----EEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADE 905
Cdd:cd07131 339 EgaTLLLGGERLTgggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNK 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1899179363 906 VARWIDGVEAGNLYVNRGTTGAIVQrQPFGGWKRSvvGAGAKAGGP 951
Cdd:cd07131 419 AFRARRDLEAGITYVNAPTIGAEVH-LPFGGVKKS--GNGHREAGT 461
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
567-944 |
3.92e-67 |
|
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: 234.45 E-value: 3.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLgleRLDGARFVPAR-------------VTL 633
Cdd:cd07097 64 ILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYYAGEAL---RLSGETLPSTRpgvevettreplgVVG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVIL 713
Cdd:cd07097 141 LITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGGYET-AELFRS-FRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQL 791
Cdd:cd07097 221 TGSTAVgRRIAAAaAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIH--DRFVEAL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPL--------------IAPADGklldalTRLAPGEswllEPRQLDEEGRVWSPGIKTGVA 857
Cdd:cd07097 299 VERTKALKVGDALDEGVDIGPVvserqlekdlryieIARSEG------AKLVYGG----ERLKRPDEGYYLAPALFAGVT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 858 PGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQrQPFGGW 937
Cdd:cd07097 369 NDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYH-VPFGGR 447
|
....*..
gi 1899179363 938 KRSVVGA 944
Cdd:cd07097 448 KGSSYGP 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
567-940 |
2.63e-66 |
|
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: 232.07 E-value: 2.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYyaeqSLGLER-LDG-------------ARFVPARVT 632
Cdd:cd07086 62 IVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDY----AVGLSRmLYGltipserpghrlmEQWNPLGVV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 633 LVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEA----GVPrEALQFVVLGDSSLGETLIADERV 708
Cdd:cd07086 138 GVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLP-PGVVNLVTGGGDGGELLVHDPRV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 709 DQVILTGGYET--------AELFrsfrpGLTLLaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGA 780
Cdd:cd07086 217 PLVSFTGSTEVgrrvgetvARRF-----GRVLL-ELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHES 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 781 VArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTRL-APGESWLLEPRQLD--EEGRVWSPGIKTGV 856
Cdd:cd07086 291 VY--DEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAvEKYLNAIEIAkSQGGTVLTGGKRIDggEPGNYVEPTIVTGV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 857 APGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWID--GVEAGNLYVNRGTTGAIVQrQPF 934
Cdd:cd07086 369 TDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGpkGSDCGIVNVNIPTSGAEIG-GAF 447
|
....*.
gi 1899179363 935 GGWKRS 940
Cdd:cd07086 448 GGEKET 453
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
567-955 |
2.82e-65 |
|
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: 229.77 E-value: 2.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLE-----------RLDGARFVPARVTLVV 635
Cdd:cd07083 82 LLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRypavevvpypgEDNESFYVGLGAGVVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 636 PPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTG 715
Cdd:cd07083 162 SPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 716 GYETAEL-----------FRSFRPgltLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArs 784
Cdd:cd07083 242 SLETGKKiyeaaarlapgQTWFKR---LYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAY-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 785 RRFHEQLLDAVRSMPVGEAWDPSSRMGPLI-APADGKLLDALTRLAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFH 863
Cdd:cd07083 317 EPVLERLLKRAERLSVGPPEENGTDLGPVIdAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIA 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMH--AATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSv 941
Cdd:cd07083 397 QEEIFGPVLSVIRykDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLS- 475
|
410
....*....|....
gi 1899179363 942 vGAGAKAGGPNYLL 955
Cdd:cd07083 476 -GTNAKTGGPHYLR 488
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
105-979 |
8.30e-64 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 237.14 E-value: 8.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 105 LAWPLRAALRVGGMVAPILPGVVVPVARAVLRRMVAHLVIDADDPRLGRALRRIRDRGARPNVNLLGEAVLGAREAARRL 184
Cdd:COG4230 143 LESSLSLASGLLRLLGRLGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 185 E--------GTRRLLARDDVDYVSIKVSATVAPHS-PWAFDEAVDDIVQALTPLYADAAAASPPKFVNLDMEEYKDLDLT 255
Cdd:COG4230 223 YayaaaaaaAIAAAGGGSGGPGPSISSSLSVLLSArHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 256 IAVFQRILDGPELRGLEAGIVLQAYLPDALGAYLRLRDWARERRAAGGAGIKVRLVKGANLPMERVDASLHDWPlatwhT 335
Cdd:COG4230 303 LLLLDLLAALLLDGGLGGGGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYV-----V 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 336 KQETDTNYkrVLDVALRPENTAHVRLGVAGHNLFDLAYARHLAAERGVADAMEIE--MLLGMAPAQAEAVRRDTGGLLL- 412
Cdd:COG4230 378 YPVTTRKV--LYDAAALALALLLLAAQPAFAPQFATHAAATAAAAAAAGGGGEFEfqCLHGMGEYLYDQVGRGKLGRPCr 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 413 -YTPVVAASDFdaaIAYLIRRL-EEGAASenfmsavfelssseqlfarerdRFLASLaeVDDTVPAPHRVQD-----RTL 485
Cdd:COG4230 456 iYAPVGSHEDL---LAYLVRRLlENGANS----------------------SFVNRI--ADEDVPVEELIADpvekaRAL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 486 PPAPAPGT-------GEGFHNAPDTDPAVAANRAWARAALERSRTTR------LGEETVAASRIP--------------- 537
Cdd:COG4230 509 GGAPHPRIplprdlyGPERRNSAGLDLSDEAVLAALSAALAAAAEKQwqaaplIAGEAASGEARPvrnpadhsdvvgtvv 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 538 --DAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQS 615
Cdd:COG4230 589 eaTAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQA 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 616 lglERLDGARFVPARVTLVV--PPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFvVL 693
Cdd:COG4230 669 ---RRLFAAPTVLRGRGVFVciSPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQL-LP 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 694 GD-SSLGETLIADERVDQVILTGGYETA-----ELFRSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQ 767
Cdd:COG4230 745 GDgETVGAALVADPRIAGVAFTGSTETArlinrTLAARDGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQ 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 768 KCSAASLAILVGAVArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLI-APADGKLLDALTRLApGESWLLEPRQLDEEgr 846
Cdd:COG4230 825 RCSALRVLCVQEDIA--DRVLEMLKGAMAELRVGDPADLSTDVGPVIdAEARANLEAHIERMR-AEGRLVHQLPLPEE-- 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 847 vWSPGikTGVAPG-------SEFHRtEYFGPVLGIM--HAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGN 917
Cdd:COG4230 900 -CANG--TFVAPTlieidsiSDLER-EVFGPVLHVVryKADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGN 975
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1899179363 918 LYVNRGTTGAIVQRQPFGGWKRSvvGAGAKAGGPNYLLGLGRVEPVAATVEPAAVDPGAERL 979
Cdd:COG4230 976 VYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGGPHYLLRFATERTVTVNTTAAGGNASLLAL 1035
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
156-1102 |
3.59e-63 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 235.64 E-value: 3.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 156 RRIRDRGARPNVNLLGEAVLGAREAARRLegtrrllarddVDY---------------------VSIKVSATVAPHSPWA 214
Cdd:PRK11809 273 RKLEEKGFRYSYDMLGEAALTEADAQAYL-----------ASYeqaihaigkasngrgiyegpgISIKLSALHPRYSRAQ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 215 FDEAVDDI---VQALTPLyadaaAASPPKFVNLDMEEYKDLDLTIAVFQRILDGPELRGLEA-GIVLQAYLPDALGAYLR 290
Cdd:PRK11809 342 YDRVMEELyprLKSLTLL-----ARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGiGFVIQAYQKRCPFVIDY 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 291 LRDWARERRAAggagIKVRLVKGANLPME----RVDAsLHDWPLATwhTKQETDTNY----KRVLDValrPEntaHVRLG 362
Cdd:PRK11809 417 LIDLARRSRRR----LMIRLVKGAYWDSEikraQVDG-LEGYPVYT--RKVYTDVSYlacaRKLLAV---PN---LIYPQ 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 363 VAGHNLFDLAYARHLAAERGVADAMEIEMLLGMA-PAQAEAVRRDTGGLL-----LYTPVvaaSDFDAAIAYLIRRLEEG 436
Cdd:PRK11809 484 FATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGePLYEQVVGKVADGKLnrpcrIYAPV---GTHETLLAYLVRRLLEN 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 437 AASENFMSAVFELSSS-EQLFARERDRfLASLAEVDDTVPAPHrvqdrtlPPAPAPGT--GEGFHNAPDTDPAVAANRAW 513
Cdd:PRK11809 561 GANTSFVNRIADTSLPlDELVADPVEA-VEKLAQQEGQLGLPH-------PKIPLPRDlyGKGRANSAGLDLANEHRLAS 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 514 ARAALERSRTTR------LGEETVAASRIP-----------------DAAGVDRVLATAAAASGSWAARGAAERAAILHR 570
Cdd:PRK11809 633 LSSALLASAHQKwqaapmLEDPVAAGEMSPvinpadprdivgyvreaTPAEVEQALESAVNAAPIWFATPPAERAAILER 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 571 AGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGleRLDGARFVPARVTLVVPPWNFPLAIPGGSTL 650
Cdd:PRK11809 713 AADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRD--DFDNDTHRPLGPVVCISPWNFPLAIFTGQVA 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 651 AALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELF-RSF--- 726
Cdd:PRK11809 791 AALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLqRNLagr 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 727 -----RPgLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVG 801
Cdd:PRK11809 871 ldpqgRP-IPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVA--DRTLKMLRGAMAECRMG 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 802 EAWDPSSRMGPLI-APADGKLLDALTRL-APGESWLLEPRQLDEEgrvWSPGikTGVAPG-------SEFHRtEYFGPVL 872
Cdd:PRK11809 948 NPDRLSTDIGPVIdAEAKANIERHIQAMrAKGRPVFQAARENSED---WQSG--TFVPPTlieldsfDELKR-EVFGPVL 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 873 GIMH--AATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSvvGAGAKAGG 950
Cdd:PRK11809 1022 HVVRynRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLS--GTGPKAGG 1099
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 951 PNYLLGLGRVEP-------VAATVEPAAVD-PGAERLIAVFGA-RGDEARRMLLRAAASDRRAWETEFGVVRDVTALAAE 1021
Cdd:PRK11809 1100 PLYLYRLLATRPedalavtLARQDAEYPVDaQLRAALLAPLTAlREWAAEREPELAALCDQYAELAQAGTTRLLPGPTGE 1179
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 1022 RNafRYRALP---VVVRAEAAADpvelARVVLAGLRAGAALTLSTDAELAPADLDALREAgVGIRSESAEEWLRSASALr 1098
Cdd:PRK11809 1180 RN--TYTLLPrerVLCLADTEQD----ALTQLAAVLAVGSQALWPDDALHRALVAALPAA-VQARIQLAKDWQLADQPF- 1251
|
....
gi 1899179363 1099 DARI 1102
Cdd:PRK11809 1252 DAVL 1255
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
567-949 |
4.20e-63 |
|
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: 219.41 E-value: 4.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLERLDGA----------RFVPARVTLVVP 636
Cdd:cd06534 21 ILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPspdpggeayvRREPLGVVGVIT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd06534 101 PWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPRVDKISFTGS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAE-LFRSFRPGLT-LLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLaILVgavarsrrfHEQLLDA 794
Cdd:cd06534 181 TAVGKaIMKAAAENLKpVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR-LLV---------HESIYDE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 795 VrsmpvgeawdpssrmgpliapadgklldaLTRLApgeswlleprqldeegrvwspGIKTGVAPGSEFHRTEYFGPVLGI 874
Cdd:cd06534 251 F-----------------------------VEKLV---------------------TVLVDVDPDMPIAQEEIFGPVLPV 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899179363 875 MHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQrQPFGGWKRSvvGAGAKAG 949
Cdd:cd06534 281 IRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGGVKNS--GIGREGG 352
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
567-940 |
5.31e-61 |
|
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: 215.60 E-value: 5.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEV---VDFAHYYAEQSLGLERLDGA------RFVPARVTLVVPP 637
Cdd:cd07095 27 ILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMagkIDISIKAYHERTGERATPMAqgravlRHRPHGVMAVFGP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 638 WNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQVILTGGY 717
Cdd:cd07095 107 FNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN-LVQGGRETGEALAAHEGIDGLLFTGSA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 718 ETAELF-RSF--RPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAvARSRRFHEQLLDA 794
Cdd:cd07095 186 ATGLLLhRQFagRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDG-AVGDAFLERLVEA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 795 VRSMPVGEAWDPSSRMGPLI--APADGKLLDALTRLAPGESWLLEPRQLDEEGRVWSPGIkTGVAPGSEFHRTEYFGPVL 872
Cdd:cd07095 265 AKRLRIGAPDAEPPFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLSPGI-IDVTDAADVPDEEIFGPLL 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899179363 873 GIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAiVQRQPFGGWKRS 940
Cdd:cd07095 344 QVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA-SSTAPFGGVGLS 410
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
567-962 |
6.98e-60 |
|
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: 214.39 E-value: 6.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLERLDGARfvPARVTLVVPPWNFPLAIPG 646
Cdd:TIGR01238 101 KLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVE--SRGVFVCISPWNFPLAIFT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 647 GSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELF--- 723
Cdd:TIGR01238 179 GQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqt 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 724 --RSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVG 801
Cdd:TIGR01238 259 laQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVA--DRVLTMIQGAMQELKVG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 802 EAWDPSSRMGPLI-APADGKLLDALTRLAPGESWLLEPRQldEEGRVWSPGikTGVAPG-------SEFHRtEYFGPVLG 873
Cdd:TIGR01238 337 VPHLLTTDVGPVIdAEAKQNLLAHIEHMSQTQKKIAQLTL--DDSRACQHG--TFVAPTlfelddiAELSE-EVFGPVLH 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 874 IM--HAATLDEAIELQNAVDYGLTAGLHSLDaDEVARWIDG-VEAGNLYVNRGTTGAIVQRQPFGGWKRSvvGAGAKAGG 950
Cdd:TIGR01238 412 VVryKARELDQIVDQINQTGYGLTMGVHSRI-ETTYRWIEKhARVGNCYVNRNQVGAVVGVQPFGGQGLS--GTGPKAGG 488
|
410
....*....|..
gi 1899179363 951 PNYLLGLGRVEP 962
Cdd:TIGR01238 489 PHYLYRLTQVQY 500
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
567-943 |
4.06e-54 |
|
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: 196.11 E-value: 4.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSlglERLDGaRFVPAR--------------VT 632
Cdd:cd07103 46 ILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEA---RRIYG-RTIPSPapgkrilvikqpvgVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 633 LVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSS-LGETLIADERVDQV 711
Cdd:cd07103 122 AAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLN-VVTGSPAeIGEALCASPRVRKI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 ILTGgyetaelfrSFRPGLTLLAETS----------GKNA-IVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILvga 780
Cdd:cd07103 201 SFTG---------STAVGKLLMAQAAdtvkrvslelGGNApFIVFDDADLDKAVDGAIASKFRNAGQTCVCAN-RIY--- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 781 VARSR--RFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQLDEEGRVWSPGIKTGV 856
Cdd:cd07103 268 VHESIydEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEdaVAKGAKVLTGGKRLGLGGYFYEPTVLTDV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 857 APGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVqrQPFGG 936
Cdd:cd07103 348 TDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE--APFGG 425
|
....*..
gi 1899179363 937 WKRSVVG 943
Cdd:cd07103 426 VKESGLG 432
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
567-945 |
7.35e-54 |
|
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: 196.20 E-value: 7.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVS---EVVDFAHYYAEQSLGlERLDGAR--------FVPARVTLVV 635
Cdd:cd07085 65 VMFKFRQLLEENLDELARLITLEHGKTLADARGDVLrglEVVEFACSIPHLLKG-EYLENVArgidtysyRQPLGVVAGI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 636 PPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQVILTG 715
Cdd:cd07085 144 TPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLN-VVHGGKEAVNALLDHPDIKAVSFVG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 716 GYETAELF--RSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARsrRFHEQLLD 793
Cdd:cd07085 223 STPVGEYIyeRAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEAD--EWIPKLVE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 794 AVRSMPVGEAWDPSSRMGPLIAP-ADGKLLDALTR-LAPGESWLLEPRQLD----EEGRVWSPGIKTGVAPGSEFHRTEY 867
Cdd:cd07085 301 RAKKLKVGAGDDPGADMGPVISPaAKERIEGLIESgVEEGAKLVLDGRGVKvpgyENGNFVGPTILDNVTPDMKIYKEEI 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899179363 868 FGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTgAIVQRQPFGGWKRSVVGAG 945
Cdd:cd07085 381 FGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGGWKGSFFGDL 457
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
567-951 |
1.51e-53 |
|
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: 193.90 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAE----------QSLGLERLDGARFVPARVTLVVP 636
Cdd:cd07104 27 ILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGlprrpegeilPSDVPGKESMVRRVPLGVVGVIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWE-AGVPREALQFVVLGDSSLGETLIADERVDQVILTG 715
Cdd:cd07104 107 PFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIFEeAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 716 ----GYETAELF-RSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARSrrFHEQ 790
Cdd:cd07104 187 stavGRHIGELAgRHLKK-VAL--ELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDE--FVEK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 791 LLDAVRSMPVGEAWDPSSRMGPLIAP-----ADGKLLDALT---RLAPGESWlleprqldeEGRVWSPGIKTGVAPGSEF 862
Cdd:cd07104 262 LVAKAKALPVGDPRDPDTVIGPLINErqvdrVHAIVEDAVAagaRLLTGGTY---------EGLFYQPTVLSDVTPDMPI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 863 HRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTT--GAIVqrqPFGGWKRS 940
Cdd:cd07104 333 FREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVndEPHV---PFGGVKAS 409
|
410
....*....|.
gi 1899179363 941 VVGagaKAGGP 951
Cdd:cd07104 410 GGG---RFGGP 417
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
567-943 |
7.03e-53 |
|
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: 191.90 E-value: 7.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYA---EQSLGLERLDGA------RFVPARVTLVVPP 637
Cdd:cd07100 26 LLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenaEAFLADEPIETDagkayvRYEPLGVVLGIMP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 638 WNFPL------AIPggstlaALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQV 711
Cdd:cd07100 106 WNFPFwqvfrfAAP------NLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQ-NLLIDSDQVEAIIADPRVRGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 ILTGgyetaelfrSFRPGlTLLAETSGKN------------AIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVG 779
Cdd:cd07100 179 TLTG---------SERAG-RAVAAEAGKNlkksvlelggsdPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 780 AVArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLiAPADgkLLDALTR-----LAPGESWLLEPRQLDEEGRVWSPGIKT 854
Cdd:cd07100 249 DVY--DEFLEKFVEAMAALKVGDPMDEDTDLGPL-ARKD--LRDELHEqveeaVAAGATLLLGGKRPDGPGAFYPPTVLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 855 GVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAivQRQPF 934
Cdd:cd07100 324 DVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSD--PRLPF 401
|
....*....
gi 1899179363 935 GGWKRSVVG 943
Cdd:cd07100 402 GGVKRSGYG 410
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
567-954 |
6.08e-52 |
|
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: 190.17 E-value: 6.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLgleRLDGA-------------RFVPARVTL 633
Cdd:cd07088 62 YLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWAR---RIEGEiipsdrpnenifiFKVPIGVVA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVIL 713
Cdd:cd07088 139 GILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGGYET-AELFRSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARsrRFHEQL 791
Cdd:cd07088 219 TGSTEAgQKIMEAAAENITKVSlELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYD--EFMEKL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLA--PGESWLLEPRQLD-EEGRVWSPGIKTGVAPGSEFHRTEYF 868
Cdd:cd07088 297 VEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMVERAveAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIF 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 869 GPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIvqrQPF-GGWKRS-VVGAGA 946
Cdd:cd07088 377 GPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAM---QGFhAGWKKSgLGGADG 453
|
....*...
gi 1899179363 947 KAGGPNYL 954
Cdd:cd07088 454 KHGLEEYL 461
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
567-943 |
7.19e-50 |
|
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: 183.57 E-value: 7.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLgleRLDGA------------RF-----VPA 629
Cdd:cd07149 48 ILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAK---RLAGEtipfdaspggegRIgftirEPI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 630 RVTLVVPPWNFPLaipggSTLA-----ALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSL-GETLI 703
Cdd:cd07149 125 GVVAAITPFNFPL-----NLVAhkvgpAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALN-VVTGSGETvGDALV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 704 ADERVDQVILTGGYETAELFRSfRPGLTLLAETSGKNA-IVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILVGAvA 782
Cdd:cd07149 199 TDPRVRMISFTGSPAVGEAIAR-KAGLKKVTLELGSNAaVIVDADADLEKAVERCVSGAFANAGQVCISVQ-RIFVHE-D 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 783 RSRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPAdgklldALTRLapgESWLLEP--------RQLDEEGRVWSPGIKT 854
Cdd:cd07149 276 IYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEA------EAERI---EEWVEEAveggarllTGGKRDGAILEPTVLT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 855 GVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTgAIVQRQPF 934
Cdd:cd07149 347 DVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSST-FRVDHMPY 425
|
....*....
gi 1899179363 935 GGWKRSVVG 943
Cdd:cd07149 426 GGVKESGTG 434
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
567-943 |
8.29e-50 |
|
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: 183.69 E-value: 8.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLERLDGARFVPARVTLV----------VP 636
Cdd:cd07118 48 VLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVlrepigvvgiIT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGg 716
Cdd:cd07118 128 PWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTG- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 yetaelfrSFRPGLTLLAETS-----------GKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARSr 785
Cdd:cd07118 207 --------STRVGKAIAAAAArnlkkvslelgGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 786 rFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTR-LAPGESWLLEPRQLDE-EGRVWSPGIKTGVAPGSEF 862
Cdd:cd07118 278 -FVAAVVARSRKVRVGDPLDPETKVGAIINEAQlAKITDYVDAgRAEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 863 HRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAivQRQPFGGWKRSVV 942
Cdd:cd07118 357 AREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGS--PELPFGGFKQSGI 434
|
.
gi 1899179363 943 G 943
Cdd:cd07118 435 G 435
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
567-943 |
3.88e-49 |
|
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: 182.00 E-value: 3.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQslgLERLDG-----------------ARFVPA 629
Cdd:cd07082 66 CLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEE---LKRLDGdslpgdwfpgtkgkiaqVRREPL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 630 RVTLVVPPWNFPLAIPGgSTLA-ALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERV 708
Cdd:cd07082 143 GVVLAIGPFNYPLNLTV-SKLIpALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 709 DQVILTGGYETAELFRSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFH 788
Cdd:cd07082 222 DVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVA--DELV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 789 EQLLDAVRSMPVGEAWDPSSRMGPLIAP--AD---GKLLDALTRlapGESWLLEPRQldEEGRVWSPGIKTGVAPGSEFH 863
Cdd:cd07082 300 ELLKEEVAKLKVGMPWDNGVDITPLIDPksADfveGLIDDAVAK---GATVLNGGGR--EGGNLIYPTLLDPVTPDMRLA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTtgaivQRQ----PFGGWKR 939
Cdd:cd07082 375 WEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKC-----QRGpdhfPFLGRKD 449
|
....
gi 1899179363 940 SVVG 943
Cdd:cd07082 450 SGIG 453
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
567-949 |
7.20e-49 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 180.63 E-value: 7.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLgleRLDGARFV-----------------PA 629
Cdd:cd07146 45 ILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEAL---RDDGESFScdltangkarkiftlrePL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 630 RVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGD-SSLGETLIADERV 708
Cdd:cd07146 122 GVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLS-VVTGEpGEIGDELITHPDV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 709 DQVILTGGYETAELFRSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFH 788
Cdd:cd07146 201 DLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVA--DEFV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 789 EQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQldeEGRVWSPGIKTGVAPGSEFHRTE 866
Cdd:cd07146 279 DLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEeaIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 867 YFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGtTGAIVQRQPFGGWKRSvvGAGA 946
Cdd:cd07146 356 TFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFGGVKDS--GLGG 432
|
...
gi 1899179363 947 KAG 949
Cdd:cd07146 433 KEG 435
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
567-943 |
2.36e-48 |
|
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: 179.36 E-value: 2.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYY---AEQSL---------GLERLdgARFVPARVTLV 634
Cdd:cd07102 45 IVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMisiAEEALadirvpekdGFERY--IRREPLGVVLI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 635 VPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQVILT 714
Cdd:cd07102 123 IAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQ-VLHLSHETSAALIADPRIDHVSFT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 715 GGYET-AELFRSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILVGAvARSRRFHEQLL 792
Cdd:cd07102 202 GSVAGgRAIQRAAAGRFIKVGlELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIE-RIYVHE-SIYDAFVEAFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 793 DAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEP---RQLDEEGRVWSPGIKTGVAPGSEFHRTEY 867
Cdd:cd07102 280 AVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAdaIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREET 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899179363 868 FGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTtgAIVQRQPFGGWKRSVVG 943
Cdd:cd07102 360 FGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCD--YLDPALAWTGVKDSGRG 433
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
529-943 |
5.10e-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: 178.40 E-value: 5.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 529 ETVAASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFA 608
Cdd:cd07094 10 EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 609 HYYAEQS---------LGLERLDGARFV-----PARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVL 674
Cdd:cd07094 90 RLAAEEAerirgeeipLDATQGSDNRLAwtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 675 TETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELFRSFRPGLTLLAETSGKNAIVVTPSADLDLAV 754
Cdd:cd07094 170 AKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAAI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 755 RDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLA--PGE 832
Cdd:cd07094 250 EALAKGGFYHAGQVCISVQRIYVHEELY--DEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEEAveAGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 833 SWLLEPRQldeEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDG 912
Cdd:cd07094 328 RLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEK 404
|
410 420 430
....*....|....*....|....*....|.
gi 1899179363 913 VEAGNLYVNRGTTGAiVQRQPFGGWKRSVVG 943
Cdd:cd07094 405 LEVGGVMVNDSSAFR-TDWMPFGGVKESGVG 434
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
567-940 |
6.48e-48 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 179.00 E-value: 6.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVD----FAHYYAEQSlGLERLDGA------RFVPARVTLVVP 636
Cdd:PRK09457 64 IVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINkiaiSIQAYHERT-GEKRSEMAdgaavlRHRPHGVVAVFG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVlGDSSLGETLIADERVDQVILTGG 716
Cdd:PRK09457 143 PYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQ-GGRETGKALAAHPDIDGLLFTGS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAE-LFRSF--RPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILVGAVARSRRFHEQLLD 793
Cdd:PRK09457 222 ANTGYlLHRQFagQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCAR-RLLVPQGAQGDAFLARLVA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 794 AVRSMPVGeAWD--PSSRMGPLI-APADGKLLDALTRL-APGESWLLEPRQLDEEGRVWSPGI--KTGVApgsEFHRTEY 867
Cdd:PRK09457 301 VAKRLTVG-RWDaePQPFMGAVIsEQAAQGLVAAQAQLlALGGKSLLEMTQLQAGTGLLTPGIidVTGVA---ELPDEEY 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899179363 868 FGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAiVQRQPFGGWKRS 940
Cdd:PRK09457 377 FGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGAS 448
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
524-952 |
2.73e-47 |
|
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: 175.94 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 524 TRLGEETVAasripDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSE 603
Cdd:cd07152 2 AVLGEVGVA-----DAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 604 VVDFAHYYAE---QSLGL------ERLDGARFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTA-AV 673
Cdd:cd07152 77 AIGELHEAAGlptQPQGEilpsapGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 674 LTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQVILTG----GYETAELFRSFRPGLTLlaETSGKNAIVVTPSAD 749
Cdd:cd07152 157 IARLFEEAGLPAGVLH-VLPGGADAGEALVEDPNVAMISFTGstavGRKVGEAAGRHLKKVSL--ELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 750 LDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARSrrFHEQLLDAVRSMPVGEAWDPSSRMGPLIApaDGKL-------- 821
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICMAAGRHLVHESVADA--YTAKLAAKAKHLPVGDPATGQVALGPLIN--ARQLdrvhaivd 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 822 --LDALTRLAPGESWlleprqldeEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLH 899
Cdd:cd07152 310 dsVAAGARLEAGGTY---------DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGII 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1899179363 900 SLDADEVARWIDGVEAGNLYVNRGTTGAIVQrQPFGGWKRSvvGAGAKAGGPN 952
Cdd:cd07152 381 SRDVGRAMALADRLRTGMLHINDQTVNDEPH-NPFGGMGAS--GNGSRFGGPA 430
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
568-965 |
2.78e-47 |
|
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: 176.26 E-value: 2.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 568 LHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSlglERLDGARFVPAR----------------V 631
Cdd:cd07099 46 LLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNA---PRVLAPRKVPTGllmpnkkatveyrpygV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 632 TLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIaDERVDQV 711
Cdd:cd07099 123 VGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQ-VVTGDGATGAALI-DAGVDKV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 ILTGGYET-----AELFRSFRPgltLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRR 786
Cdd:cd07099 201 AFTGSVATgrkvmAAAAERLIP---VVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVY--DE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 787 FHEQLLDAVRSMPVGEAWDPSSRMGPLIAPA-----DGKLLDALTRlapGESWLLEPRQLDEEGRVWSPGIKTGVAPGSE 861
Cdd:cd07099 276 FVARLVAKARALRPGADDIGDADIGPMTTARqldivRRHVDDAVAK---GAKALTGGARSNGGGPFYEPTVLTDVPHDMD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 862 FHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLD---ADEVARWIdgvEAGNLYVNRGTTGAIVQRQPFGGWK 938
Cdd:cd07099 353 VMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDlarAEAIARRL---EAGAVSINDVLLTAGIPALPFGGVK 429
|
410 420
....*....|....*....|....*..
gi 1899179363 939 RSvvgAGAKAGGPNYLLGLGRVEPVAA 965
Cdd:cd07099 430 DS---GGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
567-951 |
5.11e-47 |
|
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: 175.21 E-value: 5.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAE----------QSLGLERLDGARFVPARVTLVVP 636
Cdd:cd07150 48 ILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGecrrvrgetlPSDSPGTVSMSVRRPLGVVAGIT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTG- 715
Cdd:cd07150 128 PFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGs 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 716 ---GYETAELF-RSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARSrrFHEQL 791
Cdd:cd07150 208 tavGREIAEKAgRHLKK-ITL--ELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE--FVKKF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLIAPA-----DGKLLDALT---RLAPGESWlleprqldeEGRVWSPGIKTGVAPGSEFH 863
Cdd:cd07150 283 VARASKLKVGDPRDPDTVIGPLISPRqveriKRQVEDAVAkgaKLLTGGKY---------DGNFYQPTVLTDVTPDMRIF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGT--TGAIVqrqPFGGWKRSV 941
Cdd:cd07150 354 REETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTilDEAHV---PFGGVKASG 430
|
410
....*....|
gi 1899179363 942 VGagaKAGGP 951
Cdd:cd07150 431 FG---REGGE 437
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
567-927 |
7.59e-45 |
|
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: 169.69 E-value: 7.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYyaeqSLGLER-LDGARFVPAR-------------VT 632
Cdd:cd07130 61 IVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDF----AVGLSRqLYGLTIPSERpghrmmeqwnplgVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 633 LVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTA----AVLTETLWEAGVPrEALQFVVLGDSSLGETLIADERV 708
Cdd:cd07130 137 GVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAiavtKIVARVLEKNGLP-GAIASLVCGGADVGEALVKDPRV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 709 DQVILTG--------GYETAELFrsfrpGLTLLaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGA 780
Cdd:cd07130 216 PLVSFTGstavgrqvGQAVAARF-----GRSLL-ELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHES 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 781 VARSrrFHEQLLDAVRSMPVGEAWDPSSRMGPLIAP-ADGKLLDALTRL-APGESWLLEPRQLDEEGRVWSPGIKTGVAP 858
Cdd:cd07130 290 IYDE--VLERLKKAYKQVRIGDPLDDGTLVGPLHTKaAVDNYLAAIEEAkSQGGTVLFGGKVIDGPGNYVEPTIVEGLSD 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899179363 859 GSEFHrTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWID--GVEAGNLYVNRGTTGA 927
Cdd:cd07130 368 APIVK-EETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGpkGSDCGIVNVNIGTSGA 437
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
567-940 |
8.13e-45 |
|
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: 168.95 E-value: 8.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQS---------LGLERLDGARFVPARVTLVVPP 637
Cdd:cd07109 47 LLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAAdklhgetipLGPGYFVYTVREPHGVTGHIIP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 638 WNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGY 717
Cdd:cd07109 127 WNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 718 ETAELF-----RSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARS--RRFHEQ 790
Cdd:cd07109 207 ETGIAVmraaaENVVP-VTL--ELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLL----VHRSiyDEVLER 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 791 LLDAVRSMPVGEAW-DPSsrMGPLIAPADGKLLDALTRLAPGESWLL-----EPRQLDEEGRVWSPGIKTGVAPGSEFHR 864
Cdd:cd07109 280 LVERFRALRVGPGLeDPD--LGPLISAKQLDRVEGFVARARARGARIvaggrIAEGAPAGGYFVAPTLLDDVPPDSRLAQ 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899179363 865 TEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRqPFGGWKRS 940
Cdd:cd07109 358 EEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIEL-PFGGVKKS 432
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
567-944 |
8.89e-45 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 169.03 E-value: 8.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYY---AEQSLGLERLDGARFVPARVTL---------V 634
Cdd:cd07101 45 VFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYarrAERLLKPRRRRGAIPVLTRTTVnrrpkgvvgV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 635 VPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGD-SSLGETLIadERVDQVIL 713
Cdd:cd07101 125 ISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQ-VVTGPgSEVGGAIV--DNADYVMF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGGYETAELFRSfRPGLTLL---AETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQ 790
Cdd:cd07101 202 TGSTATGRVVAE-RAGRRLIgcsLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVY--DEFVRR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 791 LLDAVRSMPVGEAWDPSSRMGPLIAPADgklLDALTR-----LAPGESWLLEPRQLDEEG-RVWSPGIKTGVAPGSEFHR 864
Cdd:cd07101 279 FVARTRALRLGAALDYGPDMGSLISQAQ---LDRVTAhvddaVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 865 TEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQ-PFGGWKRSVVG 943
Cdd:cd07101 356 EETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLG 435
|
.
gi 1899179363 944 A 944
Cdd:cd07101 436 R 436
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
567-968 |
1.68e-44 |
|
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: 167.91 E-value: 1.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLE----RLDGARFVPARV--TLVVP---- 636
Cdd:cd07145 48 ILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRgetiPVDAYEYNERRIafTVREPigvv 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 ----PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVI 712
Cdd:cd07145 128 gaitPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMIS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 713 LTGGYETAELF--RSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQ 790
Cdd:cd07145 208 FTGSTAVGLLIasKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVY--DKFLKL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 791 LLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYFGP 870
Cdd:cd07145 286 LVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKRDEGSFFPPTVLENDTPDMIVMKEEVFGP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 871 VLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTgaivQRQ---PFGGWKRSvvgagak 947
Cdd:cd07145 366 VLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR----FRWdnlPFGGFKKS------- 434
|
410 420
....*....|....*....|.
gi 1899179363 948 aggpnyllGLGRvEPVAATVE 968
Cdd:cd07145 435 --------GIGR-EGVRYTML 446
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
561-954 |
3.39e-44 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 168.33 E-value: 3.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 561 AAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQS-------LGLERLDGARFV---PAR 630
Cdd:PLN02278 83 ASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAkrvygdiIPSPFPDRRLLVlkqPVG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 631 VTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQ 710
Cdd:PLN02278 163 VVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 711 VILTGgyetaelfrSFRPGLTLLAETS----------GKNA-IVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVG 779
Cdd:PLN02278 243 ITFTG---------STAVGKKLMAGAAatvkrvslelGGNApFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 780 AVarSRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQLDEEGRVWSPGIKTGVA 857
Cdd:PLN02278 314 GI--YDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQdaVSKGAKVLLGGKRHSLGGTFYEPTVLGDVT 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 858 PGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVqrQPFGGW 937
Cdd:PLN02278 392 EDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFGGV 469
|
410
....*....|....*...
gi 1899179363 938 KRSVVG-AGAKAGGPNYL 954
Cdd:PLN02278 470 KQSGLGrEGSKYGIDEYL 487
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
528-943 |
4.63e-44 |
|
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: 166.85 E-value: 4.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 528 EETVAASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTV-DQSDPEVSEVVD 606
Cdd:cd07115 7 GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIrAARRLDVPRAAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 607 FAHYYAEQSLGLE---------RLDGARFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTET 677
Cdd:cd07115 87 TFRYYAGWADKIEgevipvrgpFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 678 LWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAE-LFRSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVR 755
Cdd:cd07115 167 MAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRkIMQGAAGNLKRVSlELGGKSANIVFADADLDAAVR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 756 DVAYSAFGHAGQKCSAASLAILVGAVARsrRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTR-LAPGES 833
Cdd:cd07115 247 AAATGIFYNQGQMCTAGSRLLVHESIYD--EFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQfDRVLDYVDVgREEGAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 834 WLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGV 913
Cdd:cd07115 325 LLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAAL 404
|
410 420 430
....*....|....*....|....*....|
gi 1899179363 914 EAGNLYVNrgTTGAIVQRQPFGGWKRSVVG 943
Cdd:cd07115 405 KAGTVWIN--TYNRFDPGSPFGGYKQSGFG 432
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
567-943 |
1.56e-43 |
|
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: 165.56 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVsevvDFAHYYAEQSLGLERLDGARFVPA----------RVTL--- 633
Cdd:cd07151 59 ILEKAAQILEERRDEIVEWLIRESGSTRIKANIEW----GAAMAITREAATFPLRMEGRILPSdvpgkenrvyREPLgvv 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 -VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWE-AGVPREALQFVVLGDSSLGETlIADERVDQV 711
Cdd:cd07151 135 gVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLAKIFEeAGLPKGVLNVVVGAGSEIGDA-FVEHPVPRL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 I-LTG----GYETAEL-FRSF-RPGLtllaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARS 784
Cdd:cd07151 214 IsFTGstpvGRHIGELaGRHLkKVAL----ELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 785 rrFHEQLLDAVRSMPVGEAWDPSSRMGPLIapaDGKLLDALTRL-----APGESWLLEPrqlDEEGRVWSPGIKTGVAPG 859
Cdd:cd07151 290 --FVEKFVERVKALPYGDPSDPDTVVGPLI---NESQVDGLLDKieqavEEGATLLVGG---EAEGNVLEPTVLSDVTND 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 860 SEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTtgaiVQRQP---FGG 936
Cdd:cd07151 362 MEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQP----VNDEPhvpFGG 437
|
....*..
gi 1899179363 937 WKRSVVG 943
Cdd:cd07151 438 EKNSGLG 444
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
567-943 |
2.65e-43 |
|
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: 164.66 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDP-EVSEVVDFAHYYAEQSLG-----LERLDGAR----FVPARVTLVVP 636
Cdd:cd07093 46 ILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFADYILQldgesYPQDGGALnyvlRQPVGVAGLIT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGD-SSLGETLIADERVDQVILTG 715
Cdd:cd07093 126 PWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVN-VVHGFgPEAGAALVAHPDVDLISFTG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 716 GYETAELF-RSFRPGLT-LLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILVgavARS--RRFHEQL 791
Cdd:cd07093 205 ETATGRTImRAAAPNLKpVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGS-RILV---QRSiyDEFLERF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLL-----EPRQLDEEGRVW-SPGIKTGVAPGSEFHRT 865
Cdd:cd07093 281 VERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATIltgggRPELPDLEGGYFvEPTVITGLDNDSRVAQE 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899179363 866 EYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSVVG 943
Cdd:cd07093 361 EIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVN--CWLVRDLRTPFGGVKASGIG 436
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
567-943 |
8.10e-43 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 163.44 E-value: 8.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSD-PEVSEVVDFAHYYAeqslGLERLDGARFVPARV-----TLVVP---- 636
Cdd:TIGR01804 62 ILRRAADLIRERNEELAKLETLDTGKTLQETIvADMDSGADVFEFFA----GLAPALNGEIIPLGGpsfayTIREPlgvc 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 ----PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPrEALQFVVLGD-SSLGETLIADERVDQV 711
Cdd:TIGR01804 138 vgigAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLP-KGVFNVVQGDgAEVGPLLVNHPDVAKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 ILTGGYETAE-LFRSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILVGAVARSrRFHE 789
Cdd:TIGR01804 217 SFTGGVPTGKkIMAAAAGHLKHVTmELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGT-RVFVHKKIKE-RFLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 790 QLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLE------PRQLDEEGRVWSPGIKTGVAPGSEFH 863
Cdd:TIGR01804 295 RLVERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEGATLAtgggrpENVGLQNGFFVEPTVFADCTDDMTIV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSVVG 943
Cdd:TIGR01804 375 REEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWIN--TYNLYPAEAPFGGYKQSGIG 452
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
528-943 |
1.14e-42 |
|
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: 162.52 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 528 EETVAASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDF 607
Cdd:cd07110 7 EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 608 AHYYAEQSLGLER-------LDGARFV------PARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVL 674
Cdd:cd07110 87 FEYYADLAEQLDAkaeravpLPSEDFKarvrrePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 675 TETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYET--------AELFRsfrpGLTLlaETSGKNAIVVTP 746
Cdd:cd07110 167 AEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATgsqvmqaaAQDIK----PVSL--ELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 747 SADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDAL 825
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIA--DAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQyEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 826 TR-LAPGESWLLEPRQLD--EEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLD 902
Cdd:cd07110 319 ARgKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRD 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1899179363 903 ADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSVVG 943
Cdd:cd07110 399 AERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIG 437
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
567-944 |
1.26e-42 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 164.28 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQS---LGLERLDGA---------RFVPARVTLV 634
Cdd:PRK09407 81 VLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRApklLAPRRRAGAlpvltktteLRQPKGVVGV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 635 VPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGD-SSLGETLIadERVDQVIL 713
Cdd:PRK09407 161 ISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQ-VVTGPgPVVGTALV--DNADYLMF 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGGYET----AElfrsfRPGLTLL---AETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRR 786
Cdd:PRK09407 238 TGSTATgrvlAE-----QAGRRLIgfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIY--DE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 787 FHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADgklLDALTR-----LAPGESWLLEPRQLDEEG-RVWSPGIKTGVAPGS 860
Cdd:PRK09407 311 FVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ---LETVSAhvddaVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDM 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 861 EFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQ-PFGGWKR 939
Cdd:PRK09407 388 ELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKD 467
|
....*
gi 1899179363 940 SVVGA 944
Cdd:PRK09407 468 SGLGR 472
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
567-943 |
1.65e-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: 162.41 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVD-----QSDPEVSEVVDFA----HYYAEQSLG---LERLDGARFV---PARV 631
Cdd:cd07089 47 CLRQLHEALEARKEELRALLVAEVGAPVMtaramQVDGPIGHLRYFAdladSFPWEFDLPvpaLRGGPGRRVVrrePVGV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 632 TLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQV 711
Cdd:cd07089 127 VAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 ILTGGYET-AELFRSFRPGLT-LLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARSRR--F 787
Cdd:cd07089 207 SFTGSTAVgRRIMAQAAATLKrVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLL----VPRSRYdeV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 788 HEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLL-----EPRQLDeEGRVWSPGIKTGVAPGSEF 862
Cdd:cd07089 283 VEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGARLvtgggRPAGLD-KGFYVEPTLFADVDNDMRI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 863 HRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDAD---EVARWIDgveAGNLYVNRGTTGAIvqRQPFGGWKR 939
Cdd:cd07089 362 AQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDrayRVARRIR---TGSVGINGGGGYGP--DAPFGGYKQ 436
|
....
gi 1899179363 940 SVVG 943
Cdd:cd07089 437 SGLG 440
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
567-940 |
9.89e-42 |
|
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: 160.08 E-value: 9.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTV-DQSDPEVSEVVDFAHYYAE--------------QSLGLerldgARFVPARV 631
Cdd:cd07112 53 VLLRLADLIEAHRDELALLETLDMGKPIsDALAVDVPSAANTFRWYAEaidkvygevaptgpDALAL-----ITREPLGV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 632 TLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQV 711
Cdd:cd07112 128 VGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDAL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 ILTGGYETAELFRSF-------RPGLtllaETSGKNAIVVTPSA-DLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVAR 783
Cdd:cd07112 208 AFTGSTEVGRRFLEYsgqsnlkRVWL----ECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLL----VHE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 784 SRR--FHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLL----EPRQLDEEGRVWSPGIKTGVA 857
Cdd:cd07112 280 SIKdeFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLvaggKRVLTETGGFFVEPTVFDGVT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 858 PGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGW 937
Cdd:cd07112 360 PDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN--CFDEGDITTPFGGF 437
|
...
gi 1899179363 938 KRS 940
Cdd:cd07112 438 KQS 440
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
567-955 |
2.65e-41 |
|
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: 160.06 E-value: 2.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGElvEIMAAEA---GKTVDQSDPEVS-EVVDFAH---YYAEQSLGLERLDGARFVPARVT------- 632
Cdd:cd07123 96 IFLKAADLLSGKYRY--ELNAATMlgqGKNVWQAEIDAAcELIDFLRfnvKYAEELYAQQPLSSPAGVWNRLEyrplegf 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 633 -LVVPPWNFPlAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQV 711
Cdd:cd07123 174 vYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 ILTGGYET-----------AELFRSFrPglTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvga 780
Cdd:cd07123 253 HFTGSTPTfkslwkqigenLDRYRTY-P--RIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAY---- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 781 VARSR--RFHEQLLDAVRSMPVGEAWDPSSRMGPLI--------------APADgkllDALTRLAPGESwlleprqLDEE 844
Cdd:cd07123 326 VPESLwpEVKERLLEELKEIKMGDPDDFSNFMGAVIdekafdrikgyidhAKSD----PEAEIIAGGKC-------DDSV 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 845 GRVWSPGIKTGVAPGSEFHRTEYFGPVLGImHA---ATLDEAIEL-QNAVDYGLTAGLHSLD------ADEVARWidgvE 914
Cdd:cd07123 395 GYFVEPTVIETTDPKHKLMTEEIFGPVLTV-YVypdSDFEETLELvDTTSPYALTGAIFAQDrkaireATDALRN----A 469
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1899179363 915 AGNLYVNRGTTGAIVQRQPFGGWKRSvvGAGAKAGGPNYLL 955
Cdd:cd07123 470 AGNFYINDKPTGAVVGQQPFGGARAS--GTNDKAGSPLNLL 508
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
567-943 |
5.23e-41 |
|
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: 157.71 E-value: 5.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAeqslGL-ERLDGA-------------RFVPARVT 632
Cdd:cd07114 48 LLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYA----GLaDKIEGAvipvdkgdylnftRREPLGVV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 633 LVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVI 712
Cdd:cd07114 124 AAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 713 LTGGYETAELF-----RSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARS--R 785
Cdd:cd07114 204 FTGGTETGRHIaraaaENLAP-VTL--ELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLL----VQRSiyD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 786 RFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLL----EPRQLDEEGRVW--SPGIKTGVAPG 859
Cdd:cd07114 277 EFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVltggERPSGADLGAGYffEPTILADVTND 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 860 SEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKR 939
Cdd:cd07114 357 MRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVN--TYRALSPSSPFGGFKD 434
|
....
gi 1899179363 940 SVVG 943
Cdd:cd07114 435 SGIG 438
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
568-943 |
9.57e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 157.21 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 568 LHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGL---ERLDGA---------RFVPARVTLVV 635
Cdd:PRK09406 51 ANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALladEPADAAavgasrayvRYQPLGVVLAV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 636 PPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGdSSLGETLIADERVDQVILTG 715
Cdd:PRK09406 131 MPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVG-SGAVEAILRDPRVAAATLTG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 716 ----GYETAELF-RSFRPglTLLaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARSrrFHEQ 790
Cdd:PRK09406 210 sepaGRAVAAIAgDEIKK--TVL-ELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDA--FAEK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 791 LLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYF 868
Cdd:PRK09406 285 FVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDdaVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVF 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899179363 869 GPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGaiVQRQPFGGWKRSVVG 943
Cdd:PRK09406 365 GPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVS--YPELPFGGVKRSGYG 437
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
529-943 |
1.70e-40 |
|
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: 155.95 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 529 ETVAASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVD-QSDPEVSEVVDF 607
Cdd:cd07092 8 EEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHlVRDDELPGAVDN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 608 AHYYAEQSLGLERLDGARFVPARVTLV----------VPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTET 677
Cdd:cd07092 88 FRFFAGAARTLEGPAAGEYLPGHTSMIrrepigvvaqIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 678 LWEaGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYET-AELFRSFRPGLTLL-AETSGKNAIVVTPSADLDLAVR 755
Cdd:cd07092 168 AAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTgKKVARAAADTLKRVhLELGGKAPVIVFDDADLDAAVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 756 DVAYSAFGHAGQKCSAASLAILVGAVARsrRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTRLAPGESW 834
Cdd:cd07092 247 GIATAGYYNAGQDCTAACRVYVHESVYD--EFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQrERVAGFVERAPAHARV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 835 LLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVE 914
Cdd:cd07092 325 LTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLD 404
|
410 420
....*....|....*....|....*....
gi 1899179363 915 AGNLYVNrgTTGAIVQRQPFGGWKRSVVG 943
Cdd:cd07092 405 FGTVWVN--THIPLAAEMPHGGFKQSGYG 431
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
567-943 |
2.17e-40 |
|
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: 155.93 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLE----RLDGARFV-----PARVTLVVPP 637
Cdd:cd07090 46 ILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTLSgehvPLPGGSFAytrrePLGVCAGIGA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 638 WNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPrEALQFVVLGDSSLGETLIADERVDQVILTGGY 717
Cdd:cd07090 126 WNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLP-DGVFNVVQGGGETGQLLCEHPDVAKVSFTGSV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 718 ETAELFRSFRPG----LTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARSR--RFHEQL 791
Cdd:cd07090 205 PTGKKVMSAAAKgikhVTL--ELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVF----VQRSIkdEFTERL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLI-APADGKLLDALTR--------LAPGESWLLEPRQldEEGRVWSPGIKTGVAPGSEF 862
Cdd:cd07090 279 VERTKKIRIGDPLDEDTQMGALIsEEHLEKVLGYIESakqegakvLCGGERVVPEDGL--ENGFYVSPCVLTDCTDDMTI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 863 HRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNR-GTTGAIVqrqPFGGWKRSV 941
Cdd:cd07090 357 VREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSG 433
|
..
gi 1899179363 942 VG 943
Cdd:cd07090 434 FG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
567-943 |
3.66e-39 |
|
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: 152.85 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAeqslGLERLDGARFVPAR-------------VTL 633
Cdd:cd07119 64 LLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYA----GLATKETGEVYDVPphvisrtvrepvgVCG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVIL 713
Cdd:cd07119 140 LITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGGYETAE-LFRSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQL 791
Cdd:cd07119 220 TGGTATGRsIMRAAAGNVKKVAlELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIH--DKFVAAL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLEP--RQLDE----EGRVWSPGIKTGVAPGSEFHRT 865
Cdd:cd07119 298 AERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCggKRPTGdelaKGYFVEPTIFDDVDRTMRIVQE 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899179363 866 EYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSVVG 943
Cdd:cd07119 378 EIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIN--DYHPYFAEAPWGGYKQSGIG 453
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
568-954 |
5.64e-39 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 150.66 E-value: 5.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 568 LHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAE----------QSlglERLDGARFV---PARVTLV 634
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEwarryegeiiQS---DRPGENILLfkrALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 635 VPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILT 714
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 715 GGYETAE-LFRSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARsrRFHEQLL 792
Cdd:PRK10090 158 GSVSAGEkIMAAAAKNITKVClELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD--QFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 793 DAVRSMPVGeawDPSSR----MGPLIAPADGKLLDALTRLA--PGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTE 866
Cdd:PRK10090 236 EAMQAVQFG---NPAERndiaMGPLINAAALERVEQKVARAveEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 867 YFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIvqrQPF-GGWKRS-VVGA 944
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSgIGGA 389
|
410
....*....|
gi 1899179363 945 GAKAGGPNYL 954
Cdd:PRK10090 390 DGKHGLHEYL 399
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
567-940 |
8.77e-39 |
|
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: 150.42 E-value: 8.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQ-SLGLERL-------DGARFV--PARVTLVVP 636
Cdd:cd07105 27 ILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLiTQIIGGSipsdkpgTLAMVVkePVGVVLGIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLG---ETLIADERVDQVIL 713
Cdd:cd07105 107 PWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEDAPevvEALIAHPAVRKVNF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TG----GYETAELF-RSFRPgltLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArsRRFH 788
Cdd:cd07105 187 TGstrvGRIIAETAaKHLKP---VLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIA--DEFV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 789 EQLLDAVRSMPVGeawdpSSRMGPLIAPADGKLLDALTR--LAPGESWLL-EPRQLDEEGRVWSPGIKTGVAPGSEFHRT 865
Cdd:cd07105 262 EKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDdaLSKGAKLVVgGLADESPSGTSMPPTILDNVTPDMDIYSE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 866 EYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLD---ADEVARWIdgvEAGNLYVNRGTtgaiVQRQ---PFGGWKR 939
Cdd:cd07105 337 ESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlarALAVAKRI---ESGAVHINGMT----VHDEptlPHGGVKS 409
|
.
gi 1899179363 940 S 940
Cdd:cd07105 410 S 410
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
567-943 |
1.21e-38 |
|
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: 151.44 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDP-EVSEVVDFAHYYAEQS---------LGLERLDGARFV------PAR 630
Cdd:cd07113 65 ILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWAtkingetlaPSIPSMQGERYTaftrrePVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 631 VTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQ 710
Cdd:cd07113 145 VVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLN-VVNGKGAVGAQLISHPDVAK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 711 VILTGGYETAE-LFRSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARSR--R 786
Cdd:cd07113 224 VSFTGSVATGKkIGRQAASDLTRVTlELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFY----VHRSKfdE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 787 FHEQLLDAVRSMPVGEAWDPSSRMGPLIA-PADGKLLDALTRLAPGESWLLE-PRQLDEEGRVWSPGIKTGVAPGSEFHR 864
Cdd:cd07113 300 LVTKLKQALSSFQVGSPMDESVMFGPLANqPHFDKVCSYLDDARAEGDEIVRgGEALAGEGYFVQPTLVLARSADSRLMR 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899179363 865 TEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTgaIVQRQPFGGWKRSVVG 943
Cdd:cd07113 380 EETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTF--LDPAVPFGGMKQSGIG 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
575-965 |
1.37e-38 |
|
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: 150.57 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 575 LEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAeqslGLERLDGARFV-------------PARVTLVVPPWNFP 641
Cdd:cd07120 55 FEANAERLARLLALENGKILGEARFEISGAISELRYYA----GLARTEAGRMIepepgsfslvlrePMGVAGIIVPWNSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 642 LAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEA-GVPREALQFVVLGDSSLGETLIADERVDQVILTGGYET- 719
Cdd:cd07120 131 VVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATg 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 720 AELFRSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILVGAvARSRRFHEQLLDAVRSM 798
Cdd:cd07120 211 RAIMAAAAPTLKRLGlELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGS-RVLVQR-SIADEVRDRLAARLAAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 799 PVGEAWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQLDEE---GRVWSPGIKTGVAPGSEFHRTEYFGPVLG 873
Cdd:cd07120 289 KVGPGLDPASDMGPLIDRANVDRVDRMVEraIAAGAEVVLRGGPVTEGlakGAFLRPTLLEVDDPDADIVQEEIFGPVLT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 874 IMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSvvgagakaggpny 953
Cdd:cd07120 369 LETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIN--DWNKLFAEAEEGGYRQS------------- 433
|
410
....*....|..
gi 1899179363 954 llGLGRVEPVAA 965
Cdd:cd07120 434 --GLGRLHGVAA 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
567-944 |
1.45e-38 |
|
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: 150.37 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLERLDG-------ARFVPARVTLVVPPWN 639
Cdd:cd07106 46 ALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTASLDLPDEVIEDddtrrveLRRKPLGVVAAIVPWN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 640 FPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWE---AGVpreaLQfVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd07106 126 FPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEvlpPGV----LN-VVSGGDELGPALTSHPDIRKISFTGS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YET---------AELFRsfrpgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARSR-- 785
Cdd:cd07106 201 TATgkkvmasaaKTLKR-----VTL--ELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLY----VHESIyd 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 786 RFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESW--LLEPRQLDEEGRVWSPGIKTGVAPGSEFH 863
Cdd:cd07106 270 EFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAkvLAGGEPLDGPGYFIPPTIVDDPPEGSRIV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLD---ADEVARWIdgvEAGNLYVNrgTTGAIVQRQPFGGWKRS 940
Cdd:cd07106 350 DEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDlerAEAVARRL---EAGTVWIN--THGALDPDAPFGGHKQS 424
|
....
gi 1899179363 941 VVGA 944
Cdd:cd07106 425 GIGV 428
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
567-943 |
1.46e-38 |
|
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: 150.73 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEV-VDFAHYYAEQSLGL---ERLDGARFV--PARVTLVVPPWNF 640
Cdd:cd07138 63 LLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLgIGHLRAAADALKDFefeERRGNSLVVrePIGVCGLITPWNW 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 641 PLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGD-SSLGETLIADERVDQVILTGgyet 719
Cdd:cd07138 143 PLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFN-LVNGDgPVVGEALSAHPDVDMVSFTG---- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 720 aelfrSFRPGLTLLA-----------ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARSR--R 786
Cdd:cd07138 218 -----STRAGKRVAEaaadtvkrvalELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRML----VPRSRyaE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 787 FHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLE------PRQLdEEGRVWSPGIKTGVAPGS 860
Cdd:cd07138 289 AEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVaggpgrPEGL-ERGYFVKPTVFADVTPDM 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 861 EFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAivqRQPFGGWKRS 940
Cdd:cd07138 368 TIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQS 444
|
...
gi 1899179363 941 VVG 943
Cdd:cd07138 445 GNG 447
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
529-943 |
8.52e-38 |
|
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: 148.16 E-value: 8.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 529 ETVAASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFA 608
Cdd:cd07147 10 EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 609 HYYAEQSL--------------GLERLDGARFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVL 674
Cdd:cd07147 90 RIAAEEATriygevlpldisarGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 675 TETLWEAGVPREALQFVVLgDSSLGETLIADERVDQVILTGGYETAELFRSFRPGLTLLAETSGKNAIVVTPSADLDLAV 754
Cdd:cd07147 170 GEVLAETGLPKGAFSVLPC-SRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 755 RDVAYSAFGHAGQKCSAASLAILVGAVArsRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPadgkllDALTRLapgESW 834
Cdd:cd07147 249 QRIIFGAFYQAGQSCISVQRVLVHRSVY--DEFKSRLVARVKALKTGDPKDDATDVGPMISE------SEAERV---EGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 835 LLEPRQ--------LDEEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEV 906
Cdd:cd07147 318 VNEAVDagaklltgGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 1899179363 907 ARWIDGVEAGNLYVNRGTTGAiVQRQPFGGWKRSVVG 943
Cdd:cd07147 398 LRAWDELEVGGVVINDVPTFR-VDHMPYGGVKDSGIG 433
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
567-943 |
5.55e-37 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 146.20 E-value: 5.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQS-DPEVSEVVDFAHYYA---------EQSLGLERLDGARFVPARVTLVVP 636
Cdd:cd07091 70 LLNKLADLIERDRDELAALESLDNGKPLEESaKGDVALSIKCLRYYAgwadkiqgkTIPIDGNFLAYTRREPIGVCGQII 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd07091 150 PWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAELF-----RSFRPGLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILVGAVARSrRFHEQL 791
Cdd:cd07091 230 TAVGRTImeaaaKSNLKKVTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGS-RIFVQESIYD-EFVEKF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTR--------LAPGESWlleprqlDEEGRVWSPGIKTGVAPGSEF 862
Cdd:cd07091 306 KARAEKRVVGDPFDPDTFQGPQVSKAQfDKILSYIESgkkegatlLTGGERH-------GSKGYFIQPTVFTDVKDDMKI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 863 HRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSVV 942
Cdd:cd07091 379 AKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN--TYNVFDAAVPFGGFKQSGF 456
|
.
gi 1899179363 943 G 943
Cdd:cd07091 457 G 457
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
567-951 |
1.78e-36 |
|
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: 144.64 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQS-DPEVSEVVDFAHYYAEQSLGL---ERLDGA-------RFVPARVTLVV 635
Cdd:cd07139 65 VLRRLADALEARADELARLWTAENGMPISWSrRAQGPGPAALLRYYAALARDFpfeERRPGSggghvlvRREPVGVVAAI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 636 PPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQVILTG 715
Cdd:cd07139 145 VPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVN-VVPADREVGEYLVRHPGVDKVSFTG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 716 --------GYETAELFRSfrpgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAILVGAvARSRRF 787
Cdd:cd07139 224 staagrriAAVCGERLAR----VTL--ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALT-RILVPR-SRYDEV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 788 HEQLLDAVRSMPVGEAWDPSSRMGPLIAP----------ADGKLLDAltRLAPGESwllEPRQLDeEGRVWSPGIKTGVA 857
Cdd:cd07139 296 VEALAAAVAALKVGDPLDPATQIGPLASArqrervegyiAKGRAEGA--RLVTGGG---RPAGLD-RGWFVEPTLFADVD 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 858 PGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDAD---EVARWIdgvEAGNLYVNrGTTGAIVqrQPF 934
Cdd:cd07139 370 NDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVErglAVARRI---RTGTVGVN-GFRLDFG--APF 443
|
410
....*....|....*..
gi 1899179363 935 GGWKRSVVGagaKAGGP 951
Cdd:cd07139 444 GGFKQSGIG---REGGP 457
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
567-949 |
6.88e-36 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 143.82 E-value: 6.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYyaeqSLGLERLDGARFVPAR--------------VT 632
Cdd:PLN02315 83 IVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDF----AVGLSRQLNGSIIPSErpnhmmmevwnplgIV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 633 LVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTA----RTAAVLTETLWEAGVPrEALQFVVLGDSSLGETLIADERV 708
Cdd:PLN02315 159 GVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLP-GAIFTSFCGGAEIGEAIAKDTRI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 709 DQVILTGGYETAELFRSF---RPGLTLLaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVarSR 785
Cdd:PLN02315 238 PLVSFTGSSKVGLMVQQTvnaRFGKCLL-ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI--YD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 786 RFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRL--APGESWLLEPRQLDEEGRVWSPGIkTGVAPGSEFH 863
Cdd:PLN02315 315 DVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIikSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVV 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWI--DGVEAGNLYVNRGTTGAIVQrQPFGGWKRSv 941
Cdd:PLN02315 394 KEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIgpLGSDCGIVNVNIPTNGAEIG-GAFGGEKAT- 471
|
....*...
gi 1899179363 942 vGAGAKAG 949
Cdd:PLN02315 472 -GGGREAG 478
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
575-954 |
8.72e-36 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 143.33 E-value: 8.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 575 LEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQ------------SLGLERLDG-ARFVPARVTLVVPPWNFP 641
Cdd:PLN02467 85 ITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLaealdakqkapvSLPMETFKGyVLKEPLGVVGLITPWNYP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 642 LAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAE 721
Cdd:PLN02467 165 LLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 722 LFRS-----FRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARsrRFHEQLLDAVR 796
Cdd:PLN02467 245 KIMTaaaqmVKP-VSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIAS--EFLEKLVKWAK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 797 SMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLL-----EPRQLdEEGRVWSPGIKTGVAPGSEFHRTEYFGPV 871
Cdd:PLN02467 320 NIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATIlcggkRPEHL-KKGFFIEPTIITDVTTSMQIWREEVFGPV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 872 LGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSVVGAGAKAGG- 950
Cdd:PLN02467 399 LCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFGRELGEWGl 476
|
....
gi 1899179363 951 PNYL 954
Cdd:PLN02467 477 ENYL 480
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
567-943 |
1.27e-34 |
|
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: 139.03 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTV-DQSDPEVSEVVDFAHYYA----EQS-----LGLERLDGARFVPARVTLVVP 636
Cdd:cd07108 46 LLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFGglagELKgetlpFGPDVLTYTVREPLGVVGAIL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAgVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd07108 126 PWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAE-LFRSFRPGL---TLlaETSGKNAIVVTPSADLDLAVRDVAYSA-FGHAGQKCSAASLAILVGAVARSrrFHEQL 791
Cdd:cd07108 205 TEVGKiIYRAAADRLipvSL--ELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDA--FLEKL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLIAP----------ADGKLLDALTRLAPGeswlLEPRQLD-EEGRVWSPGIKTGVAPGS 860
Cdd:cd07108 281 VAKLSKLKIGDPLDEATDIGAIISEkqfakvcgyiDLGLSTSGATVLRGG----PLPGEGPlADGFFVQPTIFSGVDNEW 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 861 EFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGttGAIVQRQPFGGWKRS 940
Cdd:cd07108 357 RLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQS 434
|
...
gi 1899179363 941 VVG 943
Cdd:cd07108 435 GLG 437
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
568-954 |
1.32e-34 |
|
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: 139.45 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 568 LHRAGELLEARRGELVEIMAAEAGKTVDQS-DPEVSEVVDFAHYYAEQSLGLERlDGARFVPARVTLVVPPWNFPLAIPG 646
Cdd:cd07111 87 LYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWAQLLDT-ELAGWKPVGVVGQIVPWNFPLLMLA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 647 GSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQVILTGGYETAELFRSF 726
Cdd:cd07111 166 WKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLN-IVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 727 RPG----LTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARsrRFHEQLLDAVRSMPVGE 802
Cdd:cd07111 245 TAGtgkkLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAE--ELIRKLKERMSHLRVGD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 803 AWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATL 880
Cdd:cd07111 321 PLDKAIDMGAIVDPAQLKRIRELVEegRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899179363 881 DEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSVVG-AGAKAGGPNYL 954
Cdd:cd07111 401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN--GHNLFDAAAGFGGYRESGFGrEGGKEGLYEYL 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
567-943 |
3.65e-33 |
|
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: 134.93 E-value: 3.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSD-PEVSEVVDFAHYYA---EQSLGLE-RLDGARFV-----PARVTLVVP 636
Cdd:cd07142 70 ILLRFADLLEKHADELAALETWDNGKPYEQARyAEVPLAARLFRYYAgwaDKIHGMTlPADGPHHVytlhePIGVVGQII 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd07142 150 PWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAELF-----RSFRPGLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCsaaslailvgaVARSRRF-HEQ 790
Cdd:cd07142 230 TEVGKIImqlaaKSNLKPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCC-----------CAGSRTFvHES 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 791 LLD--------AVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTR-LAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGS 860
Cdd:cd07142 297 IYDefvekakaRALKRVVGDPFRKGVEQGPQVDKEQfEKILSYIEHgKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDM 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 861 EFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRS 940
Cdd:cd07142 377 KIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMS 454
|
...
gi 1899179363 941 VVG 943
Cdd:cd07142 455 GIG 457
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
535-943 |
9.22e-33 |
|
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: 133.27 E-value: 9.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 535 RIPDA--AGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYA 612
Cdd:cd07107 12 RVPAAsaADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 613 EQSLGL---------ERLDGARFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAgV 683
Cdd:cd07107 92 GLVTELkgetipvggRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 684 PREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELF-RSFRPGLT-LLAETSGKNAIVVTPSADLDLAVRD-VAYS 760
Cdd:cd07107 171 PPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAImRAAAEGIKhVTLELGGKNALIVFPDADPEAAADAaVAGM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 761 AFGHAGQKCSAASLAILVGAVARSrrFHEQLLDAVRSMPVGEAWDPSSRMGPLI--------------APADGKLLDALT 826
Cdd:cd07107 251 NFTWCGQSCGSTSRLFVHESIYDE--VLARVVERVAAIKVGDPTDPATTMGPLVsrqqydrvmhyidsAKREGARLVTGG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 827 RLAPGES----WLLEPRQLDEegrvwspgiktgVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLD 902
Cdd:cd07107 329 GRPEGPAleggFYVEPTVFAD------------VTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1899179363 903 ADEVARWIDGVEAGNLYVNRGTT---GAivqrqPFGGWKRSVVG 943
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRhflGA-----PFGGVKNSGIG 435
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
581-964 |
5.41e-32 |
|
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: 131.27 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 581 ELVEIMAAEAGKT-VDQSDPEV---SEVVDFAHYYAEQSLGLERLDGA----------RFVPARVTLVVPPWNFPLAIPG 646
Cdd:cd07098 59 EICRVACRDTGKTmVDASLGEIlvtCEKIRWTLKHGEKALRPESRPGGllmfykrarvEYEPLGVVGAIVSWNYPFHNLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 647 GSTLAALASGSSVVFKPARRTARTAA----VLTETLWEAGVPREALQFVV-LGDSslGETLIADERVDQVILTGGYETAE 721
Cdd:cd07098 139 GPIIAALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTcLPET--AEALTSHPVIDHITFIGSPPVGK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 722 LF-RSFRPGLT-LLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARSR--RFHEQLLDAVRS 797
Cdd:cd07098 217 KVmAAAAESLTpVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVI----VHEKIydKLLEILTDRVQA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 798 MPVGEAWDPSSRMGPLIAPAD-----GKLLDALT---RLAPGESwlLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYFG 869
Cdd:cd07098 293 LRQGPPLDGDVDVGAMISPARfdrleELVADAVEkgaRLLAGGK--RYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 870 PVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSvvGAGaKAG 949
Cdd:cd07098 371 PVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGS--GFG-RFA 447
|
410
....*....|....*
gi 1899179363 950 GPNYLLGLGRVEPVA 964
Cdd:cd07098 448 GEEGLRGLCNPKSVT 462
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
568-943 |
9.07e-31 |
|
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: 127.64 E-value: 9.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 568 LHRAGELLEARRGELVEIMAAEAGKTVDQSDP-EVSEVVDFAHYY---AEQSLG------LERLDGARFVPARVTLVVPP 637
Cdd:cd07143 74 LSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYggwADKIHGqvietdIKKLTYTRHEPIGVCGQIIP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 638 WNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGY 717
Cdd:cd07143 154 WNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGST 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 718 ETA-----ELFRSFRPGLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVarSRRFHEQLL 792
Cdd:cd07143 234 LVGrkvmeAAAKSNLKKVTL--ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGI--YDKFVKRFK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 793 DAVRSMPVGEAWDPSSRMGPLIAP--ADGKLLDALTRLAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYFGP 870
Cdd:cd07143 310 EKAKKLKVGDPFAEDTFQGPQVSQiqYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGP 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899179363 871 VLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTgaIVQRQPFGGWKRSVVG 943
Cdd:cd07143 390 VVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNL--LHHQVPFGGYKQSGIG 460
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
567-943 |
1.16e-30 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 127.69 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVdqSDPEVSEVV---DFAHYYAEQSLGLE----RLDGARFV-----PARVTLV 634
Cdd:PRK13252 71 ILRRAVDILRERNDELAALETLDTGKPI--QETSVVDIVtgaDVLEYYAGLAPALEgeqiPLRGGSFVytrrePLGVCAG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 635 VPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPrEALQFVVLGDSSLGETLIADERVDQVILT 714
Cdd:PRK13252 149 IGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLP-DGVFNVVQGDGRVGAWLTEHPDIAKVSFT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 715 GGYET-----AELFRSFRPgLTLlaETSGKNAIVVTPSADLDLAVrDVAYSA-FGHAGQKCSAASLAIlvgaVARS--RR 786
Cdd:PRK13252 228 GGVPTgkkvmAAAAASLKE-VTM--ELGGKSPLIVFDDADLDRAA-DIAMLAnFYSSGQVCTNGTRVF----VQKSikAA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 787 FHEQLLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDAL--------TRLAPGESWllePRQLDEEGRVWSPGIKTGVA 857
Cdd:PRK13252 300 FEARLLERVERIRIGDPMDPATNFGPLVSFAHrDKVLGYIekgkaegaRLLCGGERL---TEGGFANGAFVAPTVFTDCT 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 858 PGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGW 937
Cdd:PRK13252 377 DDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN--TWGESPAEMPVGGY 454
|
....*.
gi 1899179363 938 KRSVVG 943
Cdd:PRK13252 455 KQSGIG 460
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
568-943 |
2.25e-30 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 126.13 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 568 LHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSLGLERLDGA---------RFVPARVTLVVPPW 638
Cdd:PRK13968 57 LRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPTlvenqqaviEYRPLGTILAIMPW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 639 NFPL------AIPggstlaALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETlIADERVDQVI 712
Cdd:PRK13968 137 NFPLwqvmrgAVP------ILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQM-INDSRIAAVT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 713 LTGgyetaelfrSFRPGLTLLA-----------ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAV 781
Cdd:PRK13968 210 VTG---------SVRAGAAIGAqagaalkkcvlELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 782 ARsrRFHEQLLDAVRSMPVGEAWDPSSRMGPLiapADGKLLDALTR-----LAPGESWLLEPRQLDEEGRVWSPGIKTGV 856
Cdd:PRK13968 281 AS--AFTERFVAAAAALKMGDPRDEENALGPM---ARFDLRDELHHqveatLAEGARLLLGGEKIAGAGNYYAPTVLANV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 857 APGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGG 936
Cdd:PRK13968 356 TPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN--GYCASDARVAFGG 433
|
....*..
gi 1899179363 937 WKRSVVG 943
Cdd:PRK13968 434 VKKSGFG 440
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
567-954 |
4.20e-30 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 125.79 E-value: 4.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQSlglERLDG---------ARFV----PARVTL 633
Cdd:PRK11241 75 ILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEG---KRIYGdtipghqadKRLIvikqPIGVTA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVIL 713
Cdd:PRK11241 152 AITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGGYETA-ELFRSFRPGLTLLAETSGKNA-IVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVarSRRFHEQL 791
Cdd:PRK11241 232 TGSTEIGrQLMEQCAKDIKKVSLELGGNApFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV--YDRFAEKL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLI-----APADGKLLDALTRlapGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTE 866
Cdd:PRK11241 310 QQAVSKLHIGDGLEKGVTIGPLIdekavAKVEEHIADALEK---GARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 867 YFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVqrQPFGGWKRSVVG-AG 945
Cdd:PRK11241 387 TFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIKASGLGrEG 464
|
....*....
gi 1899179363 946 AKAGGPNYL 954
Cdd:PRK11241 465 SKYGIEDYL 473
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
567-943 |
7.19e-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: 125.15 E-value: 7.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTV-DQSDPEVSEVVDFAHYYA---EQSLGLE-RLDGARFV-----PARVTLVVP 636
Cdd:cd07141 74 LLNKLADLIERDRAYLASLETLDNGKPFsKSYLVDLPGAIKVLRYYAgwaDKIHGKTiPMDGDFFTytrhePVGVCGQII 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd07141 154 PWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAELF-----RSFRPGLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAAslailvgavarSRRF-HEQ 790
Cdd:cd07141 234 TEVGKLIqqaagKSNLKRVTL--ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAG-----------SRTFvQES 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 791 LLD-----AV---RSMPVGEAWDPSSRMGPLIapaDGKLLDALTRLApgESWLLEPRQLDEEGRVW-------SPGIKTG 855
Cdd:cd07141 301 IYDefvkrSVeraKKRVVGNPFDPKTEQGPQI---DEEQFKKILELI--ESGKKEGAKLECGGKRHgdkgyfiQPTVFSD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 856 VAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFG 935
Cdd:cd07141 376 VTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFG 453
|
....*...
gi 1899179363 936 GWKRSVVG 943
Cdd:cd07141 454 GYKMSGNG 461
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
567-943 |
4.15e-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: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQ-SDPEVSEVVDFAHYYAEqslGLERLDGARFVPA----RVTLVVP----- 636
Cdd:cd07144 73 LLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAG---WADKIQGKTIPTSpnklAYTLHEPygvcg 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 ---PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVIL 713
Cdd:cd07144 150 qiiPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAF 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TG----GYETAELFRSFRPGLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARsrRFHE 789
Cdd:cd07144 230 TGstatGRLVMKAAAQNLKAVTL--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYD--KFVE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 790 QLLDAVRS-MPVGEAWDPSSRMGPLIAPAD-GKLLDALTR-LAPGESWLLE---PRQLDEEGRVWSPGIKTGVAPGSEFH 863
Cdd:cd07144 306 KFVEHVKQnYKVGSPFDDDTVVGPQVSKTQyDRVLSYIEKgKKEGAKLVYGgekAPEGLGKGYFIPPTIFTDVPQDMRIV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 864 RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIvqRQPFGGWKRSVVG 943
Cdd:cd07144 386 KEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSGIG 463
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
567-945 |
6.29e-29 |
|
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: 121.76 E-value: 6.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQ---------SLGLERLDGARFV-----PARVT 632
Cdd:cd07148 49 ILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADElgqlggreiPMGLTPASAGRIAfttrePIGVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 633 LVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLgDSSLGETLIADERVDQVI 712
Cdd:cd07148 129 VAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 713 LTGGYETAELFRS-FRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCsaASLAILVGAVARSRRFHEQL 791
Cdd:cd07148 208 FIGSARVGWMLRSkLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVC--VSVQRVFVPAEIADDFAQRL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQLDEEgrVWSPGIKTGVAPGSEFHRTEYFG 869
Cdd:cd07148 286 AAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNeaVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFG 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899179363 870 PVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrGTTGAIVQRQPFGGWKRSVVGAG 945
Cdd:cd07148 364 PVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVN-DHTAFRVDWMPFAGRRQSGYGTG 438
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
573-921 |
3.57e-28 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 121.39 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 573 ELLEARRGELVEIMAAEAGKTVDQSDPEVS---EVVDFAHYYAEQSLGLERLDGARFV-------PARVTLVVPPWNFPL 642
Cdd:PLN02419 184 ELIRKNMDKLAMNITTEQGKTLKDSHGDIFrglEVVEHACGMATLQMGEYLPNVSNGVdtysirePLGVCAGICPFNFPA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 643 AIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQfVVLGDSSLGETLIADERVDQVILTGGyETAEL 722
Cdd:PLN02419 264 MIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLN-IVHGTNDTVNAICDDEDIRAVSFVGS-NTAGM 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 723 F---RSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGavaRSRRFHEQLLDAVRSMP 799
Cdd:PLN02419 342 HiyaRAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVG---DAKSWEDKLVERAKALK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 800 VGEAWDPSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQL----DEEGRVWSPGIKTGVAPGSEFHRTEYFGPVLG 873
Cdd:PLN02419 419 VTCGSEPDADLGPVISKQAKERICRLIQsgVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLV 498
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1899179363 874 IMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVN 921
Cdd:PLN02419 499 CMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
567-940 |
3.67e-28 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 119.63 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQS-DPEVSEVVDFAHYYAEQSLGLERLDGARFVPARVTLV----------V 635
Cdd:PRK13473 66 ALLKLADAIEENADEFARLESLNCGKPLHLAlNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIrrdpvgvvasI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 636 PPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAgVPREALQFVVLGDSSLGETLIADERVDQVILTG 715
Cdd:PRK13473 146 APWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 716 GYETAE--LFRSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAIlvgaVARSR--RFHEQL 791
Cdd:PRK13473 225 SIATGKhvLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIY----AQRGIydDLVAKL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 792 LDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESW---LLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYF 868
Cdd:PRK13473 301 AAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHirvVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVF 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899179363 869 GPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLD---ADEVARWIDgveAGNLYVNrgTTGAIVQRQPFGGWKRS 940
Cdd:PRK13473 381 GPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDvgrAHRVSARLQ---YGCTWVN--THFMLVSEMPHGGQKQS 450
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
567-943 |
6.09e-27 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 116.46 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTvdqsdPEVSEVVDFA------HYYAE-------QSLGLER-LDGARF-VPARV 631
Cdd:PLN02766 87 IMMKFADLIEEHIEELAALDTIDAGKL-----FALGKAVDIPaaagllRYYAGaadkihgETLKMSRqLQGYTLkEPIGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 632 TLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQV 711
Cdd:PLN02766 162 VGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 712 ILTGGYETAELF--RSFRPGLTLLA-ETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVarSRRFH 788
Cdd:PLN02766 242 SFTGSTEVGRKImqAAATSNLKQVSlELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGI--YDEFV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 789 EQLLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTR-LAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTE 866
Cdd:PLN02766 320 KKLVEKAKDWVVGDPFDPRARQGPQVDKQQfEKILSYIEHgKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDE 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899179363 867 YFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPFGGWKRSVVG 943
Cdd:PLN02766 400 IFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFG 474
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
567-940 |
7.24e-26 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 113.07 E-value: 7.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQS-DPEVSEVVDFAHYYAEqslGLERLDG----------ARFV--PARVTL 633
Cdd:PRK09847 86 VLNKLADLMEAHAEELALLETLDTGKPIRHSlRDDIPGAARAIRWYAE---AIDKVYGevattsshelAMIVrePVGVIA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVIL 713
Cdd:PRK09847 163 AIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAF 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 714 TGgyetaelfrSFRPGLTLLA------------ETSGKNA-IVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGA 780
Cdd:PRK09847 243 TG---------STRTGKQLLKdagdsnmkrvwlEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEES 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 781 VARSrrFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLeprqLDEEGRVW----SPGIKTGV 856
Cdd:PRK09847 314 IADE--FLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLL----LDGRNAGLaaaiGPTIFVDV 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 857 APGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVqrQPFGG 936
Cdd:PRK09847 388 DPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGG 465
|
....
gi 1899179363 937 WKRS 940
Cdd:PRK09847 466 YKQS 469
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
567-943 |
1.35e-25 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 112.59 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQS-DPEVSEVVDFAHYYAEQSLGLERL----DGARFV-----PARVTLVVP 636
Cdd:PLN02466 124 ILLRFADLLEKHNDELAALETWDNGKPYEQSaKAELPMFARLFRYYAGWADKIHGLtvpaDGPHHVqtlhePIGVAGQII 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:PLN02466 204 PWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAELF-----RSFRPGLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlailvgavarsRRF-HEQ 790
Cdd:PLN02466 284 TDTGKIVlelaaKSNLKPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGS-----------RTFvHER 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 791 LLD------AVRSMP--VGEAWDPSSRMGPLIapaDGKLLDALTR-----LAPGESWLLEPRQLDEEGRVWSPGIKTGVA 857
Cdd:PLN02466 351 VYDefvekaKARALKrvVGDPFKKGVEQGPQI---DSEQFEKILRyiksgVESGATLECGGDRFGSKGYYIQPTVFSNVQ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 858 PGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTT--GAIvqrqPFG 935
Cdd:PLN02466 428 DDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVfdAAI----PFG 503
|
....*...
gi 1899179363 936 GWKRSVVG 943
Cdd:PLN02466 504 GYKMSGIG 511
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
568-944 |
1.18e-24 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 109.46 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 568 LHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAEQslGLERLDGARF-------------------VP 628
Cdd:PLN00412 81 LHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEE--GVRILGEGKFlvsdsfpgnernkycltskIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 629 ARVTLVVPPWNFP--LAIpggSTLA-ALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIAD 705
Cdd:PLN00412 159 LGVVLAIPPFNYPvnLAV---SKIApALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMH 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 706 ERVDQVILTGGyETAeLFRSFRPGLT-LLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVArs 784
Cdd:PLN00412 236 PGVNCISFTGG-DTG-IAISKKAGMVpLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVA-- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 785 RRFHEQLLDAVRSMPVGEAWDpSSRMGPLIAPADGKLLDALTR--LAPGESWLLEPRQldEEGRVWsPGIKTGVAPGSEF 862
Cdd:PLN00412 312 DALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMdaKEKGATFCQEWKR--EGNLIW-PLLLDNVRPDMRI 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 863 HRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVN----RGTtgaivQRQPFGGWK 938
Cdd:PLN00412 388 AWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINsapaRGP-----DHFPFQGLK 462
|
....*.
gi 1899179363 939 RSVVGA 944
Cdd:PLN00412 463 DSGIGS 468
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
534-943 |
1.62e-24 |
|
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: 108.70 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 534 SRIPDA--AGVDRVLATAAAASGSWAARGAAERAAILHRAGELLEARRGELVEIMAAEAGKTVDQSDP-EVSEVVDFAHY 610
Cdd:cd07117 30 SEITDAtdADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 611 YAEQSLGLE---------RLDGARFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTEtLWEA 681
Cdd:cd07117 110 FAGVIRAEEgsanmidedTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAK-IIQD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 682 GVPREALQFVVLGDSSLGETLIADERVDQVILTG----GYETAELFRSFRPGLTLlaETSGKNAIVVTPSADLDLAVRDV 757
Cdd:cd07117 189 VLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGstevGRDVAIAAAKKLIPATL--ELGGKSANIIFDDANWDKALEGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 758 AYSAFGHAGQKCSAASlAILVGAvARSRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLA--PGESWL 835
Cdd:cd07117 267 QLGILFNQGQVCCAGS-RIFVQE-GIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAkeEGAKIL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 836 LEPRQLDEEGRV----WSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWID 911
Cdd:cd07117 345 TGGHRLTENGLDkgffIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVAR 424
|
410 420 430
....*....|....*....|....*....|..
gi 1899179363 912 GVEAGNLYVNrgTTGAIVQRQPFGGWKRSVVG 943
Cdd:cd07117 425 AVETGRVWVN--TYNQIPAGAPFGGYKKSGIG 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
628-943 |
1.95e-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: 108.74 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 628 PARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADER 707
Cdd:cd07140 147 PIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 708 VDQVILTGGYET-AELFRSfrPGLTLLAETS----GKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAAslailvGAVA 782
Cdd:cd07140 227 VRKLGFTGSTPIgKHIMKS--CAVSNLKKVSlelgGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAA------GRLF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 783 RSRRFHEQ----LLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTR-LAPGESWLLEPRQLDEEGRVWSPGIKTGV 856
Cdd:cd07140 299 VEESIHDEfvrrVVEEVKKMKIGDPLDRSTDHGPQNHKAHlDKLVEYCERgVKEGATLVYGGKQVDRPGFFFEPTVFTDV 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 857 APGSEFHRTEYFGPVLGI--MHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPF 934
Cdd:cd07140 379 EDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDVAAPF 456
|
....*....
gi 1899179363 935 GGWKRSVVG 943
Cdd:cd07140 457 GGFKQSGFG 465
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
625-949 |
2.38e-24 |
|
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: 107.69 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 625 RFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTEtLWEAGVPREALQfVVLGDssLGET-LI 703
Cdd:cd07135 105 RKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE-LVPKYLDPDAFQ-VVQGG--VPETtAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 704 ADERVDQVILTGG-------YETAElfRSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAI 776
Cdd:cd07135 181 LEQKFDKIFYTGSgrvgriiAEAAA--KHLTP-VTL--ELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 777 LVGAVARSrrFHEQLLDAVRSMPVGEAwDPSSRMGPLIAPADGKLLDALTRLAPGEswLLEPRQLDEEGRVWSPGIKTGV 856
Cdd:cd07135 256 VDPSVYDE--FVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTTKGK--VVIGGEMDEATRFIPPTIVSDV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 857 APGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGG 936
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGG 410
|
330
....*....|...
gi 1899179363 937 WKRSvvGAGAKAG 949
Cdd:cd07135 411 VGDS--GYGAYHG 421
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
637-943 |
6.74e-24 |
|
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: 106.66 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAgVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd07559 145 PWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAELFRSFR-----PgLTLlaETSGKNAIVVTPSA-DLDLAVRDVAYSAF-GHA---GQKCSAASLAIlvgaVARS-- 784
Cdd:cd07559 224 TTVGRLIMQYAaenliP-VTL--ELGGKSPNIFFDDAmDADDDFDDKAEEGQlGFAfnqGEVCTCPSRAL----VQESiy 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 785 RRFHEQLLDAVRSMPVGEAWDPSSRMGpliAPADGKLLDALTR------------LAPGESWLLEPrqlDEEGRVWSPGI 852
Cdd:cd07559 297 DEFIERAVERFEAIKVGNPLDPETMMG---AQVSKDQLEKILSyvdigkeegaevLTGGERLTLGG---LDKGYFYEPTL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 853 KTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQ 932
Cdd:cd07559 371 IKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQYPAHA 448
|
330
....*....|.
gi 1899179363 933 PFGGWKRSVVG 943
Cdd:cd07559 449 PFGGYKKSGIG 459
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
568-936 |
1.22e-23 |
|
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: 105.30 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 568 LHRAGELLEARRGELVEIMAAEAGKtvdqsDPEVSEVVDFAHYYAEQSLGLERLDG----------ARFVPAR------- 630
Cdd:cd07087 26 LKALKRMLTENEEEIAAALYADLGK-----PPAEAYLTEIAVVLGEIDHALKHLKKwmkprrvsvpLLLQPAKayvipep 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 631 --VTLVVPPWNFPLAIpggsTLA----ALASGSSVVFKPARRTARTAAVLTETLwEAGVPREALQfVVLGDSSLGETLIA 704
Cdd:cd07087 101 lgVVLIIGPWNYPLQL----ALApligAIAAGNTVVLKPSELAPATSALLAKLI-PKYFDPEAVA-VVEGGVEVATALLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 705 dERVDQVILTGGYETAELF-----RSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVG 779
Cdd:cd07087 175 -EPFDHIFFTGSPAVGKIVmeaaaKHLTP-VTL--ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 780 AVArsRRFHEQLLDAVRSMpVGEAWDPSSRMGPLIapaDGKLLDALTRLAPGESwLLEPRQLDEEGRVWSPGIKTGVAPG 859
Cdd:cd07087 251 SIK--DELIEELKKAIKEF-YGEDPKESPDYGRII---NERHFDRLASLLDDGK-VVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899179363 860 SEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGG 936
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
625-944 |
3.17e-21 |
|
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: 98.07 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 625 RFVPARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREAlqFVVLGDSSLGETLIa 704
Cdd:cd07134 97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFEGDAEVAQALL- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 705 DERVDQVILTGG--------YETAELFRSfrpgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAI 776
Cdd:cd07134 174 ELPFDHIFFTGSpavgkivmAAAAKHLAS----VTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD-YV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 777 LVGAvARSRRFHEQLLDAVRSMPVGEAWDP-SSRMGPLIAPAD-----GKLLDALTRLAPgeswLLEPRQLDEEGRVWSP 850
Cdd:cd07134 247 FVHE-SVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHfdrlkGLLDDAVAKGAK----VEFGGQFDAAQRYIAP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 851 GIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgttGAIVQ 930
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN----DVVLH 397
|
330
....*....|....*...
gi 1899179363 931 ----RQPFGGWKRSVVGA 944
Cdd:cd07134 398 flnpNLPFGGVNNSGIGS 415
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
628-944 |
4.86e-19 |
|
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: 91.51 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 628 PARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLweagvPR----EALQFVVLGDSSLGETLi 703
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-----PKyldkECYPVVLGGVEETTELL- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 704 aDERVDQVILTGGYETAELFRS----FRPGLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLaILVg 779
Cdd:cd07132 174 -KQRFDYIFYTGSTSVGKIVMQaaakHLTPVTL--ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDY-VLC- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 780 avarSRRFHEQLLDAVRSmpVGEAW---DP--SSRMGPLIAPADGKLLDAL---TRLAPGESWlleprqlDEEGRVWSPG 851
Cdd:cd07132 249 ----TPEVQEKFVEALKK--TLKEFygeDPkeSPDYGRIINDRHFQRLKKLlsgGKVAIGGQT-------DEKERYIAPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 852 IKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQR 931
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDS 395
|
330
....*....|...
gi 1899179363 932 QPFGGWKRSVVGA 944
Cdd:cd07132 396 LPFGGVGNSGMGA 408
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
628-949 |
5.92e-19 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 91.63 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 628 PARVTLVVPPWNFPL---AIPggsTLAALASGSSVVFKPARRTARTAAVLTEtLWEAGVPREALQfVVLGDSSLgETLIA 704
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLnltLIP---LAGAIAAGNTVVLKPSELSPHTSKLMAK-LLTKYLDPSYVR-VIEGGVEV-TTELL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 705 DERVDQVILTGGYETAELF-----RSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVG 779
Cdd:PTZ00381 183 KEPFDHIFFTGSPRVGKLVmqaaaENLTP-CTL--ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 780 AVArsRRFHEQLLDAVRSMpVGEawDPS--------------SRMGPLIAPADGKLLDAltrlapGEswlleprqLDEEG 845
Cdd:PTZ00381 260 SIK--DKFIEALKEAIKEF-FGE--DPKksedysrivnefhtKRLAELIKDHGGKVVYG------GE--------VDIEN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 846 RVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTT 925
Cdd:PTZ00381 321 KYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVF 400
|
330 340
....*....|....*....|....*
gi 1899179363 926 GAIVQRQPFGGWKRSVVGA-GAKAG 949
Cdd:PTZ00381 401 HLLNPNLPFGGVGNSGMGAyHGKYG 425
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
567-943 |
8.00e-19 |
|
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: 90.97 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTV-DQSDPEVSEVVDFAHYYA----EQSLGLERLDGARFV-----PARVTLVVP 636
Cdd:cd07116 65 ILNKIADRMEANLEMLAVAETWDNGKPVrETLAADIPLAIDHFRYFAgcirAQEGSISEIDENTVAyhfhePLGVVGQII 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 637 PWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAgVPREALQFVVLGDSSLGETLIADERVDQVILTGG 716
Cdd:cd07116 145 PWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 717 YETAELFRSFRPG----LTLlaETSGKNAIVVTPS------ADLDLAVRDVAYSAFgHAGQKCSAASLAILVGAVarSRR 786
Cdd:cd07116 224 TTTGRLIMQYASEniipVTL--ELGGKSPNIFFADvmdaddAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESI--YDR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 787 FHEQLLDAVRSMPVGEAWDPSSRMGpliAPADGKLLDALTR------------LAPGESWLLEprQLDEEGRVWSPGIKT 854
Cdd:cd07116 299 FMERALERVKAIKQGNPLDTETMIG---AQASLEQLEKILSyidigkeegaevLTGGERNELG--GLLGGGYYVPTTFKG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 855 GvaPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgTTGAIVQRQPF 934
Cdd:cd07116 374 G--NKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAF 449
|
....*....
gi 1899179363 935 GGWKRSVVG 943
Cdd:cd07116 450 GGYKQSGIG 458
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
573-951 |
1.80e-18 |
|
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: 89.60 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 573 ELLEARRGELVEIMAAEAGKTVDQS---------DPEVSEVVDFAHYYAE--QSLGLERLDGARF--VPARVTLVVPPWN 639
Cdd:cd07084 32 QRLAAKSYDIAAGAVLVTGKGWMFAenicgdqvqLRARAFVIYSYRIPHEpgNHLGQGLKQQSHGyrWPYGPVLVIGAFN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 640 FPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYET 719
Cdd:cd07084 112 FPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 720 AELFRSFRPGLTLLAETSGKNAIVVTPSAD-LDLAVRDVAYSAFGHAGQKCSAASlAILVGAVARSRRFHEQLLDAVRSM 798
Cdd:cd07084 192 AEKLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQS-MLFVPENWSKTPLVEKLKALLARR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 799 PVGeawdpSSRMGPLIAPadgkllDALTRLAPGESWLLEPRQLD--EEGRVWSPGIKTGVAPGSEF------------HR 864
Cdd:cd07084 271 KLE-----DLLLGPVQTF------TTLAMIAHMENLLGSVLLFSgkELKNHSIPSIYGACVASALFvpideilktyelVT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 865 TEYFGPVLGIM-----HAATLDEAIELQNAvdyGLTAGLHSLDADEVARWIDGVE-AGNLY-VNRGTTGAIVQRQPFGGW 937
Cdd:cd07084 340 EEIFGPFAIVVeykkdQLALVLELLERMHG---SLTAAIYSNDPIFLQELIGNLWvAGRTYaILRGRTGVAPNQNHGGGP 416
|
410
....*....|....
gi 1899179363 938 KRSvvGAGAKAGGP 951
Cdd:cd07084 417 AAD--PRGAGIGGP 428
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
628-944 |
1.58e-15 |
|
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: 80.53 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 628 PARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLwEAGVPREALQfVVLGDSSLGETLIaDER 707
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIK-VIEGGVPETTALL-EQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 708 VDQVILTGGYETAELF-----RSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFG-HAGQKCsaaslaILVGAV 781
Cdd:cd07137 178 WDKIFFTGSPRVGRIImaaaaKHLTP-VTL--ELGGKCPVIVDSTVDLKVAVRRIAGGKWGcNNGQAC------IAPDYV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 782 ARSRRFHEQLLDAVRSMP---VGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLEPRQLDEEGRVWSPGIKTGVAP 858
Cdd:cd07137 249 LVEESFAPTLIDALKNTLekfFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 859 GSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWK 938
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVG 408
|
....*.
gi 1899179363 939 RSVVGA 944
Cdd:cd07137 409 ESGFGA 414
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
631-889 |
7.47e-15 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 78.31 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 631 VTLVVPPWNFP--LAIpggSTL-AALASGSSVVFKPARRTARTAAVLTETLWEAgVPREALQfVVLGDSSLGETLIaDER 707
Cdd:cd07136 103 VVLIIAPWNYPfqLAL---APLiGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVA-VVEGGVEENQELL-DQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 708 VDQVILTGG-------YETAElfRSFRPgLTLlaETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLaILVGA 780
Cdd:cd07136 177 FDYIFFTGSvrvgkivMEAAA--KHLTP-VTL--ELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDY-VLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 781 VARSrRFHEQLLDAVRSMpVGEAWDPSSRMGPLIAPadgKLLDALTRLAPGESwLLEPRQLDEEGRVWSPGIKTGVAPGS 860
Cdd:cd07136 251 SVKE-KFIKELKEEIKKF-YGEDPLESPDYGRIINE---KHFDRLAGLLDNGK-IVFGGNTDRETLYIEPTILDNVTWDD 324
|
250 260
....*....|....*....|....*....
gi 1899179363 861 EFHRTEYFGPVLGIMHAATLDEAIELQNA 889
Cdd:cd07136 325 PVMQEEIFGPILPVLTYDTLDEAIEIIKS 353
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
623-944 |
4.37e-13 |
|
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: 72.90 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 623 GARFVPARVTL---------VVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALqfVVL 693
Cdd:cd07133 87 GLLFLPAKAEVeyqplgvvgIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA--VVT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 694 GD-------SSLgetliadeRVDQVILTGGYETAEL-FRSFRPGL---TLlaETSGKNAIVVTPSADLDLAVRDVAYSAF 762
Cdd:cd07133 165 GGadvaaafSSL--------PFDHLLFTGSTAVGRHvMRAAAENLtpvTL--ELGGKSPAIIAPDADLAKAAERIAFGKL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 763 GHAGQKCSAASLAILvgavarsrrfHEQLLDAVrsmpVGEAWDPSSRMGP-LIAPAD--------------GKLLDALTR 827
Cdd:cd07133 235 LNAGQTCVAPDYVLV----------PEDKLEEF----VAAAKAAVAKMYPtLADNPDytsiinerhyarlqGLLEDARAK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 828 LAPGESwLLEPRQLDEEGRVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVA 907
Cdd:cd07133 301 GARVIE-LNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQD 379
|
330 340 350
....*....|....*....|....*....|....*..
gi 1899179363 908 RWIDGVEAGNLYVNRGTTGAIVQRQPFGGwkrsvVGA 944
Cdd:cd07133 380 RVLRRTHSGGVTINDTLLHVAQDDLPFGG-----VGA 411
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
567-913 |
2.26e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 70.89 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 567 ILHRAGELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHYYAE--QSLGLERL--DGAR--------------FVP 628
Cdd:PRK11903 68 LLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKlgAALGDARLlrDGEAvqlgkdpafqgqhvLVP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 629 AR-VTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGV-PREALQFVVlgdSSLGETLIADE 706
Cdd:PRK11903 148 TRgVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVC---GSSAGLLDHLQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 707 RVDQVILTGGYETAELFRS----FRPGLTLLAETSGKNAIVVTP-----SADLDLAVRDVAYSAFGHAGQKCSAASlAIL 777
Cdd:PRK11903 225 PFDVVSFTGSAETAAVLRShpavVQRSVRVNVEADSLNSALLGPdaapgSEAFDLFVKEVVREMTVKSGQKCTAIR-RIF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 778 VGAvARSRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTRLAPGESWLLEPRQLDEEGRvwSPGIKTGV 856
Cdd:PRK11903 304 VPE-ALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQlAAVRAGLAALRAQAEVLFDGGGFALVDA--DPAVAACV 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899179363 857 AP----------GSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGV 913
Cdd:PRK11903 381 GPtllgasdpdaATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALEL 447
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
652-921 |
1.57e-11 |
|
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: 68.07 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 652 ALASGSSVVFKPARRTARTAAVLTETLWEAGV-PREALQFVVLGDSSLGETLiaDERvDQVILTGGYETAELFRS----F 726
Cdd:cd07128 168 ALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHL--GEQ-DVVAFTGSAATAAKLRAhpniV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 727 RPGLTLLAETSGKNAIVVTPSA-----DLDLAVRDVAYSAFGHAGQKCSAASLAI----LVGAVArsrrfhEQLLDAVRS 797
Cdd:cd07128 245 ARSIRFNAEADSLNAAILGPDAtpgtpEFDLFVKEVAREMTVKAGQKCTAIRRAFvpeaRVDAVI------EALKARLAK 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 798 MPVGEAWDPSSRMGPLI--------APADGKLLDALTRLAPGESWLLEPRQLDEEGRVWSPGIKTGVAP--GSEFHRTEY 867
Cdd:cd07128 319 VVVGDPRLEGVRMGPLVsreqredvRAAVATLLAEAEVVFGGPDRFEVVGADAEKGAFFPPTLLLCDDPdaATAVHDVEA 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1899179363 868 FGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEA--GNLYVN 921
Cdd:cd07128 399 FGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVL 454
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
577-801 |
4.05e-11 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 66.48 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 577 ARRGELVEIMAAEAGKTVDQSDPEVSEVVDFAHY-YAEQSLGLERLDGARF------VPARVTLVVPPWNFPLAIPGgST 649
Cdd:cd07077 42 SERGAYIRSLIANWIAMMGCSESKLYKNIDTERGiTASVGHIQDVLLPDNGetyvraFPIGVTMHILPSTNPLSGIT-SA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 650 LAALASGSSVVFKPARR---TARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVDQVILTGGYETAELFRSF 726
Cdd:cd07077 121 LRGIATRNQCIFRPHPSapfTNRALALLFQAADAAHGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKH 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899179363 727 RPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFgHAGQKCSAASLAILVGAVARS--RRFHEQLLDAVRSMPVG 801
Cdd:cd07077 201 SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASEQNLYVVDDVLDPlyEEFKLKLVVEGLKVPQE 276
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
572-926 |
1.76e-10 |
|
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: 64.48 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 572 GELLEARRGELVEIMAAEAGKTVDQSDPEVSEVVD----FAHYYAEQSLGLERLDGA--------------RFVPARVTL 633
Cdd:cd07129 31 ADEIEALGDELVARAHAETGLPEARLQGELGRTTGqlrlFADLVREGSWLDARIDPAdpdrqplprpdlrrMLVPLGPVA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNFPLA--IPGGSTLAALASGSSVVFK--PA--RRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADER 707
Cdd:cd07129 111 VFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAhpGTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 708 VDQVILTGgyetaelfrSFRPGLTLL-------------AETSGKNAIVVTPSAdldLAVR------DVAYSAFGHAGQK 768
Cdd:cd07129 191 IKAVGFTG---------SRRGGRALFdaaaarpepipfyAELGSVNPVFILPGA---LAERgeaiaqGFVGSLTLGAGQF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 769 CSAASLAILVgAVARSRRFHEQLLDAVRsmpvgeAWDPSSRMGPLIAPAdgkLLDALTRLA--PGESWLLEPRQLDEEGR 846
Cdd:cd07129 259 CTNPGLVLVP-AGPAGDAFIAALAEALA------AAPAQTMLTPGIAEA---YRQGVEALAaaPGVRVLAGGAAAEGGNQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 847 VwSPGIktGVAPGSEFH-----RTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDAD--EVARWIDGVE--AGN 917
Cdd:cd07129 329 A-APTL--FKVDAAAFLadpalQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDDlaLARELLPVLErkAGR 405
|
....*....
gi 1899179363 918 LYVNRGTTG 926
Cdd:cd07129 406 LLFNGWPTG 414
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
634-928 |
4.38e-10 |
|
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: 63.28 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 634 VVPPWNfPLAIPGGSTLAALASGSSVVFKPARR----TARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADERVD 709
Cdd:cd07122 102 LIPSTN-PTSTAIFKALIALKTRNAIIFSPHPRakkcSIEAAKIMREAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 710 QVILTGGyetaelfrsfrPGLTLLAETSGKNAIVVTP---------SADLDLAVRDVAYS-AFGHaGQKCSAASLAILVG 779
Cdd:cd07122 181 LILATGG-----------PGMVKAAYSSGKPAIGVGPgnvpayideTADIKRAVKDIILSkTFDN-GTICASEQSVIVDD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 780 AVArsrrfhEQLLDAVRS-----MPVGEAwdpsSRMGPLIAPADGKlldaLTRLAPGESwllePRQLDEEGrvwspGIK- 853
Cdd:cd07122 249 EIY------DEVRAELKRrgayfLNEEEK----EKLEKALFDDGGT----LNPDIVGKS----AQKIAELA-----GIEv 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 854 -----------TGVAPGSEFHRtEYFGPVLGIMHAATLDEAIELQNA-VDY---GLTAGLHSLDADEVARWIDGVEAGNL 918
Cdd:cd07122 306 pedtkvlvaeeTGVGPEEPLSR-EKLSPVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDEEVIEEFALRMPVSRI 384
|
330
....*....|.
gi 1899179363 919 YVNR-GTTGAI 928
Cdd:cd07122 385 LVNTpSSLGGI 395
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
628-944 |
8.27e-10 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 62.76 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 628 PARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLwEAGVPREALQFVvlgDSSLGET-LIADE 706
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVV---EGAVTETtALLEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 707 RVDQVILTGGYETAE-LFRSFRPGLT-LLAETSGKNAIVVTPSADLDLAVRDVAYSAFG-HAGQKCSAASLailvgaVAR 783
Cdd:PLN02174 188 KWDKIFYTGSSKIGRvIMAAAAKHLTpVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDY------ILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 784 SRRFHEQLLDAVR---SMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGS 860
Cdd:PLN02174 262 TKEYAPKVIDAMKkelETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPLDS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 861 EFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRS 940
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGES 421
|
....
gi 1899179363 941 VVGA 944
Cdd:PLN02174 422 GMGA 425
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
52-573 |
4.33e-09 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 61.04 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 52 LPVDPSARRLAGLLRDPDGLAFAVGFVDGVIRPEDPRVAARALTRLSRRPPRFLAWPLRAALRVGGMVAPILPGVVVPVA 131
Cdd:COG3321 863 LPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAAL 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 132 RAVLRRMVAHLVIDADDPRLGRALRRIRDRGARPNVNLLGEAVLGAREAARRLEGTRRLLARDDVDYVSIKVSATVAPHS 211
Cdd:COG3321 943 LALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALL 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 212 PWAFDEAVDDIVQALTPLYADAAAASPPKFVNLDMEEYKDLDLTIAVFQRILDGPELRGLEAGIVLQAYLPDALGAYLRL 291
Cdd:COG3321 1023 ALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAAL 1102
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 292 RDWARERRAAGGAGIKVRLVKGANLPMERVDASLHDWPLATWHTKQETDTNYKRVLDVALRPENTAHVRLGVAGHNLFDL 371
Cdd:COG3321 1103 AAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALA 1182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 372 AYARHLAAERGVADAMEIEMLLGMAPAQAEAVRRDTGGLLLYTPVVAASDFDAAIAYLIRRLEEGAASENFMSAVFELSS 451
Cdd:COG3321 1183 AALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAAL 1262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 452 SEQLFARERDRFLASLAEVDDTVPAPHRVQDRTLPPAPAPGTGEGFHNAPDTDPAVAANRAWARAALERSRTTRLGEETV 531
Cdd:COG3321 1263 ALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALA 1342
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1899179363 532 AASRIPDAAGVDRVLATAAAASGSWAARGAAERAAILHRAGE 573
Cdd:COG3321 1343 LAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
627-928 |
5.46e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 57.10 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 627 VPARVTLVV-----PPWNfplAIPGgsTLAALASGSSVVFKPARRT----ARTAAVLTETLWEAGV-PREALQFVVLGDS 696
Cdd:cd07127 192 VPRGVALVIgcstfPTWN---GYPG--LFASLATGNPVIVKPHPAAilplAITVQVAREVLAEAGFdPNLVTLAADTPEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 697 SLGETLIADERVDQVILTGGYETAELFRSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASlAI 776
Cdd:cd07127 267 PIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQ-NI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 777 LVGA----VARSRRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLEPRQLD----EEGRVW 848
Cdd:cd07127 346 YVPRdgiqTDDGRKSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAhpefPDARVR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 849 SPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIEL--QNAVDYG-LTAGLHSLDADEVARWIDGVEAGNLYVNRGTT 925
Cdd:cd07127 426 TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELarESVREHGaMTVGVYSTDPEVVERVQEAALDAGVALSINLT 505
|
...
gi 1899179363 926 GAI 928
Cdd:cd07127 506 GGV 508
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
628-1150 |
5.81e-08 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 57.57 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 628 PARVTLVVPPW---NFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIA 704
Cdd:COG3321 858 RRRVPLPTYPFqreDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAA 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 705 DERVDQVILTGGYETAELFRSFRPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARS 784
Cdd:COG3321 938 AAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAA 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 785 RRFHEQLLDAVRSMPVGEAWDPSSRMGPLIAPADGKLLDALTRLAPGESWLLEPRQLDEEGRVWSPGIKTGVAPGSEFHR 864
Cdd:COG3321 1018 AAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 865 TEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGL-HSLDADEVARWIDGVEAGNLYVNRGTTGAIVQRQPFGGWKRSVVG 943
Cdd:COG3321 1098 ALAALAAALLLLALLAALALAAAAAALLALAALLaAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 944 AGAKAGGPNYLLGLGRVEPVAATVEPAAVDPGAERLIAVFGARGDEARRMLLRAAASDRRAWETEFGVVRDVTALAAERN 1023
Cdd:COG3321 1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 1024 AFRYRALPVVVRAEAAADPVELARVVLAGLRAGAALTLSTDAELAPADLDALREAGVGIRSESAEEWLRSASALRDARIR 1103
Cdd:COG3321 1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1899179363 1104 LVGGSGAELLTALGGRPDIAVYDGAVTESGRVELLAFLREQAVSITA 1150
Cdd:COG3321 1338 AAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
631-960 |
1.05e-07 |
|
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: 55.73 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 631 VTLVVPPWNfPLAIPGGSTLAALASGSSVVFKPARR----TARTAAVLTETLWEAGVPREALQFVVLGDSSLGETLIADE 706
Cdd:cd07081 99 VASITPSTN-PTSTVIFKSLISLKTRNSIIFSPHPRakkvTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 707 RVDQVILTGGYETAELFRSfrPGLTLLAETSGKNAIVVTPSADLDLAVRDVAYSAFGHAGQKCSAASLAILVGAVARS-- 784
Cdd:cd07081 178 GIGLLLATGGPAVVKAAYS--SGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEvm 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 785 RRFHEQ---LLDAVRSMPVGEAWDPSSRMGPLIAPAD-GKLLDALTRLAPGESWLL--EPRQLDEEgrvwspgiktgvap 858
Cdd:cd07081 256 RLFEGQgayKLTAEELQQVQPVILKNGDVNRDIVGQDaYKIAAAAGLKVPQETRILigEVTSLAEH-------------- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 859 gsEFHRTEYFGPVLGIMHAATLDEAIELQNAV----DYGLTAGLHSLDA---DEVARWIDGVEAGNLYVNRGTT-GAIVQ 930
Cdd:cd07081 322 --EPFAHEKLSPVLAMYRAANFADADAKALALklegGCGHTSAMYSDNIkaiENMNQFANAMKTSRFVKNGPCSqGGLGD 399
|
330 340 350
....*....|....*....|....*....|....*..
gi 1899179363 931 RQPFGGWKRSVVGAGAKAG-------GPNYLLGLGRV 960
Cdd:cd07081 400 LYNFRGWPSMTLGCGTWGGnsvsenvGPKHLVNLKTV 436
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
628-943 |
1.01e-06 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 52.81 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 628 PARVTLVVPPWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETlweagVPR----EALQfVVLGDSSLGETLI 703
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAAN-----IPKyldsKAVK-VIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 704 aDERVDQVILTGGYETAELFRSFRPG-LTLLA-ETSGK-NAIV--VTPSADLDLAVRDVAYSAFGH-AGQKCSAASLaIL 777
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKhLTPVAlELGGKcPCIVdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDY-VL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 778 VgavarSRRFHEQLLDAVRSMP---VGEAWDPSSRMGPLIapaDGKLLDALTRLapgeswLLEPR---------QLDEEG 845
Cdd:PLN02203 260 V-----EERFAPILIELLKSTIkkfFGENPRESKSMARIL---NKKHFQRLSNL------LKDPRvaasivhggSIDEKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 846 RVWSPGIKTGVAPGSEFHRTEYFGPVLGIMHAATLDEAIELQNAVDYGLTAGLHSLDADEVARWIDGVEAGNLYVNrgtt 925
Cdd:PLN02203 326 LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFN---- 401
|
330 340
....*....|....*....|..
gi 1899179363 926 GAIVQRQ----PFGGWKRSVVG 943
Cdd:PLN02203 402 DAIIQYAcdslPFGGVGESGFG 423
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
278-435 |
3.35e-06 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 50.86 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 278 QAYLPDALgayLRLRDwARERRAAGGAGIKVRLVKGANLPMERVDASLHDWPLATWHTKQETDTNYKRVLDVALRPENTA 357
Cdd:PLN02681 274 QAYLKDAR---ERLRL-DLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 358 HVRLGVAGHNLFDLAYARHLAAERGVA---DAMEIEMLLGMAPAQAEAVRRDTGGLLLYTPVvaaSDFDAAIAYLIRRLE 434
Cdd:PLN02681 350 DGEVMLATHNVESGELAAAKMNELGLHkgdPRVQFAQLLGMSDNLSFGLGNAGFRVSKYLPY---GPVEEVIPYLLRRAE 426
|
.
gi 1899179363 435 E 435
Cdd:PLN02681 427 E 427
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
623-774 |
2.90e-04 |
|
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: 44.79 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 623 GARFVPARVTLVVPpWNFPLAIPGGSTLAALASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQFvVLGDSSLGETL 702
Cdd:cd07126 138 GYRWPYGPVAIITP-FNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDL-IHSDGPTMNKI 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899179363 703 IADERVDQVILTGGYETAELFRSFRPGLTLLaETSGKNAIVVTPS-ADLDLAVRDVAYSAFGHAGQKCSAASL 774
Cdd:cd07126 216 LLEANPRMTLFTGSSKVAERLALELHGKVKL-EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSI 287
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
653-761 |
2.05e-03 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 41.84 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899179363 653 LASGSSVVFKPARRTARTAAVLTETLWEAGVPREALQ--FVVLGDSSLGET--LIADERVDQVILTGGyetaelfrsfrP 728
Cdd:cd07121 122 LAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDnlVVTVEEPTIETTneLMAHPDINLLVVTGG-----------P 190
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1899179363 729 GLTLLAETSGKNAI---------VVTPSADLDLAVRDVAYSA 761
Cdd:cd07121 191 AVVKAALSSGKKAIgagagnppvVVDETADIEKAARDIVQGA 232
|
|
| |
