|
Name |
Accession |
Description |
Interval |
E-value |
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
1-1317 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 2782.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1 MATTTLGVKLDDPTRERLKAAATSIDRTPHWLIKQAIFNYLEKLEGGATLNELSGIPGKDSDDADDV--QADHAHQCFLE 78
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEAdtPAEEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 79 FAESILPQSVLRAAITSAYRRPEPEVVPMLLEQARLPAPMAEATQALAASIAEKLRNQKSAGGRAGIVQGLLQEFSLSSQ 158
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGRAGMVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 159 EGVALMCLAEALLRIPDKGTRDALIRDKISTGNWHPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAGLTSSLSRIIGKSG 238
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 239 EPMIRKGVDMAMRLMGEQFVTGETIAEALANATRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGI 318
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 319 YEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLSGWNGIG 398
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 399 FVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLAVPEAI 478
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 479 YPQFATHNAQTLAAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVSEGKLNRPCRVYAPVGTHETLLAYLVRRLLEN 558
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 559 GANTSFVNRIADHTISIQELVADPISSIEQMATQEGGFGLPHPRIPLPRDLYGSERANSSGIDMANEHRLASLSCALLAT 638
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLAS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 639 AHNDWKAAPMLGCASSNEAPAAVLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAE 718
Cdd:PRK11809 641 AHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQ 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 719 IQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVL 798
Cdd:PRK11809 721 MQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 799 AKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAQGRPIPL 878
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 879 IAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVI 958
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 959 DAEAKAGIEQHIQGMRDKGRTVYQMAIADIEECKRGTFVMPTLIELESFDELEREIFGPVLHVVRYKRKDIDQLIAQINA 1038
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQINA 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1039 SGYGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPNNAIEQSFA 1118
Cdd:PRK11809 1041 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAVTLA 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1119 KVDAITAPDTQAREALSKPLVALQGWATSQQlTALAELCSEFAAHSQSGITRLLNGPTGERNSYAILPREHVLCLAEVES 1198
Cdd:PRK11809 1121 RQDAEYPVDAQLRAALLAPLTALREWAAERE-PELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADTEQ 1199
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1199 DLLTQLAAVLAVGSSAVVPESDMAKALFARLPKEVQARITRVADWTRDEVIFDAVLHHGDSDQLRDVCQRVAKRAGAIVG 1278
Cdd:PRK11809 1200 DALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPIVS 1279
|
1290 1300 1310
....*....|....*....|....*....|....*....
gi 1403361070 1279 VQGLSQGETNIALERLVIERALSVNTAAAGGNASLMTIG 1317
Cdd:PRK11809 1280 VQGFARGETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
76-1317 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 2050.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 76 FLEFAESILPQSVLRAAITSAYRRPEPEVVPMLLEQARLPAPMAEATQALAASIAEKLRNQKSAGGragiVQGLLQEFSL 155
Cdd:PRK11905 2 FQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTG----VEALLQEYSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 156 SSQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWHPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAGLTSSLSRIIG 235
Cdd:PRK11905 78 SSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 236 KSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANATRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHG 315
Cdd:PRK11905 158 RLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 316 RGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLSGWN 395
Cdd:PRK11905 238 RGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 396 GIGFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLAVP 475
Cdd:PRK11905 318 GIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAAR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 476 EAIYPQFATHNAQTLAAIYHIAGQNYypgQYEFQCLHGMGEPLYEQVVGKvseGKLNRPCRVYAPVGTHETLLAYLVRRL 555
Cdd:PRK11905 398 DVIYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGK---EKLGRPCRIYAPVGTHETLLAYLVRRL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 556 LENGANTSFVNRIADHTISIQELVADPISSIEQMAtqeggfGLPHPRIPLPRDLYGSERANSSGIDMANEHRLASLSCAL 635
Cdd:PRK11905 472 LENGANSSFVNRIVDENVPVEELIADPVEKVAAMG------VAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEAL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 636 LATAHNDWKAAPMLGCASSNEAPAAVLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLM 715
Cdd:PRK11905 546 NAFAAKTWHAAPLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLM 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 716 EAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGN 795
Cdd:PRK11905 626 EAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGN 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 796 PVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqGRP 875
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GPP 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 876 IPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIG 955
Cdd:PRK11905 783 VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVG 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 956 PVIDAEAKAGIEQHIQGMRDKGRTVYQMAIADieECKRGTFVMPTLIELESFDELEREIFGPVLHVVRYKRKDIDQLIAQ 1035
Cdd:PRK11905 863 PVIDAEAQANIEAHIEAMRAAGRLVHQLPLPA--ETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDD 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1036 INASGYGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPNnaieq 1115
Cdd:PRK11905 941 INATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPT----- 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1116 sfakvdaiTAPDTQAREALSKPLVALQGWATSQQLTALAELCSEFAAHSQSGITRLLNGPTGERNSYAILPREHVLCLAE 1195
Cdd:PRK11905 1016 --------PIPPAHESVDTDAAARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVAD 1087
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1196 VESDLLTQLAAVLAVGSSAVVPESDMAKALFARLPKEVQARITRVADWtRDEVIFDAVLHHGDSDQLRDVCQRVAKRAGA 1275
Cdd:PRK11905 1088 TEEALLRQLAAALATGNVAVVAADSGLAAALADLPGLVAARIDWTQDW-EADDPFAGALLEGDAERARAVRQALAARPGA 1166
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|..
gi 1403361070 1276 IVGVQGlSQGETNIALERLVIERALSVNTAAAGGNASLMTIG 1317
Cdd:PRK11905 1167 IVPLIA-AEPTDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
77-1108 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1568.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 77 LEFAESILPQSVLRAAITSAYRRPEPEVVPMLLEQARLPAPMAEATQALAASIAEKLRNQKsagGRAGIVQGLLQEFSLS 156
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKK---KKLGGIDAFLQEYSLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 157 SQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWHPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAG--LTSSLSRII 234
Cdd:PRK11904 78 TEEGIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADgtPSGVLKRLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 235 GKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANATRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASH 314
Cdd:PRK11904 158 NRLGEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 315 GRGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLSGW 394
Cdd:PRK11904 238 GADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 395 NGIGFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLAV 474
Cdd:PRK11904 318 GGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 475 PEAIYPQFATHNAQTLAAIYHIAGQnyypGQYEFQCLHGMGEPLYEQVVgkvseGKLNRPCRVYAPVGTHETLLAYLVRR 554
Cdd:PRK11904 398 RGAIYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 555 LLENGANTSFVNRIADHTISIQELVADPISSIEQMATqeggfgLPHPRIPLPRDLYGSERANSSGIDMANEHRLASLSCA 634
Cdd:PRK11904 469 LLENGANSSFVHRLVDPDVPIEELVADPVEKLRSFET------LPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 635 LLATAHNDWKAAPMLGCASsneAPAAVLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADL 714
Cdd:PRK11904 543 IAAFLEKQWQAGPIINGEG---EARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 715 MEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARNDL------------TNDAH-RPLGPVVCISPWNFPLA 781
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFgapeklpgptgeSNELRlHGRGVFVCISPWNFPLA 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 782 IFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLL 861
Cdd:PRK11904 700 IFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARII 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 862 QRNIAGRldaQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAE 941
Cdd:PRK11904 780 NRTLAAR---DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAE 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 942 SRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQMAIADieECKRGTFVMPTLIELESFDELEREIFGPVLHV 1021
Cdd:PRK11904 857 LKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPA--GTENGHFVAPTAFEIDSISQLEREVFGPILHV 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1022 VRYKRKDIDQLIAQINASGYGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1101
Cdd:PRK11904 935 IRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYL 1014
|
....*..
gi 1403361070 1102 YRLLSTR 1108
Cdd:PRK11904 1015 LRFATEK 1021
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
80-1314 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1551.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 80 AESILPQSVLRAAITSAYRRPEPEVVPMLLEQARLPAPMAEATQALAASIAEKLRNQKSAGGRAGIVQGLLQEFSLSSQE 159
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 160 GVALMCLAEALLRIPDKGTRDALIRDKISTGNWHPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAGLTSS--LSRIIGKS 237
Cdd:COG4230 81 SEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLAsgLLRLLGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 238 GEPMIRKGVDMAMRLMGEQFVTGETIAEALANATRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRG 317
Cdd:COG4230 161 GRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 318 IYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLSGWNGI 397
Cdd:COG4230 241 GGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 398 GFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLAVPEA 477
Cdd:COG4230 321 GGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 478 IYPQFATHNAQTLAAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVgkvsEGKLNRPCRVYAPVGTHETLLAYLVRRLLE 557
Cdd:COG4230 401 AQPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVG----RGKLGRPCRIYAPVGSHEDLLAYLVRRLLE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 558 NGANTSFVNRIADHTISIQELVADPISSIEQMAtqeggfGLPHPRIPLPRDLYGSERANSSGIDMANEHRLASLSCALLA 637
Cdd:COG4230 477 NGANSSFVNRIADEDVPVEELIADPVEKARALG------GAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 638 TAHNDWKAAPMLGCASSNEAPAAVLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEA 717
Cdd:COG4230 551 AAEKQWQAAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEA 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 718 EIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARNDLTND-AHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:COG4230 631 HRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPtVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNT 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 797 VLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRldaQGRPI 876
Cdd:COG4230 711 VLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR---DGPIV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 877 PLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGP 956
Cdd:COG4230 788 PLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGP 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 957 VIDAEAKAGIEQHIQGMRDKGRTVYQMAIAdiEECKRGTFVMPTLIELESFDELEREIFGPVLHVVRYKRKDIDQLIAQI 1036
Cdd:COG4230 868 VIDAEARANLEAHIERMRAEGRLVHQLPLP--EECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAI 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1037 NASGYGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPnnaieqs 1116
Cdd:COG4230 946 NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERT------- 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1117 fakvdaitapdtqareaLSKPLVALQGWATsqqLTALAELCSEFAAHsqsgitRLLNGPTGERNSYAILPREHVLCLAEV 1196
Cdd:COG4230 1019 -----------------VTVNTTAAGGNAS---LLALGDWLASLLGA------LTLPGPTGERNTLTLRPRGRVLCLADS 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1197 ESDLLTQLAAVLAVGSSAVVPESdmakALFARLPKEVQARitrvadwtrdeviFDAVLHHGdsdQLRDVCQRVAKRAGAI 1276
Cdd:COG4230 1073 LEALLAQLAAALATGNRAVVAAD----LALAGLPAVLLPP-------------FDAVLFEG---RLRALRQALAARDGAI 1132
|
1210 1220 1230
....*....|....*....|....*....|....*...
gi 1403361070 1277 VGVQGLsqgetNIALERLVIEralsvntaaAGGNASLM 1314
Cdd:COG4230 1133 VPVIDA-----GYDLERLLEE---------AGGNASLM 1156
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
608-1109 |
0e+00 |
|
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: 720.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 608 DLYGSERANSSGIDMANEHRLASLSCALLATAHNDWKAAPMLGCASSNEAPAA-VLNPSDLRDVVGHVQEATVEDADNAI 686
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQpVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 687 QCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARNDLTNDAHRP 766
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 767 LGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRV 846
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 847 KGVMFTGSTEVARLLQRNIAGRLDAqgrPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQED 926
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 927 SADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQMAIADIEECKRGTFVMPTLIELES 1006
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFELDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1007 FDELEREIFGPVLHVVRYKRKDIDQLIAQINASGYGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGE 1086
Cdd:TIGR01238 398 IAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQ 477
|
490 500
....*....|....*....|...
gi 1403361070 1087 GLSGTGPKAGGPLYLYRLLSTRP 1109
Cdd:TIGR01238 478 GLSGTGPKAGGPHYLYRLTQVQY 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
112-1112 |
0e+00 |
|
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: 692.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 112 ARLPAPMAEATQALAASIAEKLRNQksaggRAGIVQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKIStgn 191
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAA-----PEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 192 whphlgNSPSLFVNAATWGLLLTgklvsthneagltsslsrIIGKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANAT 271
Cdd:COG0506 75 ------KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 272 RFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKAShgrgiYEGPGISIKLSALHPRYSRAQYERVMEELYPRL 351
Cdd:COG0506 131 KLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 352 LSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLSGWNGIGFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLV 431
Cdd:COG0506 206 RPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 432 KGAYWDSEIKRAQVEGLeGYPVYTRKVYTDVSYIACARKLLAVPEAIYPQFATHNAQTLAAIYHIAGQ-NYYPGQYEFQC 510
Cdd:COG0506 286 KGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 511 LHGMGEPLYEQVVgKVSEGKLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADHTISIQELVADPISSIEQMA 590
Cdd:COG0506 365 LYGMGEDLQRALA-AVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 591 tqeggfGLPHPRIPLPRDLYGSERANSSGIDMANEHRLASLSCALLATAHNDWKAAPML-GCASSNEAPAAVLNPSDLRD 669
Cdd:COG0506 444 ------PTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGaAAAAAAAAVAVVPAAAAAVV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 670 VVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLR 749
Cdd:COG0506 518 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAA 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 750 YYAVQARND-------LTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIP 822
Cdd:COG0506 598 AAAAAARAAappppppGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLL 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 823 EGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAQGRPIPLIAETGGQNAMIVDSSALTEQVVID 902
Cdd:COG0506 678 GGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVA 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 903 VVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQ 982
Cdd:COG0506 758 ASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLP 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 983 mAIADIEECKRGTFVMPTLIELESFDELEREIFGPVLHVVRYKRKDIDQLIAQINASGYGLTLGVHTRIDETIAKVVNNV 1062
Cdd:COG0506 838 -GGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGG 916
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1063 NAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPNNA 1112
Cdd:COG0506 917 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATA 966
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
625-1108 |
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: 662.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 625 EHRLASLSCALLATAHNDWKAAPML-GCASSNEAPAAVLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAE 703
Cdd:cd07125 13 EVPLEALADALKAFDEKEWEAIPIInGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 704 RAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARNDLT-----------NDAH-RPLGPVV 771
Cdd:cd07125 93 RAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 772 CISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMF 851
Cdd:cd07125 173 CISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 852 TGSTEVARLLQRNIAGRldaQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRV 931
Cdd:cd07125 253 TGSTETAKLINRALAER---DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 932 IEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQMAIADieecKRGTFVMPTLIELESFDELE 1011
Cdd:cd07125 330 IEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDD----GNGYFVAPGIIEIVGIFDLT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1012 REIFGPVLHVVRYKRKDIDQLIAQINASGYGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGT 1091
Cdd:cd07125 406 TEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGT 485
|
490
....*....|....*..
gi 1403361070 1092 GPKAGGPLYLYRLLSTR 1108
Cdd:cd07125 486 GPKAGGPNYLLRFGNEK 502
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
266-567 |
4.51e-154 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 465.04 E-value: 4.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 266 ALANATRFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVME 345
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 346 ELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLSGWNGIGFVIQAYQKRCPYVIDYVIDLARRSRHR 425
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 426 LMIRLVKGAYWDSEIKRAQvEGLEGYPVYTRKVYTDVSYIACARKLLAVPEAIYPQFATHNAQTLAAIYHIAGQ-NYYPG 504
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403361070 505 QYEFQCLHGMGEPLYEQVVGKvsegklNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNR 567
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAA------GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
662-1111 |
1.36e-141 |
|
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: 440.48 E-value: 1.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 662 LNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEV 741
Cdd:cd07083 37 VSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 742 REAVDFLRYYAVQARN-------------DLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07083 117 AEAIDFIRYYARAALRlrypavevvpypgEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAQGRPIPLIAETGGQNAM 888
Cdd:cd07083 197 GYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQ 968
Cdd:cd07083 277 IVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 969 HIQGMRDKGRTVYQMAIADIEeckrGTFVMPTLIELESFDE--LEREIFGPVLHVVRYKRKDIDQLIAQINASGYGLTLG 1046
Cdd:cd07083 357 YIEHGKNEGQLVLGGKRLEGE----GYFVAPTVVEEVPPKAriAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGG 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403361070 1047 VHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLS--TRPNN 1111
Cdd:cd07083 433 VYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEmkAVAER 499
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
661-1102 |
7.15e-125 |
|
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: 396.21 E-value: 7.15e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07124 50 SRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADAD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQA--------------RNDLTndaHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:cd07124 130 VAEAIDFLEYYAREMlrlrgfpvemvpgeDNRYV---YRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 807 LVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVA-RLLQRniAGRLD-AQGRPIPLIAETGG 884
Cdd:cd07124 207 VIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlRIYER--AAKVQpGQKWLKRVIAEMGG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07124 285 KNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARD 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 965 GIEQHIQGMRDKGRTVYQMAIadIEECKRGTFVMPTLIE-LESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINASGYG 1042
Cdd:cd07124 365 RIRRYIEIGKSEGRLLLGGEV--LELAAEGYFVQPTIFAdVPPDHRLAQeEIFGPVLAVIKA--KDFDEALEIANDTEYG 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1043 LTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1102
Cdd:cd07124 441 LTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLL 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
652-1097 |
2.64e-123 |
|
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: 391.03 E-value: 2.64e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 652 ASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAG 731
Cdd:COG1012 16 AAASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 732 KTYANAIAEVREAVDFLRYYAVQAR--------NDLTN-DA---HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:COG1012 95 KPLAEARGEVDRAADFLRYYAGEARrlygetipSDAPGtRAyvrREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 800 KPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLI 879
Cdd:COG1012 175 KPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVID 959
Cdd:COG1012 249 LELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLIS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 960 AEAKAGIEQHIQGMRDKGRTVyqMAIADIEECKRGTFVMPTLIE-----LESFDElerEIFGPVLHVVRYkrKDIDQLIA 1034
Cdd:COG1012 329 EAQLERVLAYIEDAVAEGAEL--LTGGRRPDGEGGYFVEPTVLAdvtpdMRIARE---EIFGPVLSVIPF--DDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403361070 1035 QINASGYGLTLGVHTRIDETIAKvvnnvnagnvyVNRNI-VGAV---------VGVQPFGGEGLSGTGPKAGG 1097
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARR-----------VARRLeAGMVwindgttgaVPQAPFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
653-1101 |
5.33e-118 |
|
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: 376.10 E-value: 5.33e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 653 SSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGK 732
Cdd:pfam00171 3 DSESETIEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 733 TYANAIAEVREAVDFLRYYAVQARND----LTNDA-------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKP 801
Cdd:pfam00171 82 PLAEARGEVDRAIDVLRYYAGLARRLdgetLPSDPgrlaytrREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 802 AEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAE 881
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAE 961
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 962 AKAGIEQHIQGMRDKGRTVyqmAIADIEECKRGTFVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQI 1036
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKL---LTGGEAGLDNGYFVEPTVLanvtpDMRIAQE---EIFGPVLSVIRF--KDEEEAIEIA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403361070 1037 NASGYGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVqPFGGEGLSGTGpKAGGPLYL 1101
Cdd:pfam00171 388 NDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGL 450
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
683-1108 |
2.47e-111 |
|
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: 356.90 E-value: 2.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 683 DNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQAR------ 756
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARrlhgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 757 ---NDLTNDA---HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLP 830
Cdd:cd07078 81 ipsPDPGELAivrREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 831 GRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNiagrldAQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDS 910
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRA------AAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 911 AGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVyqMAIADIEE 990
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKL--LCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 991 CKRGTFVMPTLIELESFDEL--EREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRiDETIAKvvnnvnagnVY 1068
Cdd:cd07078 313 GGKGYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTR-DLERAL---------RV 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1403361070 1069 VNRNIVGAV---------VGVQPFGGEGLSGTGpKAGGPLYLYRLLSTR 1108
Cdd:cd07078 381 AERLEAGTVwindysvgaEPSAPFGGVKQSGIG-REGGPYGLEEYTEPK 428
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
661-1102 |
2.03e-105 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 343.84 E-value: 2.03e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:PRK03137 54 SINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQA-----------RNDLTNDAH-RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:PRK03137 134 TAEAIDFLEYYARQMlkladgkpvesRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVA-RLLQRniAGRLDAQGRPIP-LIAETGGQN 886
Cdd:PRK03137 214 AAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYER--AAKVQPGQIWLKrVIAEMGGKD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSvDIGPVIDAEAKAGI 966
Cdd:PRK03137 292 AIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 967 EQHIQGMRDKGRTVYQMAIADieecKRGTFVMPTLI-ELESFDEL-EREIFGPVLHVVryKRKDIDQLIAQINASGYGLT 1044
Cdd:PRK03137 371 MSYIEIGKEEGRLVLGGEGDD----SKGYFIQPTIFaDVDPKARImQEEIFGPVVAFI--KAKDFDHALEIANNTEYGLT 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1403361070 1045 LGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1102
Cdd:PRK03137 445 GAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
662-1108 |
2.65e-102 |
|
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: 335.30 E-value: 2.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 662 LNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEV 741
Cdd:TIGR01237 51 INPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 742 REAVDFLRYYAVQ----ARNDLTND--------AHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:TIGR01237 131 AEAIDFMEYYARQmielAKGKPVNSregetnqyVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 810 AQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAQGRPIPLIAETGGQNAMI 889
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 890 VDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQH 969
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 970 IQGMRDKGRtvyqMAIADIEECKRGTFVMPTLielesFDELER-------EIFGPVLHVVRYkrKDIDQLIAQINASGYG 1042
Cdd:TIGR01237 371 IEIGKAEGR----LVSGGCGDDSKGYFIGPTI-----FADVDRkarlaqeEIFGPVVAFIRA--SDFDEALEIANNTEYG 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403361070 1043 LTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTR 1108
Cdd:TIGR01237 440 LTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAK 505
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
657-1098 |
2.88e-93 |
|
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: 308.79 E-value: 2.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 657 APAAVLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYAN 736
Cdd:cd07097 14 DGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 737 AIAEVREAVDFLRYYAVQA-----------RNDLTNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07097 94 ARGEVTRAGQIFRYYAGEAlrlsgetlpstRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 805 TPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRldaqGRPIPLiaETGG 884
Cdd:cd07097 174 TPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR----GARVQL--EMGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07097 248 KNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 965 GIEQHI-QGMRDKGRTVYQMAIadIEECKRGTFVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINA 1038
Cdd:cd07097 328 KDLRYIeIARSEGAKLVYGGER--LKRPDEGYYLAPALFagvtnDMRIARE---EIFGPVAAVIRV--RDYDEALAIAND 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1039 SGYGLTLGVHTRideTIAKvvnnvnagNVYVNRNIVGAVVGVQ----------PFGGEGLSGTGPKAGGP 1098
Cdd:cd07097 401 TEFGLSAGIVTT---SLKH--------ATHFKRRVEAGVVMVNlptagvdyhvPFGGRKGSSYGPREQGE 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
689-1108 |
1.95e-87 |
|
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: 288.74 E-value: 1.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 689 ALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQAR---------NDL 759
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADklggpelpsPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 760 TNDA---HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETV 836
Cdd:cd06534 83 GGEAyvrREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 837 GARLVGDDRVKGVMFTGSTEVARLLQRNiagrldAQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCS 916
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKA------AAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 917 ALRVLCLQEDSADRVIEMLKGamaesrmgnperLSVDIGPvidaeakagieqhiqgmrdkgrtvyQMAIADieeckrgtf 996
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVT------------VLVDVDP-------------------------DMPIAQ--------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 997 vmptlielesfdeleREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRiDETIAKVVNNVNAGNVYVNRNIVGA 1076
Cdd:cd06534 271 ---------------EEIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTR-DLNRALRVAERLRAGTVYINDSSIG 332
|
410 420 430
....*....|....*....|....*....|..
gi 1403361070 1077 VVGVQPFGGEGLSGTGpKAGGPLYLYRLLSTR 1108
Cdd:cd06534 333 VGPEAPFGGVKNSGIG-REGGPYGLEEYTRTK 363
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
661-1043 |
1.71e-86 |
|
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: 289.33 E-value: 1.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRdVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07103 1 VINPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQAR-------NDLTNDA-----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07103 80 VDYAASFLEWFAEEARriygrtiPSPAPGKrilviKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAM 888
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLClQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 968 QHIQGMRDKGRTVyqmAIADIEECKRGTFVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYG 1042
Cdd:cd07103 313 ALVEDAVAKGAKV---LTGGKRLGLGGYFYEPTVLtdvtdDMLIMNE---ETFGPVAPIIPF--DTEDEVIARANDTPYG 384
|
.
gi 1403361070 1043 L 1043
Cdd:cd07103 385 L 385
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
661-1096 |
1.37e-85 |
|
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: 287.54 E-value: 1.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRDVVGhVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07086 17 SRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDfLRYYAV-QAR--NDLTNDAHR----------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:cd07086 96 VQEMID-ICDYAVgLSRmlYGLTIPSERpghrlmeqwnPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 808 VAAQAVRLMLEA----GIPEGVLQLLPGRGEtVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqGRPIpliAETG 883
Cdd:cd07086 175 TAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRVL---LELG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAK 963
Cdd:cd07086 248 GNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 964 AGIEQHIQGMRDKGRTVyQMAIADIEECKRGTFVMPTLIELESfDELE---REIFGPVLHVVRYkrKDIDQLIAQINASG 1040
Cdd:cd07086 328 EKYLNAIEIAKSQGGTV-LTGGKRIDGGEPGNYVEPTIVTGVT-DDARivqEETFAPILYVIKF--DSLEEAIAINNDVP 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1403361070 1041 YGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNI--VGAVVGVqPFGGEGLSGTGPKAG 1096
Cdd:cd07086 404 QGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIptSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
662-1098 |
2.92e-80 |
|
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: 272.68 E-value: 2.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 662 LNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEV 741
Cdd:cd07131 19 RNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 742 REAVDFLRYYAVQAR--------NDLTN-DA---HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:cd07131 99 QEAIDMAQYAAGEGRrlfgetvpSELPNkDAmtrRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 810 AQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRnIAGRLdaqGRPIPLiaETGGQNAMI 889
Cdd:cd07131 179 LKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE-TCARP---NKRVAL--EMGGKNPII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 890 VDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQH 969
Cdd:cd07131 253 VMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 970 IQGMRDKGRTV-YQMAIADIEECKRGTFVMPTLIELESFDE--LEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLG 1046
Cdd:cd07131 333 NEIGKEEGATLlLGGERLTGGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEV--SSLEEAIEIANDTEYGLSSA 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1403361070 1047 VHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVqPFGGEGLSGTGPKAGGP 1098
Cdd:cd07131 411 IYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
661-1092 |
1.63e-77 |
|
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: 264.07 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07149 3 VISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQARNdLTN-----DAH------------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07149 82 VDRAIETLRLSAEEAKR-LAGetipfDASpggegrigftirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 804 QTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRnIAGRldaqgRPIPLiaETG 883
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIAR-KAGL-----KKVTL--ELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEA 962
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 963 KAGIEQHIQGMRDKGRTVYQMAIadieecKRGTFVMPTLieLESFDELER----EIFGPVLHVVRYkrKDIDQLIAQINA 1038
Cdd:cd07149 312 AERIEEWVEEAVEGGARLLTGGK------RDGAILEPTV--LTDVPPDMKvvceEVFAPVVSLNPF--DTLDEAIAMAND 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403361070 1039 SGYGLTLGVHTRIDETIAKvvnnvnagnvyVNRNI-VGAV---------VGVQPFGGEGLSGTG 1092
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALK-----------AARELeVGGVmindsstfrVDHMPYGGVKESGTG 434
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
661-1050 |
6.04e-77 |
|
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: 262.49 E-value: 6.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNV--APIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAI 738
Cdd:cd07114 1 SINPAT-GEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 739 AEVREAVDFLRYYA------------VQARNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:cd07114 80 AQVRYLAEWYRYYAgladkiegavipVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 807 LVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQN 886
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGI 966
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 967 EQHIQGMRDKG-RTVYQMAIADIEECKRGTFVMPTLIELESFDE--LEREIFGPVLHVVRYkrKDIDQLIAQINASGYGL 1043
Cdd:cd07114 314 ERYVARAREEGaRVLTGGERPSGADLGAGYFFEPTILADVTNDMriAQEEVFGPVLSVIPF--DDEEEAIALANDSEYGL 391
|
....*..
gi 1403361070 1044 TLGVHTR 1050
Cdd:cd07114 392 AAGIWTR 398
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
652-1050 |
1.33e-76 |
|
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: 261.82 E-value: 1.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 652 ASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAG 731
Cdd:cd07088 8 PSSSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 732 KTYANAIAEVREAVDFLRYYAVQAR--------NDLTND----AHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:cd07088 87 KTLSLARVEVEFTADYIDYMAEWARriegeiipSDRPNEnifiFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 800 KPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLI 879
Cdd:cd07088 167 KPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVID 959
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 960 AEAKAGIEQHIQGMRDKGRTV-YQMAIADIEeckRGTFVMPTLIE--LESFDELEREIFGPVLHVVRYkrKDIDQLIAQI 1036
Cdd:cd07088 321 EAALDKVEEMVERAVEAGATLlTGGKRPEGE---KGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELA 395
|
410
....*....|....
gi 1403361070 1037 NASGYGLTLGVHTR 1050
Cdd:cd07088 396 NDSEYGLTSYIYTE 409
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
661-1057 |
1.39e-73 |
|
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: 253.65 E-value: 1.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRdVVGHVQEATVEDADNAIQCALNVAPIWQAT-PPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA 739
Cdd:cd07082 20 VYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYyAVQARNDLTNDAHR-----------------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07082 99 EVDRTIDYIRD-TIEELKRLDGDSLPgdwfpgtkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 803 EQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRnIAGRLdaqgrpiPLIAET 882
Cdd:cd07082 178 TQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK-QHPMK-------RLVLEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEA 962
Cdd:cd07082 250 GGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 963 KAGIEQHIQGMRDKGRTVyqmaiadIEECKR--GTFVMPTLIELESfDELE---REIFGPVLHVVRYkrKDIDQLIAQIN 1037
Cdd:cd07082 330 ADFVEGLIDDAVAKGATV-------LNGGGRegGNLIYPTLLDPVT-PDMRlawEEPFGPVLPIIRV--NDIEEAIELAN 399
|
410 420
....*....|....*....|
gi 1403361070 1038 ASGYGLTLGVHTRIDETIAK 1057
Cdd:cd07082 400 KSNYGLQASIFTKDINKARK 419
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
659-1092 |
6.92e-73 |
|
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: 251.11 E-value: 6.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 659 AAVLNPSDLrDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAI 738
Cdd:cd07145 1 IEVRNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 739 AEVREAVDFLRYYAVQAR---------NDLTNDAHR-------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKvlrgetipvDAYEYNERRiaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 803 EQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAqgrpipLIAET 882
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKK------VALEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEA 962
Cdd:cd07145 234 GGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 963 KAGIEQHIQGMRDKG-RTVYQMAIADieeckrGTFVMPTLIELESFDE--LEREIFGPVLHVVRYkrKDIDQLIAQINAS 1039
Cdd:cd07145 314 VERMENLVNDAVEKGgKILYGGKRDE------GSFFPPTVLENDTPDMivMKEEVFGPVLPIAKV--KDDEEAVEIANST 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403361070 1040 GYGLTLGVHTridETIAKvvnnvnagNVYVNRNI-VGAVV---------GVQPFGGEGLSGTG 1092
Cdd:cd07145 386 EYGLQASVFT---NDINR--------ALKVARELeAGGVVindstrfrwDNLPFGGFKKSGIG 437
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
661-1118 |
1.21e-71 |
|
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: 249.43 E-value: 1.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLmgLLAREA---GKTYANA 737
Cdd:cd07123 50 QVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYE--LNAATMlgqGKNVWQA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 738 -IAEVREAVDFLR---YYAVQ------------ARNDLTndaHRPL-GPVVCISPWNFPlAIfSGQVAAALA-AGNPVLA 799
Cdd:cd07123 128 eIDAACELIDFLRfnvKYAEElyaqqplsspagVWNRLE---YRPLeGFVYAVSPFNFT-AI-GGNLAGAPAlMGNVVLW 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 800 KPAEqTPLVAAQAV-RLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAQgRPIP- 877
Cdd:cd07123 203 KPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRY-RTYPr 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 878 LIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPV 957
Cdd:cd07123 281 IVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 958 IDAEAKAGIEQHIqgmrDKGRTVYQMAIADIEEC--KRGTFVMPTLIELE--SFDELEREIFGPVLHVVRYKRKDIDQLI 1033
Cdd:cd07123 361 IDEKAFDRIKGYI----DHAKSDPEAEIIAGGKCddSVGYFVEPTVIETTdpKHKLMTEEIFGPVLTVYVYPDSDFEETL 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1034 AQIN-ASGYGLTLGVHTRIDETIAKVVNNVnagnvyvnRNIVG----------AVVGVQPFGGEGLSGTGPKAGGPLYLY 1102
Cdd:cd07123 437 ELVDtTSPYALTGAIFAQDRKAIREATDAL--------RNAAGnfyindkptgAVVGQQPFGGARASGTNDKAGSPLNLL 508
|
490
....*....|....*.
gi 1403361070 1103 RLLSTRpnnAIEQSFA 1118
Cdd:cd07123 509 RWVSPR---TIKETFV 521
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
661-1092 |
1.96e-71 |
|
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: 246.71 E-value: 1.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA- 739
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYA----------VQARNDLTNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07093 80 DIPRAAANFRFFAdyilqldgesYPQDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAM 888
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQ 968
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 969 HIQGMRDKGRTVYQMAIADIE-ECKRGTFVMPTLIELESfDELE---REIFGPVLHVVRYkrKDIDQLIAQINASGYGLT 1044
Cdd:cd07093 314 YVELARAEGATILTGGGRPELpDLEGGYFVEPTVITGLD-NDSRvaqEEIFGPVVTVIPF--DDEEEAIELANDTPYGLA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1403361070 1045 LGVHTRiDETIAkvvnnvnagnVYVNRNIVGAVVGV---------QPFGGEGLSGTG 1092
Cdd:cd07093 391 AYVWTR-DLGRA----------HRVARRLEAGTVWVncwlvrdlrTPFGGVKASGIG 436
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
660-1050 |
5.28e-70 |
|
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: 242.72 E-value: 5.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 660 AVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA 739
Cdd:cd07094 2 DVHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYAVQARN--------DLT--NDAHR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERirgeeiplDATqgSDNRLawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 804 QTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRldaqgrpiPLIAETG 883
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGK--------RIALELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAK 963
Cdd:cd07094 233 GNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 964 AGIEQHIQGMRDKGRTVYQMAIADieeckrGTFVMPTLIELESFDELER--EIFGPVLHVVRYkrKDIDQLIAQINASGY 1041
Cdd:cd07094 313 ERVERWVEEAVEAGARLLCGGERD------GALFKPTVLEDVPRDTKLSteETFGPVVPIIRY--DDFEEAIRIANSTDY 384
|
....*....
gi 1403361070 1042 GLTLGVHTR 1050
Cdd:cd07094 385 GLQAGIFTR 393
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
661-1092 |
7.99e-70 |
|
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: 242.14 E-value: 7.99e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRdVVGHVQEATVEDADNAIQCALNVAPI-WQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA 739
Cdd:cd07109 1 VFDPSTGE-VFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYAVQAR----------NDLTNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07109 80 DVEAAARYFEYYGGAADklhgetiplgPGYFVYTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAM 888
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPErLSVDIGPVIDAEAKAGIEQ 968
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 969 HIQGMRDKG-RTVYQMAIADIEECKrGTFVMPTLI-ELESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINASGYGLTL 1045
Cdd:cd07109 313 FVARARARGaRIVAGGRIAEGAPAG-GYFVAPTLLdDVPPDSRLAQeEIFGPVLAVMPF--DDEAEAIALANGTDYGLVA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1403361070 1046 GVHTRiDETIAKVVNNVNAGNVYVNrNIVGAVVGVQ-PFGGEGLSGTG 1092
Cdd:cd07109 390 GVWTR-DGDRALRVARRLRAGQVFV-NNYGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
681-1050 |
1.46e-69 |
|
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: 240.51 E-value: 1.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 681 DADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARN--- 757
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 758 -DLTNDA--------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV-RLMLEAGIPEGVLQ 827
Cdd:cd07104 81 eILPSDVpgkesmvrRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 828 LLPGRGETVGARLVGDDRVKGVMFTGSTEVArllqRNIAgrlDAQGRPIPLIA-ETGGQNAMIVDSSALTEQVVIDVVSS 906
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIG---ELAGRHLKKVAlELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 907 AFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVyqMAI 985
Cdd:cd07104 234 AFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL--LTG 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 986 ADIEeckrGTFVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTR 1050
Cdd:cd07104 311 GTYE----GLFYQPTVLsdvtpDMPIFRE---EIFGPVAPVIPF--DDDEEAVELANDTEYGLSAAVFTR 371
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
661-1057 |
2.16e-69 |
|
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: 240.51 E-value: 2.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07106 1 VINPAT-GEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQARNDLT---NDA------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQ 811
Cdd:cd07106 80 VGGAVAWLRYTASLDLPDEViedDDTrrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 812 AVRLMLEAgIPEGVLQLLPGRGEtVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgRPIPLiaETGGQNAMIVD 891
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 892 SSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQ 971
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 972 GMRDKGRTVyqMAIADIEEcKRGTFVMPTLIE--LESFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHT 1049
Cdd:cd07106 312 DAKAKGAKV--LAGGEPLD-GPGYFIPPTIVDdpPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVWS 386
|
....*...
gi 1403361070 1050 RiDETIAK 1057
Cdd:cd07106 387 S-DLERAE 393
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
651-1057 |
9.79e-69 |
|
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: 239.91 E-value: 9.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 651 CASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNV--APIWQATPPAERAAILERAADLMEAEIQPLMGLLAR 728
Cdd:cd07119 7 VEAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 729 EAGKTYANAIAEVREAVDFLRYYA--VQARNDLTNDA---------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07119 86 NTGKTLRESEIDIDDVANCFRYYAglATKETGEVYDVpphvisrtvREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 798 LAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgRPIP 877
Cdd:cd07119 166 VIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV----KKVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 878 LiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPV 957
Cdd:cd07119 242 L--ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 958 IDAEAKAGIEQHIQ-GMRDKGRTVYQMAIADIEECKRGTFVMPTLielesFDELER-------EIFGPVLHVVRYkrKDI 1029
Cdd:cd07119 320 VSAEHREKVLSYIQlGKEEGARLVCGGKRPTGDELAKGYFVEPTI-----FDDVDRtmrivqeEIFGPVLTVERF--DTE 392
|
410 420
....*....|....*....|....*...
gi 1403361070 1030 DQLIAQINASGYGLTLGVHTRiDETIAK 1057
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTK-DIARAN 419
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
660-1050 |
9.96e-69 |
|
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: 239.04 E-value: 9.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 660 AVLNPSDLRdVVGHVQEATVEDADNAIQCALNV--APIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANA 737
Cdd:cd07112 5 ATINPATGR-VLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 738 IA-EVREAVDFLRYY-----------AVQARNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQT 805
Cdd:cd07112 84 LAvDVPSAANTFRWYaeaidkvygevAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 806 PLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAgrlDAQGRPIPLiaETGGQ 885
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSG---QSNLKRVWL--ECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 886 NAMIV-DSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07112 239 SPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 965 GIEQHIQ-GMRDKGRTVYQMAIADIEEckRGTFVMPTLielesFDELER-------EIFGPVLHVVRYkrKDIDQLIAQI 1036
Cdd:cd07112 319 KVLGYIEsGKAEGARLVAGGKRVLTET--GGFFVEPTV-----FDGVTPdmriareEIFGPVLSVITF--DSEEEAVALA 389
|
410
....*....|....
gi 1403361070 1037 NASGYGLTLGVHTR 1050
Cdd:cd07112 390 NDSVYGLAASVWTS 403
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
661-1096 |
1.45e-68 |
|
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: 238.49 E-value: 1.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANA-IA 739
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYA----------VQARNDLTNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07115 80 DVPRAADTFRYYAgwadkiegevIPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgRPIPLiaETGGQNAM 888
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNL----KRVSL--ELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQ 968
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 969 HIQGMRDKGRTVYQMAIADIEeckRGTFVMPTLIE-LESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLG 1046
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGA---RGFFVEPTIFAaVPPEMRIAQeEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1047 VHTRiDETIAKVVNNVNAGNVYVNrNIVGAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:cd07115 389 VWTR-DLGRAHRVAAALKAGTVWI-NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
681-1090 |
1.88e-68 |
|
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: 237.17 E-value: 1.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 681 DADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGK------TYANA-IAEVREAVDFLRYYAV 753
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKplweaqTEVAAmAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 754 QARNDLTNDA----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLL 829
Cdd:cd07095 81 ERATPMAQGRavlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 830 PGRGETvGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAQgrpipLIAETGGQNAMIVDSSALTEQVVIDVVSSAFD 909
Cdd:cd07095 161 QGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 910 SAGQRCSALRVLCLQEDS-ADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQG-MRDKGRTVYQMAIAD 987
Cdd:cd07095 235 TAGQRCTCARRLIVPDGAvGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDlLALGGEPLLAMERLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 988 ieecKRGTFVMPTLIELESFDEL-EREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRIDETIAKVVNNVNAGN 1066
Cdd:cd07095 315 ----AGTAFLSPGIIDVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI 388
|
410 420
....*....|....*....|....
gi 1403361070 1067 VYVNRNIVGAvVGVQPFGGEGLSG 1090
Cdd:cd07095 389 VNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
651-1042 |
3.01e-68 |
|
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: 238.19 E-value: 3.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 651 CASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREA 730
Cdd:cd07085 10 VESKTTEWLDVYNPAT-GEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 731 GKTYANAIAEVR---EAVDF--------LRYYAVQARNDLtnDAH---RPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:cd07085 89 GKTLADARGDVLrglEVVEFacsiphllKGEYLENVARGI--DTYsyrQPLGVVAGITPFNFPAMIPLWMFPMAIACGNT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 797 VLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGArLVGDDRVKGVMFTGSTEVARLLQRNIAgrldAQGRPI 876
Cdd:cd07085 167 FVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYERAA----ANGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 877 plIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGP 956
Cdd:cd07085 242 --QALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 957 VIDAEAKAGIEQHIQGMRDKGRTVyqmaIAD-----IEECKRGTFVMPTLI-----ELESFDElerEIFGPVLHVVRYkr 1026
Cdd:cd07085 320 VISPAAKERIEGLIESGVEEGAKL----VLDgrgvkVPGYENGNFVGPTILdnvtpDMKIYKE---EIFGPVLSIVRV-- 390
|
410
....*....|....*.
gi 1403361070 1027 KDIDQLIAQINASGYG 1042
Cdd:cd07085 391 DTLDEAIAIINANPYG 406
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
661-1098 |
9.68e-68 |
|
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: 236.07 E-value: 9.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07150 3 DLNPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQARN----DLTNDA--------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07150 82 TTFTPELLRAAAGECRRvrgeTLPSDSpgtvsmsvRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVArllqRNIAGRLDAQGRPIPLiaETGGQNAM 888
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRHLKKITL--ELGGKNPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQ 968
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 969 HIQGMRDKGrtvyqmAIADIEECKRGTFVMPTLIE--LESFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLG 1046
Cdd:cd07150 316 QVEDAVAKG------AKLLTGGKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPA--KDAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403361070 1047 VHTRiDETIAkvvnnvnagnVYVNRNIVGAVVGVQ----------PFGGEGLSGTGpKAGGP 1098
Cdd:cd07150 388 ILTN-DLQRA----------FKLAERLESGMVHINdptildeahvPFGGVKASGFG-REGGE 437
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
661-1050 |
1.37e-67 |
|
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: 236.34 E-value: 1.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPI--WQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTY-ANA 737
Cdd:cd07091 23 TINPAT-EEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLeESA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 738 IAEVREAVDFLRYYAVQA-----------RNDLTNDAHRPLGpvVC--ISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07091 102 KGDVALSIKCLRYYAGWAdkiqgktipidGNFLAYTRREPIG--VCgqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 805 TPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAgrlDAQGRPIPLiaETGG 884
Cdd:cd07091 180 TPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAA---KSNLKKVTL--ELGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKgAMAESR-MGNPERLSVDIGPVIDAEAK 963
Cdd:cd07091 255 KSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFK-ARAEKRvVGDPFDPDTFQGPQVSKAQF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 964 AGIEQHIQ-GMRDKGRTVYQMAIADieecKRGTFVMPTL---------IELEsfdelerEIFGPVLHVVRYkrKDIDQLI 1033
Cdd:cd07091 334 DKILSYIEsGKKEGATLLTGGERHG----SKGYFIQPTVftdvkddmkIAKE-------EIFGPVVTILKF--KTEDEVI 400
|
410
....*....|....*..
gi 1403361070 1034 AQINASGYGLTLGVHTR 1050
Cdd:cd07091 401 ERANDTEYGLAAGVFTK 417
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
661-1092 |
2.21e-67 |
|
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: 235.21 E-value: 2.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIW-QATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA 739
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 -EVREAVDFLRYYAVQARN-----DLTNDA-----------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSfpwefDLPVPAlrggpgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 803 EQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgRPIPLiaET 882
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEA 962
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 963 KAGIEQHIQGMRDKG-RTVYQMAIADIEEckRGTFVMPTLielesFDELE-------REIFGPVLHVVRYkrKDIDQLIA 1034
Cdd:cd07089 314 RDRVEGYIARGRDEGaRLVTGGGRPAGLD--KGFYVEPTL-----FADVDndmriaqEEIFGPVLVVIPY--DDDDEAVR 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403361070 1035 QINASGYGLTLGVHTRiDETIAkvvnnvnagnVYVNRNIVGAVVGVQ---------PFGGEGLSGTG 1092
Cdd:cd07089 385 IANDSDYGLSGGVWSA-DVDRA----------YRVARRIRTGSVGINggggygpdaPFGGYKQSGLG 440
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
661-1050 |
1.51e-66 |
|
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: 232.64 E-value: 1.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTY-ANAIA 739
Cdd:cd07108 1 VINPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYAVQA-----------RNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLv 808
Cdd:cd07108 80 EAAVLADLFRYFGGLAgelkgetlpfgPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAM 888
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSA-FDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 968 QHIQ-GMRDKGRTVYQMAIADIE-ECKRGTFVMPTLI-ELESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINASGYGL 1043
Cdd:cd07108 313 GYIDlGLSTSGATVLRGGPLPGEgPLADGFFVQPTIFsGVDNEWRLAReEIFGPVLCAIPW--KDEDEVIAMANDSHYGL 390
|
....*..
gi 1403361070 1044 TLGVHTR 1050
Cdd:cd07108 391 AAYVWTR 397
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
650-1050 |
5.32e-66 |
|
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: 231.71 E-value: 5.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 650 GCASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLARE 729
Cdd:cd07130 5 GEWGGGGGVVTSISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 730 AGKTYANAIAEVREAVDFLRYYAVQAR--NDLT----NDAHR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07130 84 MGKILPEGLGEVQEMIDICDFAVGLSRqlYGLTipseRPGHRmmeqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 798 LAKPAEQTPLVAAQAVRLMLEA----GIPEGVLQLLPGRGEtVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqG 873
Cdd:cd07130 164 VWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 874 RpipLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVD 953
Cdd:cd07130 240 R---SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 954 IGPVIDAEA----KAGIEQHI-QGmrdkGRTVYQMAIADIEeckrGTFVMPTLIELESFDEL-EREIFGPVLHVVRYkrK 1027
Cdd:cd07130 317 VGPLHTKAAvdnyLAAIEEAKsQG----GTVLFGGKVIDGP----GNYVEPTIVEGLSDAPIvKEETFAPILYVLKF--D 386
|
410 420
....*....|....*....|...
gi 1403361070 1028 DIDQLIAQINASGYGLTLGVHTR 1050
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTT 409
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
670-1050 |
1.99e-65 |
|
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: 229.42 E-value: 1.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 670 VVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLR 749
Cdd:cd07099 8 VLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 750 YYA-----------VQARNDLTNDA----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVR 814
Cdd:cd07099 88 WAArnaprvlaprkVPTGLLMPNKKatveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 815 LMLEAGIPEGVLQLLPGRGETvGARLVgDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:cd07099 168 AWAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGSVATGRKVMAAAAERL------IPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMR 974
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403361070 975 DKGRTVyqmAIADIEECKRGTFVMPTLI--ELESFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTR 1050
Cdd:cd07099 320 AKGAKA---LTGGARSNGGGPFYEPTVLtdVPHDMDVMREETFGPVLPVMPV--ADEDEAIALANDSRYGLSASVFSR 392
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
661-1096 |
7.22e-65 |
|
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: 227.63 E-value: 7.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPiwqATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07146 3 VRNPYT-GEVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQARN--------DLTNDAHR--------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07146 79 VGRAADVLRFAAAEALRddgesfscDLTANGKArkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 805 TPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRldaqgrpiPLIAETGG 884
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 965 GIEQHIQGMRDKGRTVYQMAIadieecKRGTFVMPTLIELESFD-EL-EREIFGPVLHVVRYkrKDIDQLIAQINASGYG 1042
Cdd:cd07146 311 QIENRVEEAIAQGARVLLGNQ------RQGALYAPTVLDHVPPDaELvTEETFGPVAPVIRV--KDLDEAIAISNSTAYG 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403361070 1043 LTLGVHTRIDETIAKVVNNVNagnvyvnrniVGAVV-----GVQ----PFGGEGLSGTGPKAG 1096
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLD----------VGTVNvnevpGFRselsPFGGVKDSGLGGKEG 435
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
669-1096 |
1.16e-62 |
|
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: 221.98 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 669 DVVGHVQEATVEDADNAIQCA---LNVAPiWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANA-IAEVREA 744
Cdd:cd07142 30 EVIAHVAEGDAEDVDRAVKAArkaFDEGP-WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 745 VDFLRYYAVQARN----DLTNDA-------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV 813
Cdd:cd07142 109 ARLFRYYAGWADKihgmTLPADGphhvytlHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 814 RLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQrniagRLDAQGRPIPLIAETGGQNAMIVDSS 893
Cdd:cd07142 189 KLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIM-----QLAAKSNLKPVTLELGGKSPFIVCED 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 894 ALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGM 973
Cdd:cd07142 264 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 974 RDKGRTVYQ--MAIADieeckRGTFVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLG 1046
Cdd:cd07142 344 KEEGATLITggDRIGS-----KGYYIQPTIFsdvkdDMKIARD---EIFGPVQSILKF--KTVDEVIKRANNSKYGLAAG 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1403361070 1047 VHTRIDETIakvvnnvnagnVYVNRNIVGAVVGVQ---------PFGGEGLSGTGPKAG 1096
Cdd:cd07142 414 VFSKNIDTA-----------NTLSRALKAGTVWVNcydvfdasiPFGGYKMSGIGREKG 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
661-1050 |
1.52e-62 |
|
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: 220.97 E-value: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRdVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07147 3 VTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQA-RND---LTNDAHR------------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07147 82 VARAIDTFRIAAEEAtRIYgevLPLDISArgegrqglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 805 TPLVAAQAVRLMLEAGIPEGVLQLLPGRGETvGARLVGDDRVKGVMFTGSTEVARLLqRNIAGRldaqgRPIPLiaETGG 884
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-----KKVVL--ELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAK 963
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 964 AGIEQHIQGMRDKGRTVYqmaiadieeC---KRGTFVMPTLIE-LESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINA 1038
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLL---------TggkRDGALLEPTILEdVPPDMEVNCeEVFGPVVTVEPY--DDFDEALAAVND 380
|
410
....*....|..
gi 1403361070 1039 SGYGLTLGVHTR 1050
Cdd:cd07147 381 SKFGLQAGVFTR 392
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
669-1050 |
2.16e-62 |
|
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: 220.64 E-value: 2.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 669 DVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFL 748
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 749 RYYAVQARNDL--------------TNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVR 814
Cdd:cd07101 87 RYYARRAERLLkprrrrgaipvltrTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 815 LMLEAGIPEGVLQLLPGRGETVGARLVgdDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:cd07101 167 LLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMR 974
Cdd:cd07101 239 DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 975 DKGRTVYQ--MAIADIeeckrGT-FVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLG 1046
Cdd:cd07101 319 AKGATVLAggRARPDL-----GPyFYEPTVLtgvteDMELFAE---ETFGPVVSIYRV--ADDDEAIELANDTDYGLNAS 388
|
....
gi 1403361070 1047 VHTR 1050
Cdd:cd07101 389 VWTR 392
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
652-1054 |
2.41e-62 |
|
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: 220.84 E-value: 2.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 652 ASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAG 731
Cdd:cd07138 9 APAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 732 --KTYAN------AIAEVREAVDFLRYYAVQARNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07138 88 apITLARaaqvglGIGHLRAAADALKDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 804 QTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLD--AQgrpipliaE 881
Cdd:cd07138 168 VAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKrvAL--------E 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSAL-RVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDA 960
Cdd:cd07138 240 LGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 961 EAKagieQHIQGMRDKGrtvyqmaiadIEE--------------CKRGTFVMPTLI-ELESFDELER-EIFGPVLHVVRY 1024
Cdd:cd07138 319 AQF----DRVQGYIQKG----------IEEgarlvaggpgrpegLERGYFVKPTVFaDVTPDMTIAReEIFGPVLSIIPY 384
|
410 420 430
....*....|....*....|....*....|
gi 1403361070 1025 krKDIDQLIAQINASGYGLTLGVHTRIDET 1054
Cdd:cd07138 385 --DDEDEAIAIANDTPYGLAGYVWSADPER 412
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
682-1050 |
1.11e-61 |
|
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: 217.71 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 682 ADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARNDLTN 761
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 762 D-----------AHRPLGPVVCISPWNFPLAifsgQV----AAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVL 826
Cdd:cd07100 81 EpietdagkayvRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 827 QLLPGRGETVgARLVGDDRVKGVMFTGSTEvarllqrniAGRLDAQ--GRPI-PLIAETGGQNAMIVDSSALTEQVVIDV 903
Cdd:cd07100 157 QNLLIDSDQV-EAIIADPRVRGVTLTGSER---------AGRAVAAeaGKNLkKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 904 VSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTV-Y 981
Cdd:cd07100 227 VKGRLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLlL 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403361070 982 QMAIADieecKRGTFVMPTLI-----ELESFDElerEIFGPVLHVvrYKRKDIDQLIAQINASGYGLTLGVHTR 1050
Cdd:cd07100 306 GGKRPD----GPGAFYPPTVLtdvtpGMPAYDE---ELFGPVAAV--IKVKDEEEAIALANDSPFGLGGSVFTT 370
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
669-1098 |
2.24e-61 |
|
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: 217.16 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 669 DVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFL 748
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 749 RYYA---VQARNDL-------TNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV-RLM 816
Cdd:cd07152 82 HEAAglpTQPQGEIlpsapgrLSLARRvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 817 LEAGIPEGVLQLLPGRGEtVGARLVGDDRVKGVMFTGSTEVARLLQRniagrldAQGRPIPLIA-ETGGQNAMIVDSSAL 895
Cdd:cd07152 162 EEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGE-------AAGRHLKKVSlELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 896 TEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMR 974
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 975 DKGRTVYQMAIADieeckrGTFVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHT 1049
Cdd:cd07152 313 AAGARLEAGGTYD------GLFYRPTVLsgvkpGMPAFDE---EIFGPVAPVTVF--DSDEEAVALANDTEYGLSAGIIS 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1403361070 1050 RIDETIAKVVNNVNAGNVYVNRNIVGAVVgVQPFGGEGLSGTGPKAGGP 1098
Cdd:cd07152 382 RDVGRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
146-257 |
2.68e-61 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 204.66 E-value: 2.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 146 VQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWHPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAG 225
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 1403361070 226 LTSSLSRIIGKSGEPMIRKGVDMAMRLMGEQF 257
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
669-1096 |
9.09e-61 |
|
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: 215.66 E-value: 9.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 669 DVVGHVQEATVEDADNAIQ---CALNVAPiWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAV 745
Cdd:cd07118 8 VVVARYAEGTVEDVDAAVAaarKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 746 DFLRYYAVQARNdLTNDAHRPLGP-------------VVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQA 812
Cdd:cd07118 87 DLWRYAASLART-LHGDSYNNLGDdmlglvlrepigvVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLML 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 813 VRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAQGrpipliAETGGQNAMIVDS 892
Cdd:cd07118 166 AELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 893 SALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQG 972
Cdd:cd07118 240 DADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 973 MRDKGRTVYQMaiADIEECKRGTFVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGV 1047
Cdd:cd07118 320 GRAEGATLLLG--GERLASAAGLFYQPTIFtdvtpDMAIARE---EIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGV 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1403361070 1048 HTR-IDETIAkvvnnvnagnvyVNRNIVGAVVGVQ---------PFGGEGLSGTGPKAG 1096
Cdd:cd07118 393 WSKdIDTALT------------VARRIRAGTVWVNtfldgspelPFGGFKQSGIGRELG 439
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
669-1050 |
4.21e-60 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 215.90 E-value: 4.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 669 DVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFL 748
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 749 RYYAVQARNDL--------------TNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVR 814
Cdd:PRK09407 123 RYYARRAPKLLaprrragalpvltkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 815 LMLEAGIPEGVLQLLPGRGETVGARLVgdDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:PRK09407 203 LLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRL------IGFSLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMR 974
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 975 DKGRTVYQ--MAIADIEECkrgtFVMPTLI-----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGV 1047
Cdd:PRK09407 355 AKGATVLAggKARPDLGPL----FYEPTVLtgvtpDMELARE---ETFGPVVSVYPV--ADVDEAVERANDTPYGLNASV 425
|
...
gi 1403361070 1048 HTR 1050
Cdd:PRK09407 426 WTG 428
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
652-1098 |
4.88e-60 |
|
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: 214.36 E-value: 4.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 652 ASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAI---QCALNVAPiWQATPPAERAAILERAADLMEAEIQPLMGLLAR 728
Cdd:cd07139 9 APSGSETIDVVSPAT-EEVVGRVPEATPADVDAAVaaaRRAFDNGP-WPRLSPAERAAVLRRLADALEARADELARLWTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 729 EAGKTYA-NAIAEVREAVDFLRYYAVQARnDLTNDAHR-------------PLGPVVCISPWNFPLAIFSGQVAAALAAG 794
Cdd:cd07139 87 ENGMPISwSRRAQGPGPAALLRYYAALAR-DFPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 795 NPVLAKPAEQTPLVA---AQAVRlmlEAGIPEGVLQLLPGrGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLda 871
Cdd:cd07139 166 CTVVLKPSPETPLDAyllAEAAE---EAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 872 qgRPIPLiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSAL-RVLCLQEdSADRVIEMLKGAMAESRMGNPERL 950
Cdd:cd07139 240 --ARVTL--ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVPRS-RYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 951 SVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYqMAIADIEECKRGTFVMPTLI-ELESFDELER-EIFGPVLHVVRYkrKD 1028
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLV-TGGGRPAGLDRGWFVEPTLFaDVDNDMRIAQeEIFGPVLSVIPY--DD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1029 IDQLIAQINASGYGLTLGVHTRIDET---IAkvvnnvnagnvyvnRNIVGAVVGVQ--------PFGGEGLSGTGpKAGG 1097
Cdd:cd07139 392 EDDAVRIANDSDYGLSGSVWTADVERglaVA--------------RRIRTGTVGVNgfrldfgaPFGGFKQSGIG-REGG 456
|
.
gi 1403361070 1098 P 1098
Cdd:cd07139 457 P 457
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
660-1092 |
1.65e-59 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 213.40 E-value: 1.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 660 AVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA 739
Cdd:PLN02278 43 PVYNPAT-GEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYAVQARN---DL--TNDA-------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKRvygDIipSPFPdrrllvlKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 808 VAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgRPIPLiaETGGQNA 887
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV----KRVSL--ELGGNAP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 888 MIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGI 966
Cdd:PLN02278 276 FIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 967 EQHIQGMRDKGRTVyqmaiadIEECKR----GTFVMPTLIELESFDEL--EREIFGPVLHVVRYkrKDIDQLIAQINASG 1040
Cdd:PLN02278 355 ESHVQDAVSKGAKV-------LLGGKRhslgGTFYEPTVLGDVTEDMLifREEVFGPVAPLTRF--KTEEEAIAIANDTE 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403361070 1041 YGLTLGVHT-------RIDETIakvvnnvnagnvyvNRNIVGAVVG-----VQPFGGEGLSGTG 1092
Cdd:PLN02278 426 AGLAAYIFTrdlqrawRVSEAL--------------EYGIVGVNEGlisteVAPFGGVKQSGLG 475
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
662-1053 |
1.49e-58 |
|
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: 209.41 E-value: 1.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 662 LNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEV 741
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 742 REAVDFLRYYAVQARNDLTND------------AHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:cd07102 80 RGMLERARYMISIAEEALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 810 AQAVRLMLEAGIPEGVLQLLPGRGETvGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMI 889
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRF------IKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 890 VDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQH 969
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 970 IQGMRDKGrtvyqmAIADIEE------CKRGTFVMPT-LIELE-SFDELEREIFGPVLHVvrYKRKDIDQLIAQINASGY 1041
Cdd:cd07102 313 IADAIAKG------ARALIDGalfpedKAGGAYLAPTvLTNVDhSMRVMREETFGPVVGI--MKVKSDAEAIALMNDSEY 384
|
410
....*....|..
gi 1403361070 1042 GLTLGVHTRIDE 1053
Cdd:cd07102 385 GLTASVWTKDIA 396
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
653-1050 |
2.05e-58 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 209.77 E-value: 2.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 653 SSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGK 732
Cdd:PRK13473 13 AGEGEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 733 TYANAIA-EVREAVDFLRYYAVQARN-----------DLTNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:PRK13473 92 PLHLALNdEIPAIVDVFRFFAGAARClegkaageyleGHTSMIRRdPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 800 KPAEQTPLVAAQAVRLMLEAgIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVArllqRNIAGRLDAQGRPIPLi 879
Cdd:PRK13473 172 KPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATG----KHVLSAAADSVKRTHL- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 880 aETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVID 959
Cdd:PRK13473 246 -ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 960 AEAKAGIEQHIQGMRDKG--RTVYQMAIADieecKRGTFVMPTLIE--LESFDELEREIFGPVLHVVRYkrKDIDQLIAQ 1035
Cdd:PRK13473 325 AAHRDRVAGFVERAKALGhiRVVTGGEAPD----GKGYYYEPTLLAgaRQDDEIVQREVFGPVVSVTPF--DDEDQAVRW 398
|
410
....*....|....*
gi 1403361070 1036 INASGYGLTLGVHTR 1050
Cdd:PRK13473 399 ANDSDYGLASSVWTR 413
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
661-1050 |
3.48e-58 |
|
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: 208.33 E-value: 3.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA- 739
Cdd:cd07092 1 VVDPAT-GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYAVQARN-----------DLTNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTlegpaageylpGHTSMIRRePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 808 VAAQAVRLMLEaGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAqgrpipLIAETGGQNA 887
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR------VHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 888 MIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGI 966
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 967 EQHIQGMRDKGRTVYQMAIADieecKRGTFVMPTLI-ELESFDEL-EREIFGPVLHVVRYkrKDIDQLIAQINASGYGLT 1044
Cdd:cd07092 312 AGFVERAPAHARVLTGGRRAE----GPGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPF--DDEDEAIELANDVEYGLA 385
|
....*.
gi 1403361070 1045 LGVHTR 1050
Cdd:cd07092 386 SSVWTR 391
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
661-1050 |
1.60e-57 |
|
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: 206.46 E-value: 1.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQA-----------RNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:cd07107 80 VMVAAALLDYFAGLVtelkgetipvgGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 810 AQAVRLMLEAgIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDaqgrpiPLIAETGGQNAMI 889
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 890 VDSSALTEQVVIDVVSSA-FDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQ 968
Cdd:cd07107 233 VFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 969 HIQGMRDKG-RTVYQMAIADIEECKRGTFVMPT-LIELESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINASGYGLTL 1045
Cdd:cd07107 313 YIDSAKREGaRLVTGGGRPEGPALEGGFYVEPTvFADVTPGMRIAReEIFGPVLSVLRW--RDEAEMVAQANGVEYGLTA 390
|
....*
gi 1403361070 1046 GVHTR 1050
Cdd:cd07107 391 AIWTN 395
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
661-1096 |
1.65e-57 |
|
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: 207.38 E-value: 1.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNV--APIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAI 738
Cdd:cd07143 26 VYNPST-GKLITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 739 A-EVREAVDFLRYYAVQARND-----------LTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:cd07143 105 RvDVQASADTFRYYGGWADKIhgqvietdikkLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 807 LVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAgrlDAQGRPIPLiaETGGQN 886
Cdd:cd07143 185 LSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA---KSNLKKVTL--ELGGKS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGI 966
Cdd:cd07143 260 PNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 967 EQHIQGMRDKGRTVyqmAIADIEECKRGTFVMPTLIE--LESFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLT 1044
Cdd:cd07143 340 MSYIESGKAEGATV---ETGGKRHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKF--KTEEEAIKRANDSTYGLA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1403361070 1045 LGVHTR-IDETIAKVVNNVNAGNVYVNRNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07143 415 AAVFTNnINNAIRVANALKAGTVWVNCYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
651-1050 |
1.69e-57 |
|
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: 207.26 E-value: 1.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 651 CASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNV-APIWQATPPAERAAILERAADLMEAEIQPLMGLLARE 729
Cdd:cd07144 17 VKSSDGETIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 730 AGKTY-ANAIAEVREAVDFLRYYAVQA-----------RNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07144 96 SGKPYhSNALGDLDEIIAVIRYYAGWAdkiqgktiptsPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 798 LAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAqgrpIP 877
Cdd:cd07144 176 VIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA----VT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 878 LiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAE-SRMGNPERLSVDIGP 956
Cdd:cd07144 252 L--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 957 VIDAEAKAGIEQHI-QGMRDKGRTVYQMAIADIEECKrGTFVMPTLIE--LESFDELEREIFGPVlhVVRYKRKDIDQLI 1033
Cdd:cd07144 330 QVSKTQYDRVLSYIeKGKKEGAKLVYGGEKAPEGLGK-GYFIPPTIFTdvPQDMRIVKEEIFGPV--VVISKFKTYEEAI 406
|
410
....*....|....*..
gi 1403361070 1034 AQINASGYGLTLGVHTR 1050
Cdd:cd07144 407 KKANDTTYGLAAAVFTK 423
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
675-1090 |
3.17e-57 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 206.35 E-value: 3.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 675 QEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVD----FLRY 750
Cdd:PRK09457 32 NDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINkiaiSIQA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 751 YAV---QARNDLTNDA----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPE 823
Cdd:PRK09457 112 YHErtgEKRSEMADGAavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 824 GVLQLLPGRGETvGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDV 903
Cdd:PRK09457 192 GVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPE-----KILALEMGGNNPLVIDEVADIDAAVHLI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 904 VSSAFDSAGQRCSALRVLCLQEDS-ADRVIEMLKGAMAESRMGNPerlsvD------IGPVIDAEAKAGI---EQHIQGM 973
Cdd:PRK09457 266 IQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRW-----DaepqpfMGAVISEQAAQGLvaaQAQLLAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 974 rdKGRTVYQMAIADieecKRGTFVMPTLIELESFDEL-EREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRID 1052
Cdd:PRK09457 341 --GGKSLLEMTQLQ----AGTGLLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDFDEAIRLANNTRFGLSAGLLSDDR 412
|
410 420 430
....*....|....*....|....*....|....*...
gi 1403361070 1053 ETIAKVVNNVNAGNVYVNRNIVGAvVGVQPFGGEGLSG 1090
Cdd:PRK09457 413 EDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
662-1050 |
3.91e-57 |
|
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: 205.27 E-value: 3.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 662 LNPSDlRDVVGHVQEATVEDADNAIQCALN--VAPIWqATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA 739
Cdd:cd07120 2 IDPAT-GEVIGTYADGGVAEAEAAIAAARRafDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYAVQARN----------DLTNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07120 80 EISGAISELRYYAGLARTeagrmiepepGSFSLVLRePMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEA-GIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAQGrpipliAETGGQNA 887
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 968 QHIQGMRDKGRTVYQMAIADIEECKRGTFVMPTLIELE--SFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTL 1045
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGLAKGAFLRPTLLEVDdpDADIVQEEIFGPVLTLETF--DDEAEAVALANDTDYGLAA 391
|
....*
gi 1403361070 1046 GVHTR 1050
Cdd:cd07120 392 SVWTR 396
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
661-1050 |
1.45e-56 |
|
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: 204.08 E-value: 1.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07151 14 VLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYA-----VQAR---NDLTNDAHR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07151 93 WGAAMAITREAAtfplrMEGRilpSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPIT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAV-RLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVArllqRNIaGRLdaQGRPIPLIA-ETGGQN 886
Cdd:cd07151 173 GGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG----RHI-GEL--AGRHLKKVAlELGGNN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGI 966
Cdd:cd07151 246 PFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 967 EQHIQGMRDKGRTVyqMAIADIEeckrGTFVMPT-LIELESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINASGYGLT 1044
Cdd:cd07151 326 LDKIEQAVEEGATL--LVGGEAE----GNVLEPTvLSDVTNDMEIAReEIFGPVAPIIKA--DDEEEALELANDTEYGLS 397
|
....*.
gi 1403361070 1045 LGVHTR 1050
Cdd:cd07151 398 GAVFTS 403
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
661-1050 |
1.45e-56 |
|
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: 203.74 E-value: 1.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQARN------------DLTNDAHR---PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQT 805
Cdd:cd07110 80 VDDVAGCFEYYADLAEQldakaeravplpSEDFKARVrrePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 806 PLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAgrldAQGRPIPLiaETGGQ 885
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA----QDIKPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 886 NAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAG 965
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 966 IEQHIQGMRDKGRTVYQMAIADiEECKRGTFVMPTLI-ELESFDELER-EIFGPVLHVVRYKRKdiDQLIAQINASGYGL 1043
Cdd:cd07110 314 VLSFIARGKEEGARLLCGGRRP-AHLEKGYFIAPTVFaDVPTDSRIWReEIFGPVLCVRSFATE--DEAIALANDSEYGL 390
|
....*..
gi 1403361070 1044 TLGVHTR 1050
Cdd:cd07110 391 AAAVISR 397
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
660-1096 |
1.80e-56 |
|
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: 204.12 E-value: 1.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 660 AVLNPSDlRDVVGHVQEATVEDADNAIQC---ALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYAN 736
Cdd:cd07141 25 PTINPAT-GEKICEVQEGDKADVDKAVKAaraAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 737 A-IAEVREAVDFLRYYAVQAR-----------NDLTNDAHRPLGpvVC--ISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07141 104 SyLVDLPGAIKVLRYYAGWADkihgktipmdgDFFTYTRHEPVG--VCgqIIPWNFPLLMAAWKLAPALACGNTVVLKPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 803 EQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNiAGRLDAqgRPIPLiaET 882
Cdd:cd07141 182 EQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA-AGKSNL--KRVTL--EL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADrviEMLKGAM--AESR-MGNPERLSVDIGPVID 959
Cdd:cd07141 257 GGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYD---EFVKRSVerAKKRvVGNPFDPKTEQGPQID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 960 AEAKAGIEQHIQGMRDKGRtvyQMAIADIEECKRGTFVMPTLIElESFDEL---EREIFGPVLHVVRYkrKDIDQLIAQI 1036
Cdd:cd07141 334 EEQFKKILELIESGKKEGA---KLECGGKRHGDKGYFIQPTVFS-DVTDDMriaKEEIFGPVQQIFKF--KTIDEVIERA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403361070 1037 NASGYGLTLGVHTR-IDETIAKVVNNVNAGNVYVNRNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07141 408 NNTTYGLAAAVFTKdIDKAITFSNALRAGTVWVNCYNVVSPQA---PFGGYKMSGNGRELG 465
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
661-1050 |
6.83e-55 |
|
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: 199.49 E-value: 6.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRdVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGK----TYAn 736
Cdd:cd07559 20 NYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKpireTLA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 737 aiAEVREAVDFLRYYAVQAR------NDLTNDA-----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQT 805
Cdd:cd07559 98 --ADIPLAIDHFRYFAGVIRaqegslSEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 806 PLVAAQAVRLMLEAgIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQ 885
Cdd:cd07559 176 PLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------IPVTLELGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 886 NAMIVDSSALTEQVVID------VVSSAFDSaGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVID 959
Cdd:cd07559 249 SPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 960 AEAKAGIEQHIQGMRDKGRTVYQMAIADIEE-CKRGTFVMPTLIE-----LESFDElerEIFGPVLHVVRYkrKDIDQLI 1033
Cdd:cd07559 328 KDQLEKILSYVDIGKEEGAEVLTGGERLTLGgLDKGYFYEPTLIKggnndMRIFQE---EIFGPVLAVITF--KDEEEAI 402
|
410
....*....|....*..
gi 1403361070 1034 AQINASGYGLTLGVHTR 1050
Cdd:cd07559 403 AIANDTEYGLGGGVWTR 419
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
662-1090 |
5.46e-54 |
|
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 274486 Cd Length: 484 Bit Score: 196.86 E-value: 5.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 662 LNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEV 741
Cdd:TIGR03240 18 RNPAT-QEVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVIARETGKPLWETRTEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 742 REAVD----FLRYYAVQ---ARNDLTNDA----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAA 810
Cdd:TIGR03240 97 ASMIGkvaiSIKAYHERtgeSENPMPDGRavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPSELTPWVAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 811 QAVRLMLEAGIPEGVLQLLPGRGETvGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDaqgrpIPLIAETGGQNAMIV 890
Cdd:TIGR03240 177 ETVKLWEKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFGGRPE-----KILALEMGGNNPLIV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 891 DSSALTEQVVIDVVSSAFDSAGQRCS-ALRVLCLQEDSADRVIEMLKGAMAESRMGN----PERLsvdIGPVIDAEAKAG 965
Cdd:TIGR03240 251 DEVADIDAAVHHIIQSAFISAGQRCTcARRLLVPDGAQGDAFLARLVEVAERLTVGAwdaePQPF---MGAVISLRAAQR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 966 I---EQHIQGMrdKGRTVYQMaiadiEECKRGT-FVMPTLIELESFDEL-EREIFGPVLHVVRYkrKDIDQLIAQINASG 1040
Cdd:TIGR03240 328 LlaaQAKLLAL--GGKSLLEM-----RQLDPGAaFLTPGIIDVTGVAELpDEEHFGPLLQVIRY--TDFDEAIAIANNTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1041 YGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAvVGVQPFGGEGLSG 1090
Cdd:TIGR03240 399 FGLSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
669-1096 |
5.87e-54 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 198.49 E-value: 5.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 669 DVVGHVQEATVEDADNAIQCA---LNVAPiWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAI-AEVREA 744
Cdd:PLN02466 84 EVIAHVAEGDAEDVNRAVAAArkaFDEGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 745 VDFLRYYAVQAR--NDLTNDA---------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV 813
Cdd:PLN02466 163 ARLFRYYAGWADkiHGLTVPAdgphhvqtlHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 814 RLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQrniagRLDAQGRPIPLIAETGGQNAMIVDSS 893
Cdd:PLN02466 243 KLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVL-----ELAAKSNLKPVTLELGGKSPFIVCED 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 894 ALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGM 973
Cdd:PLN02466 318 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 974 RDKGRTVyqmaiadieEC------KRGTFVMPTLIELESFDEL--EREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTL 1045
Cdd:PLN02466 398 VESGATL---------ECggdrfgSKGYYIQPTVFSNVQDDMLiaQDEIFGPVQSILKF--KDLDEVIRRANNTRYGLAA 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1403361070 1046 GVHT-RIDETIAKVVNNVNAGNVYVNRNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:PLN02466 467 GVFTqNLDTANTLSRALRVGTVWVNCFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
663-1049 |
8.96e-54 |
|
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: 196.08 E-value: 8.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 663 NPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKtyanAIAEVR 742
Cdd:cd07111 43 NPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK----PIRESR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 743 E-----AVDFLRYYAVQAR-NDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLM 816
Cdd:cd07111 118 DcdiplVARHFYHHAGWAQlLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEIC 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 817 LEAGIPEGVLQLLPGRGETvGARLVGDDRVKGVMFTGSTEVARLLQRNIAGrldaQGRPIPLiaETGGQNAMIVDSSALT 896
Cdd:cd07111 198 AEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAG----TGKKLSL--ELGGKSPFIVFDDADL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 897 EQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDK 976
Cdd:cd07111 271 DSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAE 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403361070 977 GRTVYQmaiADIEECKRGTFVMPTLIE-LESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHT 1049
Cdd:cd07111 351 GADVFQ---PGADLPSKGPFYPPTLFTnVPPASRIAQeEIFGPVLVVLTF--RTAKEAVALANNTPYGLAASVWS 420
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
652-1049 |
1.60e-53 |
|
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: 195.35 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 652 ASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQA-TPPAERAAILERAADLMEAEIQPLMGLLAREA 730
Cdd:cd07113 10 AGQSEKRLDITNPAT-EQVIASVASATEADVDAAVASAWRAFVSAWAkTTPAERGRILLRLADLIEQHGEELAQLETLCS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 731 GKTYANAIA-EVREAVDFLRYYAVQAR--NDLTNDA---------------HRPLGPVVCISPWNFPLAIFSGQVAAALA 792
Cdd:cd07113 89 GKSIHLSRAfEVGQSANFLRYFAGWATkiNGETLAPsipsmqgerytaftrREPVGVVAGIVPWNFSVMIAVWKIGAALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 793 AGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGEtVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAq 872
Cdd:cd07113 169 TGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTR- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 873 grpipLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSV 952
Cdd:cd07113 247 -----VTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 953 DIGPVIDAEAKAGIEQHIQGMRDKGRTVYQMAIADIEEckrGTFVMPTLIELESFDE--LEREIFGPVLHVVRYkrKDID 1030
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGE---GYFVQPTLVLARSADSrlMREETFGPVVSFVPY--EDEE 396
|
410
....*....|....*....
gi 1403361070 1031 QLIAQINASGYGLTLGVHT 1049
Cdd:cd07113 397 ELIQLINDTPFGLTASVWT 415
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
681-1050 |
1.26e-52 |
|
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: 191.25 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 681 DADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQARNDLT 760
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 761 N----DAH--------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQL 828
Cdd:cd07105 81 GsipsDKPgtlamvvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 829 L---PGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRnIAGR-LdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVV 904
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAE-TAAKhL------KPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 905 SSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRMGnperlSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQM 983
Cdd:cd07105 234 FGAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVG 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403361070 984 AIADIEEckRGTFVMPTLIE-----LESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTR 1050
Cdd:cd07105 308 GLADESP--SGTSMPPTILDnvtpdMDIYSE---ESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR 372
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
661-1050 |
1.15e-51 |
|
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: 189.44 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDLRdVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRYYAVQARN------DLTNDA-----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:cd07090 80 IDSSADCLEYYAGLAPTlsgehvPLPGGSfaytrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 810 AQAVRLMLEAGIPEGVLQLLPGRGETvGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgRPIPLiaETGGQNAMI 889
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 890 VDSSALTEQVVIDVVSSAFDSAGQRCS-ALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQ 968
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 969 HIQGMRDKGRTVYQ--MAIADIEECKRGTFVMPTLIElESFDELE---REIFGPVLHVVRYkrKDIDQLIAQINASGYGL 1043
Cdd:cd07090 312 YIESAKQEGAKVLCggERVVPEDGLENGFYVSPCVLT-DCTDDMTivrEEIFGPVMSILPF--DTEEEVIRRANDTTYGL 388
|
....*..
gi 1403361070 1044 TLGVHTR 1050
Cdd:cd07090 389 AAGVFTR 395
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
669-1096 |
2.00e-51 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 190.03 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 669 DVVGHVQEATVEDADNAIQC---ALNVAPiWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYA-NAIAEVREA 744
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAareAFDHGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 745 VDFLRYYAVQA-----------RNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV 813
Cdd:PLN02766 126 AGLLRYYAGAAdkihgetlkmsRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 814 RLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAgrlDAQGRPIPLiaETGGQNAMIVDSS 893
Cdd:PLN02766 206 HLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAA---TSNLKQVSL--ELGGKSPLLIFDD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 894 ALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGM 973
Cdd:PLN02766 281 ADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 974 RDKGRTVYQ--MAIADieeckRGTFVMPTLIE--LESFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHT 1049
Cdd:PLN02766 361 KREGATLLTggKPCGD-----KGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAGIVT 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1403361070 1050 RiDETIAKvvnnvnagnvYVNRNIVGAVVGVQ---------PFGGEGLSGTGPKAG 1096
Cdd:PLN02766 434 K-DLDVAN----------TVSRSIRAGTIWVNcyfafdpdcPFGGYKMSGFGRDQG 478
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
660-1101 |
1.15e-50 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 187.04 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 660 AVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIA 739
Cdd:PRK11241 29 DVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 740 EVREAVDFLRYYAVQARNDL--TNDAHR----------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:PRK11241 108 EISYAASFIEWFAEEGKRIYgdTIPGHQadkrlivikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 808 VAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgRPIPLiaETGGQNA 887
Cdd:PRK11241 188 SALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI----KKVSL--ELGGNAP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:PRK11241 262 FIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 968 QHIQGMRDKGRTVYQMAIADIEEckrGTFVMPT-LIELESFDELER-EIFGPVLHVVRYkrKDIDQLIAQINASGYGLTL 1045
Cdd:PRK11241 342 EHIADALEKGARVVCGGKAHELG---GNFFQPTiLVDVPANAKVAKeETFGPLAPLFRF--KDEADVIAQANDTEFGLAA 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403361070 1046 GVHTRIDETIAKVVNNVNAgnvyvnrNIVGAVVG-----VQPFGG---EGLSGTGPKAGGPLYL 1101
Cdd:PRK11241 417 YFYARDLSRVFRVGEALEY-------GIVGINTGiisneVAPFGGikaSGLGREGSKYGIEDYL 473
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
661-1050 |
2.31e-49 |
|
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: 182.62 E-value: 2.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCA----LNVApiwQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYAN 736
Cdd:cd07148 3 VVNPFD-LKPIGEVPTVDWAAIDKALDTAhalfLDRN---NWLPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 737 AIAEVREAVDFLRYYAVQARN--------DLTN-DAHR-------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAK 800
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQlggreipmGLTPaSAGRiafttrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 801 PAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGEtVGARLVGDDRVKGVMFTGSTEVARLLQRNIAgrldaQGRPIPLia 880
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-----PGTRCAL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 881 ETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDA 960
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 961 EAKAGIEQHIQGMRDKGRTVyqmaiadIEECKR--GTFVMPTLIELESFDEL--EREIFGPVlhVVRYKRKDIDQLIAQI 1036
Cdd:cd07148 311 REVDRVEEWVNEAVAAGARL-------LCGGKRlsDTTYAPTVLLDPPRDAKvsTQEIFGPV--VCVYSYDDLDEAIAQA 381
|
410
....*....|....
gi 1403361070 1037 NASGYGLTLGVHTR 1050
Cdd:cd07148 382 NSLPVAFQAAVFTK 395
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
653-1050 |
9.08e-49 |
|
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: 181.50 E-value: 9.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 653 SSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGK 732
Cdd:cd07117 12 GSSGETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 733 tyanAIAEVRE-----AVDFLRYYAVQAR------NDLTNDA-----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:cd07117 91 ----PIRETRAvdiplAADHFRYFAGVIRaeegsaNMIDEDTlsivlREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 797 VLAKPAEQTPLVAAQAVRLMLEAgIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpI 876
Cdd:cd07117 167 VVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------I 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 877 PLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGP 956
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 957 VIDAEAKAGIEQHIQGMRDKGRTVYQMAIADIE-ECKRGTFVMPTLIELESFDE--LEREIFGPVLHVVRYkrKDIDQLI 1033
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEnGLDKGFFIEPTLIVNVTNDMrvAQEEIFGPVATVIKF--KTEDEVI 397
|
410
....*....|....*..
gi 1403361070 1034 AQINASGYGLTLGVHTR 1050
Cdd:cd07117 398 DMANDSEYGLGGGVFTK 414
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
662-1050 |
5.86e-48 |
|
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: 179.23 E-value: 5.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 662 LNPSDlRDVVGHVQEATVEDADNAIQCA---LNVAPiWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAI 738
Cdd:cd07140 26 INPTD-GSVICKVSLATVEDVDRAVAAAkeaFENGE-WGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 739 -AEVREAVDFLRYYA-------------VQAR--NDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07140 104 kTHVGMSIQTFRYFAgwcdkiqgktipiNQARpnRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 803 EQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAgrlDAQGRPIPLiaET 882
Cdd:cd07140 184 QVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA---VSNLKKVSL--EL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSAD----RVIEMLKgamaESRMGNPERLSVDIGPvi 958
Cdd:cd07140 259 GGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDefvrRVVEEVK----KMKIGDPLDRSTDHGP-- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 959 dAEAKAGIEQHI----QGMRDKGRTVYQMAIADieecKRGTFVMPTL---IELESFDELErEIFGPVLHVVRYKRKDIDQ 1031
Cdd:cd07140 333 -QNHKAHLDKLVeyceRGVKEGATLVYGGKQVD----RPGFFFEPTVftdVEDHMFIAKE-ESFGPIMIISKFDDGDVDG 406
|
410
....*....|....*....
gi 1403361070 1032 LIAQINASGYGLTLGVHTR 1050
Cdd:cd07140 407 VLQRANDTEYGLASGVFTK 425
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
661-1050 |
9.54e-47 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 175.45 E-value: 9.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:TIGR01722 20 VTNPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VR---EAVDFLRYYAVQARNDLTNDAHR---------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:TIGR01722 99 VArglEVVEHACGVNSLLKGETSTQVATrvdvysirqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGaRLVGDDRVKGVMFTGSTEVARLlqrnIAGRLDAQGRPIPliAETGGQNAM 888
Cdd:TIGR01722 179 AVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRY----IHTTGSAHGKRVQ--ALGGAKNHM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQeDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQ 968
Cdd:TIGR01722 252 VVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVAS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 969 HI-QGMRDKGRTVYQMAIADIEECKRGTFVMPTLIE-----LESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYG 1042
Cdd:TIGR01722 331 LIaGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLErvpptMKAYQE---EIFGPVLCVLEA--DTLEEAIALINASPYG 405
|
....*...
gi 1403361070 1043 LTLGVHTR 1050
Cdd:TIGR01722 406 NGTAIFTR 413
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
653-1055 |
1.31e-46 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 175.71 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 653 SSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGK 732
Cdd:PLN00412 27 SSSGKSVAITNPST-RKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 733 TYANAIAEVREAVDFLRYYAVQ-------------------ARNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAA 793
Cdd:PLN00412 106 PAKDAVTEVVRSGDLISYTAEEgvrilgegkflvsdsfpgnERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 794 GNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFT-GSTEVArllqrniagrLDAQ 872
Cdd:PLN00412 186 GNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA----------ISKK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 873 GRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERlSV 952
Cdd:PLN00412 256 AGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DC 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 953 DIGPVIDAEAKAGIEQHIQGMRDKGRTVYQmaiadieECKR-GTFVMPTLIELESFDE--LEREIFGPVLHVVRYkrKDI 1029
Cdd:PLN00412 335 DITPVVSESSANFIEGLVMDAKEKGATFCQ-------EWKReGNLIWPLLLDNVRPDMriAWEEPFGPVLPVIRI--NSV 405
|
410 420
....*....|....*....|....*..
gi 1403361070 1030 DQLIAQINASGYGLTLGVHTR-IDETI 1055
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRdINKAI 432
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
652-1050 |
6.47e-46 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 173.14 E-value: 6.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 652 ASSNEAPAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAG 731
Cdd:PRK13252 17 EATSGETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 732 KTYANAI-AEVREAVDFLRYYA----------VQAR-NDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:PRK13252 96 KPIQETSvVDIVTGADVLEYYAglapalegeqIPLRgGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 800 KPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGEtVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDaqgrpiPLI 879
Cdd:PRK13252 176 KPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK------EVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCS-ALRVLcLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVI 958
Cdd:PRK13252 249 MELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 959 DAEAKAGIEQHI-QGMRDKGRTVYQMAIADIEECKRGTFVMPTLielesF----DELE---REIFGPVLHVVRYkrKDID 1030
Cdd:PRK13252 328 SFAHRDKVLGYIeKGKAEGARLLCGGERLTEGGFANGAFVAPTV-----FtdctDDMTivrEEIFGPVMSVLTF--DDED 400
|
410 420
....*....|....*....|
gi 1403361070 1031 QLIAQINASGYGLTLGVHTR 1050
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTA 420
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
662-1096 |
1.95e-45 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 172.33 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 662 LNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEV 741
Cdd:PLN02315 39 VNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 742 REAVDFLRYYAVQAR------------NDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:PLN02315 118 QEIIDMCDFAVGLSRqlngsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 810 AQAVRLMLEA----GIPEGVLQLLPGrGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqGRpipLIAETGGQ 885
Cdd:PLN02315 198 IAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GK---CLLELSGN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 886 NAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAG 965
Cdd:PLN02315 271 NAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 966 IEQHIQGMRDKG-RTVYQMAIADIEeckrGTFVMPTLIELE-SFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGL 1043
Cdd:PLN02315 351 FEKGIEIIKSQGgKILTGGSAIESE----GNFVQPTIVEISpDADVVKEELFGPVLYVMKF--KTLEEAIEINNSVPQGL 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1403361070 1044 TLGVHTRIDETIAKVVNNVNAGNVYVNRNIV--GAVVGvQPFGGEGLSGTGPKAG 1096
Cdd:PLN02315 425 SSSIFTRNPETIFKWIGPLGSDCGIVNVNIPtnGAEIG-GAFGGEKATGGGREAG 478
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
705-1050 |
1.14e-43 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 164.52 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 705 AAILERAADLMEaeiqplmgLLAREAGKTYANAIAEVREAVDFLRYYAVQAR--------NDLTNDA----HRPLGPVVC 772
Cdd:PRK10090 6 AGIRERASEISA--------LIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegeiiqSDRPGENillfKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 773 ISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFT 852
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 853 GSTEvarllqrniAGR--LDAQGRPIPLIA-ETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSAD 929
Cdd:PRK10090 158 GSVS---------AGEkiMAAAAKNITKVClELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 930 RVIEMLKGAMAESRMGNP-ERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVyqmAIADIEECKRGTFVMPTLIE--LES 1006
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARV---ALGGKAVEGKGYYYPPTLLLdvRQE 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1403361070 1007 FDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTR 1050
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQ 347
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
674-1050 |
2.01e-43 |
|
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: 165.70 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 674 VQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAI-AEVREAVDFLRYYA 752
Cdd:cd07116 32 VPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 753 VQAR------NDLTNDA-----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAgI 821
Cdd:cd07116 112 GCIRaqegsiSEIDENTvayhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-L 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 822 PEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQvvi 901
Cdd:cd07116 191 PPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI------IPVTLELGGKSPNIFFADVMDAD--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 902 dvvSSAFDSA-----------GQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHI 970
Cdd:cd07116 262 ---DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 971 QGMRDKGRTVYQ-MAIADIEECKRGTFVMPTLI----ELESFDElerEIFGPVLHVVRYkrKDIDQLIAQINASGYGLTL 1045
Cdd:cd07116 339 DIGKEEGAEVLTgGERNELGGLLGGGYYVPTTFkggnKMRIFQE---EIFGPVLAVTTF--KDEEEALEIANDTLYGLGA 413
|
....*
gi 1403361070 1046 GVHTR 1050
Cdd:cd07116 414 GVWTR 418
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
658-1050 |
9.79e-43 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 162.98 E-value: 9.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 658 PAAVLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANA 737
Cdd:PRK09406 2 PIATINPAT-GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 738 IAEVREAVDFLRYYAVQARN---DLTNDA-----------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEAllaDEPADAaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 804 QTPLVAAQAVRLMLEAGIPEGVLQ-LLPGRGETvgARLVGDDRVKGVMFTGStevarllqrNIAGRLDAQ--GRPI-PLI 879
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGS---------EPAGRAVAAiaGDEIkKTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVID 959
Cdd:PRK09406 230 LELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 960 AEAKAGIEQHIQGMRDKGRTVYqmaiadieeC------KRGTFVMPTLI-----ELESFDElerEIFGPVLHVvrYKRKD 1028
Cdd:PRK09406 310 EQGRDEVEKQVDDAVAAGATIL---------CggkrpdGPGWFYPPTVItditpDMRLYTE---EVFGPVASL--YRVAD 375
|
410 420
....*....|....*....|..
gi 1403361070 1029 IDQLIAQINASGYGLTLGVHTR 1050
Cdd:PRK09406 376 IDEAIEIANATTFGLGSNAWTR 397
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
651-1050 |
2.41e-41 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 160.06 E-value: 2.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 651 CASSNEAPAAVLNPSDLRDVvGHVQEATVEDADNAIQCALNV--APIWQATPPAERAAILERAADLMEAEIQPLMGLLAR 728
Cdd:PRK09847 29 TAAAENETFETVDPVTQAPL-AKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 729 EAGKTYANAIAE-VREAVDFLRYYAVQA-----------RNDLTNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:PRK09847 108 DTGKPIRHSLRDdIPGAARAIRWYAEAIdkvygevattsSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 797 VLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNiAGrlDAQGRPI 876
Cdd:PRK09847 188 VILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKD-AG--DSNMKRV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 877 PLiaETGGQNAMIV--DSSALtEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDI 954
Cdd:PRK09847 265 WL--EAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 955 GPVIDAEAKAGIEQHIQGMRDKGRTvyqmaIADIEECKRGTFVMPT-LIELESFDELER-EIFGPVLHVVRYKRKdiDQL 1032
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKGQL-----LLDGRNAGLAAAIGPTiFVDVDPNASLSReEIFGPVLVVTRFTSE--EQA 414
|
410
....*....|....*...
gi 1403361070 1033 IAQINASGYGLTLGVHTR 1050
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTR 432
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
661-1047 |
2.48e-41 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 159.90 E-value: 2.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCA-----LNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYA 735
Cdd:PLN02467 27 VVNPAT-EETIGDIPAATAEDVDAAVEAArkafkRNKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 736 NAIAEVREAVDFLRYYAVQARN-DLTNDA--------------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAK 800
Cdd:PLN02467 106 EAAWDMDDVAGCFEYYADLAEAlDAKQKApvslpmetfkgyvlKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 801 PAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgRPIPLia 880
Cdd:PLN02467 186 PSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMV----KPVSL-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 881 ETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDA 960
Cdd:PLN02467 260 ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 961 EAKAGIEQHIQGMRDKGRTVYQMAIADiEECKRGTFVMPTLI-ELESFDELER-EIFGPVLHVVRYKRKdiDQLIAQINA 1038
Cdd:PLN02467 340 GQYEKVLKFISTAKSEGATILCGGKRP-EHLKKGFFIEPTIItDVTTSMQIWReEVFGPVLCVKTFSTE--DEAIELAND 416
|
....*....
gi 1403361070 1039 SGYGLTLGV 1047
Cdd:PLN02467 417 SHYGLAGAV 425
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
661-1042 |
4.67e-35 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 142.96 E-value: 4.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 661 VLNPSDlRDVVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAE 740
Cdd:PLN02419 133 VINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 741 VREAVDFLRY-----------YAVQARNDL-TNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:PLN02419 212 IFRGLEVVEHacgmatlqmgeYLPNVSNGVdTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 809 AAQAVRLMLEAGIPEGVLQLLPGRGETVGArLVGDDRVKGVMFTGSTEVArllqRNIAGRLDAQGRPIPliAETGGQNAM 888
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAG----MHIYARAAAKGKRIQ--SNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSA---DRVIEMLKgAMAESRMGNPErlsVDIGPVIDAEAKAG 965
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVERAK-ALKVTCGSEPD---ADLGPVISKQAKER 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 966 IEQHIQ-GMRDKGRTVYQMAIADIEECKRGTFVMPTLI-----ELESFDElerEIFGPVLhvVRYKRKDIDQLIAQINAS 1039
Cdd:PLN02419 441 ICRLIQsGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILsgvtpDMECYKE---EIFGPVL--VCMQANSFDEAISIINKN 515
|
...
gi 1403361070 1040 GYG 1042
Cdd:PLN02419 516 KYG 518
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
683-1049 |
4.69e-35 |
|
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: 140.37 E-value: 4.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 683 DNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYA--------VQ 754
Cdd:cd07129 2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFAdlvregswLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 755 ARNDLTNDA------------HRPLGPVVCISPWNFPLAiFS---GQVAAALAAGNPVLAK--PA--EQTPLVAAQAVRL 815
Cdd:cd07129 82 ARIDPADPDrqplprpdlrrmLVPLGPVAVFGASNFPLA-FSvagGDTASALAAGCPVVVKahPAhpGTSELVARAIRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 816 MLEAGIPEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDaqgrPIPLIAETGGQNAMIVDSSAL 895
Cdd:cd07129 161 LRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGSVNPVFILPGAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 896 TE---QVVIDVVSSAFDSAGQRCSALRVLCLQEDSA-DRVIEMLKGAMAES---RMGNPerlsvdigPVIDA--EAKAGI 966
Cdd:cd07129 237 AErgeAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAApaqTMLTP--------GIAEAyrQGVEAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 967 EQHiqgmrDKGRTVYQMAIADIEECKRGTFVMPTLIELESFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLG 1046
Cdd:cd07129 309 AAA-----PGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLADPALQEEVFGPASLVVRY--DDAAELLAVAEALEGQLTAT 381
|
...
gi 1403361070 1047 VHT 1049
Cdd:cd07129 382 IHG 384
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
764-1092 |
7.66e-35 |
|
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: 138.81 E-value: 7.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLmLEAGIPEGVLQLLPGrGETVGARLVgD 843
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEG-GVEVATALL-A 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 844 DRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCL 923
Cdd:cd07087 175 EPFDHIFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 924 QEDSADRVIEMLKGAMAEsRMGNPERLSVDIGPVIDaeakagiEQHIQGMRD--KGRTVYQMAIADIEECkrgtFVMPTL 1001
Cdd:cd07087 249 HESIKDELIEELKKAIKE-FYGEDPKESPDYGRIIN-------ERHFDRLASllDDGKVVIGGQVDKEER----YIAPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1002 IELESFDE--LEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRiDETIAKVVNNVNAGnvyvnrnivGAV-- 1077
Cdd:cd07087 317 LDDVSPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSE-DKAVQERVLAETSS---------GGVcv 384
|
330 340
....*....|....*....|...
gi 1403361070 1078 ------VGVQ--PFGGEGLSGTG 1092
Cdd:cd07087 385 ndvllhAAIPnlPFGGVGNSGMG 407
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
670-1096 |
3.10e-33 |
|
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: 135.12 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 670 VVGHVQEATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANA-IAEVREAVDFL 748
Cdd:cd07098 8 HLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEILVTCEKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 749 RY--------YAVQARNDLTNDAHR-------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV 813
Cdd:cd07098 88 RWtlkhgekaLRPESRPGGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 814 RLMLEA----GIPEGVLQLLPGRGETvGARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMI 889
Cdd:cd07098 168 SIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 890 VDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQH 969
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 970 IQGMRDKG-RTVYQMAIADIEECKRGTFVMPTLIE--LESFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLG 1046
Cdd:cd07098 321 VADAVEKGaRLLAGGKRYPHPEYPQGHYFPPTLLVdvTPDMKIAQEEVFGPVMVVMKA--SDDEEAVEIANSTEYGLGAS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403361070 1047 VHTRIDETIAKvvnnvnagnvyVNRNIVGAVVGVQ-----------PFGGEGLSGTGPKAG 1096
Cdd:cd07098 399 VFGKDIKRARR-----------IASQLETGMVAINdfgvnyyvqqlPFGGVKGSGFGRFAG 448
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
677-1056 |
7.53e-32 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 130.75 E-value: 7.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 677 ATVEDADNAIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYA---- 752
Cdd:PRK13968 26 AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAehgp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 753 --VQARNDLTND-----AHRPLGPVVCISPWNFPL-AIFSGQVAAALAaGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEG 824
Cdd:PRK13968 106 amLKAEPTLVENqqaviEYRPLGTILAIMPWNFPLwQVMRGAVPILLA-GNGYLLKHAPNVMGCAQLIAQVFKDAGIPQG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 825 VLQLLPGRGETVgARLVGDDRVKGVMFTGSTEVARLLQRNIAGRLDAqgrpipLIAETGGQNAMIVDSSALTEQVVIDVV 904
Cdd:PRK13968 185 VYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDPFIVLNDADLELAVKAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 905 SSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTvyqMA 984
Cdd:PRK13968 258 AGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGAR---LL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403361070 985 IADIEECKRGTFVMPTLI-----ELESFDElerEIFGPVLHVVryKRKDIDQLIAQINASGYGLTLGVHTrIDETIA 1056
Cdd:PRK13968 335 LGGEKIAGAGNYYAPTVLanvtpEMTAFRE---ELFGPVAAIT--VAKDAEHALELANDSEFGLSATIFT-TDETQA 405
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
704-1097 |
1.16e-30 |
|
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: 126.57 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 704 RAAILERAADLMEAeiqplmglLAREAGKTYA--------NAIAEVREAVDFLRYYA--VQARNDLTNDA------HRPL 767
Cdd:cd07134 30 KKAILARREEIIAA--------LAADFRKPAAevdlteilPVLSEINHAIKHLKKWMkpKRVRTPLLLFGtkskirYEPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 768 GPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVlQLLPGRGETVGARLvgDDRVK 847
Cdd:cd07134 102 GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEGDAEVAQALL--ELPFD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 848 GVMFTGSTEVARLLQRNIAGRLdaqgRPIPLiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDS 927
Cdd:cd07134 179 HIFFTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 928 ADRVIEMLKGAMAESRMGNPERL-SVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQMAIADIEECkrgtFVMPTLIE--L 1004
Cdd:cd07134 253 KDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR----YIAPTVLTnvT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1005 ESFDELEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAVVGVQPFG 1084
Cdd:cd07134 329 PDMKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFG 406
|
410
....*....|...
gi 1403361070 1085 GEGLSGTGpKAGG 1097
Cdd:cd07134 407 GVNNSGIG-SYHG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
685-1049 |
7.13e-30 |
|
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: 124.66 E-value: 7.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 685 AIQCALNVAPIWQATPPAERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYAVQAR-------- 756
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSyriphepg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 757 ----NDLTNDAHR---PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGI-PEGVLQL 828
Cdd:cd07084 84 nhlgQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 829 LPGRGETvGARLVGDDRVKGVMFTGSTEVARLLqrniagRLDAqgRPIPLIAETGGQNAMIVDSSALTEQVVID-VVSSA 907
Cdd:cd07084 164 INGDGKT-MQALLLHPNPKMVLFTGSSRVAEKL------ALDA--KQARIYLELAGFNWKVLGPDAQAVDYVAWqCVQDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 908 FDSAGQRCSALRVLCLQEDSADR-VIEMLKGAMAESRMGnperlSVDIGPVIDAEAKAGIEQhiqgMRDKGRTV------ 980
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQTFTTLAMIAH----MENLLGSVllfsgk 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403361070 981 ---YQMAIADIEECKRGTFVMPTLIELESFDELEREIFGPVLHVVRYKRKDIDQLIAQINASGYGLTLGVHT 1049
Cdd:cd07084 306 elkNHSIPSIYGACVASALFVPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYS 377
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
766-1092 |
2.65e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 120.52 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVaAQAVRLMLEAGIPEGVLQLLPGrGETVGARLVgDDR 845
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT-SKLMAKLLTKYLDPSYVRVIEG-GVEVTTELL-KEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 846 VKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQE 925
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 926 DSADRVIEMLKGAMAEsRMGNPERLSVDIGPVIDaeakagiEQHIQGM----RDKGRTVYQMAIADIEEckrgTFVMPTL 1001
Cdd:PTZ00381 260 SIKDKFIEALKEAIKE-FFGEDPKKSEDYSRIVN-------EFHTKRLaeliKDHGGKVVYGGEVDIEN----KYVAPTI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1002 IELESFDE--LEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRiDETIAKVVNNVNAGNVYVNRNIVGAVVG 1079
Cdd:PTZ00381 328 IVNPDLDSplMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGE-DKRHKELVLENTSSGAVVINDCVFHLLN 404
|
330
....*....|....
gi 1403361070 1080 VQ-PFGGEGLSGTG 1092
Cdd:PTZ00381 405 PNlPFGGVGNSGMG 418
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
764-1092 |
2.54e-27 |
|
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: 116.94 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAgIPEGVLQLLPGRGETVGARLvgD 843
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 844 DRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALR-VLC 922
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIAEAAAKHL------TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDyVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 923 lQEDSADRVIEMLKGAMAESRMGNPERLSvDIGPVIDAEAKAGIEQHIQgmRDKGRTVYQmaiADIEECKRgtFVMPTLI 1002
Cdd:cd07135 257 -DPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLD--TTKGKVVIG---GEMDEATR--FIPPTIV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 1003 ELESFDE--LEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTR----IDETIAKvvnnvnAGNVYVNRNIVGA 1076
Cdd:cd07135 328 SDVSWDDslMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDdkseIDHILTR------TRSGGVVINDTLI 399
|
330
....*....|....*...
gi 1403361070 1077 VVGVQ--PFGGEGLSGTG 1092
Cdd:cd07135 400 HVGVDnaPFGGVGDSGYG 417
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
764-1092 |
1.84e-25 |
|
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: 111.04 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAqAVRLMLEAGIPEGVLQLLPGRGEtVGA---RL 840
Cdd:cd07133 99 YQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSA-LLAELLAEYFDEDEVAVVTGGAD-VAAafsSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 841 VGDDrvkgVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRV 920
Cdd:cd07133 177 PFDH----LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 921 LCLQEDSADRVIEMLKGAMAE---SRMGNPerlsvDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQMAIADIEECKRGTFV 997
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKmypTLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDFAATRKLP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 998 mPTLIeLESFDE---LEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRIDETIAKvvnnvnagnvYVNRNIV 1074
Cdd:cd07133 322 -PTLV-LNVTDDmrvMQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDR----------VLRRTHS 387
|
330 340
....*....|....*....|....*...
gi 1403361070 1075 GAV--------VGV--QPFGGEGLSGTG 1092
Cdd:cd07133 388 GGVtindtllhVAQddLPFGGVGASGMG 415
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
702-1057 |
4.22e-25 |
|
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: 111.21 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 702 AERAAILERAADLMEAEIQPLMGLLAReAGKTYANAIAEVREAVDFLRYYAVQARNDLTNDAHRPLGPV----------- 770
Cdd:cd07128 59 HERAAMLKALAKYLMERKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVeplskdgtfvg 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 771 -----------VCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGI-PEGVLQLLPGRGETVGA 838
Cdd:cd07128 138 qhiltprrgvaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLD 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 839 RLVGDDRVKgvmFTGSTEVARLLQRNIAgrldAQGRPIPLIAETGGQNAMIV--DSSALTEQ---VVIDVVSSAFDSAGQ 913
Cdd:cd07128 218 HLGEQDVVA---FTGSAATAAKLRAHPN----IVARSIRFNAEADSLNAAILgpDATPGTPEfdlFVKEVAREMTVKAGQ 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 914 RCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVID----AEAKAGIEQHIQG--MRDKGRTVYQMAIAD 987
Cdd:cd07128 291 KCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSreqrEDVRAAVATLLAEaeVVFGGPDRFEVVGAD 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403361070 988 IEeckRGTFVMPTLIELESFDEL----EREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRIDETIAK 1057
Cdd:cd07128 371 AE---KGAFFPPTLLLCDDPDAAtavhDVEAFGPVATLMPY--DSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
702-1025 |
3.06e-22 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 102.48 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 702 AERAAILERAADLMEAEIQPLMGLLAREAGKTYANAIAEVREAVDFLRYYA-----------------VQ-ARNDLTNDA 763
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalgdarllrdgeaVQlGKDPAFQGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 764 H--RPL-GPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGI-PEGVLQLLPGRGETVGAR 839
Cdd:PRK11903 143 HvlVPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 840 LVGDDRVKgvmFTGSTEVARLLQRNIAgrldAQGRPIPLIAETGGQNAMI-----VDSSALTEQVVIDVVSSAFDSAGQR 914
Cdd:PRK11903 223 LQPFDVVS---FTGSAETAAVLRSHPA----VVQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 915 CSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVY---QMAIADIEEC 991
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFdggGFALVDADPA 375
|
330 340 350
....*....|....*....|....*....|....*...
gi 1403361070 992 KrGTFVMPTLIELESFDEL----EREIFGPVLHVVRYK 1025
Cdd:PRK11903 376 V-AACVGPTLLGASDPDAAtavhDVEVFGPVATLLPYR 412
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
704-1038 |
1.13e-21 |
|
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: 99.89 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 704 RAAILERAADLMEAeiqplmglLAREAGK----TYANAIA----EVREAVDFLRYYA--VQARNDLTNDAHR------PL 767
Cdd:cd07136 30 KQAIKKYENEILEA--------LKKDLGKsefeAYMTEIGfvlsEINYAIKHLKKWMkpKRVKTPLLNFPSKsyiyyePY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 768 GPVVCISPWNFP--LAIfsGQVAAALAAGNPVLAKPAEQTPLVAAqAVRLMLEAGIPEGVLQLLPGRGETVGARLvgDDR 845
Cdd:cd07136 102 GVVLIIAPWNYPfqLAL--APLIGAIAAGNTAVLKPSELTPNTSK-VIAKIIEETFDEEYVAVVEGGVEENQELL--DQK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 846 VKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQE 925
Cdd:cd07136 177 FDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 926 DSADRVIEMLKGAmAESRMGNPERLSVDIGPVIDaeakagiEQH---IQGMRDKGRTVYQmAIADIEEckrgTFVMPTLI 1002
Cdd:cd07136 251 SVKEKFIKELKEE-IKKFYGEDPLESPDYGRIIN-------EKHfdrLAGLLDNGKIVFG-GNTDRET----LYIEPTIL 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 1403361070 1003 ELESFDE--LEREIFGPVLHVVRYkrKDIDQLIAQINA 1038
Cdd:cd07136 318 DNVTWDDpvMQEEIFGPILPVLTY--DTLDEAIEIIKS 353
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
725-1047 |
2.31e-20 |
|
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: 96.41 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 725 LLAREAGKTYANAIAEVREAVDFLRYYA-----VQARNDLTNDAHR---------PLGPVVCISPWNFPLAIFSGQVAAA 790
Cdd:cd07126 87 LIQRVAPKSDAQALGEVVVTRKFLENFAgdqvrFLARSFNVPGDHQgqqssgyrwPYGPVAIITPFNFPLEIPALQLMGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 791 LAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGaRLVGDDRVKGVMFTGSTEVARLLQRNIAGRLD 870
Cdd:cd07126 167 LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPRMTLFTGSSKVAERLALELHGKVK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 871 aqgrpiplIAETGgqnamiVDSSALTEQVV-IDVVS-----SAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRm 944
Cdd:cd07126 246 --------LEDAG------FDWKILGPDVSdVDYVAwqcdqDAYACSGQKCSAQSILFAHENWVQAGILDKLKALAEQR- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 945 gNPERLSvdIGPVIDAEAKAgIEQH------IQGMRDK--GRTVYQMAIADIEECKRGTFVMPTLIEL---ESFDELERE 1013
Cdd:cd07126 311 -KLEDLT--IGPVLTWTTER-ILDHvdkllaIPGAKVLfgGKPLTNHSIPSIYGAYEPTAVFVPLEEIaieENFELVTTE 386
|
330 340 350
....*....|....*....|....*....|....
gi 1403361070 1014 IFGPVLHVVRYKRKDIDQLIAQINASGYGLTLGV 1047
Cdd:cd07126 387 VFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAV 420
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
766-1092 |
5.84e-20 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 94.79 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAqavrlMLEAGIPE----GVLQLLPGrGETVGARLV 841
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPKyldsKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 842 gDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVD---SSALTEQVVIDVVSSAFDS-AGQRCSA 917
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 918 LRVLCLQEDSADRVIEMLKgAMAESRMGNPERLSVDIGPVIDaeakagiEQHIQGMRD--KGRTVyQMAI---ADIEECK 992
Cdd:PLN02203 255 IDYVLVEERFAPILIELLK-STIKKFFGENPRESKSMARILN-------KKHFQRLSNllKDPRV-AASIvhgGSIDEKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 993 rgTFVMPTLIELESFDE--LEREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRiDETIAKVVNNVNAGNVYVN 1070
Cdd:PLN02203 326 --LFIEPTILLNPPLDSdiMTEEIFGPLLPIITV--KKIEDSIAFINSKPKPLAIYAFTN-NEKLKRRILSETSSGSVTF 400
|
330 340
....*....|....*....|...
gi 1403361070 1071 RN-IVGAVVGVQPFGGEGLSGTG 1092
Cdd:PLN02203 401 NDaIIQYACDSLPFGGVGESGFG 423
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
764-1092 |
3.81e-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: 91.90 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEqtplVAAQAVRLMLE---------------AGIPEgVLQL 828
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE----VSPATAKLLAElipkyldkecypvvlGGVEE-TTEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 829 LpgrgetvgarlvgDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAF 908
Cdd:cd07132 173 L-------------KQRFDYIFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAWGKF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 909 DSAGQRCSALR-VLCLQEdSADRVIEMLKGAMAESrMGNPERLSVDIGPVIDAEAKagieQHIQGMRDKGRTVY--QMai 985
Cdd:cd07132 234 INAGQTCIAPDyVLCTPE-VQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHF----QRLKKLLSGGKVAIggQT-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 986 aDIEECkrgtFVMPT-LIELESFDEL-EREIFGPVLHVVRYkrKDIDQLIAQINASGYGLTLGVHTRIDETIAKVVNNVN 1063
Cdd:cd07132 306 -DEKER----YIAPTvLTDVKPSDPVmQEEIFGPILPIVTV--NNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTS 378
|
330 340
....*....|....*....|....*....
gi 1403361070 1064 AGNVYVNRNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07132 379 SGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
87-134 |
1.89e-18 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 79.82 E-value: 1.89e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1403361070 87 SVLRAAITSAYRRPEPEVVPMLLEQARLPAPMAEATQALAASIAEKLR 134
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
766-1092 |
4.89e-18 |
|
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: 88.62 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAA------------QAVRLmLEAGIPEGVlQLLpgrg 833
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSAllaklipeyldtKAIKV-IEGGVPETT-ALL---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 834 etvgarlvgDDRVKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDS-AG 912
Cdd:cd07137 175 ---------EQKWDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 913 QRCSALRVLCLQEDSADRVIEMLKgAMAESRMGNPERLSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQMAIADieeck 992
Cdd:cd07137 240 QACIAPDYVLVEESFAPTLIDALK-NTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDE----- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 993 RGTFVMPTLIELESFDEL--EREIFGPVLHVVryKRKDIDQLIAQINASGYGLTLGVHTRIDETIAKVVNNVNAGNVYVN 1070
Cdd:cd07137 314 KNLYIEPTILLDPPLDSSimTEEIFGPLLPII--TVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN 391
|
330 340
....*....|....*....|..
gi 1403361070 1071 RNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07137 392 DTVVQYAIDTLPFGGVGESGFG 413
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-45 |
1.61e-13 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 66.77 E-value: 1.61e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1403361070 2 ATTTLGVKLDDPTRERLKAAATSIDRTPHWLIKQAIFNYLEKLE 45
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREE 44
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
766-1022 |
1.60e-12 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 71.62 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLmLEAGIPEGVLQLLPGRGETVGARLvgDDR 845
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 846 VKGVMFTGSTEVARLLQRNIAGRLdaqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFD-SAGQRCSALRVLCLQ 924
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 925 EDSADRVIEMLKGAMAESRMGNPERlSVDIGPVIDAEAKAGIEQHIQGMRDKGRTVYQmAIADIEECKrgtfVMPTLIEL 1004
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYG-GEKDRENLK----IAPTILLD 336
|
250 260
....*....|....*....|
gi 1403361070 1005 ESFDEL--EREIFGPVLHVV 1022
Cdd:PLN02174 337 VPLDSLimSEEIFGPLLPIL 356
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
681-1077 |
6.42e-12 |
|
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: 69.81 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 681 DADNAIQCALNVAPIWQATPPAERAA----ILERAADLMEAEIQPLMG------LLAREAGKTYA-----NAIAEVREAV 745
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGvcleILQRLNARSFEMAHAVMHttgqafMMAFQAGGPHAqdrglEAVAYAWREM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 746 DFL----RYYAVQARND-LTNDAH-----RPLGPVVCISP---WNFPLAIFsgqvaAALAAGNPVLAKPAEQTPLVAAQA 812
Cdd:cd07127 165 SRIpptaEWEKPQGKHDpLAMEKTftvvpRGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAIT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 813 VR----LMLEAGI-PEGVLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNIAGrldAQgrpipLIAETGGQNA 887
Cdd:cd07127 240 VQvareVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQ-----VYTEKAGVNT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 888 MIVDSsalTEQVVIDVVSSAFDSA---GQRCSALRVLCLQED---------SADRVIEMLkGAMAESRMGNPERLSVDIG 955
Cdd:cd07127 312 VVVDS---TDDLKAMLRNLAFSLSlysGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADL-AAAIDGLLADPARAAALLG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 956 PVIDAEAKAGIEQHIQGmrdkGRTVYQMAIADIEECKRGTFVMPTLIELESFDE--LEREIFGPVLHVVRYKRKD--IDQ 1031
Cdd:cd07127 388 AIQSPDTLARIAEARQL----GEVLLASEAVAHPEFPDARVRTPLLLKLDASDEaaYAEERFGPIAFVVATDSTDhsIEL 463
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1403361070 1032 LIAQINASGyGLTLGVHTRIDETIAKVVNNVNAGNVYVNRNIVGAV 1077
Cdd:cd07127 464 ARESVREHG-AMTVGVYSTDPEVVERVQEAALDAGVALSINLTGGV 508
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
175-558 |
8.00e-10 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 62.80 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 175 DKGTRDALIRDKISTGNWHPH----LGNSPSLFVNAATWGLL---------LTGKLVsTHNEAGLTSSLSRIIGKSGEPM 241
Cdd:PLN02681 1 PAGPAATVPPAVTSTTTPASDdvldFSDHAALFAGLSTSELLrsllvlqlcAIGPLV-DLGEWLLTSPLMVLGRAIVLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 242 IRKGVdmamrlmGEQFVTGETIAEALANATRFEAKGFR----YSYDMLGEAALTEHDAQKYLASYEQAIHSIGKAS---- 313
Cdd:PLN02681 80 VKATF-------YSHFCAGEDAEEAARTVRRLWELGLGgildYAAEDAGDNAACDRNLEKFLAAIRAAATLPPSSSsaav 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 314 ---------------------HGRGIYEGPGI--SIKLSALH-PRYS--------RAQYERVMEELYPRLLSLTLLAKQY 361
Cdd:PLN02681 153 kitalcppsllervsdllrwqDRDPNGKLPWKqwSFPLFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 362 DIGLNIDAEEAdRLELSLDlleRLCFEPQLSGWNGIGF-----VIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYW 436
Cdd:PLN02681 233 GVPLLIDAEYT-SLQPAID---YITYDLAREFNKGKDRpivygTYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 437 DSEIKRAQVEGLEGyPVYTRKVYTDVSYIACARKLL--AVPEAIYPQFATHNAQTLAAIYHIA---GQNYYPGQYEFQCL 511
Cdd:PLN02681 309 SLERRLAASLGVPS-PVHDTIQDTHACYNRCAEFLLekASNGDGEVMLATHNVESGELAAAKMnelGLHKGDPRVQFAQL 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1403361070 512 HGMGEPLyeqvvgkvSEGKLNRPCRV--YAPVGTHETLLAYLVRRLLEN 558
Cdd:PLN02681 388 LGMSDNL--------SFGLGNAGFRVskYLPYGPVEEVIPYLLRRAEEN 428
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-45 |
3.27e-09 |
|
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar proteins; This family includes the N-terminal ribbon-helix-helix (RHH) domain of Shewanella oneidensis CopA(SO), a newly identified type II antitoxin, as well as the N-terminal RHH domain of Escherichia coli PutA flavoprotein, among other similar proteins, many of which are as yet uncharacterized. CopA(SO) is a typical RHH antitoxin that includes an ordered N-terminal domain (CopA(SO)-N) and a disordered C-terminal domain (CopA(SO)-C). Biophysical investigation indicates allosteric effects of CopA(SO)-N on CopA(SO)-C; DNA binding of CopA(SO)-N appears to induce CopA(SO)-C to fold and self-associate the C-terminal domain. The multifunctional E. coli proline utilization A (PutA) flavoprotein functions as a membrane-associated proline catabolic enzyme as well as a transcriptional repressor of the proline utilization genes putA and putP. The N-terminal domain of PutA is a transcriptional regulator with an RHH fold; structure studies show that it forms a homodimer to bind one DNA duplex. This family also includes orphan antitoxin ParD2, an antitoxin component of a non-functional type II toxin-antitoxin (TA system); it does not neutralize the effect of any of the RelE or ParE toxins.
Pssm-ID: 409023 Cd Length: 44 Bit Score: 53.53 E-value: 3.27e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1403361070 4 TTLGVKLDDPTRERLKAAATSIDRTPHWLIKQAIFNYLEKLE 45
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREE 42
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
671-967 |
4.23e-09 |
|
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: 60.31 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 671 VGHVQEATVEDAdnaiQCALNVAPIWQATPPAERAAILERAADLMEAE---IQPLMGLLAREAGKTYANAIAEVR-EAVD 746
Cdd:cd07077 5 NAQRTLAVNHDE----QRDLIINAIANALYDTRQRLASEAVSERGAYIrslIANWIAMMGCSESKLYKNIDTERGiTASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 747 FLRYYAVQARNDLTNDAHRPLGPVVCISPWNFPLA-IFSgqVAAALAAGNPVLAKPAEQTPlVAAQAVRLMLEAGIPEG- 824
Cdd:cd07077 81 GHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLSgITS--ALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 825 ---VLQLLPGRGETVGARLVGDDRVKGVMFTGSTEVARLLQRNiagrldaqGRPIPLIAETGGQNAMIVDSSALTEQVVI 901
Cdd:cd07077 158 pkiLVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASG 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403361070 902 DVVSSA-FDSAGqrCSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07077 230 SVHDSKfFDQNA--CASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFDDEALE 294
|
|
| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-45 |
4.95e-07 |
|
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins; This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.
Pssm-ID: 409020 Cd Length: 42 Bit Score: 47.50 E-value: 4.95e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1403361070 4 TTLGVKLDDPTRERLKAAATSIDRTPHWLIKQAIFNYLEKLE 45
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLERLE 42
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
766-1057 |
8.62e-04 |
|
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: 43.41 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGvlqllpgrgetvgarlvGDDR 845
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAG-----------------APEN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 846 VKGVMFTGSTEVA-RLLQRNIAGRLDAQGRPI----------PLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQR 914
Cdd:cd07081 158 LIGWIDNPSIELAqRLMKFPGIGLLLATGGPAvvkaayssgkPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 915 CSALRVLCLQEDSADRVIEMLKGAMAESRMGNPERlsvDIGPVI--DAEAKAGIeqhiqgmrdKGRTVYQMAIADIEECK 992
Cdd:cd07081 238 CASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQ---QVQPVIlkNGDVNRDI---------VGQDAYKIAAAAGLKVP 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403361070 993 RGTFVMptLIELESFDELE---REIFGPVLHVVRYKRKDIDQLIAQ--INASGYGLTLGVHTRIDETIAK 1057
Cdd:cd07081 306 QETRIL--IGEVTSLAEHEpfaHEKLSPVLAMYRAANFADADAKALalKLEGGCGHTSAMYSDNIKAIEN 373
|
|
| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
1-45 |
1.10e-03 |
|
Predicted DNA-binding protein with an HTH domain [General function prediction only];
Pssm-ID: 443745 Cd Length: 76 Bit Score: 39.11 E-value: 1.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1403361070 1 MATTTlgVKLDDPTRERLKAAATSIDRTPHWLIKQAIFNYLEKLE 45
Cdd:COG4710 1 MKMLS--IRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
|
|
| |
