|
Name |
Accession |
Description |
Interval |
E-value |
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
1-1352 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 2314.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1 MGATTTGIKMDEALRQRVRLAADRLGRTPHWLIKQATLNMVEHIERGEFSLDT-LSSTEKPSQPGTPHDEPEGAtyptpf 79
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELpALLSGAANESEEADTPAEEP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 80 stpfPTPFLDWAQNVLPQTDLRAAITAAWHRPEPECLPMLIELAQIPDATQRAAvRQMAERLVEGVRARREMGG----VE 155
Cdd:PRK11809 75 ----HQPFLEFAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAA-HKLAYQLAEKLRNQKSAGGragmVQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 156 ALVQEFSLSSQEGVALMCLAEALLRIPDNATRDALIRDKISRGDWQAHLGHSPSVFVNAAVWGLMLTGRLTATTSEKGLA 235
Cdd:PRK11809 150 GLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 236 SALSRLIGKGGEPLIRQGVQRAMRLMGEQFVTGQTIAEALANSRPQEKKGFRYSYDMLGEAAITEADAQRYFTAYEQALH 315
Cdd:PRK11809 230 SSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 316 AIGKASHGRGIFEGPGLSVKLSALHPRYTRAQYARVMDELLPRLTALVELARRYDVGINIDAEEADRLELSLDLLETLCF 395
Cdd:PRK11809 310 AIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 396 NPALKGWNGIGFVVQAYQKRCPFVIDYLIDLARRSGHRLMVRLVKGAYWDSEIKRAQIDGLDGYPVYTRKVHTDVSYLAC 475
Cdd:PRK11809 390 EPELAGWNGIGFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLAC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 476 AHKLLAAPDAAYPQFATHNAQTVASIMQMAGENYYAGQYEFQCLHGMGEPLYDQVVGPVSAGKLARPCRIYAPVGTHDTL 555
Cdd:PRK11809 470 ARKLLAVPNLIYPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 556 LAYLVRRLLENGANTSFVNRIGDDAVPVSELVTDPVDEARAIAVETSVLGAPHPRIPLPRQLFsglgAQARLNSAGLNLA 635
Cdd:PRK11809 550 LAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLY----GKGRANSAGLDLA 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 636 NEQQLASLSAALLRSAQHMAYASPTVAEqpPPADNAQAaavgwvPVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPI 715
Cdd:PRK11809 626 NEHRLASLSSALLASAHQKWQAAPMLED--PVAAGEMS------PVINPADPRDIVGYVREATPAEVEQALESAVNAAPI 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 716 WQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQFDNATHRPLGVVLCISP 795
Cdd:PRK11809 698 WFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISP 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 796 WNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGST 875
Cdd:PRK11809 778 WNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGST 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 876 EVAQLISRTVSKRLSPQGRSIVLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMI 955
Cdd:PRK11809 858 EVARLLQRNLAGRLDPQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKML 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 956 RDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESG--GLGTFVRPTLIELDTIDRLQREVF 1033
Cdd:PRK11809 938 RGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEdwQSGTFVPPTLIELDSFDELKREVF 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1034 GPVLHVLRYRREQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKA 1113
Cdd:PRK11809 1018 GPVLHVVRYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKA 1097
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1114 GGPLYLHRLVQPLPQANSALPANLAAAAAecskitpePASLAALRDLLAAVQNHTMNLDDEdTTRAQAACEHYLAHSPIS 1193
Cdd:PRK11809 1098 GGPLYLYRLLATRPEDALAVTLARQDAEY--------PVDAQLRAALLAPLTALREWAAER-EPELAALCDQYAELAQAG 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1194 SVYTLPGPTGESNRYRLLPRsGGVWCIPQTVLGLVHHIAATLATGNLALIeapSPDSPLATFLDALPPAVKAYVRSCPPT 1273
Cdd:PRK11809 1169 TTRLLPGPTGERNTYTLLPR-ERVLCLADTEQDALTQLAAVLAVGSQALW---PDDALHRALVAALPAAVQARIQLAKDW 1244
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294339260 1274 QRDAlPELSVVLFEGDADALARLQDQLAQRDGLILRIESLRPaqlaDGAMMDLTALVHEQSLSVNTAAAGGNAQLMTLG 1352
Cdd:PRK11809 1245 QLAD-QPFDAVLFHGDSDQLRALCEQVAQRDGPIVSVQGFAR----GETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
86-1352 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1896.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 86 PFLDWAQNVLPQTDLRAAITAAWHRPEPECLPMLIELAQIPDAtQRAAVRQMAERLVEGVRARREMGGVEALVQEFSLSS 165
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDE-ARAAIRERARKLVEALRAKRKGTGVEALLQEYSLSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 166 QEGVALMCLAEALLRIPDNATRDALIRDKISRGDWQAHLGHSPSVFVNAAVWGLMLTGRLTATTSEKGLASALSRLIGKG 245
Cdd:PRK11905 80 QEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIARL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 246 GEPLIRQGVQRAMRLMGEQFVTGQTIAEALANSRPQEKKGFRYSYDMLGEAAITEADAQRYFTAYEQALHAIGKASHGRG 325
Cdd:PRK11905 160 GEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 326 IFEGPGLSVKLSALHPRYTRAQYARVMDELLPRLTALVELARRYDVGINIDAEEADRLELSLDLLETLCFNPALKGWNGI 405
Cdd:PRK11905 240 VYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 406 GFVVQAYQKRCPFVIDYLIDLARRSGHRLMVRLVKGAYWDSEIKRAQIDGLDGYPVYTRKVHTDVSYLACAHKLLAAPDA 485
Cdd:PRK11905 320 GFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 486 AYPQFATHNAQTVASIMQMAGENYyagQYEFQCLHGMGEPLYDQVVGPvsaGKLARPCRIYAPVGTHDTLLAYLVRRLLE 565
Cdd:PRK11905 400 IYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGK---EKLGRPCRIYAPVGTHETLLAYLVRRLLE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 566 NGANTSFVNRIGDDAVPVSELVTDPVDEARAIAVetsvlgAPHPRIPLPRQLFsglgAQARLNSAGLNLANEQQLASLSA 645
Cdd:PRK11905 474 NGANSSFVNRIVDENVPVEELIADPVEKVAAMGV------APHPQIPLPRDLY----GPERRNSKGLDLSDEATLAALDE 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 646 ALLRSAQHMAYASPTVAEQPPPadnaqaaaVGWVPVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERA 725
Cdd:PRK11905 544 ALNAFAAKTWHAAPLLAGGDVD--------GGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERA 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 726 ACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQFDNATHRPLGVVLCISPWNFPLSIFCG 805
Cdd:PRK11905 616 AILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTG 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 806 QVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTV 885
Cdd:PRK11905 696 QIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTL 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 886 SKRLSPQgrsIVLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLG 965
Cdd:PRK11905 776 AKRSGPP---VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIG 852
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 966 NPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGGLGTFVRPTLIELDTIDRLQREVFGPVLHVLRYRRE 1045
Cdd:PRK11905 853 DPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKAD 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1046 QLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLVQP 1125
Cdd:PRK11905 933 ELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1126 LPQansalpanlaaaaaecskitpEPASLAALRDLLAAVQNHTMNLDDEDTTRAQAACEHYLAHSPISSVYTLPGPTGES 1205
Cdd:PRK11905 1013 APT---------------------PIPPAHESVDTDAAARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGES 1071
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1206 NRYRLLPRsGGVWCIPQTVLGLVHHIAATLATGNLALIEApspDSPLATFLDALPPAVKAYVRSCPPTQRDAlpELSVVL 1285
Cdd:PRK11905 1072 NLLSLHPR-GRVLCVADTEEALLRQLAAALATGNVAVVAA---DSGLAAALADLPGLVAARIDWTQDWEADD--PFAGAL 1145
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294339260 1286 FEGDADALARLQDQLAQRDGLILRIESLRPaqladGAMMDLTALVHEQSLSVNTAAAGGNAQLMTLG 1352
Cdd:PRK11905 1146 LEGDAERARAVRQALAARPGAIVPLIAAEP-----TDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
100-1124 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1511.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 100 LRAAITAAWHRPEPECLPMLIELAQIPDAtQRAAVRQMAERLVEGVRAR-REMGGVEALVQEFSLSSQEGVALMCLAEAL 178
Cdd:PRK11904 13 LRAAISALYRVDEAAYLRELLELAPLSPE-EKARVTARATQLVEAVRAKkKKLGGIDAFLQEYSLSTEEGIALMCLAEAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 179 LRIPDNATRDALIRDKISRGDWQAHLGHSPSVFVNAAVWGLMLTGRLTATTSEKG--LASALSRLIGKGGEPLIRQGVQR 256
Cdd:PRK11904 92 LRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADgtPSGVLKRLVNRLGEPVIRKAMRQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 257 AMRLMGEQFVTGQTIAEALANSRPQEKKGFRYSYDMLGEAAITEADAQRYFTAYEQALHAIGKASHGRGIFEGPGLSVKL 336
Cdd:PRK11904 172 AMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADLPARPGISIKL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 337 SALHPRYTRAQYARVMDELLPRLTALVELARRYDVGINIDAEEADRLELSLDLLETLCFNPALKGWNGIGFVVQAYQKRC 416
Cdd:PRK11904 252 SALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLAVQAYQKRA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 417 PFVIDYLIDLARRSGHRLMVRLVKGAYWDSEIKRAQIDGLDGYPVYTRKVHTDVSYLACAHKLLAAPDAAYPQFATHNAQ 496
Cdd:PRK11904 332 LPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAIYPQFATHNAH 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 497 TVASIMQMAGEnyyaGQYEFQCLHGMGEPLYDQVVgpvsaGKLARPCRIYAPVGTHDTLLAYLVRRLLENGANTSFVNRI 576
Cdd:PRK11904 412 TVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSFVHRL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 577 GDDAVPVSELVTDPVDEARAIAvetsvlGAPHPRIPLPRQLFSGlgaqARLNSAGLNLANEQQLASLSAALLRSAQHMAY 656
Cdd:PRK11904 483 VDPDVPIEELVADPVEKLRSFE------TLPNPKIPLPRDIFGP----ERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 657 ASPTVaeqpppaDNAQAAAvgwvPVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALE 736
Cdd:PRK11904 553 AGPII-------NGEGEAR----PVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLE 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 737 QQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQFDNATH-------------RPLGVVLCISPWNFPLSIF 803
Cdd:PRK11904 622 ANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKlpgptgesnelrlHGRGVFVCISPWNFPLAIF 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 804 CGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISR 883
Cdd:PRK11904 702 LGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINR 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 884 TVSKRlspQGRSIVLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWS 963
Cdd:PRK11904 782 TLAAR---DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELK 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 964 LGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGGLGTFVRPTLIELDTIDRLQREVFGPVLHVLRYR 1043
Cdd:PRK11904 859 VGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYK 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1044 REQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLV 1123
Cdd:PRK11904 939 ASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFA 1018
|
.
gi 294339260 1124 Q 1124
Cdd:PRK11904 1019 T 1019
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
85-1349 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1401.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 85 TPFLDWAQNVLPQTDLRAAITAAWHRPEPECLPMLiELAQIPDATQRAAVRQMAERLVEGVRARREMGGVEALVQEFSLS 164
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAAL-LAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 165 SQEGVALMCLAEALLRIPDNATRDALIRDKISRGDWQAHLGHSPSVFVNAAVWGLMLTGRLTATTSEKGLASALSRLIGK 244
Cdd:COG4230 80 SSEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 245 GGEPLIRQGVQRAMRLMGEQFVTGQTIAEALANSRPQEKKGFRYSYDMLGEAAITEADAQRYFTAYEQALHAIGKASHGR 324
Cdd:COG4230 160 LGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 325 GIFEGPGLSVKLSALHPRYTRAQYARVMDELLPRLTALVELARRYDVGINIDAEEADRLELSLDLLETLCFNPALKGWNG 404
Cdd:COG4230 240 SGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 405 IGFVVQAYQKRCPFVIDYLIDLARRSGHRLMVRLVKGAYWDSEIKRAQIDGLDGYPVYTRKVHTDVSYLACAHKLLAAPD 484
Cdd:COG4230 320 GGGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 485 AAYPQFATHNAQTVASIMQMAGENYYAGQYEFQCLHGMGEPLYDQVVgpvsAGKLARPCRIYAPVGTHDTLLAYLVRRLL 564
Cdd:COG4230 400 AAQPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVG----RGKLGRPCRIYAPVGSHEDLLAYLVRRLL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 565 ENGANTSFVNRIGDDAVPVSELVTDPVDEARAIAvetsvlGAPHPRIPLPRQLFsglgAQARLNSAGLNLANEQQLASLS 644
Cdd:COG4230 476 ENGANSSFVNRIADEDVPVEELIADPVEKARALG------GAPHPRIPLPRDLY----GPERRNSAGLDLSDEAVLAALS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 645 AALLRSAQHMAYASPTVAEQPPPADnaqaaavgWVPVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGER 724
Cdd:COG4230 546 AALAAAAEKQWQAAPLIAGEAASGE--------ARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 725 AACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQFDNAT-HRPLGVVLCISPWNFPLSIF 803
Cdd:COG4230 618 AAILERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvLRGRGVFVCISPWNFPLAIF 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 804 CGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISR 883
Cdd:COG4230 698 TGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINR 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 884 TVSKRlspQGRSIVLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWS 963
Cdd:COG4230 778 TLAAR---DGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELR 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 964 LGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGGLGTFVRPTLIELDTIDRLQREVFGPVLHVLRYR 1043
Cdd:COG4230 855 VGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYK 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1044 REQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLV 1123
Cdd:COG4230 935 ADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFA 1014
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1124 QPLPQANsalpanlaaaaaecskitpepaslaalRDLLAAVQNHTMNLDDEDTTRAQAAcehylahspissvyTLPGPTG 1203
Cdd:COG4230 1015 TERTVTV---------------------------NTTAAGGNASLLALGDWLASLLGAL--------------TLPGPTG 1053
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1204 ESNRYRLLPRsGGVWCIPQTVLGLVHHIAATLATGNLALIEAPSPdsplatfLDALPPAVkayvrscpptqrdaLPELSV 1283
Cdd:COG4230 1054 ERNTLTLRPR-GRVLCLADSLEALLAQLAAALATGNRAVVAADLA-------LAGLPAVL--------------LPPFDA 1111
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1284 VLFEGDADALARlqdQLAQRDGLILRIEslrpaqladGAMMDLTALVHEqslsvntaaAGGNAQLM 1349
Cdd:COG4230 1112 VLFEGRLRALRQ---ALAARDGAIVPVI---------DAGYDLERLLEE---------AGGNASLM 1156
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
126-1130 |
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: 654.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 126 PDATQRAAVRQMAERLVEGVRARREmGGVEALVQEFSLSSQEGVALMCLAEALLRIPDNATRDALIRDKISrgdwqahlg 205
Cdd:COG0506 5 LDEALRARAVALARRLVEAIRAAPE-GGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 206 HSPSVFVNAAVWGLMLTgrltattsekglasalsrLIGKGGEPLIRQGVQRAMRLMGEQFVTGQTIAEALANSRPQEKKG 285
Cdd:COG0506 75 KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 286 FRYSYDMLGEAAITEADAQRYFTAYEQALHAIGKAShgrgiFEGPGLSVKLSALHPRYTRAQYARVMDELLPRLTALVEL 365
Cdd:COG0506 137 YRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 366 ARRYDVGINIDAEEADRLELSLDLLETLCFNPALKGWNGIGFVVQAYQKRCPFVIDYLIDLARRSGHRLMVRLVKGAYWD 445
Cdd:COG0506 212 AREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAYWD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 446 SEIKRAQIDGLDgYPVYTRKVHTDVSYLACAHKLLAAPDAAYPQFATHNAQTVASIMQMAGE-NYYAGQYEFQCLHGMGE 524
Cdd:COG0506 292 PEIVRAQVHGWP-YPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQMLYGMGE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 525 PLYDQVVGpVSAGKLARPCRIYAPVGTHDTLLAYLVRRLLENGANTSFVNRIGDDAVPVSELVTDPVDEARAIAVetsvl 604
Cdd:COG0506 371 DLQRALAA-VDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAP----- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 605 gAPHPRIPLPRQLFsglgAQARLNSAGLNLANEQQLASLSAALLRSAQhmayasptvAEQPPPADNAQAAAVGWVPVLNP 684
Cdd:COG0506 445 -TPPPPPPLRRQRR----RRRRARGGALAAALAAAAAAAALAAAAAAA---------AALAAAAAGAAAAAAAAAVAVVP 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 685 ADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREA 764
Cdd:COG0506 511 AAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAA 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 765 VDFLRYYAAQTAAQFDNATHRPLGVVL---------CISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHA 835
Cdd:COG0506 591 AAAAAAAAAAAAARAAAPPPPPPGGLVallplgplaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAL 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 836 LHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQGRSIVLIAETGGQNALIADSSAL 915
Cdd:COG0506 671 AALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAA 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 916 AEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQA 995
Cdd:COG0506 751 AAVAAVAASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELG 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 996 AGLCVTRLGRDESGGLGTFVRPTLIELDTIDRLQREVFGPVLHVLRYRR-EQLGAVLDAINATGYGLTFGVHSRIDETVA 1074
Cdd:COG0506 831 EEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALdLAALIGLGLTGGLLGGGGGIVGRRGGGGGA 910
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1075 ELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLVQPLPQAN 1130
Cdd:COG0506 911 GGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATA 966
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
621-1124 |
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: 626.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 621 LGAQARLNSAGLNLANEQQLASLSAALLRSAQHMAYASPTVAEQPPPADNAQaaavgwvPVLNPADPRDQVGWVRQTTRT 700
Cdd:TIGR01238 2 LYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQ-------PVTNPADRRDIVGQVFHANLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 701 EVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQFD 780
Cdd:TIGR01238 75 HVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 781 NATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAAL 860
Cdd:TIGR01238 155 EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 861 VAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQGRsivLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRL 940
Cdd:TIGR01238 235 TSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVP---LIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 941 LCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGGL--GTFVRPT 1018
Cdd:TIGR01238 312 LCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACqhGTFVAPT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1019 LIELDTIDRLQREVFGPVLHVLRYRREQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGV 1098
Cdd:TIGR01238 392 LFELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGV 471
|
490 500
....*....|....*....|....*.
gi 294339260 1099 QPFGGMGRSGTGPKAGGPLYLHRLVQ 1124
Cdd:TIGR01238 472 QPFGGQGLSGTGPKAGGPHYLYRLTQ 497
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
640-1123 |
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: 615.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 640 LASLSAALLRSAQHMAYASPTVAEQPPPADNAQaaavgwvPVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVT 719
Cdd:cd07125 16 LEALADALKAFDEKEWEAIPIINGEETETGEGA-------PVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 720 PPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQF------------DNATHRPL 787
Cdd:cd07125 89 PVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFsdpelpgptgelNGLELHGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 788 GVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVA 867
Cdd:cd07125 169 GVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 868 GVMFTGSTEVAQLISRTVSKRLSPQgrsIVLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDV 947
Cdd:cd07125 249 GVIFTGSTETAKLINRALAERDGPI---LPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 948 ADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGGlgTFVRPTLIELDTIDR 1027
Cdd:cd07125 326 AERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNG--YFVAPGIIEIVGIFD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1028 LQREVFGPVLHVLRYRREQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRS 1107
Cdd:cd07125 404 LTTEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLS 483
|
490
....*....|....*.
gi 294339260 1108 GTGPKAGGPLYLHRLV 1123
Cdd:cd07125 484 GTGPKAGGPNYLLRFG 499
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
274-575 |
1.89e-155 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 469.67 E-value: 1.89e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 274 ALANSRPQEKKGFRYSYDMLGEAAITEADAQRYFTAYEQALHAIGKASHGRGIFEGPGLSVKLSALHPRYTRAQYARVMD 353
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 354 ELLPRLTALVELARRYDVGINIDAEEADRLELSLDLLETLCFNPALKGWNGIGFVVQAYQKRCPFVIDYLIDLARRSGHR 433
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 434 LMVRLVKGAYWDSEIKRAQIdGLDGYPVYTRKVHTDVSYLACAHKLLAAPDAAYPQFATHNAQTVASIMQMAGE-NYYAG 512
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294339260 513 QYEFQCLHGMGEPLYDQVVgpvsagKLARPCRIYAPVGTHDTLLAYLVRRLLENGANTSFVNR 575
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALV------AAGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
682-1131 |
2.16e-130 |
|
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: 411.59 E-value: 2.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 682 LNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEV 761
Cdd:cd07083 37 VSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 762 REAVDFLRYYAAQtAAQF-------------DNAT-HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTAL 827
Cdd:cd07083 117 AEAIDFIRYYARA-ALRLrypavevvpypgeDNESfYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 828 IAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQGRSIVLIAETGGQNA 907
Cdd:cd07083 196 VGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 908 LIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLE 987
Cdd:cd07083 276 IIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 988 AHIARMQAAGLCVTRLGRDEsgGLGTFVRPTLIELDT--IDRLQREVFGPVLHVLRYRREQLGAVLDAINATGYGLTFGV 1065
Cdd:cd07083 356 SYIEHGKNEGQLVLGGKRLE--GEGYFVAPTVVEEVPpkARIAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGV 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1066 HSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLVQPLPQANS 1131
Cdd:cd07083 434 YSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEMKAVAER 499
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
680-1125 |
9.40e-113 |
|
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: 364.24 E-value: 9.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG 759
Cdd:cd07124 49 ESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAAQ----------TAAQFDNATH-RPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALI 828
Cdd:cd07124 129 DVAEAIDFLEYYAREmlrlrgfpveMVPGEDNRYVyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 829 AAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQGRSIVLIAETGGQNAL 908
Cdd:cd07124 209 AAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 909 IADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEA 988
Cdd:cd07124 289 IVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 989 HIARMQAAGLCVTRLGRDESGGLGTFVRPTLIE-LDTIDRL-QREVFGPVLHVLRYRreQLGAVLDAINATGYGLTFGVH 1066
Cdd:cd07124 369 YIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFAdVPPDHRLaQEEIFGPVLAVIKAK--DFDEALEIANDTEYGLTGGVF 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 294339260 1067 SRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLVQP 1125
Cdd:cd07124 447 SRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQP 505
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
673-1115 |
3.86e-108 |
|
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: 350.58 E-value: 3.86e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 673 AAAVGWVPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGK 752
Cdd:COG1012 17 AASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 753 TLPDAIGEVREAVDFLRYYAAQ-----------TAAQFDNATHR-PLGVVLCISPWNFPLSIFCGqvaaalaagnavlaK 820
Cdd:COG1012 96 PLAEARGEVDRAADFLRYYAGEarrlygetipsDAPGTRAYVRRePLGVVGAITPWNFPLALAAWklapalaagntvvlK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 821 PAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIA 900
Cdd:COG1012 176 PAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKR------VTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 901 ETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDA 980
Cdd:COG1012 250 ELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 981 EARDNLEAHIARMQAAGLCVTRLGRDESGGLGTFVRPTLIE-LDTIDRL-QREVFGPVLHVLRYRREQlgAVLDAINATG 1058
Cdd:COG1012 330 AQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLAdVTPDMRIaREEIFGPVLSVIPFDDEE--EAIALANDTE 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 294339260 1059 YGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGvQPFGGMGRSGTGPKAGG 1115
Cdd:COG1012 408 YGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
679-1120 |
6.39e-105 |
|
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: 341.05 E-value: 6.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:pfam00171 9 IEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRYYAA-------QTAAQFDNAT----HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTAL 827
Cdd:pfam00171 88 GEVDRAIDVLRYYAGlarrldgETLPSDPGRLaytrREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 828 IAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNA 907
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKR------VTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 908 LIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLE 987
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 988 AHIARMQAAGL-CVTrlGRDESGGLGTFVRPTLIE-LDTIDRLQR-EVFGPVLHVLRYRREQlgavlDAI---NATGYGL 1061
Cdd:pfam00171 322 KYVEDAKEEGAkLLT--GGEAGLDNGYFVEPTVLAnVTPDMRIAQeEIFGPVLSVIRFKDEE-----EAIeiaNDTEYGL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 294339260 1062 TFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVqPFGGMGRSGTGpKAGGPLYLH 1120
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLE 451
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
703-1121 |
8.60e-99 |
|
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: 323.01 E-value: 8.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 703 DEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQ-------- 774
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLarrlhgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 775 ---TAAQFDNAT-HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVP 850
Cdd:cd07078 81 ipsPDPGELAIVrREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 851 GDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNALIADSSALAEQLVADVLTSAFDS 930
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKR------VTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 931 AGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGG 1010
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1011 LGTFVRPTLIE-LDTIDRL-QREVFGPVLHVLRYRREQLgaVLDAINATGYGLTFGVHSRiDETVA-ELSERIHAGNVYV 1087
Cdd:cd07078 315 KGYFVPPTVLTdVDPDMPIaQEEIFGPVLPVIPFKDEEE--AIELANDTEYGLAAGVFTR-DLERAlRVAERLEAGTVWI 391
|
410 420 430
....*....|....*....|....*....|....
gi 294339260 1088 NRNLIGAVVGvQPFGGMGRSGTGpKAGGPLYLHR 1121
Cdd:cd07078 392 NDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEE 423
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
657-1125 |
1.62e-95 |
|
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: 316.81 E-value: 1.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 657 ASPTVAEQ-----PPPADNAQAAAVGWVPVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRA 731
Cdd:TIGR01237 21 ALATVKEQlgktyPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 732 ADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQT---AAQ-----FDNATHR----PLGVVLCISPWNFP 799
Cdd:TIGR01237 101 AAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMielAKGkpvnsREGETNQyvytPTGVTVVISPWNFP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 800 LSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQ 879
Cdd:TIGR01237 181 FAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 880 LISRTVSKRLSPQGRSIVLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAM 959
Cdd:TIGR01237 261 RIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEIT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 960 DDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVtrLGRDESGGLGTFVRPTLI-ELDTIDRL-QREVFGPVL 1037
Cdd:TIGR01237 341 ESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLV--SGGCGDDSKGYFIGPTIFaDVDRKARLaQEEIFGPVV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1038 HVLRYRREQlgAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPL 1117
Cdd:TIGR01237 419 AFIRASDFD--EALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPD 496
|
....*...
gi 294339260 1118 YLHRLVQP 1125
Cdd:TIGR01237 497 YLALFMQA 504
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
679-1119 |
8.90e-92 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 306.48 E-value: 8.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:PRK03137 52 IVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRYYAAQT------------AAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA 826
Cdd:PRK03137 132 ADTAEAIDFLEYYARQMlkladgkpvesrPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 827 LIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISrTVSKRLSPQGRSIV-LIAETGGQ 905
Cdd:PRK03137 212 VIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIY-ERAAKVQPGQIWLKrVIAEMGGK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 906 NALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRmHTDLGPVIDAEARDN 985
Cdd:PRK03137 291 DAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 986 LEAHIARMQAAGLCVTRLGRDESGGLgtFVRPTLI-ELDTIDRL-QREVFGPVLHVLRYRREQlgAVLDAINATGYGLTF 1063
Cdd:PRK03137 370 IMSYIEIGKEEGRLVLGGEGDDSKGY--FIQPTIFaDVDPKARImQEEIFGPVVAFIKAKDFD--HALEIANNTEYGLTG 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1064 GVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYL 1119
Cdd:PRK03137 446 AVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYL 501
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
674-1116 |
9.28e-81 |
|
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: 274.13 E-value: 9.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 674 AAVGWVPVLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKT 753
Cdd:cd07097 11 AGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 754 LPDAIGEVREAVDFLRYYAAQT--------AAQFDNA---THR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKP 821
Cdd:cd07097 91 LPEARGEVTRAGQIFRYYAGEAlrlsgetlPSTRPGVeveTTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 822 AEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRlspqGRSIVLiaE 901
Cdd:cd07097 171 AELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR----GARVQL--E 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 902 TGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAE 981
Cdd:cd07097 245 MGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSER 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 982 ARDNLEAHI--ARMQAAGLcVTRLGRDESGGLGTFVRPTLIELDTID-RLQR-EVFGPVLHVLRYRreQLGAVLDAINAT 1057
Cdd:cd07097 325 QLEKDLRYIeiARSEGAKL-VYGGERLKRPDEGYYLAPALFAGVTNDmRIAReEIFGPVAAVIRVR--DYDEALAIANDT 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 294339260 1058 GYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVqPFGGMGRSGTGPKAGGP 1116
Cdd:cd07097 402 EFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
682-1116 |
1.11e-73 |
|
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: 254.19 E-value: 1.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 682 LNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEV 761
Cdd:cd07131 19 RNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 762 REAVDFLRYYAAQT------------AAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIA 829
Cdd:cd07131 99 QEAIDMAQYAAGEGrrlfgetvpselPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 830 AALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRlspqGRSIVLiaETGGQNALI 909
Cdd:cd07131 179 LKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP----NKRVAL--EMGGKNPII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 910 ADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAH 989
Cdd:cd07131 253 VMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 990 --IARMQAAGLCVTRLGRDESGGL-GTFVRPTLIELDTIDR--LQREVFGPVLHVLRYRR-EQLGAVLdaiNATGYGLTF 1063
Cdd:cd07131 333 neIGKEEGATLLLGGERLTGGGYEkGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEVSSlEEAIEIA---NDTEYGLSS 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 294339260 1064 GVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVqPFGGMGRSGTGPKAGGP 1116
Cdd:cd07131 410 AIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
707-1125 |
1.85e-72 |
|
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: 246.76 E-value: 1.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 707 RRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQ-----------T 775
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLadklggpelpsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 776 AAQFDNAT-HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGG 854
Cdd:cd06534 81 DPGGEAYVrREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 855 TVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQR 934
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKP------VTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 935 CSALRLLCIQEDVADRVIGMirdamddwslgnpdrmhtdLGPVIDAEARDNLEAHiarmqaaglcvtrlgrdesgglgtf 1014
Cdd:cd06534 235 CTAASRLLVHESIYDEFVEK-------------------LVTVLVDVDPDMPIAQ------------------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1015 vrptlieldtidrlqREVFGPVLHVLRYRREQLgaVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGA 1094
Cdd:cd06534 271 ---------------EEIFGPVLPVIRFKDEEE--AIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV 333
|
410 420 430
....*....|....*....|....*....|.
gi 294339260 1095 VVGvQPFGGMGRSGTGpKAGGPLYLHRLVQP 1125
Cdd:cd06534 334 GPE-APFGGVKNSGIG-REGGPYGLEEYTRT 362
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
672-1114 |
6.22e-72 |
|
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: 249.02 E-value: 6.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 672 QAAAVGWVPVLNPADPRDQVGwVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAG 751
Cdd:cd07086 8 VGSGGETFTSRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 752 KTLPDAIGEVREAVDfLRYYAAQTAAQFDNAT-------HR------PLGVVLCISPWNFPLSIF---------CGQvaa 809
Cdd:cd07086 87 KILPEGLGEVQEMID-ICDYAVGLSRMLYGLTipserpgHRlmeqwnPLGVVGVITAFNFPVAVPgwnaaialvCGN--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 810 alaagnAVLAKPAEQTALIAAAL----VHALHAAGVPTDAVQLVPGdGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTV 885
Cdd:cd07086 163 ------TVVWKPSETTPLTAIAVtkilAEVLEKNGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 886 SKRLspqGRSivlIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLG 965
Cdd:cd07086 236 ARRF---GRV---LLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 966 NPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCV----TRLGRDESgglGTFVRPTLIELDTIDR--LQREVFGPVLHV 1039
Cdd:cd07086 310 DPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVltggKRIDGGEP---GNYVEPTIVTGVTDDAriVQEETFAPILYV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1040 LRYRREQlgavlDAI---NATGYGLTFGVHSRiDETVAELSER---IHAGNVYVNRNLIGAVVGVqPFGGMGRSGTGPKA 1113
Cdd:cd07086 387 IKFDSLE-----EAIainNDVPQGLSSSIFTE-DLREAFRWLGpkgSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRES 459
|
.
gi 294339260 1114 G 1114
Cdd:cd07086 460 G 460
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
681-1110 |
1.47e-67 |
|
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: 235.50 E-value: 1.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADPrDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:cd07106 1 VINPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVDFLRYYAAQTA---AQFDNAT------HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAA 831
Cdd:cd07106 80 VGGAVAWLRYTASLDLpdeVIEDDDTrrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 832 LVHALHAAgVPTDAVQLVPGdGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLspqgRSIVLiaETGGQNALI-- 909
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGNDAAIvl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 910 --ADSSALAEQLVAdvltSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLE 987
Cdd:cd07106 232 pdVDIDAVAPKLFW----GAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 988 AHIARMQAAGLCVTRLGRDESGGlGTFVRPTLI-ELDTIDRL-QREVFGPVLHVLRYRREQlgAVLDAINATGYGLTFGV 1065
Cdd:cd07106 308 ELVEDAKAKGAKVLAGGEPLDGP-GYFIPPTIVdDPPEGSRIvDEEQFGPVLPVLKYSDED--EVIARANDSEYGLGASV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 294339260 1066 HSRIDETVAELSERIHAGNVYVNRnlIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07106 385 WSSDLERAEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
681-1110 |
7.98e-66 |
|
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: 230.58 E-value: 7.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADPRDqVGWVRQTTRTEVDEATRRAQSAAPIWQV-TPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG 759
Cdd:cd07109 1 VFDPSTGEV-FARIARGGAADVDRAVQAARRAFESGWLrLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAAQT----------AAQFDNATHR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALI 828
Cdd:cd07109 80 DVEAAARYFEYYGGAAdklhgetiplGPGYFVYTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 829 AAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGGQNAL 908
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVP----VTL--ELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 909 IADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGnPDRMHTDLGPVIDAEARDNLEA 988
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 989 HIARMQAAGLCVTRLGRDESGGL--GTFVRPTLI-ELDTIDRL-QREVFGPVLHVLRYRREQlgavlDAI---NATGYGL 1061
Cdd:cd07109 313 FVARARARGARIVAGGRIAEGAPagGYFVAPTLLdDVPPDSRLaQEEIFGPVLAVMPFDDEA-----EAIalaNGTDYGL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 294339260 1062 TFGVHSRIDETVAELSERIHAGNVYVNRnlIGAVVGVQ-PFGGMGRSGTG 1110
Cdd:cd07109 388 VAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
154-265 |
1.29e-65 |
|
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: 216.99 E-value: 1.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 154 VEALVQEFSLSSQEGVALMCLAEALLRIPDNATRDALIRDKISRGDWQAHLGHSPSVFVNAAVWGLMLTGRLTATTSEKG 233
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 294339260 234 LASALSRLIGKGGEPLIRQGVQRAMRLMGEQF 265
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
681-1110 |
1.31e-65 |
|
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: 230.01 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:cd07103 1 VINPAT-GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVDFLRYYAAQTA--------AQFDNA----THRPLGVVLCISPWNFPLSIF-----------CgqvaaalaagnAV 817
Cdd:cd07103 80 VDYAASFLEWFAEEARriygrtipSPAPGKrilvIKQPVGVVAAITPWNFPAAMItrkiapalaagC-----------TV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 818 LAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISR----TVsKRLSPqg 893
Cdd:cd07103 149 VLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAqaadTV-KRVSL-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 894 rsivliaETGGQNALIADSSALAEQLVADVLTSAFDSAGQRC-SALRLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHT 972
Cdd:cd07103 226 -------ELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCvCANRIY-VHESIYDEFVEKLVERVKKLKVGNGLDEGT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 973 DLGPVIDAEARDNLEAHIARMQAAGL-CVTRLGRDESGGLgtFVRPTLIE--LDTIDRLQREVFGPVLHVLRYRREQlga 1049
Cdd:cd07103 298 DMGPLINERAVEKVEALVEDAVAKGAkVLTGGKRLGLGGY--FYEPTVLTdvTDDMLIMNEETFGPVAPIIPFDTED--- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294339260 1050 vlDAI---NATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVvgVQPFGGMGRSGTG 1110
Cdd:cd07103 373 --EVIaraNDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
681-1126 |
2.69e-65 |
|
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: 231.32 E-value: 2.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADAL------EQQMQNLLGlivreAGKTL 754
Cdd:cd07123 50 QVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgkyryELNAATMLG-----QGKNV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 755 PDA-IGEVREAVDFLR---YYAAQTAAQ---------FDNATHRPL-GVVLCISPWNFPlSIFCGQVAAALAAGNAVLAK 820
Cdd:cd07123 125 WQAeIDAACELIDFLRfnvKYAEELYAQqplsspagvWNRLEYRPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 821 PAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLS-----PQgrs 895
Cdd:cd07123 204 PSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPR--- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 896 ivLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLG 975
Cdd:cd07123 281 --IVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 976 PVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGGLGTFVRPTLIEL-DTIDRL-QREVFGPVLHVLRYRREQLGAVLDA 1053
Cdd:cd07123 359 AVIDEKAFDRIKGYIDHAKSDPEAEIIAGGKCDDSVGYFVEPTVIETtDPKHKLmTEEIFGPVLTVYVYPDSDFEETLEL 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1054 INATG-YGLTFGVHSRIDETVAELSERIH--AGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLVQPL 1126
Cdd:cd07123 439 VDTTSpYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPR 514
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
681-1114 |
3.45e-65 |
|
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: 228.97 E-value: 3.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADprDQVgW--VRQTTRTEVDEATRRAQSA--APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPD 756
Cdd:cd07114 1 SINPAT--GEP-WarVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 757 AIGEVREAVDFLRYYAA------------QTAAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQ 824
Cdd:cd07114 78 TRAQVRYLAEWYRYYAGladkiegavipvDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 825 TALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGG 904
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAP------VTLELGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALIADSSALAEQLVADVLTSAFDSAGQRCSA-LRLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEAR 983
Cdd:cd07114 232 KSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAgSRLL-VQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 984 DNLEAHIARMQAAG-LCVTRLGRDESGGL--GTFVRPTLIELDTIDR--LQREVFGPVLHVLRYRREQlgavlDAI---N 1055
Cdd:cd07114 311 EKVERYVARAREEGaRVLTGGERPSGADLgaGYFFEPTILADVTNDMriAQEEVFGPVLSVIPFDDEE-----EAIalaN 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294339260 1056 ATGYGLTFGVHSRiDETVA-ELSERIHAGNVYVN--RnligAVVGVQPFGGMGRSGTGPKAG 1114
Cdd:cd07114 386 DSEYGLAAGIWTR-DLARAhRVARAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
673-1110 |
1.09e-64 |
|
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: 227.92 E-value: 1.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 673 AAAVGWVPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGK 752
Cdd:cd07088 9 SSSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 753 TLPDAIGEVREAVDFLRYYAAQT------AAQFDNA------THRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAK 820
Cdd:cd07088 88 TLSLARVEVEFTADYIDYMAEWArriegeIIPSDRPnenifiFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 821 PAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIA 900
Cdd:cd07088 168 PSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK------VSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 901 ETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDA 980
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 981 EARDNLEAHIARMQAAGLCVTRLGRDESGGLGTFVRPTLIE--LDTIDRLQREVFGPVLHVLRYRreQLGAVLDAINATG 1058
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKFS--SLDEAIELANDSE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 294339260 1059 YGLTFGVHSRIDETVAELSERIHAGNVYVNRnliGAVVGVQPF-GGMGRSGTG 1110
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINR---ENFEAMQGFhAGWKKSGLG 449
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
679-1110 |
5.11e-64 |
|
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: 225.31 E-value: 5.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:cd07145 1 IEVRNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRYyAAQTAAQFDNATHR-----------------PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKP 821
Cdd:cd07145 80 VEVERTIRLFKL-AAEEAKVLRGETIPvdayeynerriaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 822 AEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLIsrtvSKRLSPQGRSIVLiaE 901
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI----ASKAGGTGKKVAL--E 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 902 TGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAE 981
Cdd:cd07145 233 LGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 982 ARDNLEAHIAR-MQAAGLCVTRLGRDEsgglGTFVRPTLIELDTIDR--LQREVFGPVLHVLRYRREQlgAVLDAINATG 1058
Cdd:cd07145 313 AVERMENLVNDaVEKGGKILYGGKRDE----GSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDDE--EAVEIANSTE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 294339260 1059 YGLTFGVHSRIDETVAELSERIHAGNVYVNR-------NLigavvgvqPFGGMGRSGTG 1110
Cdd:cd07145 387 YGLQASVFTNDINRALKVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG 437
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
678-1110 |
7.21e-63 |
|
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: 222.45 E-value: 7.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 678 WVPVLNPADPRdQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPG-ERAACLQRAADALEQQMQNLLGLIVREAGKTLPD 756
Cdd:cd07082 17 TIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTMPLeERIDCLHKFADLLKENKEEVANLLMWEIGKTLKD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 757 AIGEVREAVDFLRYYAA------QTAAQFDNATHR----------PLGVVLCISPWNFPL---------SIFCGQvaaal 811
Cdd:cd07082 96 ALKEVDRTIDYIRDTIEelkrldGDSLPGDWFPGTkgkiaqvrrePLGVVLAIGPFNYPLnltvsklipALIMGN----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 812 aagnAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLIsrtvsKRLSP 891
Cdd:cd07082 171 ----TVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL-----KKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 892 QGRsivLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMH 971
Cdd:cd07082 242 MKR---LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 972 TDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRdesGGLGTFVRPTLIELDTID-RL-QREVFGPVLHVLRYRREQlgA 1049
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG---REGGNLIYPTLLDPVTPDmRLaWEEPFGPVLPIIRVNDIE--E 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294339260 1050 VLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVN----RNligavVGVQPFGGMGRSGTG 1110
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRG-----PDHFPFLGRKDSGIG 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
680-1110 |
7.75e-63 |
|
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: 221.70 E-value: 7.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG 759
Cdd:cd07149 2 EVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYyAAQTAAQ-------FDNA----------THRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPA 822
Cdd:cd07149 81 EVDRAIETLRL-SAEEAKRlagetipFDASpggegrigftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 823 EQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKrlspqgRSIVLiaET 902
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGL------KKVTL--EL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 903 GGQNALIADSSALAEQLVADVLTSAFDSAGQRC-SALRLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAE 981
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 982 ARDNLEAHIARMQAAGLCVTRLGRDEsgglGTFVRPTLIELDTID-RLQ-REVFGPVLHVLRYRReqLGAVLDAINATGY 1059
Cdd:cd07149 311 EAERIEEWVEEAVEGGARLLTGGKRD----GAILEPTVLTDVPPDmKVVcEEVFAPVVSLNPFDT--LDEAIAMANDSPY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1060 GLTFGVHSRIDETVAELSERIHAGNVYVN-----RnligavVGVQPFGGMGRSGTG 1110
Cdd:cd07149 385 GLQAGVFTNDLQKALKAARELEVGGVMINdsstfR------VDHMPYGGVKESGTG 434
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
677-1110 |
2.48e-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: 2.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 677 GWVPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTL-- 754
Cdd:cd07138 14 ETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPItl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 755 ------PDAIGEVREAVDFLRYYAAQTAAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALI 828
Cdd:cd07138 93 araaqvGLGIGHLRAAADALKDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 829 AAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGST----EVAQLISRTVsKRLSpqgrsivliAETGG 904
Cdd:cd07138 173 AIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTragkRVAEAAADTV-KRVA---------LELGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALIADSSALAEQLVADVLTSAFDSAGQRCSAL-RLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEAR 983
Cdd:cd07138 243 KSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 984 DNLEAHIARMQAAG--LCVTRLGRDESGGLGTFVRPTLIELDTID-RLQR-EVFGPVLHVLRYRREQlgavlDAI---NA 1056
Cdd:cd07138 322 DRVQGYIQKGIEEGarLVAGGPGRPEGLERGYFVKPTVFADVTPDmTIAReEIFGPVLSIIPYDDED-----EAIaiaND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 294339260 1057 TGYGLTFGVHSRIDETVAELSERIHAGNVYVNrnliGAVVGVQ-PFGGMGRSGTG 1110
Cdd:cd07138 397 TPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
681-1110 |
2.76e-60 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 214.35 E-value: 2.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI-G 759
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAA----------QTAAQFDNATHR-PLGVVLCISPWNFPL---------SIFCGQvaaalaagnAVLA 819
Cdd:cd07093 80 DIPRAAANFRFFADyilqldgesyPQDGGALNYVLRqPVGVAGLITPWNLPLmlltwkiapALAFGN---------TVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 820 KPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLI 899
Cdd:cd07093 151 KPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKP------VS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 900 AETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVID 979
Cdd:cd07093 225 LELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLIS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 980 AEARDNLEAHIARMQAAGLCVTRLG-RDESGGL--GTFVRPTLIE-LDTIDRL-QREVFGPVLHVLRYRREQlgAVLDAI 1054
Cdd:cd07093 305 KEHLEKVLGYVELARAEGATILTGGgRPELPDLegGYFVEPTVITgLDNDSRVaQEEIFGPVVTVIPFDDEE--EAIELA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1055 NATGYGLTFGVHSRIDETVAELSERIHAGNVYVN----RNLigavvgVQPFGGMGRSGTG 1110
Cdd:cd07093 383 NDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNcwlvRDL------RTPFGGVKASGIG 436
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
681-1125 |
5.37e-60 |
|
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: 213.45 E-value: 5.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDA-IG 759
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAA----------QTAAQFDNATHR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALI 828
Cdd:cd07115 80 DVPRAADTFRYYAGwadkiegeviPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 829 AAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVS---KRLSpqgrsivliAETGGQ 905
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAgnlKRVS---------LELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 906 NALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDN 985
Cdd:cd07115 231 SANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 986 LEAHIARMQAAGLCVTRLGRdESGGLGTFVRPTLIE-LDTIDRL-QREVFGPVLHVLRYRREQLGAVLdaINATGYGLTF 1063
Cdd:cd07115 311 VLDYVDVGREEGARLLTGGK-RPGARGFFVEPTIFAaVPPEMRIaQEEIFGPVVSVMRFRDEEEALRI--ANGTEYGLAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294339260 1064 GVHSRIDETVAELSERIHAGNVYVnrNLIGAVVGVQPFGGMGRSGTGpKAGGPLYLHRLVQP 1125
Cdd:cd07115 388 GVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEV 446
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
681-1114 |
4.56e-59 |
|
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: 210.68 E-value: 4.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADpRDQVGWVRQTTRTEVDEAtrrAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:cd07146 3 VRNPYT-GEVVGTVPAGTEEALREA---LALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVDFLRYYAAQT------AAQFDNATHR----------PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQ 824
Cdd:cd07146 79 VGRAADVLRFAAAEAlrddgeSFSCDLTANGkarkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 825 TALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSkrlspqGRSIVLiaETGG 904
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG------YKRQLL--ELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARD 984
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 985 NLEAHIARMQAAGLCVTRLGRDEsgglGTFVRPTLieLDTIDR----LQREVFGPVLHVLRYRreQLGAVLDAINATGYG 1060
Cdd:cd07146 311 QIENRVEEAIAQGARVLLGNQRQ----GALYAPTV--LDHVPPdaelVTEETFGPVAPVIRVK--DLDEAIAISNSTAYG 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 294339260 1061 LTFGVHSRIDETVAELSERIHAGNVYVNrNLIGAVVGVQPFGGMGRSGTGPKAG 1114
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
682-1125 |
1.40e-58 |
|
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: 209.38 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 682 LNPADPRDqVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEV 761
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 762 REAVDFLRYYAAQTA-------AQFDNAT--------HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA 826
Cdd:cd07099 80 LLALEAIDWAARNAPrvlaprkVPTGLLMpnkkatveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 827 LIAAALVHALHAAGVPTDAVQLVPGDGGTvGAALVAHPaVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQN 906
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIP------VVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 907 ALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNL 986
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 987 EAHIARMQAAGLCVTRLGRDESGGlGTFVRPT-LIELD-TIDRLQREVFGPVLHVLRYRREQlgAVLDAINATGYGLTFG 1064
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGG-GPFYEPTvLTDVPhDMDVMREETFGPVLPVMPVADED--EAIALANDSRYGLSAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294339260 1065 VHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGpKAGGPLYLHRLVQP 1125
Cdd:cd07099 389 VFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRP 448
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
681-1110 |
2.14e-58 |
|
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: 208.83 E-value: 2.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:cd07094 3 VHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVDFLRYYAAQTA----------AQFDNATHR------PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQ 824
Cdd:cd07094 82 VDRAIDTLRLAAEEAErirgeeipldATQGSDNRLawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 825 TALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSkrlspqGRSIVLiaETGG 904
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG------GKRIAL--ELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARD 984
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 985 NLEAHIARmqaaglCVTRLGRDESGGL--GTFVRPTLIELDTIDRLQR--EVFGPVLHVLRYRREQLGavLDAINATGYG 1060
Cdd:cd07094 314 RVERWVEE------AVEAGARLLCGGErdGALFKPTVLEDVPRDTKLSteETFGPVVPIIRYDDFEEA--IRIANSTDYG 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 294339260 1061 LTFGVHSRIDETVAELSERIHAGNVYVNRNLIgAVVGVQPFGGMGRSGTG 1110
Cdd:cd07094 386 LQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
701-1108 |
4.48e-58 |
|
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: 207.51 E-value: 4.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 701 EVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREA---VDFL------RYY 771
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMagkIDISikayheRTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 772 AAQTAAQFDNA--THRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLV 849
Cdd:cd07095 81 ERATPMAQGRAvlRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 850 PGdGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSkrlspqGRSIVLIA-ETGGQNALIADSSALAEQLVADVLTSAF 928
Cdd:cd07095 161 QG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 929 DSAGQRCS-ALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAG----LCVTRL 1003
Cdd:cd07095 234 LTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGgeplLAMERL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1004 grDESGGlgtFVRPTLIELDTIDRLQ-REVFGPVLHVLRYrrEQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHA 1082
Cdd:cd07095 314 --VAGTA---FLSPGIIDVTDAADVPdEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420
....*....|....*....|....*.
gi 294339260 1083 GNVYVNRNLIGAvVGVQPFGGMGRSG 1108
Cdd:cd07095 387 GIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
701-1116 |
1.67e-57 |
|
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: 205.84 E-value: 1.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 701 EVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQ------ 774
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLprrpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 775 ------TAAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA-----LIaaalVHALHAAGVPT 843
Cdd:cd07104 81 eilpsdVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLI----AEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 844 DAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGGQNALIADSSALAEQLVADV 923
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKK----VAL--ELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 924 LTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRL 1003
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1004 GRDEsgglGTFVRPTLieLDTIDR----LQREVFGPVLHVLRYRREQlgavlDAI---NATGYGLTFGVHSRIDETVAEL 1076
Cdd:cd07104 311 GTYE----GLFYQPTV--LSDVTPdmpiFREEIFGPVAPVIPFDDDE-----EAVelaNDTEYGLSAAVFTRDLERAMAF 379
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 294339260 1077 SERIHAGNVYVNRNLI--GAVVgvqPFGGMGRSGTGpKAGGP 1116
Cdd:cd07104 380 AERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
681-1113 |
1.88e-57 |
|
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: 206.44 E-value: 1.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTL-PDAIG 759
Cdd:cd07108 1 VINPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAaQTAA------------QFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQ--- 824
Cdd:cd07108 80 EAAVLADLFRYFG-GLAGelkgetlpfgpdVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDapl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 825 TALIAAALVHALHAAGVptdaVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGG 904
Cdd:cd07108 159 AVLLLAEILAQVLPAGV----LNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIP------VSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALIADSSALAEQLVADVLTSA-FDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEAR 983
Cdd:cd07108 229 KSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 984 DNLEAHIAR-MQAAGLCVTRLGRDESGGL---GTFVRPTLIE-LDTIDRLQR-EVFGPVLHVLRYRREQlgAVLDAINAT 1057
Cdd:cd07108 309 AKVCGYIDLgLSTSGATVLRGGPLPGEGPladGFFVQPTIFSgVDNEWRLAReEIFGPVLCAIPWKDED--EVIAMANDS 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1058 GYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLiGAVVGvQPFGGMGRSGTGPKA 1113
Cdd:cd07108 387 HYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGG-GQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
678-1110 |
2.39e-57 |
|
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: 206.60 E-value: 2.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 678 WVPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDA 757
Cdd:cd07085 17 WLDVYNPAT-GEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 758 IGEVR---EAVDF--------LRYYAAQTAAQFDNATHR-PLGVVLCISPWNFP---------LSIFCGQvaaalaagnA 816
Cdd:cd07085 96 RGDVLrglEVVEFacsiphllKGEYLENVARGIDTYSYRqPLGVVAGITPFNFPamiplwmfpMAIACGN---------T 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 817 VLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGaALVAHPAVAGVMFTGSTEVAQLISRTVS---KRlspqg 893
Cdd:cd07085 167 FVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEYIYERAAangKR----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 894 rsiVLiAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTD 973
Cdd:cd07085 241 ---VQ-ALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 974 LGPVIDAEARDNLEAHIARMQAAGLCVTRLGRD---ESGGLGTFVRPTLIELDTIDR--LQREVFGPVLHVLRYrrEQLG 1048
Cdd:cd07085 317 MGPVISPAAKERIEGLIESGVEEGAKLVLDGRGvkvPGYENGNFVGPTILDNVTPDMkiYKEEIFGPVLSIVRV--DTLD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294339260 1049 AVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNrnlIGAVVGVQ--PFGGMGRSGTG 1110
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLAffSFGGWKGSFFG 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
681-1110 |
4.12e-57 |
|
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: 205.55 E-value: 4.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADprDQV-GWVRQTTRTEVDEATRRAQSAAPIWQV-TPPGERAACLQRAADALEQQMQNLLGLIVREAGKT----- 753
Cdd:cd07089 1 VINPAT--EEViGTAPDAGAADVDAAIAAARRAFDTGDWsTDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmtar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 754 ---LPDAIGEVREAVDFLRYYAAQTA----AQFDNATHR-----PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKP 821
Cdd:cd07089 79 amqVDGPIGHLRYFADLADSFPWEFDlpvpALRGGPGRRvvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 822 AEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaE 901
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKR----VLL--E 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 902 TGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAE 981
Cdd:cd07089 233 LGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 982 ARDNLEAHIARMQAAGL-CVTRLGRDESGGLGTFVRPTLI-ELDTIDRL-QREVFGPVLHVLRYRREQlgavlDAI---N 1055
Cdd:cd07089 313 QRDRVEGYIARGRDEGArLVTGGGRPAGLDKGFYVEPTLFaDVDNDMRIaQEEIFGPVLVVIPYDDDD-----EAVriaN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 294339260 1056 ATGYGLTFGVHSRIDETVAELSERIHAGNVYVNrnliGAVVGV--QPFGGMGRSGTG 1110
Cdd:cd07089 388 DSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
680-1110 |
5.42e-56 |
|
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: 202.06 E-value: 5.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADPRdQVGWVRQTTRTEVDEATRRAQSA--APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDA 757
Cdd:cd07112 5 ATINPATGR-VLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 758 I-GEVREAVDFLRYYA-------AQTAAQFDNA----THRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQT 825
Cdd:cd07112 84 LaVDVPSAANTFRWYAeaidkvyGEVAPTGPDAlaliTREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 826 ALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLIsrtvskrLSPQGRS----IVLiaE 901
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRF-------LEYSGQSnlkrVWL--E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 902 TGGQNALI-----ADSSALAEQLVAdvltSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGP 976
Cdd:cd07112 235 CGGKSPNIvfadaPDLDAAAEAAAA----GIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 977 VIDAEARDNLEAHIARMQAAGL-CVTRLGRDESGGLGTFVRPTLIE-LDTIDRL-QREVFGPVLHVLRYRREQlgavlDA 1053
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGArLVAGGKRVLTETGGFFVEPTVFDgVTPDMRIaREEIFGPVLSVITFDSEE-----EA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1054 I---NATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRnlIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07112 386 ValaNDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNC--FDEGDITTPFGGFKQSGNG 443
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
680-1110 |
5.57e-56 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 203.38 E-value: 5.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADPrDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG 759
Cdd:PLN02278 43 PVYNPATG-EVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAAQTAAQFDN------------ATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTAL 827
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKRVYGDiipspfpdrrllVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 828 IAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLI----SRTVsKRLSpqgrsivliAETG 903
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLmagaAATV-KRVS---------LELG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 904 GQNALIADSSALAEQLVADVLTSAFDSAGQRC-SALRLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEA 982
Cdd:PLN02278 272 GNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 983 RDNLEAHIARMQAAGLCVTRLGRDESGGlGTFVRPTLIELDTIDRL--QREVFGPVLHVLRYRREQlgavlDAI---NAT 1057
Cdd:PLN02278 351 VQKVESHVQDAVSKGAKVLLGGKRHSLG-GTFYEPTVLGDVTEDMLifREEVFGPVAPLTRFKTEE-----EAIaiaNDT 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 294339260 1058 GYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGvqPFGGMGRSGTG 1110
Cdd:PLN02278 425 EAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
681-1110 |
8.78e-56 |
|
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: 201.40 E-value: 8.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADPRdQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI-G 759
Cdd:cd07092 1 VVDPATGE-EIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAAqtAAQFDNAT--------------HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQT 825
Cdd:cd07092 80 ELPGAVDNFRFFAG--AARTLEGPaageylpghtsmirREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 826 ALiAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSpqgrsiVLIAETGGQ 905
Cdd:cd07092 158 PL-TTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLK------RVHLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 906 NALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDN 985
Cdd:cd07092 231 APVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 986 LEAHIARMqAAGLCVTRLGRdESGGLGTFVRPTLI-ELDTIDRL-QREVFGPVLHVLRYRREQlgavlDAI---NATGYG 1060
Cdd:cd07092 311 VAGFVERA-PAHARVLTGGR-RAEGPGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPFDDED-----EAIelaNDVEYG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 294339260 1061 LTFGVHSRIDETVAELSERIHAGNVYVNRNLIgaVVGVQPFGGMGRSGTG 1110
Cdd:cd07092 384 LASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
681-1114 |
1.01e-55 |
|
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: 201.43 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVDFLRYYAAQtAAQFDNATHR----------------PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQ 824
Cdd:cd07110 80 VDDVAGCFEYYADL-AEQLDAKAERavplpsedfkarvrrePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 825 TALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGG 904
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKP----VSL--ELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARD 984
Cdd:cd07110 233 KSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 985 NLEAHIARMQAAGL-CVTRLGRDESGGLGTFVRPTLI-ELDTIDRLQR-EVFGPVLHVLRYRREQlgAVLDAINATGYGL 1061
Cdd:cd07110 313 KVLSFIARGKEEGArLLCGGRRPAHLEKGYFIAPTVFaDVPTDSRIWReEIFGPVLCVRSFATED--EAIALANDSEYGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 294339260 1062 TFGVHSRIDETVAELSERIHAGNVYVNRNligAVVGVQ-PFGGMGRSGTGPKAG 1114
Cdd:cd07110 391 AAAVISRDAERCDRVAEALEAGIVWINCS---QPCFPQaPWGGYKRSGIGRELG 441
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
680-1110 |
1.48e-55 |
|
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: 201.39 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADpRDQVGWVRQTTRTEVDEATRRAQSA--APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDA 757
Cdd:cd07119 16 DIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 758 IGEVREAVDFLRYYA----AQTAAQFDNA-------THRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA 826
Cdd:cd07119 95 EIDIDDVANCFRYYAglatKETGEVYDVPphvisrtVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 827 LIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLspqgRSIVLiaETGGQN 906
Cdd:cd07119 175 LTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV----KKVAL--ELGGKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 907 ALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNL 986
Cdd:cd07119 249 PNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 987 EAHIARMQAAGlCVTRLG--RDESGGL--GTFVRPTLI-ELDTIDRL-QREVFGPVLHVLRYRREQlgavlDAI---NAT 1057
Cdd:cd07119 329 LSYIQLGKEEG-ARLVCGgkRPTGDELakGYFVEPTIFdDVDRTMRIvQEEIFGPVLTVERFDTEE-----EAIrlaNDT 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 294339260 1058 GYGLTFGVHSRiDETVAE-LSERIHAGNVYVNRnlIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07119 403 PYGLAGAVWTK-DIARANrVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
698-1116 |
2.98e-55 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 199.44 E-value: 2.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 698 TRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAA---- 773
Cdd:cd07152 11 DAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGlptq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 774 -------QTAAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA-----LIaaalVHALHAAGV 841
Cdd:cd07152 91 pqgeilpSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggvVI----ARLFEEAGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 842 PTDAVQLVPGdGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLspqgRSIVLiaETGGQNALIADSSALAEQLVA 921
Cdd:cd07152 167 PAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHL----KKVSL--ELGGKNALIVLDDADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 922 DVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGlcvt 1001
Cdd:cd07152 240 NGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1002 rlGRDESGGL--GTFVRPTLIELDTIDR--LQREVFGPVLHVLRYRREQLGAVLdaINATGYGLTFGVHSRIDETVAELS 1077
Cdd:cd07152 316 --ARLEAGGTydGLFYRPTVLSGVKPGMpaFDEEIFGPVAPVTVFDSDEEAVAL--ANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 294339260 1078 ERIHAGNVYVNRNLIGAVVgVQPFGGMGRSGTGPKAGGP 1116
Cdd:cd07152 392 DRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
689-1114 |
7.67e-55 |
|
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: 198.69 E-value: 7.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 689 DQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFL 768
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 769 RYYAAqTAAQFDN---------------ATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALV 833
Cdd:cd07101 87 RYYAR-RAERLLKprrrrgaipvltrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 834 HALHAAGVPTDAVQLVPGDGGTVGAALVAHpaVAGVMFTGSTEVAQLISRTVSKRLspqgrsIVLIAETGGQNALIADSS 913
Cdd:cd07101 166 ELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 914 ALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARM 993
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 994 QAAGLCVTRLGRDESgGLGT-FVRPTLIELDTIDRLQR--EVFGPVLHVLRYRREQlgAVLDAINATGYGLTFGVHSRID 1070
Cdd:cd07101 318 VAKGATVLAGGRARP-DLGPyFYEPTVLTGVTEDMELFaeETFGPVVSIYRVADDD--EAIELANDTDYGLNASVWTRDG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 294339260 1071 ETVAELSERIHAGNVYVNRNLIGAVVGVQ-PFGGMGRSGTGPKAG 1114
Cdd:cd07101 395 ARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
702-1110 |
1.19e-54 |
|
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: 197.30 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 702 VDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQtAAQF-- 779
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEN-AEAFla 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 780 --------DNA--THRPLGVVLCISPWNFPL---------SIFCGQvaaalaagnAVLAKPAEQTALIAAALVHALHAAG 840
Cdd:cd07100 80 depietdaGKAyvRYEPLGVVLGIMPWNFPFwqvfrfaapNLMAGN---------TVLLKHASNVPGCALAIEELFREAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 841 VPTDAVQLVPGDGGTVgAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGGQNALIADSSALAEQLV 920
Cdd:cd07100 151 FPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKK----SVL--ELGGSDPFIVLDDADLDKAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 921 ADVLTSAFDSAGQRC-SALRLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGlC 999
Cdd:cd07100 224 KTAVKGRLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAG-A 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1000 VTRLGRDESGGLGTFVRPTLIELDTID-RLQR-EVFGPVLHVLRYRREQlgavlDAI---NATGYGLTFGVHSRiDETVA 1074
Cdd:cd07100 302 TLLLGGKRPDGPGAFYPPTVLTDVTPGmPAYDeELFGPVAAVIKVKDEE-----EAIalaNDSPFGLGGSVFTT-DLERA 375
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 294339260 1075 E-LSERIHAGNVYVNrnligAVVGVQ---PFGGMGRSGTG 1110
Cdd:cd07100 376 ErVARRLEAGMVFIN-----GMVKSDprlPFGGVKRSGYG 410
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
680-1120 |
6.31e-53 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 192.93 E-value: 6.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADprDQV-GWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:cd07150 2 DDLNPAD--GSVyARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRYYAAQ------------TAAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA 826
Cdd:cd07150 80 FETTFTPELLRAAAGEcrrvrgetlpsdSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 827 LIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGGQN 906
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKK----ITL--ELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 907 ALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNL 986
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 987 EAHIARMQAAGLCVTRLGRDEsgglGTFVRPTLIELDTID-RLQR-EVFGPVLHVLRYRREQlgavlDAI---NATGYGL 1061
Cdd:cd07150 314 KRQVEDAVAKGAKLLTGGKYD----GNFYQPTVLTDVTPDmRIFReETFGPVTSVIPAKDAE-----EALelaNDTEYGL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294339260 1062 TFGVHSRIDETVAELSERIHAGNVYVNRNLI--GAVVgvqPFGGMGRSGTGpKAGGPLYLH 1120
Cdd:cd07150 385 SAAILTNDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSME 441
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
680-1114 |
1.32e-52 |
|
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: 192.81 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPI--WQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDA 757
Cdd:cd07091 22 PTINPAT-EEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 758 I-GEVREAVDFLRYYAA----------QTAAQFDNATHR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQT 825
Cdd:cd07091 101 AkGDVALSIKCLRYYAGwadkiqgktiPIDGNFLAYTRRePIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 826 ALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVS----KRLSpqgrsivliAE 901
Cdd:cd07091 181 PLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAksnlKKVT---------LE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 902 TGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAE 981
Cdd:cd07091 252 LGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 982 ARDNLEAHIARMQAAGL-CVTrlGRDESGGLGTFVRPTlIELDTIDRL---QREVFGPVLHVLRYRREQlgAVLDAINAT 1057
Cdd:cd07091 332 QFDKILSYIESGKKEGAtLLT--GGERHGSKGYFIQPT-VFTDVKDDMkiaKEEIFGPVVTILKFKTED--EVIERANDT 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 294339260 1058 GYGLTFGVHSRIDETVAELSERIHAGNVYVNR-NLIGAVVgvqPFGGMGRSGTGPKAG 1114
Cdd:cd07091 407 EYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
681-1110 |
1.91e-52 |
|
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: 191.82 E-value: 1.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADPRdQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:cd07107 1 VINPATGQ-VLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVDFLRYYAA-------QTAAQFDNA----THRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIA 829
Cdd:cd07107 80 VMVAAALLDYFAGlvtelkgETIPVGGRNlhytLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 830 AALVHALHAAgVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNALI 909
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKH------VTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 910 ----ADSSALAEQLVADVltsAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDN 985
Cdd:cd07107 233 vfpdADPEAAADAAVAGM---NFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 986 LEAHIARMQAAGL-CVTRLGRDESGGL--GTFVRPT-LIELDTIDRLQR-EVFGPVLHVLRYRREQlgAVLDAINATGYG 1060
Cdd:cd07107 310 VMHYIDSAKREGArLVTGGGRPEGPALegGFYVEPTvFADVTPGMRIAReEIFGPVLSVLRWRDEA--EMVAQANGVEYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 294339260 1061 LTFGVHSRIDETVAELSERIHAGNVYVN---RNLIGAvvgvqPFGGMGRSGTG 1110
Cdd:cd07107 388 LTAAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
679-1043 |
2.11e-51 |
|
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: 188.95 E-value: 2.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADPRdQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:cd07130 14 VTSISPANGE-PIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRyYAAQTAAQFDNAT-------HR------PLGVVLCISPWNFP---------LSIFCGQvaaalaagnA 816
Cdd:cd07130 93 GEVQEMIDICD-FAVGLSRQLYGLTipserpgHRmmeqwnPLGVVGVITAFNFPvavwgwnaaIALVCGN---------V 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 817 VLAKPAEQTALIAAAL----VHALHAAGVPTDAVQLVPGdGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLspq 892
Cdd:cd07130 163 VVWKPSPTTPLTAIAVtkivARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 893 GRSIVliaETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHT 972
Cdd:cd07130 239 GRSLL---ELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294339260 973 DLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGGlGTFVRPTLIE-LDTIDRLQREVFGPVLHVLRYR 1043
Cdd:cd07130 316 LVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGP-GNYVEPTIVEgLSDAPIVKEETFAPILYVLKFD 386
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
668-1110 |
2.21e-51 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 190.47 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 668 ADNAQAAAVGWVPVLNPADPRdQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIV 747
Cdd:PRK09407 23 TARVDGAAGPTREVTAPFTGE-PLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 748 REAGKTLPDAIGEVREAVDFLRYYAAqTAAQF-------------DNAT--HRPLGVVLCISPWNFPLSIFCGQVAAALA 812
Cdd:PRK09407 102 LETGKARRHAFEEVLDVALTARYYAR-RAPKLlaprrragalpvlTKTTelRQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 813 AGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHpaVAGVMFTGSTEVAQLISRTVSKRLspq 892
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRL--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 893 grsIVLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHT 972
Cdd:PRK09407 256 ---IGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 973 DLGPVIDAEARDNLEAHIARMQAAGLCVtrlgrdESGG-----LGT-FVRPTLIELDTID-RLQR-EVFGPVLHVLRYRR 1044
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATV------LAGGkarpdLGPlFYEPTVLTGVTPDmELAReETFGPVVSVYPVAD 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294339260 1045 EQlgAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQ-PFGGMGRSGTG 1110
Cdd:PRK09407 407 VD--EAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
678-1116 |
9.04e-51 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 187.01 E-value: 9.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 678 WVPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSA--APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLP 755
Cdd:cd07139 15 TIDVVSPAT-EEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 756 -DAIGEVREAVDFLRYYAAqTAAQFDNATHR-------------PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKP 821
Cdd:cd07139 94 wSRRAQGPGPAALLRYYAA-LARDFPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 822 AEQTALIAAALVHALHAAGVPTDAVQLVPGDGGtVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaE 901
Cdd:cd07139 173 SPETPLDAYLLAEAAEEAGLPPGVVNVVPADRE-VGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLAR----VTL--E 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 902 TGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSAL-RLLCIQEDvADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDA 980
Cdd:cd07139 246 LGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVPRSR-YDEVVEALAAAVAALKVGDPLDPATQIGPLASA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 981 EARDNLEAHIARMQAAGLCVTRLGRDESG-GLGTFVRPTLI-ELDTIDRL-QREVFGPVLHVLRYRREQlgavlDAI--- 1054
Cdd:cd07139 325 RQRERVEGYIAKGRAEGARLVTGGGRPAGlDRGWFVEPTLFaDVDNDMRIaQEEIFGPVLSVIPYDDED-----DAVria 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294339260 1055 NATGYGLTFGVHSRIDETVAELSERIHAGNVYVNrnliGAVVGVQ-PFGGMGRSGTGpKAGGP 1116
Cdd:cd07139 400 NDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGP 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
686-1114 |
1.48e-50 |
|
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: 186.55 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 686 DPR--DQVGWVRQTTRTEVDEATRRAQSA---APiWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDA-IG 759
Cdd:cd07142 25 DPRngEVIAHVAEGDAEDVDRAVKAARKAfdeGP-WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAA-----------QTAAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALI 828
Cdd:cd07142 104 EVPLAARLFRYYAGwadkihgmtlpADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 829 AAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSK-RLSPqgrsivLIAETGGQNA 907
Cdd:cd07142 184 ALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLKP------VTLELGGKSP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 908 LIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLE 987
Cdd:cd07142 258 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKIL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 988 AHIARMQAAGlcvTRL--GRDESGGLGTFVRPTLIELDTIDRL--QREVFGPVLHVLRYRreQLGAVLDAINATGYGLTF 1063
Cdd:cd07142 338 SYIEHGKEEG---ATLitGGDRIGSKGYYIQPTIFSDVKDDMKiaRDEIFGPVQSILKFK--TVDEVIKRANNSKYGLAA 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 294339260 1064 GVHSRIDETVAELSERIHAGNVYVN-RNLIGAVVgvqPFGGMGRSGTGPKAG 1114
Cdd:cd07142 413 GVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
698-1114 |
2.06e-50 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 185.62 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 698 TRTEVD---EATRRAQSAAPiWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYyAAQ 774
Cdd:cd07118 17 TVEDVDaavAAARKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRY-AAS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 775 TAAQFDNATH-------------RPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGV 841
Cdd:cd07118 95 LARTLHGDSYnnlgddmlglvlrEPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 842 PTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQGrsivliAETGGQNALIADSSALAEQLVA 921
Cdd:cd07118 175 PAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQIVFADADLDAAAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 922 DVLTSAFDSAGQRC-SALRLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCV 1000
Cdd:cd07118 249 AVVFGVYFNAGECCnSGSRLL-VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1001 TRLGRDESGGLGTFVRPTLIELDTID-RLQR-EVFGPVLHVLRYrrEQLGAVLDAINATGYGLTFGVHSRIDETVAELSE 1078
Cdd:cd07118 328 LLGGERLASAAGLFYQPTIFTDVTPDmAIAReEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDTALTVAR 405
|
410 420 430
....*....|....*....|....*....|....*.
gi 294339260 1079 RIHAGNVYVNRNLIGAVvgVQPFGGMGRSGTGPKAG 1114
Cdd:cd07118 406 RIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
681-1110 |
7.36e-50 |
|
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: 184.04 E-value: 7.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADPRdQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVDFLRYYA--AQTAA----QFDNA----THR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIA 829
Cdd:cd07090 80 IDSSADCLEYYAglAPTLSgehvPLPGGsfayTRRePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 830 AALVHALHAAGVPTDAVQLVPGDGGTvGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNALI 909
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH------VTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 910 ADSSALAEQLVADVLTSAFDSAGQRCS-ALRLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEA 988
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 989 HIARMQAAGLCVTRLGR--DESGGL--GTFVRPTLIE--LDTIDRLQREVFGPVLHVLRYRREQlgAVLDAINATGYGLT 1062
Cdd:cd07090 312 YIESAKQEGAKVLCGGErvVPEDGLenGFYVSPCVLTdcTDDMTIVREEIFGPVMSILPFDTEE--EVIRRANDTTYGLA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 294339260 1063 FGVHSRIDETVAELSERIHAGNVYVNR-NLIGAVVgvqPFGGMGRSGTG 1110
Cdd:cd07090 390 AGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
679-1114 |
3.22e-49 |
|
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: 183.11 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADPRdQVGWVRQTTRTEVDEATRRAQSA--APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPD 756
Cdd:cd07143 24 VKVYNPSTGK-LITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 757 AIG-EVREAVDFLRYYAA-------QT----AAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQ 824
Cdd:cd07143 103 AKRvDVQASADTFRYYGGwadkihgQVietdIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 825 TALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRlspQGRSIVLiaETGG 904
Cdd:cd07143 183 TPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS---NLKKVTL--ELGG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARD 984
Cdd:cd07143 258 KSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 985 NLEAHIARMQAAGLCVTrLGRDESGGLGTFVRPTLIELDTIDR--LQREVFGPVLHVLRYRREQlgAVLDAINATGYGLT 1062
Cdd:cd07143 338 RIMSYIESGKAEGATVE-TGGKRHGNEGYFIEPTIFTDVTEDMkiVKEEIFGPVVAVIKFKTEE--EAIKRANDSTYGLA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 294339260 1063 FGVHSRIDETVAELSERIHAGNVYVN-RNLIGAVVgvqPFGGMGRSGTGPKAG 1114
Cdd:cd07143 415 AAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
679-1110 |
3.65e-49 |
|
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: 182.64 E-value: 3.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSA-APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKT--LP 755
Cdd:cd07113 17 LDITNPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSihLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 756 DAIgEVREAVDFLRYYAAQT----------------AAQFDNATHR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVL 818
Cdd:cd07113 96 RAF-EVGQSANFLRYFAGWAtkingetlapsipsmqGERYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 819 AKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGtVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSpqgRSIVl 898
Cdd:cd07113 175 IKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLT---RVTL- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 899 iaETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVI 978
Cdd:cd07113 250 --ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 979 DAEARDNLEAHIARMQAAGLCVTRLGRDESGGlGTFVRPTLIEL-DTIDRL-QREVFGPVLHVLRYRREQlgAVLDAINA 1056
Cdd:cd07113 328 NQPHFDKVCSYLDDARAEGDEIVRGGEALAGE-GYFVQPTLVLArSADSRLmREETFGPVVSFVPYEDEE--ELIQLIND 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 294339260 1057 TGYGLTFGVHSRIDETVAELSERIHAGNVYVN-RNLIGAVVgvqPFGGMGRSGTG 1110
Cdd:cd07113 405 TPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
682-1110 |
7.21e-49 |
|
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: 181.00 E-value: 7.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 682 LNPADpRDQVGWVRQTTRTEVDEATRRAQSA--APIWqVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG 759
Cdd:cd07120 2 IDPAT-GEVIGTYADGGVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EVREAVDFLRYYAAQTAAQFDNA----------THR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALI 828
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMiepepgsfslVLRePMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 829 AAALVHA-LHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQGrsivliAETGGQNA 907
Cdd:cd07120 160 NAAIIRIlAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 908 LI----ADSSALAEQLVAdvltSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEAR 983
Cdd:cd07120 234 CIvfddADLDAALPKLER----ALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 984 DNLEAHIAR-MQAAGLCVTRLGR-DESGGLGTFVRPTLIELD--TIDRLQREVFGPVLHVLRYRREQlGAVLDAiNATGY 1059
Cdd:cd07120 310 DRVDRMVERaIAAGAEVVLRGGPvTEGLAKGAFLRPTLLEVDdpDADIVQEEIFGPVLTLETFDDEA-EAVALA-NDTDY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 294339260 1060 GLTFGVHSRIDETVAELSERIHAGNVYVNRNliGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07120 388 GLAASVWTRDLARAMRVARAIRAGTVWINDW--NKLFAEAEEGGYRQSGLG 436
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
680-1110 |
5.30e-48 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 179.33 E-value: 5.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADPrDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG 759
Cdd:PRK13473 20 PVYNPATG-EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 -EVREAVDFLRYYA-------AQTAAQFDnATH------RPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQT 825
Cdd:PRK13473 99 dEIPAIVDVFRFFAgaarcleGKAAGEYL-EGHtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEIT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 826 ---ALIAAALVHALHAAGVptdaVQLVPGDGGTVGAALVAHPAVAGVMFTGST----EVAQLISRTVsKRLSpqgrsivl 898
Cdd:PRK13473 178 pltALKLAELAADILPPGV----LNVVTGRGATVGDALVGHPKVRMVSLTGSIatgkHVLSAAADSV-KRTH-------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 899 iAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVI 978
Cdd:PRK13473 245 -LELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 979 DAEARDNLEAHIARMQAAGLCVTRLGRDESGGLGTFVRPTLI----ELDTIdrLQREVFGPVLHVLRYRREQlgAVLDAI 1054
Cdd:PRK13473 324 SAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLagarQDDEI--VQREVFGPVVSVTPFDDED--QAVRWA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1055 NATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIgaVVGVQPFGGMGRSGTG 1110
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
701-1110 |
1.37e-47 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 176.61 E-value: 1.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 701 EVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQFD 780
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 781 NATH------------RPLGVVLCISPWNFPL-----SIF----CGQvaaalaagnAVLAKPAEQTALIAAALVHALHAA 839
Cdd:cd07105 81 GSIPsdkpgtlamvvkEPVGVVLGIAPWNAPVilgtrAIAyplaAGN---------TVVLKASELSPRTHWLIGRVFHEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 840 GVPTDAVQLV---PGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsiVLIaETGGQNALIADSSALA 916
Cdd:cd07105 152 GLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKP-----VLL-ELGGKAPAIVLEDADL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 917 EQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGnpdrmHTDLGPVIDAEARDNLEAHIARMQAA 996
Cdd:cd07105 226 DAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 997 GLCVTRLGRDESGGLGTFVRPTLIELDTID-RLQR-EVFGPVLHVLRYRREQlgAVLDAINATGYGLTFGVHSRiDETVA 1074
Cdd:cd07105 301 GAKLVVGGLADESPSGTSMPPTILDNVTPDmDIYSeESFGPVVSIIRVKDEE--EAVRIANDSEYGLSAAVFTR-DLARA 377
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 294339260 1075 -ELSERIHAGNVYVNrnliGAVVGVQ---PFGGMGRSGTG 1110
Cdd:cd07105 378 lAVAKRIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
679-1125 |
5.51e-47 |
|
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: 176.43 E-value: 5.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKtlpdAI 758
Cdd:cd07111 39 FPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK----PI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVRE-----AVDFLRYYAAQTAAQ-FDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAAL 832
Cdd:cd07111 114 RESRDcdiplVARHFYHHAGWAQLLdTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 833 VHALHAAGVPTDAVQLVPGDGGTvGAALVAHPAVAGVMFTGSTEVAQLISRTV---SKRLSpqgrsivliAETGGQNALI 909
Cdd:cd07111 194 AEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATagtGKKLS---------LELGGKSPFI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 910 ADSSALAEQLVADVLTSAFDSAGQRCSA-LRLLcIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEA 988
Cdd:cd07111 264 VFDDADLDSAVEGIVDAIWFNQGQVCCAgSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 989 HIARMQAAGLCVTRLGRDESGGlGTFVRPTLIE-LDTIDRL-QREVFGPVLHVLRYRREQlGAVLDAiNATGYGLTFGVH 1066
Cdd:cd07111 343 LVEEGRAEGADVFQPGADLPSK-GPFYPPTLFTnVPPASRIaQEEIFGPVLVVLTFRTAK-EAVALA-NNTPYGLAASVW 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1067 SRIDETVAELSERIHAGNVYVN-RNLIGAVVgvqPFGGMGRSGTGpKAGGPLYLHRLVQP 1125
Cdd:cd07111 420 SENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEYLRP 475
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
682-1108 |
7.92e-47 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 175.92 E-value: 7.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 682 LNPADprDQVGWVRQT-TRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:PRK09457 20 RNPVS--GEVLWQGNDaTAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVD----FLRYYAAQTAAQFDNAT-------HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIA 829
Cdd:PRK09457 98 VTAMINkiaiSIQAYHERTGEKRSEMAdgaavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 830 AALVHALHAAGVPTDAVQLVPGDGGTvGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRlsPQgrsIVLIAETGGQNALI 909
Cdd:PRK09457 178 ELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQ--PE---KILALEMGGNNPLV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 910 ADSSALAEQLVADVLTSAFDSAGQRCS-ALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTD-LGPVIDAEARDNLE 987
Cdd:PRK09457 252 IDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQGLV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 988 AHIARMQAAG----LCVTRLgrdeSGGLGtFVRPTLIEL-DTIDRLQREVFGPVLHVLRYrrEQLGAVLDAINATGYGLT 1062
Cdd:PRK09457 332 AAQAQLLALGgkslLEMTQL----QAGTG-LLTPGIIDVtGVAELPDEEYFGPLLQVVRY--DDFDEAIRLANNTRFGLS 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 294339260 1063 FGVHSRIDETVAELSERIHAGNVYVNRNLIGAvVGVQPFGGMGRSG 1108
Cdd:PRK09457 405 AGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
680-1110 |
7.39e-46 |
|
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: 172.49 E-value: 7.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG 759
Cdd:cd07151 13 DVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 EV-------REAVDF-LRYYAAQTAAQFDNATHR----PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTAL 827
Cdd:cd07151 92 EWgaamaitREAATFpLRMEGRILPSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 828 IA-AALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPaVAGVM-FTGSTEVAQLISRTVskrlspqGRSIVLIA-ETGG 904
Cdd:cd07151 172 TGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHP-VPRLIsFTGSTPVGRHIGELA-------GRHLKKVAlELGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARD 984
Cdd:cd07151 244 NNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 985 NLEAHIARMQAAGLCVTRLGRDEsgglGTFVRPTLIELDTIDR--LQREVFGPVLHVLRYRREQlgAVLDAINATGYGLT 1062
Cdd:cd07151 324 GLLDKIEQAVEEGATLLVGGEAE----GNVLEPTVLSDVTNDMeiAREEIFGPVAPIIKADDEE--EALELANDTEYGLS 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 294339260 1063 FGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVqPFGGMGRSGTG 1110
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
682-1108 |
1.22e-45 |
|
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: 172.59 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 682 LNPADprDQVGWVRQT-TRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGE 760
Cdd:TIGR03240 18 RNPAT--QEVLWQGAAaSADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVIARETGKPLWETRTE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 761 VREAVD----FLRYYAAQTAAQfDNAT--------HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALI 828
Cdd:TIGR03240 96 VASMIGkvaiSIKAYHERTGES-ENPMpdgravlrHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPSELTPWV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 829 AAALVHALHAAGVPTDAVQLVPGDGGTvGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRlsPQgrsIVLIAETGGQNAL 908
Cdd:TIGR03240 175 AEETVKLWEKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFGGR--PE---KILALEMGGNNPL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 909 IADSSALAEQLVADVLTSAFDSAGQRCS-ALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTD-LGPVIDAEARDNL 986
Cdd:TIGR03240 249 IVDEVADIDAAVHHIIQSAFISAGQRCTcARRLLVPDGAQGDAFLARLVEVAERLTVGAWDAEPQPfMGAVISLRAAQRL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 987 EAHIARMQAAG-LCVTRLGRDESGglGTFVRPTLIELDTI-DRLQREVFGPVLHVLRYRreQLGAVLDAINATGYGLTFG 1064
Cdd:TIGR03240 329 LAAQAKLLALGgKSLLEMRQLDPG--AAFLTPGIIDVTGVaELPDEEHFGPLLQVIRYT--DFDEAIAIANNTRFGLSAG 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 294339260 1065 VHSRIDETVAELSERIHAGNVYVNRNLIGAvVGVQPFGGMGRSG 1108
Cdd:TIGR03240 405 LLSDDRELYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
679-1110 |
1.08e-44 |
|
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: 169.45 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADPRDQVGWVRQTTRtEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:cd07559 18 FDNYNPVNGKVLCEIPRSTAE-DVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 G-EVREAVDFLRYYA----AQ--TAAQFDNAT-----HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA 826
Cdd:cd07559 97 AaDIPLAIDHFRYFAgvirAQegSLSEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 827 LIAAALVHALHAAgVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQN 906
Cdd:cd07559 177 LSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP------VTLELGGKS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 907 ALIADSSALAEQ------LVADVLTSAFDSaGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDA 980
Cdd:cd07559 250 PNIFFDDAMDADddfddkAEEGQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 981 EARDNLEAH--IARMQAAgLCVTRLGRDESGGL--GTFVRPTLIELDTID-RL-QREVFGPVLHVLRYRREQlgAVLDAI 1054
Cdd:cd07559 329 DQLEKILSYvdIGKEEGA-EVLTGGERLTLGGLdkGYFYEPTLIKGGNNDmRIfQEEIFGPVLAVITFKDEE--EAIAIA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 294339260 1055 NATGYGLTFGVHSRIDETVAELSERIHAGNVYVN-RNLIGAVVgvqPFGGMGRSGTG 1110
Cdd:cd07559 406 NDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
682-1089 |
3.70e-44 |
|
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: 167.04 E-value: 3.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 682 LNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEV 761
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 762 REAVDFLRYY--------AAQTAAQFDNAT----HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIA 829
Cdd:cd07102 80 RGMLERARYMisiaeealADIRVPEKDGFEryirREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 830 AALVHALHAAGVPTDAVQLVPGDGGTvGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQGrsivliAETGGQNALI 909
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVG------LELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 910 ADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAH 989
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 990 IARMQAAG---LCVTRLGRDESGGlGTFVRPT-LIELD-TIDRLQREVFGPVLHVLRYRREQLGAVLdaINATGYGLTFG 1064
Cdd:cd07102 313 IADAIAKGaraLIDGALFPEDKAG-GAYLAPTvLTNVDhSMRVMREETFGPVVGIMKVKSDAEAIAL--MNDSEYGLTAS 389
|
410 420
....*....|....*....|....*
gi 294339260 1065 VHSRIDETVAELSERIHAGNVYVNR 1089
Cdd:cd07102 390 VWTKDIARAEALGEQLETGTVFMNR 414
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
668-1110 |
1.08e-43 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 166.62 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 668 ADNAQAaavgwVPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIV 747
Cdd:PRK11241 22 ANNGEV-----IDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 748 REAGKTLPDAIGEVREAVDFLRYYAAQTAAQFDNAT------------HRPLGVVLCISPWNFPLSIFCGQVAAALAAGN 815
Cdd:PRK11241 96 LEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIpghqadkrliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 816 AVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEvaqlISRTVSKRLSPQGRS 895
Cdd:PRK11241 176 TMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE----IGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 896 IVLiaETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLG 975
Cdd:PRK11241 252 VSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 976 PVIDAEARDNLEAHIARMQAAGLCVTRLGRDESGGlGTFVRPT-LIELDTIDRLQR-EVFGPVLHVLRYRREqlGAVLDA 1053
Cdd:PRK11241 330 PLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG-GNFFQPTiLVDVPANAKVAKeETFGPLAPLFRFKDE--ADVIAQ 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 294339260 1054 INATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGvqPFGGMGRSGTG 1110
Cdd:PRK11241 407 ANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGLG 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
679-1110 |
1.55e-43 |
|
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: 165.50 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADPRDqVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:cd07147 1 LEVTNPYTGEV-VARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRYyAAQTAAQFD-----------NATHR------PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKP 821
Cdd:cd07147 80 GEVARAIDTFRI-AAEEATRIYgevlpldisarGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 822 AEQTALIAAALVHALHAAGVPTDAVQLVP--GDGgtvGAALVAHPAVAGVMFTGSTEVAQLISRTVSKrlspqgRSIVLi 899
Cdd:cd07147 159 ASRTPLSALILGEVLAETGLPKGAFSVLPcsRDD---ADLLVTDERIKLLSFTGSPAVGWDLKARAGK------KKVVL- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 900 aETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVID 979
Cdd:cd07147 229 -ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 980 AEARDNLEAHI--ARMQAAGLcVTRLGRDesgglGTFVRPTLIE-LDTIDRLQR-EVFGPVLHVLRYRREQlgAVLDAIN 1055
Cdd:cd07147 308 ESEAERVEGWVneAVDAGAKL-LTGGKRD-----GALLEPTILEdVPPDMEVNCeEVFGPVVTVEPYDDFD--EALAAVN 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 294339260 1056 ATGYGLTFGVHSRIDETVAELSERIHAGNVyvnrnLIGAV----VGVQPFGGMGRSGTG 1110
Cdd:cd07147 380 DSKFGLQAGVFTRDLEKALRAWDELEVGGV-----VINDVptfrVDHMPYGGVKDSGIG 433
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
673-1114 |
1.80e-43 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 166.04 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 673 AAAVGW-VPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSA-APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREA 750
Cdd:cd07144 18 KSSDGEtIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 751 GKTL-PDAIGEVREAVDFLRYYA-----------AQTAAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVL 818
Cdd:cd07144 97 GKPYhSNALGDLDEIIAVIRYYAgwadkiqgktiPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 819 AKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLspqgRSIVL 898
Cdd:cd07144 177 IKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL----KAVTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 899 iaETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAM-DDWSLGNPDRMHTDLGPV 977
Cdd:cd07144 253 --ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 978 IDAEARDNLEAHI--ARMQAAGLCVTRLGRDESGGLGTFVRPTlIELDTIDR---LQREVFGPVLHVLRYRREQlgavlD 1052
Cdd:cd07144 331 VSKTQYDRVLSYIekGKKEGAKLVYGGEKAPEGLGKGYFIPPT-IFTDVPQDmriVKEEIFGPVVVISKFKTYE-----E 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1053 AI---NATGYGLTFGVHSRiDETVA-ELSERIHAGNVYVNRNLIGAvVGVqPFGGMGRSGTGPKAG 1114
Cdd:cd07144 405 AIkkaNDTTYGLAAAVFTK-DIRRAhRVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
680-1114 |
2.53e-43 |
|
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: 165.60 E-value: 2.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADpRDQVGWVRQTTRTEVDEATRRAQSA----APiWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLP 755
Cdd:cd07141 25 PTINPAT-GEKICEVQEGDKADVDKAVKAARAAfklgSP-WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 756 DA-IGEVREAVDFLRYYAAQT-----------AAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAE 823
Cdd:cd07141 103 KSyLVDLPGAIKVLRYYAGWAdkihgktipmdGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 824 QTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVS----KRLSpqgrsivli 899
Cdd:cd07141 183 QTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGksnlKRVT--------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 900 AETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVID 979
Cdd:cd07141 254 LELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 980 AEARDNLEAHI-------ARMQAAGlcvtrlgrDESGGLGTFVRPTLIElDTIDRL---QREVFGPVLHVLRYrrEQLGA 1049
Cdd:cd07141 334 EEQFKKILELIesgkkegAKLECGG--------KRHGDKGYFIQPTVFS-DVTDDMriaKEEIFGPVQQIFKF--KTIDE 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1050 VLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNrnlIGAVVGVQ-PFGGMGRSGTGPKAG 1114
Cdd:cd07141 403 VIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
686-1114 |
1.00e-42 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 164.22 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 686 DPR--DQVGWVRQTTRTEVDEATRRAQSA---APiWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGK--TLPDAI 758
Cdd:PLN02766 42 DPRtgEVIARIAEGDKEDVDLAVKAAREAfdhGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKlfALGKAV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 gEVREAVDFLRYYAA----------QTAAQFDNAT-HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTAL 827
Cdd:PLN02766 121 -DIPAAAGLLRYYAGaadkihgetlKMSRQLQGYTlKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 828 IAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSK-RLSPqgrsivLIAETGGQN 906
Cdd:PLN02766 200 SALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQ------VSLELGGKS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 907 ALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNL 986
Cdd:PLN02766 274 PLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 987 EAHI--ARMQAAGLCVtrlGRDESGGLGTFVRPTLIELDTIDRL--QREVFGPVLHVLRYRreqlgAVLDAI---NATGY 1059
Cdd:PLN02766 354 LSYIehGKREGATLLT---GGKPCGDKGYYIEPTIFTDVTEDMKiaQDEIFGPVMSLMKFK-----TVEEAIkkaNNTKY 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 294339260 1060 GLTFGVHSRIDETVAELSERIHAGNVYVNRNLigAVVGVQPFGGMGRSGTGPKAG 1114
Cdd:PLN02766 426 GLAAGIVTKDLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
679-1110 |
1.32e-41 |
|
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: 160.31 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADPRDQVGWVRqTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:cd07117 18 IDSYNPANGETLSEITD-ATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 G-EVREAVDFLRYYAA------QTAAQFDNAT-----HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA 826
Cdd:cd07117 97 AvDIPLAADHFRYFAGviraeeGSANMIDEDTlsivlREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 827 LIAAALVHALHAAgVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQgrsivlIAETGGQN 906
Cdd:cd07117 177 LSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA------TLELGGKS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 907 ALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNL 986
Cdd:cd07117 250 ANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 987 EAHI-ARMQAAGLCVTRLGRDESGGL--GTFVRPTLIELDTID-RL-QREVFGPVLHVLRYRREQlgAVLDAINATGYGL 1061
Cdd:cd07117 330 LSYVdIAKEEGAKILTGGHRLTENGLdkGFFIEPTLIVNVTNDmRVaQEEIFGPVATVIKFKTED--EVIDMANDSEYGL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 294339260 1062 TFGVHSRiDETVA-ELSERIHAGNVYVNR-NLIGAVVgvqPFGGMGRSGTG 1110
Cdd:cd07117 408 GGGVFTK-DINRAlRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
679-1114 |
5.78e-41 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 159.13 E-value: 5.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSA-----APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKT 753
Cdd:PLN02467 25 IPVVNPAT-EETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 754 LPDAIGEVREAVDFLRYYAAQTAA--------------QFDNATHR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVL 818
Cdd:PLN02467 104 LDEAAWDMDDVAGCFEYYADLAEAldakqkapvslpmeTFKGYVLKePLGVVGLITPWNYPLLMATWKVAPALAAGCTAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 819 AKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivL 898
Cdd:PLN02467 184 LKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKP------V 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 899 IAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVI 978
Cdd:PLN02467 258 SLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 979 DAEARDNLEAHIARMQAAGlcVTRL---GRDESGGLGTFVRPTLI-ELDTIDRLQR-EVFGPVLHVLRYRREQlgAVLDA 1053
Cdd:PLN02467 338 SEGQYEKVLKFISTAKSEG--ATILcggKRPEHLKKGFFIEPTIItDVTTSMQIWReEVFGPVLCVKTFSTED--EAIEL 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294339260 1054 INATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNligavvgvQ------PFGGMGRSGTGPKAG 1114
Cdd:PLN02467 414 ANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCS--------QpcfcqaPWGGIKRSGFGRELG 472
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
679-1088 |
2.35e-38 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 151.06 E-value: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADPRDQVGwVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:PLN00412 33 VAITNPSTRKTQYK-VQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRYYAAQ-----TAAQFDN--------------ATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLA 819
Cdd:PLN00412 112 TEVVRSGDLISYTAEEgvrilGEGKFLVsdsfpgnernkyclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 820 KPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFT-GSTEVAqlISRtvskrlspQGRSIVL 898
Cdd:PLN00412 192 KPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA--ISK--------KAGMVPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 899 IAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRmHTDLGPVI 978
Cdd:PLN00412 262 QMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 979 DAEARDNLEAHI--ARMQAAGLCvTRLGRDesgglGTFVRPTLIELDTID-RLQ-REVFGPVLHVLRYRREQLGavLDAI 1054
Cdd:PLN00412 341 SESSANFIEGLVmdAKEKGATFC-QEWKRE-----GNLIWPLLLDNVRPDmRIAwEEPFGPVLPVIRINSVEEG--IHHC 412
|
410 420 430
....*....|....*....|....*....|....*
gi 294339260 1055 NATGYGLTFGVHSR-IDETVAeLSERIHAGNVYVN 1088
Cdd:PLN00412 413 NASNFGLQGCVFTRdINKAIL-ISDAMETGTVQIN 446
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
667-1114 |
3.86e-38 |
|
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: 149.76 E-value: 3.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 667 PADNAQaaaVGWVPVLNPADprdqvgwvrqttrteVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLI 746
Cdd:cd07098 3 PATGQH---LGSVPADTPED---------------VDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 747 VREAGKTLPDA-IGEVREAVDFLRYYAA--QTAAQFD------NATHR-------PLGVVLCISPWNFPL---------S 801
Cdd:cd07098 65 CRDTGKTMVDAsLGEILVTCEKIRWTLKhgEKALRPEsrpgglLMFYKrarveyePLGVVGAIVSWNYPFhnllgpiiaA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 802 IFCGQvaaalaagnAVLAKPAEQTA----LIAAALVHALHAAGVPTDAVQLVPGDGGTvGAALVAHPAVAGVMFTGSTEV 877
Cdd:cd07098 145 LFAGN---------AIVVKVSEQVAwssgFFLSIIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 878 AQLISRTVSKRLSPqgrsivLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRD 957
Cdd:cd07098 215 GKKVMAAAAESLTP------VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 958 AMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAG---LCVTRLGRDESGGLGTFVRPTLIELDTIDR--LQREV 1032
Cdd:cd07098 289 RVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGarlLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMkiAQEEV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1033 FGPVLHVLRYRREQlgavlDAI---NATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRnlIGAVVGVQ--PFGGMGRS 1107
Cdd:cd07098 369 FGPVMVVMKASDDE-----EAVeiaNSTEYGLGASVFGKDIKRARRIASQLETGMVAIND--FGVNYYVQqlPFGGVKGS 441
|
....*..
gi 294339260 1108 GTGPKAG 1114
Cdd:cd07098 442 GFGRFAG 448
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
728-1110 |
1.52e-37 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 146.80 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 728 LQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQT------AAQFDNATH------RPLGVVLCISP 795
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWArryegeIIQSDRPGEnillfkRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 796 WNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGST 875
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 876 EVAQLISRTVSKRLspqgrsIVLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMI 955
Cdd:PRK10090 161 SAGEKIMAAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 956 RDAMDDWSLGNP-DRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTrLGRDESGGLGTFVRPTLIeLDT---IDRLQRE 1031
Cdd:PRK10090 235 GEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVA-LGGKAVEGKGYYYPPTLL-LDVrqeMSIMHEE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294339260 1032 VFGPVLHVLRYrrEQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQpfGGMGRSGTG 1110
Cdd:PRK10090 313 TFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSGIG 387
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
671-1103 |
3.74e-37 |
|
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: 146.95 E-value: 3.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 671 AQAAAVGWVPVLNPADpRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREA 750
Cdd:TIGR01722 10 AEGASGTYIPVTNPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 751 GKTLPDAIGEVREAVDFLRY-----------YAAQTAAQFDNATHR-PLGVVLCISP---------WNFPLSIFCGQvaa 809
Cdd:TIGR01722 89 GKTHSDALGDVARGLEVVEHacgvnsllkgeTSTQVATRVDVYSIRqPLGVCAGITPfnfpamiplWMFPIAIACGN--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 810 alaagnAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGaALVAHPAVAGVMFTGSTEVAQLISRTVS--- 886
Cdd:TIGR01722 166 ------TFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTTGSahg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 887 KRLSpqgrsivliAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLcIQEDVADRVIGMIRDAMDDWSLGN 966
Cdd:TIGR01722 239 KRVQ---------ALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAA-VLVGAADEWVPEIRERAEKIRIGP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 967 PDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRD---ESGGLGTFVRPTLIE--LDTIDRLQREVFGPVLHVLR 1041
Cdd:TIGR01722 309 GDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGykvDGYEEGNWVGPTLLErvPPTMKAYQEEIFGPVLCVLE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294339260 1042 YrrEQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNlIGAVVGVQPFGG 1103
Cdd:TIGR01722 389 A--DTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP-IPVPLPYFSFTG 447
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
681-1110 |
1.07e-36 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 146.19 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADPRdQVGWVRQTTRTEVDEATRRAQSA--APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTL---- 754
Cdd:PRK09847 39 TVDPVTQA-PLAKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIrhsl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 755 ----PDAIGEVR---EAVDFLRYYAAQTAAQFDNATHR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTA 826
Cdd:PRK09847 118 rddiPGAARAIRwyaEAIDKVYGEVATTSSHELAMIVRePVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 827 LIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTevaqlisRTVSKRLSPQGRSIV--LIAETGG 904
Cdd:PRK09847 198 LSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGST-------RTGKQLLKDAGDSNMkrVWLEAGG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 905 QNALI--ADSSALaEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEA 982
Cdd:PRK09847 271 KSANIvfADCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAH 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 983 RDNLEAHIARMQAAGlcvTRLGRDESGGLGTFVRPT-LIELDTIDRLQR-EVFGPVLHVLRYRREQlgAVLDAINATGYG 1060
Cdd:PRK09847 350 ADSVHSFIREGESKG---QLLLDGRNAGLAAAIGPTiFVDVDPNASLSReEIFGPVLVVTRFTSEE--QALQLANDSQYG 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 294339260 1061 LTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVvgVQPFGGMGRSGTG 1110
Cdd:PRK09847 425 LGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
705-1114 |
7.31e-36 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 144.57 E-value: 7.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 705 ATRRAQSAAPiWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG-EVREAVDFLRYYAAQtAAQFDNAT 783
Cdd:PLN02466 103 AARKAFDEGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGW-ADKIHGLT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 784 ------------HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPG 851
Cdd:PLN02466 181 vpadgphhvqtlHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 852 DGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSK-RLSPqgrsivLIAETGGQNALIADSSALAEQLVADVLTSAFDS 930
Cdd:PLN02466 261 FGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsNLKP------VTLELGGKSPFIVCEDADVDKAVELAHFALFFN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 931 AGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVtRLGRDESGG 1010
Cdd:PLN02466 335 QGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATL-ECGGDRFGS 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1011 LGTFVRPTLIElDTIDRL---QREVFGPVLHVLRYRreQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYV 1087
Cdd:PLN02466 414 KGYYIQPTVFS-NVQDDMliaQDEIFGPVQSILKFK--DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWV 490
|
410 420
....*....|....*....|....*...
gi 294339260 1088 N-RNLIGAVVgvqPFGGMGRSGTGPKAG 1114
Cdd:PLN02466 491 NcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
682-1114 |
1.24e-35 |
|
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: 142.63 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 682 LNPADpRDQVGWVRQTTRTEVDEATRRAQSA--APIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG 759
Cdd:cd07140 26 INPTD-GSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 760 -EVREAVDFLRYYAA------------QTAAQFDNAT---HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAE 823
Cdd:cd07140 105 tHVGMSIQTFRYFAGwcdkiqgktipiNQARPNRNLTltkREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 824 QTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVS----KRLSpqgrsivli 899
Cdd:cd07140 185 VTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAvsnlKKVS--------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 900 AETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPvid 979
Cdd:cd07140 256 LELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP--- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 980 aearDNLEAHIARMqaagLCVTRLGRDESGGL----------GTFVRPTLIElDTIDRL---QREVFGPVLHVLRYRREQ 1046
Cdd:cd07140 333 ----QNHKAHLDKL----VEYCERGVKEGATLvyggkqvdrpGFFFEPTVFT-DVEDHMfiaKEESFGPIMIISKFDDGD 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294339260 1047 LGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGvqPFGGMGRSGTGPKAG 1114
Cdd:cd07140 404 VDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLG 469
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
694-1110 |
3.32e-35 |
|
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: 141.44 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 694 VRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIG-EVREAVDFLRYYA 772
Cdd:cd07116 32 VPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAaDIPLAIDHFRYFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 773 ----AQ--TAAQFDNAT-----HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTAlIAAALVHALHAAGV 841
Cdd:cd07116 112 gcirAQegSISEIDENTvayhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTP-ASILVLMELIGDLL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 842 PTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQ--NALIADssalaeql 919
Cdd:cd07116 191 PPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP------VTLELGGKspNIFFAD-------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 920 VADVLTSAFDSA-----------GQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEA 988
Cdd:cd07116 257 VMDADDAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 989 HIARMQAAGLCVTRLG-RDESGGL--GTFVRPTLIELDTIDRL-QREVFGPVLHVLRYRREQlgAVLDAINATGYGLTFG 1064
Cdd:cd07116 337 YIDIGKEEGAEVLTGGeRNELGGLlgGGYYVPTTFKGGNKMRIfQEEIFGPVLAVTTFKDEE--EALEIANDTLYGLGAG 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 294339260 1065 VHSRIDETVAELSERIHAGNVYVnrNLIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07116 415 VWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
679-1121 |
1.37e-34 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 139.97 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 679 VPVLNPADPRdQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI 758
Cdd:PLN02315 36 VSSVNPANNQ-PIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRYyAAQTAAQFDNA-------TH------RPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQT 825
Cdd:PLN02315 115 GEVQEIIDMCDF-AVGLSRQLNGSiipserpNHmmmevwNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 826 ALIAAALVHALHAA----GVPTDAVQLVPGdGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLspqGRSIVliaE 901
Cdd:PLN02315 194 PLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GKCLL---E 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 902 TGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAE 981
Cdd:PLN02315 267 LSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 982 ARDNLEAHIARMQAAGLCVTRLGRDESGGlGTFVRPTLIELD-TIDRLQREVFGPVLHVLRYRreQLGAVLDAINATGYG 1060
Cdd:PLN02315 347 SKKNFEKGIEIIKSQGGKILTGGSAIESE-GNFVQPTIVEISpDADVVKEELFGPVLYVMKFK--TLEEAIEINNSVPQG 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1061 LTFGVHSRIDETVAEL--SERIHAGNVYVNRNLIGAVVGvQPFGGMGRSGTGPKAGG---PLYLHR 1121
Cdd:PLN02315 424 LSSSIFTRNPETIFKWigPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSdswKQYMRR 488
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
680-1110 |
5.21e-34 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 137.70 E-value: 5.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 680 PVLNPADPrDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAI- 758
Cdd:PRK13252 25 EVINPATG-EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 759 GEVREAVDFLRYYAAQTAAQFDNA----------THR-PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTAL 827
Cdd:PRK13252 104 VDIVTGADVLEYYAGLAPALEGEQiplrggsfvyTRRePLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 828 IAAALVHALHAAGVPTDAVQLVPGDgGTVGAALVAHPAVAGVMFTGSTEvaqlisrTVSKRLSPQGRSI--VLIaETGGQ 905
Cdd:PRK13252 184 TALKLAEIYTEAGLPDGVFNVVQGD-GRVGAWLTEHPDIAKVSFTGGVP-------TGKKVMAAAAASLkeVTM-ELGGK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 906 NALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDN 985
Cdd:PRK13252 255 SPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 986 LEAHIARMQAAG---LC-VTRLGRDESGGlGTFVRPTLIE--LDTIDRLQREVFGPVLHVLRYRREQlgAVLDAINATGY 1059
Cdd:PRK13252 335 VLGYIEKGKAEGarlLCgGERLTEGGFAN-GAFVAPTVFTdcTDDMTIVREEIFGPVMSVLTFDDED--EVIARANDTEY 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 294339260 1060 GLTFGVHSRiDETVA-ELSERIHAGNVYVNR-NLIGAVVgvqPFGGMGRSGTG 1110
Cdd:PRK13252 412 GLAAGVFTA-DLSRAhRVIHQLEAGICWINTwGESPAEM---PVGGYKQSGIG 460
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
701-1110 |
2.36e-33 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 135.25 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 701 EVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYaAQTAAQF- 779
Cdd:PRK09406 24 EVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYY-AEHAEALl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 780 -----DNAT---------HRPLGVVLCISPWNFPL---SIFCGQVAAALAAGNAVLAKPAEQTALIaaaLVHALHAAGVP 842
Cdd:PRK09406 103 adepaDAAAvgasrayvrYQPLGVVLAVMPWNFPLwqvVRFAAPALMAGNVGLLKHASNVPQTALY---LADLFRRAGFP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 843 TDAVQLVPGDGGTVGAALvAHPAVAGVMFTGStevaqlisrtvskrlSPQGRSIVLIA---------ETGGQNALIADSS 913
Cdd:PRK09406 180 DGCFQTLLVGSGAVEAIL-RDPRVAAATLTGS---------------EPAGRAVAAIAgdeikktvlELGGSDPFIVMPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 914 ALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARM 993
Cdd:PRK09406 244 ADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 994 QAAGLCVtRLGRDESGGLGTFVRPTLIELDTID-RLQR-EVFGPVLHVlrYRREQLGAVLDAINATGYGLTFGVHSRIDE 1071
Cdd:PRK09406 324 VAAGATI-LCGGKRPDGPGWFYPPTVITDITPDmRLYTeEVFGPVASL--YRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 294339260 1072 TVAELSERIHAGNVYVNrnliGAVVGVQ--PFGGMGRSGTG 1110
Cdd:PRK09406 401 EQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
681-1110 |
8.39e-29 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 121.76 E-value: 8.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 681 VLNPADpRDQVGWVRQTTRTEVDEATRRAQSA---APIWqvTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDA 757
Cdd:cd07148 3 VVNPFD-LKPIGEVPTVDWAAIDKALDTAHALfldRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 758 IGEVREAVDFLRYyAAQTAAQFDN-----------------ATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAK 820
Cdd:cd07148 80 KVEVTRAIDGVEL-AADELGQLGGreipmgltpasagriafTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 821 PAEQTALIAAALVHALHAAGVPTDAVQLVPGDgGTVGAALVAHPAVAGVMFTGSTEVAQLISrtvSKrLSPQGRSIVlia 900
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWMLR---SK-LAPGTRCAL--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 901 ETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDA 980
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 981 EARDNLEAHIARMQAAGlcvtrlGRDESGG--LG-TFVRPTLIeLDTIDRL---QREVFGPVLHVLRYRreQLGAVLDAI 1054
Cdd:cd07148 311 REVDRVEEWVNEAVAAG------ARLLCGGkrLSdTTYAPTVL-LDPPRDAkvsTQEIFGPVVCVYSYD--DLDEAIAQA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1055 NATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNlIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07148 382 NSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
784-1110 |
3.07e-28 |
|
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: 119.55 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 784 HRPLGVVLCISPWNFPLS---------IFCGQvaaalaagnAVLAKPAEQT----ALIaaalvHALHAAGVPTDAVQLVP 850
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQlalapligaIAAGN---------TVVLKPSELApatsALL-----AKLIPKYFDPEAVAVVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 851 GdGGTVGAALVAHPaVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNALIADSSALAEQLVADVLTSAFDS 930
Cdd:cd07087 164 G-GVEVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTP------VTLELGGKSPCIVDKDANLEVAARRIAWGKFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 931 AGQRCSALRLLCIQEDVADRVIGMIRDAMDDWsLGNPDRMHTDLGPVIDaeardnlEAHIARMQA---AGLCVTRLGRDE 1007
Cdd:cd07087 236 AGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIIN-------ERHFDRLASlldDGKVVIGGQVDK 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1008 SgglGTFVRPTLIELDTIDR--LQREVFGPVLHVLRYrrEQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNV 1085
Cdd:cd07087 308 E---ERYIAPTILDDVSPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV 382
|
330 340
....*....|....*....|....*
gi 294339260 1086 YVNRNLIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07087 383 CVNDVLLHAAIPNLPFGGVGNSGMG 407
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
654-1110 |
5.27e-26 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 113.42 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 654 MAYASPTVAEQPPPADNAQAAAVGWvpvlnpadprdqvgwvrqTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAAD 733
Cdd:PRK13968 1 MTITPATHAISVNPATGEQLSVLPW------------------AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 734 ALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQFDNAT-----------HRPLGVVLCISPWNFPLSI 802
Cdd:PRK13968 63 ALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPtlvenqqavieYRPLGTILAIMPWNFPLWQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 803 FCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVgAALVAHPAVAGVMFTGSTEVAQLIS 882
Cdd:PRK13968 143 VMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 883 RTVSKRLspqgRSIVLiaETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDW 962
Cdd:PRK13968 222 AQAGAAL----KKCVL--ELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 963 SLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTrLGRDESGGLGTFVRPTLIELDTIDR--LQREVFGPVLHVL 1040
Cdd:PRK13968 296 KMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLL-LGGEKIAGAGNYYAPTVLANVTPEMtaFREELFGPVAAIT 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1041 RYRREQlgAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRnlIGAVVGVQPFGGMGRSGTG 1110
Cdd:PRK13968 375 VAKDAE--HALELANDSEFGLSATIFTTDETQARQMAARLECGGVFING--YCASDARVAFGGVKKSGFG 440
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
784-1115 |
1.59e-25 |
|
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: 111.16 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 784 HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQT----ALIAAALVHAlhaagVPTDAVQLVPGDgGTVGAA 859
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTphtsAVIAKIIREA-----FDEDEVAVFEGD-AEVAQA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 860 LVAHPaVAGVMFTGSTEVAQLISRTVSKRLSpqgrSIVLiaETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALR 939
Cdd:cd07134 172 LLELP-FDHIFFTGSPAVGKIVMAAAAKHLA----SVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 940 LLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHT-DLGPVIDAEARDNLEAHIARMQAAGLCVtrlgrdESGGL----GTF 1014
Cdd:cd07134 245 YVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKV------EFGGQfdaaQRY 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1015 VRPTLIELDTIDR--LQREVFGPVLHVLRYrrEQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLI 1092
Cdd:cd07134 319 IAPTVLTNVTPDMkiMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVL 396
|
330 340
....*....|....*....|...
gi 294339260 1093 GAVVGVQPFGGMGRSGTGpKAGG 1115
Cdd:cd07134 397 HFLNPNLPFGGVNNSGIG-SYHG 418
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
626-1088 |
1.95e-22 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 103.67 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 626 RLNSAGLNLANEQQLASLSAALLRSAQHmayasPTVAEQPPPADN------AQAAAVGWVPVLNPADpRDQVGWVRQTTR 699
Cdd:PLN02419 77 RISGNNLRPLRPQFLALRSSWLSTSPEQ-----STQPQMPPRVPNliggsfVESQSSSFIDVINPAT-QEVVSKVPLTTN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 700 TEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQF 779
Cdd:PLN02419 151 EEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQM 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 780 DN------------ATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQ 847
Cdd:PLN02419 231 GEylpnvsngvdtySIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 848 LVPGDGGTVGaALVAHPAVAGVMFTGSTEVAQLIsrtvSKRLSPQGRSIVliAETGGQNALIADSSALAEQLVADVLTSA 927
Cdd:PLN02419 311 IVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHI----YARAAAKGKRIQ--SNMGAKNHGLVLPDANIDATLNALLAAG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 928 FDSAGQRCSALRLLCIQEDVA---DRVIGMIRdAMDDWSLGNPDrmhTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLG 1004
Cdd:PLN02419 384 FGAAGQRCMALSTVVFVGDAKsweDKLVERAK-ALKVTCGSEPD---ADLGPVISKQAKERICRLIQSGVDDGAKLLLDG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1005 RD---ESGGLGTFVRPTLIELDTIDR--LQREVFGPVLHVLryRREQLGAVLDAINATGYGLTFGVHSRIDETVAELSER 1079
Cdd:PLN02419 460 RDivvPGYEKGNFIGPTILSGVTPDMecYKEEIFGPVLVCM--QANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMD 537
|
....*....
gi 294339260 1080 IHAGNVYVN 1088
Cdd:PLN02419 538 IEAGQIGIN 546
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
786-1110 |
2.12e-22 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 102.80 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 786 PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAE---QTALIAAALVHALhaagVPTDAVQLVPGdGGTVGAALVA 862
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSElspHTSKLMAKLLTKY----LDPSYVRVIEG-GVEVTTELLK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 863 HPaVAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALRLLC 942
Cdd:PTZ00381 184 EP-FDHIFFTGSPRVGKLVMQAAAENLTP------CTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 943 IQEDVADRVIGMIRDAMDDWsLGNPDRMHTDLGPVIDaeardnlEAHIARMQaaGLCVTRLGRDESGG----LGTFVRPT 1018
Cdd:PTZ00381 257 VHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVN-------EFHTKRLA--ELIKDHGGKVVYGGevdiENKYVAPT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1019 LIELDTIDR--LQREVFGPVLHVLRYrrEQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVV 1096
Cdd:PTZ00381 327 IIVNPDLDSplMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLN 404
|
330
....*....|....
gi 294339260 1097 GVQPFGGMGRSGTG 1110
Cdd:PTZ00381 405 PNLPFGGVGNSGMG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
709-1125 |
1.95e-21 |
|
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: 99.23 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 709 AQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQTAAQFDNAT----- 783
Cdd:cd07084 8 ADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHEPgnhlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 784 -------HR---PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAG-VPTDAVQLVPGD 852
Cdd:cd07084 88 qglkqqsHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 853 GGTvGAALVAHPAVAGVMFTGSTEVAQ-LISrtvskrLSPQGRsivLIAETGGQNALIADSSALAEQLVAD-VLTSAFDS 930
Cdd:cd07084 168 GKT-MQALLLHPNPKMVLFTGSSRVAEkLAL------DAKQAR---IYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 931 AGQRCSALRLLCIQED-----VADRVIGMIRDAMDDWSLgnpdrmhtdLGPVIdaeaRDNLEAHIARMQAAGLCVTRLG- 1004
Cdd:cd07084 238 SGQKCTAQSMLFVPENwsktpLVEKLKALLARRKLEDLL---------LGPVQ----TFTTLAMIAHMENLLGSVLLFSg 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1005 -----RDESGGLGTFVRPTL-IELDTIDRLQ----REVFGPVLHVLRYRREQLGAVLDAINATGYGLTFGVHSRIDETVA 1074
Cdd:cd07084 305 kelknHSIPSIYGACVASALfVPIDEILKTYelvtEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQ 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 294339260 1075 ELSER--IHAGNVYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLVQP 1125
Cdd:cd07084 385 ELIGNlwVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRC 437
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
784-1110 |
7.95e-21 |
|
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: 96.91 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 784 HRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQT----ALIaaalvHALHAAGVPTDAVQLVPGDGGTVGAA 859
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTphtaALL-----AELVPKYLDPDAFQVVQGGVPETTAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 860 L---VAHpavagVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCS 936
Cdd:cd07135 181 LeqkFDK-----IFYTGSGRVGRIIAEAAAKHLTP----VTL--ELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 937 ALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRmHTDLGPVIDAEARDNLEAHIARmqAAGLCVTRLGRDESgglGTFVR 1016
Cdd:cd07135 250 APDYVLVDPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDT--TKGKVVIGGEMDEA---TRFIP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1017 PTLIELDTIDR--LQREVFGPVLHVLRYRREQlgAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGA 1094
Cdd:cd07135 324 PTIVSDVSWDDslMSEELFGPVLPIIKVDDLD--EAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHV 401
|
330
....*....|....*.
gi 294339260 1095 VVGVQPFGGMGRSGTG 1110
Cdd:cd07135 402 GVDNAPFGGVGDSGYG 417
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
702-1054 |
1.95e-20 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 96.07 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 702 VDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAAQ------T 775
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLvregswL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 776 AAQFDNA--------------THRPLGVVLCISPWNFPL--SIFCGQVAAALAAGNAVLAK--PA--EQTALIAAALVHA 835
Cdd:cd07129 81 DARIDPAdpdrqplprpdlrrMLVPLGPVAVFGASNFPLafSVAGGDTASALAAGCPVVVKahPAhpGTSELVARAIRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 836 LHAAGVPTDAVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLIAETGGQN-------AL 908
Cdd:cd07129 161 LRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEP----IPFYAELGSVNpvfilpgAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 909 IADSSALAEQLVADVLTsafdSAGQRCSALRLLCIQEDVA-DRVIGMIRDAMDDWSlgnPDRMhtdLGPVIdaeaRDNLE 987
Cdd:cd07129 237 AERGEAIAQGFVGSLTL----GAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAP---AQTM---LTPGI----AEAYR 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294339260 988 AHIARMQAAGLcVTRLGRDESGGLGTFVRPTLIELDTID-----RLQREVFGPVLHVLRYR-REQLGAVLDAI 1054
Cdd:cd07129 303 QGVEALAAAPG-VRVLAGGAAAEGGNQAAPTLFKVDAAAfladpALQEEVFGPASLVVRYDdAAELLAVAEAL 374
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
783-1110 |
1.01e-16 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 84.46 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 783 THRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQT----ALIAAALVHALhaagvPTDAVQLVPGdGGTVGA 858
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTprtsALLAELLAEYF-----DEDEVAVVTG-GADVAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 859 ALVA----HpavagVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGGQNALIADSSALAEQLVADVLTSAFDSAGQR 934
Cdd:cd07133 172 AFSSlpfdH-----LLFTGSTAVGRHVMRAAAENLTP----VTL--ELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 935 CSALRLLCIQEDVADRVIGMIRDAMD----DWsLGNPdrmhtDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGR-DESG 1009
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAkmypTL-ADNP-----DYTSIINERHYARLQGLLEDARAKGARVIELNPaGEDF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1010 GLGTFVRPTLIeLDTIDR---LQREVFGPVLHVLRYRReqLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVY 1086
Cdd:cd07133 315 AATRKLPPTLV-LNVTDDmrvMQEEIFGPILPILTYDS--LDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVT 391
|
330 340
....*....|....*....|....
gi 294339260 1087 VNRNLIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07133 392 INDTLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
786-1110 |
5.89e-16 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 82.07 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 786 PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAE----QTALIAAALVHAlhaagVPTDAVQLVPGdGGTVGAALV 861
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSElapaTSALLAKLIPEY-----LDTKAIKVIEG-GVPETTALL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 862 AHpAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGGQNALIADSSALAEQLVADVLTSAFDS-AGQRCSALRL 940
Cdd:cd07137 175 EQ-KWDKIFFTGSPRVGRIIMAAAAKHLTP----VTL--ELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 941 LCIQEDVADRVIGMIRDAMDDWSLGNPdRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESgglGTFVRPTLI 1020
Cdd:cd07137 248 VLVEESFAPTLIDALKNTLEKFFGENP-KESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEK---NLYIEPTIL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1021 ELDTIDRL--QREVFGPVLHVLRYRREQLGavLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGV 1098
Cdd:cd07137 324 LDPPLDSSimTEEIFGPLLPIITVKKIEES--IEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
330
....*....|..
gi 294339260 1099 QPFGGMGRSGTG 1110
Cdd:cd07137 402 LPFGGVGESGFG 413
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
98-146 |
1.34e-15 |
|
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: 71.73 E-value: 1.34e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 294339260 98 TDLRAAITAAWHRPEPECLPMLIELAQIPDAtQRAAVRQMAERLVEGVR 146
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPA-ERAAIRALARKLVEALR 48
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
723-1115 |
5.05e-14 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 76.67 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 723 ERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREAVDFLRYYAaQTAAQFDNATHRP---------------- 786
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYA-KLGAALGDARLLRdgeavqlgkdpafqgq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 787 ------LGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGV-PTDAVQLVPGDGGTVGAA 859
Cdd:PRK11903 143 hvlvptRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 860 LVAHPAVAgvmFTGSTEVAQLIsrtvskRLSPQ--GRSIVLIAETGGQNALI-----ADSSALAEQLVADVLTSAFDSAG 932
Cdd:PRK11903 223 LQPFDVVS---FTGSAETAAVL------RSHPAvvQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 933 QRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGR----DES 1008
Cdd:PRK11903 294 QKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGfalvDAD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1009 GGLGTFVRPTLIELDTIDRLQR----EVFGPVLHVLRYRREQLGAVL-----DAINATGYGLTFGVHSRIDETVAELSER 1079
Cdd:PRK11903 374 PAVAACVGPTLLGASDPDAATAvhdvEVFGPVATLLPYRDAAHALALarrgqGSLVASVYSDDAAFLAAAALELADSHGR 453
|
410 420 430
....*....|....*....|....*....|....*....
gi 294339260 1080 IHAGNVYVNRNLIGAVVgVQP---FGGMGRSGTGPKAGG 1115
Cdd:PRK11903 454 VHVISPDVAALHTGHGN-VMPqslHGGPGRAGGGEELGG 491
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
757-1110 |
4.55e-13 |
|
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: 73.02 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 757 AIGEVREAVDFLRYYAAQT------AAQFDNA--THRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAE---QT 825
Cdd:cd07132 63 VKNEIKYAISNLPEWMKPEpvkknlATLLDDVyiYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEvspAT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 826 A-LIAAAlvhalhaagVP----TDAVQLVPGdGGTVGAALVAHpAVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLia 900
Cdd:cd07132 143 AkLLAEL---------IPkyldKECYPVVLG-GVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTP----VTL-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 901 ETGGQNALIADSSALAEQLVADVLTSAFDSAGQRCSALR-LLCIQEdVADRVIGMIRDAMDDWsLGNPDRMHTDLGPVID 979
Cdd:cd07132 206 ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDyVLCTPE-VQEKFVEALKKTLKEF-YGEDPKESPDYGRIIN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 980 AEARDNLEAHIARMQAA-GLCVTRLGRdesgglgtFVRPTLI----ELDTIdrLQREVFGPVLHVLRYRreQLGAVLDAI 1054
Cdd:cd07132 284 DRHFQRLKKLLSGGKVAiGGQTDEKER--------YIAPTVLtdvkPSDPV--MQEEIFGPILPIVTVN--NLDEAIEFI 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 294339260 1055 NATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07132 352 NSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
820-1043 |
5.84e-12 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 69.99 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 820 KPAEQTALIAAALVHALHAAGV-PTDAVQLVPGDGGTVGAALVAHPAVAgvmFTGSTEVAQLIsrtvskRLSP--QGRSI 896
Cdd:cd07128 178 KPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVVA---FTGSAATAAKL------RAHPniVARSI 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 897 VLIAEtggqnaliADS---SALAEQLVADvlTSAFD------------SAGQRCSALRLLCIQEDVADRVIGMIRDAMDD 961
Cdd:cd07128 249 RFNAE--------ADSlnaAILGPDATPG--TPEFDlfvkevaremtvKAGQKCTAIRRAFVPEARVDAVIEALKARLAK 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 962 WSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRlGRDESGGLGT------FVRPTLIELDTIDRLQR----E 1031
Cdd:cd07128 319 VVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFG-GPDRFEVVGAdaekgaFFPPTLLLCDDPDAATAvhdvE 397
|
250
....*....|..
gi 294339260 1032 VFGPVLHVLRYR 1043
Cdd:cd07128 398 AFGPVATLMPYD 409
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
786-1110 |
9.05e-11 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 65.90 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 786 PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTAliaaaLVHALHAAGVPT----DAVQLVPGdGGTVGAALV 861
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAP-----ATSAFLAANIPKyldsKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 862 AHPAvAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNALIADSSALA---EQLVADVLTSAFDS-AGQRCSA 937
Cdd:PLN02203 182 QHKW-DKIFFTGSPRVGRIIMTAAAKHLTP------VALELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 938 LRLLCIQEDVADRVIGMIRDAMDDWSLGNPDRMHtDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESgglGTFVRP 1017
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEK---KLFIEP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1018 TLI---ELDTiDRLQREVFGPVLHVLRYRREQlgAVLDAINATGYGLTFGVHSRiDETvaeLSERI----HAGNVYVNRN 1090
Cdd:PLN02203 331 TILlnpPLDS-DIMTEEIFGPLLPIITVKKIE--DSIAFINSKPKPLAIYAFTN-NEK---LKRRIlsetSSGSVTFNDA 403
|
330 340
....*....|....*....|
gi 294339260 1091 LIGAVVGVQPFGGMGRSGTG 1110
Cdd:PLN02203 404 IIQYACDSLPFGGVGESGFG 423
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
786-1110 |
2.50e-10 |
|
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: 64.45 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 786 PLGVVLCISPWNFPL---------SIFCGQvaaalaagnAVLAKPAEQTA--------LIAAAlvhalhaagVPTDAVQL 848
Cdd:cd07136 100 PYGVVLIIAPWNYPFqlalapligAIAAGN---------TAVLKPSELTPntskviakIIEET---------FDEEYVAV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 849 VPGdGGTVGAALVAHPaVAGVMFTGSTEVAQLISRTVSKRLSPqgrsIVLiaETGGQNALIADSSALAEQLVADVLTSAF 928
Cdd:cd07136 162 VEG-GVEENQELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTP----VTL--ELGGKSPCIVDEDANLKLAAKRIVWGKF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 929 DSAGQRCSALRLLCIQEDVADRVIGMIRDAMDDWSLGNPdRMHTDLGPVIDaeardnlEAHIARMqaAGLcvtrLGRDE- 1007
Cdd:cd07136 234 LNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDP-LESPDYGRIIN-------EKHFDRL--AGL----LDNGKi 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1008 -SGGLGT----FVRPTLIELDTIDR--LQREVFGPVLHVLRYrrEQLGAVLDAINATGYGLTFGVHSRiDETVAE-LSER 1079
Cdd:cd07136 300 vFGGNTDretlYIEPTILDNVTWDDpvMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSE-DKKVEKkVLEN 376
|
330 340 350
....*....|....*....|....*....|.
gi 294339260 1080 IHAGNVYVNRNLIGAVVGVQPFGGMGRSGTG 1110
Cdd:cd07136 377 LSFGGGCINDTIMHLANPYLPFGGVGNSGMG 407
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
333-566 |
1.44e-09 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 62.03 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 333 SVKLSALH-PRYT--------RAQYARVMDELLPRLTALVELARRYDVGINIDAEEA------DRLELSLdlleTLCFNp 397
Cdd:PLN02681 187 SFPLFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYTslqpaiDYITYDL----AREFN- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 398 ALKGWNGIGFVVQAYQKRCPFVIDYLIDLARRSGHRLMVRLVKGAYWDSEIKRAQIDGLDGyPVYTRKVHTDVSYLACAH 477
Cdd:PLN02681 262 KGKDRPIVYGTYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 478 KLL--AAPDAAYPQFATHNAQTV---ASIMQMAGENYYAGQYEFQCLHGMGEPLydqVVGPVSAGKLARPcriYAPVGTH 552
Cdd:PLN02681 341 FLLekASNGDGEVMLATHNVESGelaAAKMNELGLHKGDPRVQFAQLLGMSDNL---SFGLGNAGFRVSK---YLPYGPV 414
|
250
....*....|....
gi 294339260 553 DTLLAYLVRRLLEN 566
Cdd:PLN02681 415 EEVIPYLLRRAEEN 428
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
786-1114 |
1.67e-09 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 61.99 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 786 PLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEqTALIAAALVHALHAAGVPTDAVQLVpgDGGTVGAALVAHPA 865
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSE-LAPASSALLAKLLEQYLDSSAVRVV--EGAVTETTALLEQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 866 VAGVMFTGSTEVAQLISRTVSKRLSPqgrsivLIAETGGQNALIADSSALAEQLVADVLTSAFD-SAGQRCSALRLLCIQ 944
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHLTP------VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 945 EDVADRVIGMIRDAMDDWSLGNPDRmHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLGRDESgglGTFVRPTLIELDT 1024
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRE---NLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1025 IDRL--QREVFGPVLHVLRYrrEQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGNVYVNRNLIGAVVGVQPFG 1102
Cdd:PLN02174 339 LDSLimSEEIFGPLLPILTL--NNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFG 416
|
330
....*....|..
gi 294339260 1103 GMGRSGTGPKAG 1114
Cdd:PLN02174 417 GVGESGMGAYHG 428
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-48 |
3.53e-08 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 51.36 E-value: 3.53e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 294339260 2 GATTTGIKMDEALRQRVRLAADRLGRTPHWLIKQATLNMVEHIERGE 48
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWRE 47
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
745-1067 |
7.11e-08 |
|
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: 56.74 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 745 LIVREAGKTLPDAIGEVREAVDFLRYYAAQT--------------AAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAA 810
Cdd:cd07126 87 LIQRVAPKSDAQALGEVVVTRKFLENFAGDQvrflarsfnvpgdhQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 811 LAAGNAVLAKPAEQTALIAAALVHALHAAGVPTDAVQLVPGDGGTVGAALV-AHPAVagVMFTGSTEVAQLISRTVSKRL 889
Cdd:cd07126 167 LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANPRM--TLFTGSSKVAERLALELHGKV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 890 SpqgrsivliAETGGQNALIADSSALAEQLVADVL-TSAFDSAGQRCSALRLLCIQEDVADRVIgmirdaMDDWSLGNPD 968
Cdd:cd07126 245 K---------LEDAGFDWKILGPDVSDVDYVAWQCdQDAYACSGQKCSAQSILFAHENWVQAGI------LDKLKALAEQ 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 969 RMHTDL--GPVI--DAEArdnLEAHIARM-QAAGLCVTRLGRDESGG-----LGTfVRPT--LIELDTI------DRLQR 1030
Cdd:cd07126 310 RKLEDLtiGPVLtwTTER---ILDHVDKLlAIPGAKVLFGGKPLTNHsipsiYGA-YEPTavFVPLEEIaieenfELVTT 385
|
330 340 350
....*....|....*....|....*....|....*..
gi 294339260 1031 EVFGPVLHVLRYRREQLGAVLDAINATGYGLTFGVHS 1067
Cdd:cd07126 386 EVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVS 422
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1194-1310 |
1.31e-05 |
|
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: 49.50 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1194 SVYTLPGPTGESNRYRLLPRsgGVW-CIP------QTVLGlvhHIAATLATGNlALIEAPSPDSPLAT------FLDA-L 1259
Cdd:cd07125 149 SDPELPGPTGELNGLELHGR--GVFvCISpwnfplAIFTG---QIAAALAAGN-TVIAKPAEQTPLIAaravelLHEAgV 222
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 294339260 1260 PPAVKAYVrscpPTQRD-------ALPELSVVLFEGDADALARLQDQLAQRDGLILRI 1310
Cdd:cd07125 223 PRDVLQLV----PGDGEeigealvAHPRIDGVIFTGSTETAKLINRALAERDGPILPL 276
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
539-1129 |
1.04e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.79 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 539 LARPCRIYAPVGTHDTLLAyLVRRLLENGANTSFV---NRIGDDAVPVSELVTD------PVDEARAIAvetsvlGAPHP 609
Cdd:COG3321 787 LADGVRVFLEVGPGPVLTG-LVRQCLAAAGDAVVLpslRRGEDELAQLLTALAQlwvagvPVDWSALYP------GRGRR 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 610 RIPLP-----RQLFSGLGAQARLNSAGLNLANEQQLASLSAALLRSAQHMAYASPTVAEQPPPADNAQAAAVGWVPVLNP 684
Cdd:COG3321 860 RVPLPtypfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 685 ADPRDQVGWVRQTTRTEVDEATRRAQSAAPIWQVTPPGERAACLQRAADALEQQMQNLLGLIVREAGKTLPDAIGEVREA 764
Cdd:COG3321 940 AALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAA 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 765 VDFLRYYAAQTAAQFDNATHRPLGVVLCISPWNFPLSIFCGQVAAALAAGNAVLAKPAEQTALIAAALVHALHAAGVPTD 844
Cdd:COG3321 1020 ALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALAL 1099
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 845 AVQLVPGDGGTVGAALVAHPAVAGVMFTGSTEVAQLISRTVSKRLSPQGRSIVLIAETGGQNALIADSSALAEQLVADVL 924
Cdd:COG3321 1100 AALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALAL 1179
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 925 TSAFDSAgqrcsalrllciqeDVADRVIGMIRDAMDDWSLGNPDRMHTDLGPVIDAEARDNLEAHIARMQAAGLCVTRLG 1004
Cdd:COG3321 1180 ALAAALA--------------AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAV 1245
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1005 RDESGGLGTFVRPTLIELDTIDRLQREVFGPVLHVLRYRREQLGAVLDAINATGYGLTFGVHSRIDETVAELSERIHAGN 1084
Cdd:COG3321 1246 AALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAAL 1325
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 294339260 1085 VYVNRNLIGAVVGVQPFGGMGRSGTGPKAGGPLYLHRLVQPLPQA 1129
Cdd:COG3321 1326 LAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAA 1370
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-42 |
1.87e-04 |
|
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: 40.05 E-value: 1.87e-04
10 20 30
....*....|....*....|....*....|....*....
gi 294339260 4 TTTGIKMDEALRQRVRLAADRLGRTPHWLIKQATLNMVE 42
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLE 39
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1197-1308 |
2.21e-04 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 45.96 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294339260 1197 TLPGPTGESNRYRLLPRsgGVW-CI-----PQTV-LGlvhHIAATLATGNlALIEAPSPDSPL------ATFLDA-LPPA 1262
Cdd:PRK11904 669 KLPGPTGESNELRLHGR--GVFvCIspwnfPLAIfLG---QVAAALAAGN-TVIAKPAEQTPLiaaeavKLLHEAgIPKD 742
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 294339260 1263 VKAYVRSCPPTQRDAL---PELSVVLFEGDADALARLQDQLAQRDGLIL 1308
Cdd:PRK11904 743 VLQLLPGDGATVGAALtadPRIAGVAFTGSTETARIINRTLAARDGPIV 791
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1326-1350 |
6.68e-03 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 40.95 E-value: 6.68e-03
10 20
....*....|....*....|....*
gi 294339260 1326 LTALVHEQSLSVNTAAAGGNAQLMT 1350
Cdd:PRK11904 1014 LLRFATEKTVTVNTTAAGGNASLLS 1038
|
|
| |
