|
Name |
Accession |
Description |
Interval |
E-value |
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
1-1317 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 2832.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1 MATTTLGVKLDDPTRERLKAAAASIDRTPHWLIKQAIFNYLEKLEGGATLTELSSATAKDGEDAGEV--QTDHAHQCFLE 78
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEAdtPAEEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 79 FAESILPQSVLRASITAAYRRPEPEVVPMLLEQARLPAATAEAANKLAASIAEKLRNQKSAGGRAGIVQGLLQEFSLSSQ 158
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGRAGMVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 159 EGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAGLTSSLSRIIGKSG 238
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 239 EPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGI 318
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 319 YEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLTGWNGIG 398
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 399 FVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLSVPEVI 478
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 479 YPQFATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVAEGKLNRPCRVYAPVGTHETLLAYLVRRLLEN 558
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 559 GANTSFVNRIADQSISIQELVADPVTQIEQMATLEGGFGLPHPRIPLPRDLYGAERANSAGIDMANEHRLASLSCALLAT 638
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLAS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 639 AHNNWKAAPMLGCAASSETPAPVLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGE 718
Cdd:PRK11809 641 AHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQ 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 719 IQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVL 798
Cdd:PRK11809 721 MQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 799 AKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGRPIPL 878
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 879 IAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVI 958
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 959 DAEAKAGIEKHIQAMRDKGRNVYQMAIADGEECKRGTFVMPTLIELESFDELQREIFGPVLHVVRYKRKEIDQLIAQINA 1038
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQINA 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1039 SGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPVDAIEQSFA 1118
Cdd:PRK11809 1041 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAVTLA 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1119 RGDAENAPDLRLREVLSKPLNALQAWAeSSKLAELAILCKQFAGQSQSGITRQLTGPTGERNSYAILPREHVLCLAEVEG 1198
Cdd:PRK11809 1121 RQDAEYPVDAQLRAALLAPLTALREWA-AEREPELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADTEQ 1199
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1199 DLLTQLAAVLAVGGSAVWPESEISKALFARLPKEVQARIQRVADWSKDEVVFDAVLHHGDSDQLRSVCQQVAQRAGAIVG 1278
Cdd:PRK11809 1200 DALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPIVS 1279
|
1290 1300 1310
....*....|....*....|....*....|....*....
gi 68348298 1279 VQGLSHGETAIALERLVIERALSVNTAAAGGNASLMTIG 1317
Cdd:PRK11809 1280 VQGFARGETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
76-1317 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 2098.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 76 FLEFAESILPQSVLRASITAAYRRPEPEVVPMLLEQARLPAATAEAANKLAASIAEKLRNQKSAGGragiVQGLLQEFSL 155
Cdd:PRK11905 2 FQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTG----VEALLQEYSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 156 SSQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAGLTSSLSRIIG 235
Cdd:PRK11905 78 SSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 236 KSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHG 315
Cdd:PRK11905 158 RLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 316 RGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLTGWN 395
Cdd:PRK11905 238 RGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 396 GIGFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLSVP 475
Cdd:PRK11905 318 GIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAAR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 476 EVIYPQFATHNAHTLSAIYHIAGQNYypgQYEFQCLHGMGEPLYEQVVGKvaeGKLNRPCRVYAPVGTHETLLAYLVRRL 555
Cdd:PRK11905 398 DVIYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGK---EKLGRPCRIYAPVGTHETLLAYLVRRL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 556 LENGANTSFVNRIADQSISIQELVADPVTQIEQMAtleggfGLPHPRIPLPRDLYGAERANSAGIDMANEHRLASLSCAL 635
Cdd:PRK11905 472 LENGANSSFVNRIVDENVPVEELIADPVEKVAAMG------VAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEAL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 636 LATAHNNWKAAPMLGCAASSETPAPVLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLM 715
Cdd:PRK11905 546 NAFAAKTWHAAPLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLM 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 716 EGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGN 795
Cdd:PRK11905 626 EAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGN 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 796 PVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqGRP 875
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GPP 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 876 IPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIG 955
Cdd:PRK11905 783 VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVG 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 956 PVIDAEAKAGIEKHIQAMRDKGRNVYQMAIADgeECKRGTFVMPTLIELESFDELQREIFGPVLHVVRYKRKEIDQLIAQ 1035
Cdd:PRK11905 863 PVIDAEAQANIEAHIEAMRAAGRLVHQLPLPA--ETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDD 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1036 INASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPVdaieq 1115
Cdd:PRK11905 941 INATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPT----- 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1116 SFARGDAENAPDLrlrevlskPLNALQAWAESSKLAELAILCKQFAGQSQSGITRQLTGPTGERNSYAILPREHVLCLAE 1195
Cdd:PRK11905 1016 PIPPAHESVDTDA--------AARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVAD 1087
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1196 VEGDLLTQLAAVLAVGGSAVWPESEISKALFARLPKEVQARIQRVADWSKDeVVFDAVLHHGDSDQLRSVCQQVAQRAGA 1275
Cdd:PRK11905 1088 TEEALLRQLAAALATGNVAVVAADSGLAAALADLPGLVAARIDWTQDWEAD-DPFAGALLEGDAERARAVRQALAARPGA 1166
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|..
gi 68348298 1276 IVGVQGLSHGEtAIALERLVIERALSVNTAAAGGNASLMTIG 1317
Cdd:PRK11905 1167 IVPLIAAEPTD-AYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
77-1110 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1616.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 77 LEFAESILPQSVLRASITAAYRRPEPEVVPMLLEQARLPAATAEAANKLAASIAEKLRNQKsagGRAGIVQGLLQEFSLS 156
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKK---KKLGGIDAFLQEYSLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 157 SQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAG--LTSSLSRII 234
Cdd:PRK11904 78 TEEGIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADgtPSGVLKRLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 235 GKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASH 314
Cdd:PRK11904 158 NRLGEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 315 GRGIYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLTGW 394
Cdd:PRK11904 238 GADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 395 NGIGFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLSV 474
Cdd:PRK11904 318 GGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 475 PEVIYPQFATHNAHTLSAIYHIAGQnyypGQYEFQCLHGMGEPLYEQVVgkvaeGKLNRPCRVYAPVGTHETLLAYLVRR 554
Cdd:PRK11904 398 RGAIYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 555 LLENGANTSFVNRIADQSISIQELVADPVTQIEQMATleggfgLPHPRIPLPRDLYGAERANSAGIDMANEHRLASLSCA 634
Cdd:PRK11904 469 LLENGANSSFVHRLVDPDVPIEELVADPVEKLRSFET------LPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 635 LLATAHNNWKAAPMLGCAAsseTPAPVLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADL 714
Cdd:PRK11904 543 IAAFLEKQWQAGPIINGEG---EARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 715 MEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFSNDAHRPlGPV--------------VCISPWNFPL 780
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLP-GPTgesnelrlhgrgvfVCISPWNFPL 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 781 AIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARL 860
Cdd:PRK11904 699 AIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARI 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 861 LQRNIAGRldnQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMA 940
Cdd:PRK11904 779 INRTLAAR---DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMA 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 941 ENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQMAIadGEECKRGTFVMPTLIELESFDELQREIFGPVLH 1020
Cdd:PRK11904 856 ELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPL--PAGTENGHFVAPTAFEIDSISQLEREVFGPILH 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1021 VVRYKRKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLY 1100
Cdd:PRK11904 934 VIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHY 1013
|
1050
....*....|
gi 68348298 1101 LYRLLSTRPV 1110
Cdd:PRK11904 1014 LLRFATEKTV 1023
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
80-1314 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1614.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 80 AESILPQSVLRASITAAYRRPEPEVVPMLLEQARLPAATAEAANKLAASIAEKLRNQKSAGGRAGIVQGLLQEFSLSSQE 159
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 160 GVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAGLTSS--LSRIIGKS 237
Cdd:COG4230 81 SEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLAsgLLRLLGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 238 GEPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRG 317
Cdd:COG4230 161 GRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 318 IYEGPGISIKLSALHPRYSRAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLTGWNGI 397
Cdd:COG4230 241 GGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 398 GFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLSVPEV 477
Cdd:COG4230 321 GGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 478 IYPQFATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVgkvaEGKLNRPCRVYAPVGTHETLLAYLVRRLLE 557
Cdd:COG4230 401 AQPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVG----RGKLGRPCRIYAPVGSHEDLLAYLVRRLLE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 558 NGANTSFVNRIADQSISIQELVADPVTQIEQMAtleggfGLPHPRIPLPRDLYGAERANSAGIDMANEHRLASLSCALLA 637
Cdd:COG4230 477 NGANSSFVNRIADEDVPVEELIADPVEKARALG------GAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 638 TAHNNWKAAPMLGCAASSETPAPVLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEG 717
Cdd:COG4230 551 AAEKQWQAAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEA 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 718 EIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFSND-AHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:COG4230 631 HRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPtVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNT 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 797 VLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRldnQGRPI 876
Cdd:COG4230 711 VLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR---DGPIV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 877 PLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGP 956
Cdd:COG4230 788 PLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGP 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 957 VIDAEAKAGIEKHIQAMRDKGRNVYQMAIadGEECKRGTFVMPTLIELESFDELQREIFGPVLHVVRYKRKEIDQLIAQI 1036
Cdd:COG4230 868 VIDAEARANLEAHIERMRAEGRLVHQLPL--PEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAI 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1037 NASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPVDAIEQS 1116
Cdd:COG4230 946 NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTA 1025
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1117 FArGDAenapdlrlrevlskPLNALQAWAEssklaelailckqfagqSQSGiTRQLTGPTGERNSYAILPREHVLCLAEV 1196
Cdd:COG4230 1026 AG-GNA--------------SLLALGDWLA-----------------SLLG-ALTLPGPTGERNTLTLRPRGRVLCLADS 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1197 EGDLLTQLAAVLAVGGSAVWPESeiskALFARLPKEVQARiqrvadwskdevvFDAVLHHGdsdQLRSVCQQVAQRAGAI 1276
Cdd:COG4230 1073 LEALLAQLAAALATGNRAVVAAD----LALAGLPAVLLPP-------------FDAVLFEG---RLRALRQALAARDGAI 1132
|
1210 1220 1230
....*....|....*....|....*....|....*...
gi 68348298 1277 VGVQGLshgetAIALERLVIEralsvntaaAGGNASLM 1314
Cdd:COG4230 1133 VPVIDA-----GYDLERLLEE---------AGGNASLM 1156
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
608-1109 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 749.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 608 DLYGAERANSAGIDMANEHRLASLSCALLATAHNNWKAAPMLGCAASSETPA-PVLNPSDHRDVVGHVQEATVEDVDNAI 686
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAqPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 687 QCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFSNDAHRP 766
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 767 LGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERV 846
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 847 KGVMFTGSTEVARLLQRNIAGRLDNqgrPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQED 926
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 927 SADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQMAIADGEECKRGTFVMPTLIELES 1006
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFELDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1007 FDELQREIFGPVLHVVRYKRKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGE 1086
Cdd:TIGR01238 398 IAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQ 477
|
490 500
....*....|....*....|...
gi 68348298 1087 GLSGTGPKAGGPLYLYRLLSTRP 1109
Cdd:TIGR01238 478 GLSGTGPKAGGPHYLYRLTQVQY 500
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
625-1108 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 702.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 625 EHRLASLSCALLATAHNNWKAAPML-GCAASSETPAPVLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAE 703
Cdd:cd07125 13 EVPLEALADALKAFDEKEWEAIPIInGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 704 RAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFS-----------NDAH-RPLGPVV 771
Cdd:cd07125 93 RAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 772 CISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMF 851
Cdd:cd07125 173 CISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 852 TGSTEVARLLQRNIAGRldnQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRV 931
Cdd:cd07125 253 TGSTETAKLINRALAER---DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 932 IEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQMAIADGEeckrGTFVMPTLIELESFDELQ 1011
Cdd:cd07125 330 IEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGN----GYFVAPGIIEIVGIFDLT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1012 REIFGPVLHVVRYKRKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGT 1091
Cdd:cd07125 406 TEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGT 485
|
490
....*....|....*..
gi 68348298 1092 GPKAGGPLYLYRLLSTR 1108
Cdd:cd07125 486 GPKAGGPNYLLRFGNEK 502
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
112-1112 |
0e+00 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 698.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 112 ARLPAATAEAANKLAASIAEKLRNQksaggRAGIVQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKIStgn 191
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAA-----PEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 192 wqphlgNSPSLFVNAATWGLLLTgklvsthneagltsslsrIIGKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANAS 271
Cdd:COG0506 75 ------KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 272 KFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKAShgrgiYEGPGISIKLSALHPRYSRAQYERVMEELYPRL 351
Cdd:COG0506 131 KLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 352 LSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLTGWNGIGFVIQAYQKRCPYVIDYVIDLARRSRHRLMIRLV 431
Cdd:COG0506 206 RPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 432 KGAYWDSEIKRAQVEGLeGYPVYTRKVYTDVSYIACARKLLSVPEVIYPQFATHNAHTLSAIYHIAGQ-NYYPGQYEFQC 510
Cdd:COG0506 286 KGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 511 LHGMGEPLYEQVVgKVAEGKLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADQSISIQELVADPVTQIEQMA 590
Cdd:COG0506 365 LYGMGEDLQRALA-AVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 591 tleggfGLPHPRIPLPRDLYGAERANSAGIDMANEHRLASLSCALLATAHNNWKAAPML-GCAASSETPAPVLNPSDHRD 669
Cdd:COG0506 444 ------PTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGaAAAAAAAAVAVVPAAAAAVV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 670 VVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLR 749
Cdd:COG0506 518 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAA 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 750 YYAVQARNDF-------SNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIP 822
Cdd:COG0506 598 AAAAAARAAAppppppgGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLL 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 823 EGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGRPIPLIAETGGQNAMIVDSSALTEQVVID 902
Cdd:COG0506 678 GGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVA 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 903 VVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQ 982
Cdd:COG0506 758 ASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLP 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 983 mAIADGEECKRGTFVMPTLIELESFDELQREIFGPVLHVVRYKRKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNV 1062
Cdd:COG0506 838 -GGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGG 916
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|
gi 68348298 1063 HAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPVDA 1112
Cdd:COG0506 917 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATA 966
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
662-1110 |
1.17e-154 |
|
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: 475.15 E-value: 1.17e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 662 LNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEV 741
Cdd:cd07083 37 VSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 742 REAVDFLRYYAVQARN-------------DFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07083 117 AEAIDFIRYYARAALRlrypavevvpypgEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGRPIPLIAETGGQNAM 888
Cdd:cd07083 197 GYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07083 277 IVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 969 HIQAMRDKGRNVYQMAIADGEeckrGTFVMPTLIELESFDE--LQREIFGPVLHVVRYKRKEIDQLIAQINASGYGLTLG 1046
Cdd:cd07083 357 YIEHGKNEGQLVLGGKRLEGE----GYFVAPTVVEEVPPKAriAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGG 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1047 VHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPV 1110
Cdd:cd07083 433 VYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEMKAV 496
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
266-567 |
6.32e-154 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 464.66 E-value: 6.32e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 266 ALANASKFEAKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVME 345
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 346 ELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPQLTGWNGIGFVIQAYQKRCPYVIDYVIDLARRSRHR 425
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 426 LMIRLVKGAYWDSEIKRAQvEGLEGYPVYTRKVYTDVSYIACARKLLSVPEVIYPQFATHNAHTLSAIYHIAGQ-NYYPG 504
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68348298 505 QYEFQCLHGMGEPLYEQVVGKvaegklNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNR 567
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAA------GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
652-1110 |
4.43e-137 |
|
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: 427.62 E-value: 4.43e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETPAPVLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAG 731
Cdd:COG1012 16 AAASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 732 KTFANAIAEVREAVDFLRYYAVQARN---DFSNDA---------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:COG1012 95 KPLAEARGEVDRAADFLRYYAGEARRlygETIPSDapgtrayvrREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 800 KPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLI 879
Cdd:COG1012 175 KPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVID 959
Cdd:COG1012 249 LELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLIS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 960 AEAKAGIEKHIQAMRDKGRNVyqmaIADGE--ECKRGTFVMPTLIEL--ESFDELQREIFGPVLHVVRYkrKEIDQLIAQ 1035
Cdd:COG1012 329 EAQLERVLAYIEDAVAEGAEL----LTGGRrpDGEGGYFVEPTVLADvtPDMRIAREEIFGPVLSVIPF--DDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68348298 1036 INASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGvQPFGGEGLSGTGPKaGGPLYLYRLLSTRPV 1110
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGRE-GGREGLEEYTETKTV 475
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
660-1110 |
1.02e-134 |
|
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: 422.79 E-value: 1.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:cd07124 49 ESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQA----------RNDFSNDAH-RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07124 129 DVAEAIDFLEYYAREMlrlrgfpvemVPGEDNRYVyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVA-RLLQRniAGRLD-NQGRPIPLIAETGGQN 886
Cdd:cd07124 209 AAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlRIYER--AAKVQpGQKWLKRVIAEMGGKN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGI 966
Cdd:cd07124 287 AIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 967 EKHIQAMRDKGRNVYQMAIADGEEckRGTFVMPTLIE-LESFDEL-QREIFGPVLHVVRYkrKEIDQLIAQINASGYGLT 1044
Cdd:cd07124 367 RRYIEIGKSEGRLLLGGEVLELAA--EGYFVQPTIFAdVPPDHRLaQEEIFGPVLAVIKA--KDFDEALEIANDTEYGLT 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68348298 1045 LGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPV 1110
Cdd:cd07124 443 GGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTV 508
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
653-1110 |
2.25e-129 |
|
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: 406.53 E-value: 2.25e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 653 ASSETPAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGK 732
Cdd:pfam00171 3 DSESETIEVINPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 733 TFANAIAEVREAVDFLRYYAVQARND----FSNDA-------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKP 801
Cdd:pfam00171 82 PLAEARGEVDRAIDVLRYYAGLARRLdgetLPSDPgrlaytrREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 802 AEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAE 881
Cdd:pfam00171 162 SELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAE 961
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 962 AKAGIEKHIQAMRDKGrnvYQMAIADGEECKRGTFVMPTLIE-LESFDELQR-EIFGPVLHVVRYkrKEIDQLIAQINAS 1039
Cdd:pfam00171 316 QLERVLKYVEDAKEEG---AKLLTGGEAGLDNGYFVEPTVLAnVTPDMRIAQeEIFGPVLSVIRF--KDEEEAIEIANDT 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68348298 1040 GYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVqPFGGEGLSGTGpKAGGPLYLYRLLSTRPV 1110
Cdd:pfam00171 391 EYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
683-1110 |
2.55e-119 |
|
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: 378.47 E-value: 2.55e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 683 DNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQAR------ 756
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARrlhgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 757 ------NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLP 830
Cdd:cd07078 81 ipspdpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 831 GQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDS 910
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 911 AGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVyqmaIADGE- 989
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKL----LCGGKr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 990 -ECKRGTFVMPTLIELESFDEL--QREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGN 1066
Cdd:cd07078 311 lEGGKGYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGT 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 68348298 1067 VYVNRNIVGAVVGvQPFGGEGLSGTGpKAGGPLYLYRLLSTRPV 1110
Cdd:cd07078 389 VWINDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
661-1110 |
1.82e-114 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 368.49 E-value: 1.82e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:PRK03137 54 SINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRYYAVQA-----------RNDFSNDAH-RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:PRK03137 134 TAEAIDFLEYYARQMlkladgkpvesRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVA-RLLQRniAGRL-DNQGRPIPLIAETGGQN 886
Cdd:PRK03137 214 AAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYER--AAKVqPGQIWLKRVIAEMGGKD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSvDIGPVIDAEAKAGI 966
Cdd:PRK03137 292 AIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 967 EKHIQAMRDKGRNVYQMAIADGEeckrGTFVMPTLI-ELESFDEL-QREIFGPVLHVVryKRKEIDQLIAQINASGYGLT 1044
Cdd:PRK03137 371 MSYIEIGKEEGRLVLGGEGDDSK----GYFIQPTIFaDVDPKARImQEEIFGPVVAFI--KAKDFDHALEIANNTEYGLT 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68348298 1045 LGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPV 1110
Cdd:PRK03137 445 GAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTV 510
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
662-1110 |
8.04e-109 |
|
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: 353.02 E-value: 8.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 662 LNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEV 741
Cdd:TIGR01237 51 INPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 742 REAVDFLRYYAVQA--------RNDFSNDAHR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:TIGR01237 131 AEAIDFMEYYARQMielakgkpVNSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 810 AQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGRPIPLIAETGGQNAMI 889
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 890 VDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKH 969
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 970 IQAMRDKGRnvyqMAIADGEECKRGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGV 1047
Cdd:TIGR01237 371 IEIGKAEGR----LVSGGCGDDSKGYFIGPTIFaDVDRKARLaQEEIFGPVVAFIRA--SDFDEALEIANNTEYGLTGGV 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68348298 1048 HTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPV 1110
Cdd:TIGR01237 445 ISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTV 507
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
655-1098 |
5.64e-99 |
|
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: 324.59 E-value: 5.64e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 655 SETPAPVLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTF 734
Cdd:cd07097 12 GGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 735 ANAIAEVREAVDFLRYYAVQA-----------RNDFSNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07097 92 PEARGEVTRAGQIFRYYAGEAlrlsgetlpstRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 803 EQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRldnqGRPIPLiaET 882
Cdd:cd07097 172 ELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR----GARVQL--EM 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07097 246 GGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 963 KAGIEKHIQAMRDKGRNVyqmaIADGEECKRGT---FVMPTLIELESFDE--LQREIFGPVLHVVRYkrKEIDQLIAQIN 1037
Cdd:cd07097 326 LEKDLRYIEIARSEGAKL----VYGGERLKRPDegyYLAPALFAGVTNDMriAREEIFGPVAAVIRV--RDYDEALAIAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68348298 1038 ASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVqPFGGEGLSGTGPKAGGP 1098
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
689-1110 |
2.14e-94 |
|
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: 308.00 E-value: 2.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 689 ALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQAR------------ 756
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADklggpelpspdp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 757 NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESV 836
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 837 GARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCS 916
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 917 ALRVLCLQEDSADRVIEMLKGamaenrlgnperLSVDIGPvidaeakagiekhiqamrdkgrnvyQMAIAdgeeckrgtf 996
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVT------------VLVDVDP-------------------------DMPIA---------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 997 vmptlielesfdelQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGA 1076
Cdd:cd06534 270 --------------QEEIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV 333
|
410 420 430
....*....|....*....|....*....|....
gi 68348298 1077 VVGvQPFGGEGLSGTGpKAGGPLYLYRLLSTRPV 1110
Cdd:cd06534 334 GPE-APFGGVKNSGIG-REGGPYGLEEYTRTKTV 365
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
661-1092 |
1.18e-93 |
|
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: 309.36 E-value: 1.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:cd07103 1 VINPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRYYAVQARNDF------SNDAHR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYgrtipsPAPGKRilvikqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAM 888
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 889 IVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLClQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 968 KHIQAMRDKGRNVyqmaIADGEEC-KRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLT 1044
Cdd:cd07103 313 ALVEDAVAKGAKV----LTGGKRLgLGGYFYEPTVLTdvTDDMLIMNEETFGPVAPIIPF--DTEDEVIARANDTPYGLA 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 68348298 1045 LGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVvgVQPFGGEGLSGTG 1092
Cdd:cd07103 387 AYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
652-1096 |
5.40e-92 |
|
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: 305.64 E-value: 5.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETPAPVLNPSDHRDVVGhVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAG 731
Cdd:cd07086 8 VGSGGETFTSRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 732 KTFANAIAEVREAVDfLRYYAV-QAR------------NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVL 798
Cdd:cd07086 87 KILPEGLGEVQEMID-ICDYAVgLSRmlygltipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 799 AKPAEQTPLVAAQAVRLLLEA----GIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqGR 874
Cdd:cd07086 166 WKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 875 PIpliAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDI 954
Cdd:cd07086 242 VL---LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 955 GPVIDAEAKAGIEKHIQAMRDKGRNV-YQMAIADGEEckRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYkrKEIDQ 1031
Cdd:cd07086 319 GPLINQAAVEKYLNAIEIAKSQGGTVlTGGKRIDGGE--PGNYVEPTIVTGVTDDAriVQEETFAPILYVIKF--DSLEE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68348298 1032 LIAQINASGYGLTLGVHTRIDETIAKVVDN--VHAGNVYVNRNIVGAVVGVqPFGGEGLSGTGPKAG 1096
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
652-1098 |
9.45e-91 |
|
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: 302.34 E-value: 9.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETpAPVLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAG 731
Cdd:cd07131 10 SASGET-FDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 732 KTFANAIAEVREAVDFLRYYAVQAR------------NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:cd07131 89 KPLAEGRGDVQEAIDMAQYAAGEGRrlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 800 KPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRnIAGRLdnqGRPIPLi 879
Cdd:cd07131 169 KPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE-TCARP---NKRVAL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 aETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVID 959
Cdd:cd07131 244 -EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 960 AEAKAGIEKHIQAMRDKGRNV-YQMAIADGEECKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYkrKEIDQLIAQI 1036
Cdd:cd07131 323 EAQLEKVLNYNEIGKEEGATLlLGGERLTGGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEV--SSLEEAIEIA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68348298 1037 NASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVqPFGGEGLSGTGPKAGGP 1098
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
661-1118 |
4.07e-85 |
|
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: 287.95 E-value: 4.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLmgLLAREA---GKTFANA 737
Cdd:cd07123 50 QVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYE--LNAATMlgqGKNVWQA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 738 -IAEVREAVDFLR---YYAVQARND--FSNDA-------HRPL-GPVVCISPWNFPlAIfSGQVAAALA-AGNPVLAKPA 802
Cdd:cd07123 128 eIDAACELIDFLRfnvKYAEELYAQqpLSSPAgvwnrleYRPLeGFVYAVSPFNFT-AI-GGNLAGAPAlMGNVVLWKPS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 803 EqTPLVAAQAV-RLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQgRPIP-LIA 880
Cdd:cd07123 206 D-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRY-RTYPrIVG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 881 ETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDA 960
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 961 EAKAGIEKHIqamrDKGRNVYQMAIADGEEC--KRGTFVMPTLIELE--SFDELQREIFGPVLHVVRYKRKEIDQLIAQI 1036
Cdd:cd07123 364 KAFDRIKGYI----DHAKSDPEAEIIAGGKCddSVGYFVEPTVIETTdpKHKLMTEEIFGPVLTVYVYPDSDFEETLELV 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1037 N-ASGYGLTLGVHTRiDETIAKVVDNVH---AGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRpvdA 1112
Cdd:cd07123 440 DtTSPYALTGAIFAQ-DRKAIREATDALrnaAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPR---T 515
|
....*.
gi 68348298 1113 IEQSFA 1118
Cdd:cd07123 516 IKETFV 521
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
660-1092 |
3.62e-84 |
|
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: 282.95 E-value: 3.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:cd07149 2 EVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQARNDFSN----DAH------------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGEtipfDASpggegrigftirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 804 QTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRnIAGRldnqgRPIPLiaETG 883
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIAR-KAGL-----KKVTL--ELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 963 KAGIEKHIQAMRDKGRNVyqmaIADGEecKRGTFVMPTLieLESFDELQR----EIFGPVLHVVRYkrKEIDQLIAQINA 1038
Cdd:cd07149 312 AERIEEWVEEAVEGGARL----LTGGK--RDGAILEPTV--LTDVPPDMKvvceEVFAPVVSLNPF--DTLDEAIAMAND 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1039 SGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
652-1110 |
1.47e-82 |
|
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: 278.76 E-value: 1.47e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETpAPVLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAG 731
Cdd:cd07088 9 SSSGET-IDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 732 KTFANAIAEVREAVDFLRYYAVQAR--------NDFSND----AHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:cd07088 87 KTLSLARVEVEFTADYIDYMAEWARriegeiipSDRPNEnifiFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 800 KPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLI 879
Cdd:cd07088 167 KPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVID 959
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 960 AEAKAGIEKHIQAMRDKG-RNVYQMAIADGEeckRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQI 1036
Cdd:cd07088 321 EAALDKVEEMVERAVEAGaTLLTGGKRPEGE---KGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1037 NASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQpfGGEGLSGTGpKAGGPLYLYRLLSTRPV 1110
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLG-GADGKHGLEEYLQTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
661-1096 |
3.15e-82 |
|
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: 277.51 E-value: 3.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRdVVGHVQEATVEDVDNAIQCALNA--APIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAI 738
Cdd:cd07114 1 SINPATGE-PWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 739 AEVREAVDFLRYYA------------VQARNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:cd07114 80 AQVRYLAEWYRYYAgladkiegavipVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 807 LVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQN 886
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLkGAMAEN-RLGNPERLSVDIGPVIDAEAKAG 965
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERL-VARARAiRVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 966 IEKHIQAMRDKG-RNVYQMAIADGEECKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYKRKeiDQLIAQINASGYG 1042
Cdd:cd07114 313 VERYVARAREEGaRVLTGGERPSGADLGAGYFFEPTILADVTNDMriAQEEVFGPVLSVIPFDDE--EEAIALANDSEYG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 68348298 1043 LTLGVHTRiDETIA-KVVDNVHAGNVYVN--RnivgAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:cd07114 391 LAAGIWTR-DLARAhRVARAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
661-1092 |
8.30e-78 |
|
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: 264.81 E-value: 8.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA- 739
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYA----------VQARNDFSNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07093 80 DIPRAAANFRFFAdyilqldgesYPQDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAM 888
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEakagiek 968
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 969 HiqamRDKGRNVYQMAIADG------------EECKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYKRKEidQLIA 1034
Cdd:cd07093 307 H----LEKVLGYVELARAEGatiltgggrpelPDLEGGYFVEPTVITGLDNDSrvAQEEIFGPVVTVIPFDDEE--EAIE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 68348298 1035 QINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVvgVQPFGGEGLSGTG 1092
Cdd:cd07093 381 LANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDL--RTPFGGVKASGIG 436
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
652-1096 |
2.61e-77 |
|
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: 264.07 E-value: 2.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETpAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPI--WQATPPAERAAILERAADLMEGEIQPLMGLLARE 729
Cdd:cd07091 15 SVSGKT-FPTINPATE-EVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 730 AGKTF-ANAIAEVREAVDFLRYYAVQA-----------RNDFSNDAHRPLGpvVC--ISPWNFPLAIFSGQVAAALAAGN 795
Cdd:cd07091 93 NGKPLeESAKGDVALSIKCLRYYAGWAdkiqgktipidGNFLAYTRREPIG--VCgqIIPWNFPLLMLAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 796 PVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRP 875
Cdd:cd07091 171 TVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAA---KSNLKK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 876 IPLiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIG 955
Cdd:cd07091 248 VTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 956 PVIDAEAKAGIEKHIQAMRDKGRNVyqmaIADGEE-CKRGTFVMPTLielesF----DEL---QREIFGPVLHVVRYkrK 1027
Cdd:cd07091 326 PQVSKAQFDKILSYIESGKKEGATL----LTGGERhGSKGYFIQPTV-----FtdvkDDMkiaKEEIFGPVVTILKF--K 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1028 EIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNR-NIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07091 395 TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
661-1092 |
5.25e-77 |
|
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: 262.56 E-value: 5.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPI-WQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:cd07109 1 VFDPSTGE-VFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQAR----------NDFSNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07109 80 DVEAAARYFEYYGGAADklhgetiplgPGYFVYTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAM 888
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPErLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 969 HIQAMRDKG-RNVYQMAIADGEECKrGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTL 1045
Cdd:cd07109 313 FVARARARGaRIVAGGRIAEGAPAG-GYFVAPTLLdDVPPDSRLaQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 68348298 1046 GVHTRIDETIAKVVDNVHAGNVYVNRniVGAVVGVQ-PFGGEGLSGTG 1092
Cdd:cd07109 390 GVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
659-1092 |
8.76e-77 |
|
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: 261.90 E-value: 8.76e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 659 APVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAI 738
Cdd:cd07145 1 IEVRNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 739 AEVREAVDFLRYYAVQAR---------NDFSNDAHR-------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKvlrgetipvDAYEYNERRiaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 803 EQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAET 882
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKK------VALEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07145 234 GGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 963 KAGIEKHI-QAMRDKGRNVYqmaiadGEECKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYkrKEIDQLIAQINAS 1039
Cdd:cd07145 314 VERMENLVnDAVEKGGKILY------GGKRDEGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKV--KDDEEAVEIANST 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1040 GYGLTLGVHTRIDETIAKVVDNVHAGNVYVNR-------NIvgavvgvqPFGGEGLSGTG 1092
Cdd:cd07145 386 EYGLQASVFTNDINRALKVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG 437
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
660-1092 |
1.45e-76 |
|
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: 262.12 E-value: 1.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQAT-PPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAI 738
Cdd:cd07082 19 EVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 739 AEVREAVDFLRYYAVQAR---NDFSN-DAHR------------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07082 98 KEVDRTIDYIRDTIEELKrldGDSLPgDWFPgtkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 803 EQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRnIAGRLdnqgrpiPLIAET 882
Cdd:cd07082 178 TQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK-QHPMK-------RLVLEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07082 250 GGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 963 KAGIEKHIQAMRDKGRNVYQmaiadGEECKRGTFVMPTLIELESfDELQ---REIFGPVLHVVRYkrKEIDQLIAQINAS 1039
Cdd:cd07082 330 ADFVEGLIDDAVAKGATVLN-----GGGREGGNLIYPTLLDPVT-PDMRlawEEPFGPVLPIIRV--NDIEEAIELANKS 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 68348298 1040 GYGLTLGVHTRIDETIAKVVDNVHAGNVYVN----RNIvgavvGVQPFGGEGLSGTG 1092
Cdd:cd07082 402 NYGLQASIFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIG 453
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
681-1090 |
2.64e-76 |
|
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: 259.90 E-value: 2.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 681 DVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVReavdflryyAVQARNDFS 760
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVA---------AMAGKIDIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 761 NDA--------------------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAG 820
Cdd:cd07095 72 IKAyhertgeratpmaqgravlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 821 IPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQgrpipLIAETGGQNAMIVDSSALTEQVV 900
Cdd:cd07095 152 LPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 901 IDVVSSAFDSAGQRCSALRVLCLQEDS-ADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQ-AMRDKGR 978
Cdd:cd07095 226 YLIVQSAFLTAGQRCTCARRLIVPDGAvGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQdLLALGGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 979 NVYQMAIADGeeckRGTFVMPTLIELESFDELQ-REIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAK 1057
Cdd:cd07095 306 PLLAMERLVA----GTAFLSPGIIDVTDAADVPdEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFER 379
|
410 420 430
....*....|....*....|....*....|...
gi 68348298 1058 VVDNVHAGNVYVNRNIVGAvVGVQPFGGEGLSG 1090
Cdd:cd07095 380 FLARIRAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
661-1092 |
4.85e-76 |
|
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: 259.38 E-value: 4.85e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSdHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:cd07106 1 VINPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRYYAVQARND---FSNDA------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQ 811
Cdd:cd07106 80 VGGAVAWLRYTASLDLPDeviEDDDTrrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 812 AVRLLLEAgIPEGVLQLLPGqGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNAMIVD 891
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 892 SSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQ 971
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 972 AMRDKGRNVyqmaIADGE-ECKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVH 1048
Cdd:cd07106 312 DAKAKGAKV----LAGGEpLDGPGYFIPPTIVDdpPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 68348298 1049 TRiDETIA-KVVDNVHAGNVYVNRNivGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07106 386 SS-DLERAeAVARRLEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
661-1096 |
9.49e-76 |
|
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: 258.91 E-value: 9.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANA-IA 739
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYA----------VQARNDFSNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07115 80 DVPRAADTFRYYAgwadkiegevIPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGGQNAM 888
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKR------VSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 969 HIQAMRDKGRNVYQMAIADGEeckRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYKRKEIDQLIAqiNASGYGLTLG 1046
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGA---RGFFVEPTIFAAVPPEMriAQEEIFGPVVSVMRFRDEEEALRIA--NGTEYGLAAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 68348298 1047 VHTRIDETIAKVVDNVHAGNVYVnrNIVGAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:cd07115 389 VWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
681-1098 |
2.73e-75 |
|
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: 257.07 E-value: 2.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 681 DVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARN--- 757
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 758 ---------DFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV-RLLLEAGIPEGVLQ 827
Cdd:cd07104 81 eilpsdvpgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 828 LLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRnIAGRLdnqgrpIPLIA-ETGGQNAMIVDSSALTEQVVIDVVSS 906
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGE-LAGRH------LKKVAlELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 907 AFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVyqmaI 985
Cdd:cd07104 234 AFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL----L 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 986 ADGEEckRGTFVMPTLI-----ELESFDElqrEIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVD 1060
Cdd:cd07104 309 TGGTY--EGLFYQPTVLsdvtpDMPIFRE---EIFGPVAPVIPF--DDDEEAVELANDTEYGLSAAVFTRDLERAMAFAE 381
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 68348298 1061 NVHAGNVYVNRNIV--GAVVgvqPFGGEGLSGTGpKAGGP 1098
Cdd:cd07104 382 RLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
651-1092 |
6.07e-75 |
|
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: 257.45 E-value: 6.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 651 CAASSETPAPVLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREA 730
Cdd:cd07085 10 VESKTTEWLDVYNPATGE-VIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 731 GKTFANAIAEVR---EAVDF--------LRYYAVQARNDFsnDAH---RPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:cd07085 89 GKTLADARGDVLrglEVVEFacsiphllKGEYLENVARGI--DTYsyrQPLGVVAGITPFNFPAMIPLWMFPMAIACGNT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 797 VLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGArLVGDERVKGVMFTGSTEVARLLQRNIAgrldNQGRPI 876
Cdd:cd07085 167 FVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYERAA----ANGKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 877 plIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGP 956
Cdd:cd07085 242 --QALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 957 VIDAEAKAGIEKHIQAMRDKGRNVyqmaIADG-----EECKRGTFVMPTLI-----ELESFDElqrEIFGPVLHVVRYkr 1026
Cdd:cd07085 320 VISPAAKERIEGLIESGVEEGAKL----VLDGrgvkvPGYENGNFVGPTILdnvtpDMKIYKE---EIFGPVLSIVRV-- 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 68348298 1027 KEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIvgAV-VGVQPFGGEGLSGTG 1092
Cdd:cd07085 391 DTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPI--PVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
661-1092 |
6.78e-74 |
|
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: 254.09 E-value: 6.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIW-QATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:cd07089 1 VINPATE-EVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 -EVREAVDFLRYYAVQARN-----DFSNDA-----------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSfpwefDLPVPAlrggpgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 803 EQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaET 882
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 963 KAGIEKHIQAMRDKG-RNVYQMAIADGEEckRGTFVMPTLielesFDEL-------QREIFGPVLHVVRYkrKEIDQLIA 1034
Cdd:cd07089 314 RDRVEGYIARGRDEGaRLVTGGGRPAGLD--KGFYVEPTL-----FADVdndmriaQEEIFGPVLVVIPY--DDDDEAVR 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1035 QINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNrnivGAVVGV--QPFGGEGLSGTG 1092
Cdd:cd07089 385 IANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
651-1092 |
2.00e-73 |
|
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: 253.39 E-value: 2.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 651 CAASSETPAPVLNPSDhRDVVGHVQEATVEDVDNAIQCALNA--APIWQATPPAERAAILERAADLMEGEIQPLMGLLAR 728
Cdd:cd07119 7 VEAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 729 EAGKTFANAIAEVREAVDFLRYYA--VQARNDFSNDA---------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07119 86 NTGKTLRESEIDIDDVANCFRYYAglATKETGEVYDVpphvisrtvREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 798 LAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpIP 877
Cdd:cd07119 166 VIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK----VA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 878 LiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPV 957
Cdd:cd07119 242 L--ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 958 IDAEAKAGIEKHIQAMRDKG-RNVYQMAIADGEECKRGTFVMPTLielesFDELQR-------EIFGPVLHVVRYKRKEi 1029
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGaRLVCGGKRPTGDELAKGYFVEPTI-----FDDVDRtmrivqeEIFGPVLTVERFDTEE- 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1030 dQLIAQINASGYGLTLGVHTRiDETIA-KVVDNVHAGNVYVNRniVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07119 394 -EAIRLANDTPYGLAGAVWTK-DIARAnRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
661-1092 |
2.07e-73 |
|
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: 252.35 E-value: 2.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:cd07094 3 VHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRYYAVQARNDFSN----DAHR------------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEeiplDATQgsdnrlawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 805 TPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRldnqgrpiPLIAETGG 884
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGK--------RIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 965 GIEKHI-QAMRDKGRnvyqmAIADGEecKRGTFVMPTLIELESFDELQR--EIFGPVLHVVRYkrKEIDQLIAQINASGY 1041
Cdd:cd07094 314 RVERWVeEAVEAGAR-----LLCGGE--RDGALFKPTVLEDVPRDTKLSteETFGPVVPIIRY--DDFEEAIRIANSTDY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 68348298 1042 GLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVgAVVGVQPFGGEGLSGTG 1092
Cdd:cd07094 385 GLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
670-1092 |
3.15e-73 |
|
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: 251.76 E-value: 3.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 670 VVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLR 749
Cdd:cd07099 8 VLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 750 YYA-----------VQARNDFSNDA----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVR 814
Cdd:cd07099 88 WAArnaprvlaprkVPTGLLMPNKKatveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 815 LLLEAGIPEGVLQLLPGQGEsVGARLVgDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:cd07099 168 AWAAAGPPQGVLQVVTGDGA-TGAALI-DAGVDKVAFTGSVATGRKVMAAAAERL------IPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMR 974
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 975 DKGRNVyqmAIADGEECKRGTFVMPTLI--ELESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRID 1052
Cdd:cd07099 320 AKGAKA---LTGGARSNGGGPFYEPTVLtdVPHDMDVMREETFGPVLPVMPV--ADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 68348298 1053 ETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
660-1092 |
5.34e-73 |
|
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: 251.37 E-value: 5.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHRdVVGHVQEATVEDVDNAIQCALNA--APIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANA 737
Cdd:cd07112 5 ATINPATGR-VLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 738 IA-EVREAVDFLRYY-----------AVQARNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQT 805
Cdd:cd07112 84 LAvDVPSAANTFRWYaeaidkvygevAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 806 PLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPIPLiaETGGQ 885
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSG---QSNLKRVWL--ECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 886 NAMIV-DSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07112 239 SPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 965 GIEKHIQAMRDKGRNVYQMAIADGEECKrGTFVMPTLielesFDEL-------QREIFGPVLHVVRYKRkeIDQLIAQIN 1037
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVLTETG-GFFVEPTV-----FDGVtpdmriaREEIFGPVLSVITFDS--EEEAVALAN 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 68348298 1038 ASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVnrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
660-1098 |
9.08e-72 |
|
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: 247.63 E-value: 9.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:cd07150 2 DDLNPADG-SVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQARN------------DFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:cd07150 81 ETTFTPELLRAAAGECRRvrgetlpsdspgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 808 VAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVArllqRNIAGRLDNQGRPIPLiaETGGQNA 887
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRHLKKITL--ELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 968 KHIQAMRDKGRNVyqmaIADGEEckRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYKRKEidQLIAQINASGYGLTL 1045
Cdd:cd07150 315 RQVEDAVAKGAKL----LTGGKY--DGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPAKDAE--EALELANDTEYGLSA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 68348298 1046 GVHTRiDETIA-KVVDNVHAGNVYVNRNIV--GAVVgvqPFGGEGLSGTGpKAGGP 1098
Cdd:cd07150 387 AILTN-DLQRAfKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGE 437
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
661-1096 |
9.80e-72 |
|
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: 247.27 E-value: 9.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPiwqATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:cd07146 3 VRNPYTG-EVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRYYAVQARND----FSNDA-----------HR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07146 79 VGRAADVLRFAAAEALRDdgesFSCDLtangkarkiftLRePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 805 TPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRldnqgrpiPLIAETGG 884
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 965 GIEKHI-QAMRDKGRNVYqmaiadGEEcKRGTFVMPTLIELESFD-EL-QREIFGPVLHVVRYkrKEIDQLIAQINASGY 1041
Cdd:cd07146 311 QIENRVeEAIAQGARVLL------GNQ-RQGALYAPTVLDHVPPDaELvTEETFGPVAPVIRV--KDLDEAIAISNSTAY 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 68348298 1042 GLTLGVHTRIDETIAKVVDNVHAGNVYVNrNIVGAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:cd07146 382 GLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
652-1096 |
1.07e-71 |
|
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: 248.18 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETpAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNA---APiWQATPPAERAAILERAADLMEGEIQPLMGLLAR 728
Cdd:cd07142 15 AASGKT-FPTIDPRNG-EVIAHVAEGDAEDVDRAVKAARKAfdeGP-WPRMTGYERSRILLRFADLLEKHADELAALETW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 729 EAGKTFANA-IAEVREAVDFLRYYAVQA-----------RNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:cd07142 92 DNGKPYEQArYAEVPLAARLFRYYAGWAdkihgmtlpadGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 797 VLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPI 876
Cdd:cd07142 172 IVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA---KSNLKPV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 877 PLiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGP 956
Cdd:cd07142 249 TL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 957 VIDAEAKAGIEKHIQAMRDKGRNVyqmaIADGEEC-KRGTFVMPTLIELESFDEL--QREIFGPVLHVVRYkrKEIDQLI 1033
Cdd:cd07142 327 QVDKEQFEKILSYIEHGKEEGATL----ITGGDRIgSKGYYIQPTIFSDVKDDMKiaRDEIFGPVQSILKF--KTVDEVI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1034 AQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVN-RNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
661-1095 |
2.31e-71 |
|
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: 246.50 E-value: 2.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSdHRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTF-ANAIA 739
Cdd:cd07108 1 VINPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQA-----------RNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLv 808
Cdd:cd07108 80 EAAVLADLFRYFGGLAgelkgetlpfgPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAM 888
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 889 IVDSSALTEQVVIDVVSSA-FDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 968 KHIQAMRDK--GRNVYQMAIADGEECKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGL 1043
Cdd:cd07108 313 GYIDLGLSTsgATVLRGGPLPGEGPLADGFFVQPTIFSgvDNEWRLAREEIFGPVLCAIPW--KDEDEVIAMANDSHYGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 68348298 1044 TLGVHTRIDETIAKVVDNVHAGNVYVNRNiVGAVVGvQPFGGEGLSGTGPKA 1095
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
652-1092 |
9.40e-69 |
|
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: 239.33 E-value: 9.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETPAPVLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAG 731
Cdd:cd07138 9 APAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 732 --KTFANAiAEVREAVDFLRYYAVQARN-DFSNDA------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07138 88 apITLARA-AQVGLGIGHLRAAADALKDfEFEERRgnslvvREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 803 EQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAET 882
Cdd:cd07138 167 EVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR------VALEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSAL-RVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAE 961
Cdd:cd07138 241 GGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 962 AKAGIEKHIQAMRDKGRNVyqmaIADGEE----CKRGTFVMPTLielesFDEL-------QREIFGPVLHVVRYkrKEID 1030
Cdd:cd07138 320 QFDRVQGYIQKGIEEGARL----VAGGPGrpegLERGYFVKPTV-----FADVtpdmtiaREEIFGPVLSIIPY--DDED 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68348298 1031 QLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNrnivGAVVGVQ-PFGGEGLSGTG 1092
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
650-1097 |
1.60e-68 |
|
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: 239.03 E-value: 1.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 650 GCAASSETPAPVLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLARE 729
Cdd:cd07130 5 GEWGGGGGVVTSISPANGE-PIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 730 AGKTFANAIAEVREAVDFLRYYAVQAR------------NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07130 84 MGKILPEGLGEVQEMIDICDFAVGLSRqlygltipserpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 798 LAKPAEQTPL--VAAQAV--RLLLEAGIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqG 873
Cdd:cd07130 164 VWKPSPTTPLtaIAVTKIvaRVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 874 RpipLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVD 953
Cdd:cd07130 240 R---SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 954 IGPVIDAEAKAGIEKHIQAMRDKGRNVyqmaIADGEECKR-GTFVMPTLIELESFDEL-QREIFGPVLHVVRYkrKEIDQ 1031
Cdd:cd07130 317 VGPLHTKAAVDNYLAAIEEAKSQGGTV----LFGGKVIDGpGNYVEPTIVEGLSDAPIvKEETFAPILYVLKF--DTLEE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68348298 1032 LIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNI--VGAVVGvQPFGGEGLSGTGPKAGG 1097
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIgtSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
669-1098 |
2.01e-68 |
|
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: 237.58 E-value: 2.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 669 DVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFL 748
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 749 RYYA---VQARND-FSNDA-------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV-RLL 816
Cdd:cd07152 82 HEAAglpTQPQGEiLPSAPgrlslarRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 817 LEAGIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNAMIVDSSALT 896
Cdd:cd07152 162 EEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHL----KKVSL--ELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 897 EQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRD 975
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 976 KGRNVYQMAIADgeeckrGTFVMPTLI-----ELESFDElqrEIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTR 1050
Cdd:cd07152 314 AGARLEAGGTYD------GLFYRPTVLsgvkpGMPAFDE---EIFGPVAPVTVF--DSDEEAVALANDTEYGLSAGIISR 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 68348298 1051 IDETIAKVVDNVHAGNVYVNRNIVGAVVgVQPFGGEGLSGTGPKAGGP 1098
Cdd:cd07152 383 DVGRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
667-1096 |
4.52e-68 |
|
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: 236.85 E-value: 4.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 667 HRDVVGHVQEATVEDVDNAIQ---CALNAAPiWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVRE 743
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAaarKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 744 AVDFLRYYAVQARNdFSNDAHRPLGP-------------VVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAA 810
Cdd:cd07118 85 AADLWRYAASLART-LHGDSYNNLGDdmlglvlrepigvVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 811 QAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGrpipliAETGGQNAMIV 890
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 891 DSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHI 970
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 971 QAMRDKGRNVYQMAIADGEEckRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVH 1048
Cdd:cd07118 318 DAGRAEGATLLLGGERLASA--AGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVW 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 68348298 1049 TRIDETIAKVVDNVHAGNVYVNRNIVGAVvgVQPFGGEGLSGTGPKAG 1096
Cdd:cd07118 394 SKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
660-1092 |
5.18e-68 |
|
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: 236.76 E-value: 5.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:cd07147 2 EVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQARN----------DFSNDAHR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07147 81 EVARAIDTFRIAAEEATRiygevlpldiSARGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 804 QTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESvGARLVGDERVKGVMFTGSTEVARLLqRNIAGRldnqgRPIPLiaETG 883
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-----KKVVL--ELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 963 KAGIEKHIQAMRDKGRNVyqmaIADGEecKRGTFVMPTLIE-LESFDELQR-EIFGPVLHVVRYKRkeIDQLIAQINASG 1040
Cdd:cd07147 311 AERVEGWVNEAVDAGAKL----LTGGK--RDGALLEPTILEdVPPDMEVNCeEVFGPVVTVEPYDD--FDEALAAVNDSK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 68348298 1041 YGLTLGVHTRIDETIAKVVDNVHAGNVYVNrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07147 383 FGLQAGVFTRDLEKALRAWDELEVGGVVIN-DVPTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
669-1096 |
1.50e-67 |
|
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: 235.67 E-value: 1.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 669 DVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFL 748
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 749 RYYAVQARNDF--------------SNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVR 814
Cdd:cd07101 87 RYYARRAERLLkprrrrgaipvltrTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 815 LLLEAGIPEGVLQLLPGQGESVGARLVgdERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:cd07101 167 LLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMR 974
Cdd:cd07101 239 DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 975 DKGRNVyqmaIADGEecKRGT----FVMPTLI-----ELESFDElqrEIFGPVLHVVRYKRkeIDQLIAQINASGYGLTL 1045
Cdd:cd07101 319 AKGATV----LAGGR--ARPDlgpyFYEPTVLtgvteDMELFAE---ETFGPVVSIYRVAD--DDEAIELANDTDYGLNA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 68348298 1046 GVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQ-PFGGEGLSGTGPKAG 1096
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
651-1096 |
4.87e-66 |
|
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: 232.30 E-value: 4.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 651 CAASSETPAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNA-APIWQATPPAERAAILERAADLMEGEIQPLMGLLARE 729
Cdd:cd07144 17 VKSSDGETIKTVNPSTG-EVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 730 AGKTF-ANAIAEVREAVDFLRYYAVQA-----------RNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07144 96 SGKPYhSNALGDLDEIIAVIRYYAGWAdkiqgktiptsPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 798 LAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpIP 877
Cdd:cd07144 176 VIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA----VT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 878 LiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAEN-RLGNPERLSVDIGP 956
Cdd:cd07144 252 L--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 957 VIDAEAKAGIEKHIQAMRDKGRNVYQMAIADGEECKRGTFVMPTLIE--LESFDELQREIFGPVlhVVRYKRKEIDQLIA 1034
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIFTdvPQDMRIVKEEIFGPV--VVISKFKTYEEAIK 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68348298 1035 QINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAvVGVqPFGGEGLSGTGPKAG 1096
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
652-1110 |
5.39e-66 |
|
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: 231.70 E-value: 5.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETPAPVLNPSDHRdVVGHVQEATVEDVDNAIQCALNA--APIWQATPPAERAAILERAADLMEGEIQPLMGLLARE 729
Cdd:cd07139 9 APSGSETIDVVSPATEE-VVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 730 AGKTFA-NAIAEVREAVDFLRYYAVQARnDFSNDAHR-------------PLGPVVCISPWNFPLAIFSGQVAAALAAGN 795
Cdd:cd07139 88 NGMPISwSRRAQGPGPAALLRYYAALAR-DFPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 796 PVLAKPAEQTPLVA---AQAVRlllEAGIPEGVLQLLPGqGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnq 872
Cdd:cd07139 167 TVVLKPSPETPLDAyllAEAAE---EAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 873 gRPIPLiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSAL-RVLCLQEdSADRVIEMLKGAMAENRLGNPERLS 951
Cdd:cd07139 240 -ARVTL--ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVPRS-RYDEVVEALAAAVAALKVGDPLDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 952 VDIGPVIDAEAKAGIEKHIQAMRDKGRNVyqmaIADGEECK---RGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYkr 1026
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARL----VTGGGRPAgldRGWFVEPTLFaDVDNDMRIaQEEIFGPVLSVIPY-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1027 KEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNrnivGAVVGVQ-PFGGEGLSGTGpKAGGPLYLYRLL 1105
Cdd:cd07139 390 DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGPEGLDAYL 464
|
....*
gi 68348298 1106 STRPV 1110
Cdd:cd07139 465 ETKSI 469
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
660-1096 |
8.69e-66 |
|
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: 231.47 E-value: 8.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHrDVVGHVQEATVEDVDNAIQCALNA----APiWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFA 735
Cdd:cd07141 25 PTINPATG-EKICEVQEGDKADVDKAVKAARAAfklgSP-WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 736 NA-IAEVREAVDFLRYYAVQAR-----------NDFSNDAHRPLGpvVC--ISPWNFPLAIFSGQVAAALAAGNPVLAKP 801
Cdd:cd07141 103 KSyLVDLPGAIKVLRYYAGWADkihgktipmdgDFFTYTRHEPVG--VCgqIIPWNFPLLMAAWKLAPALACGNTVVLKP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 802 AEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNiAGRlDNQGRpipLIAE 881
Cdd:cd07141 181 AEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA-AGK-SNLKR---VTLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAE 961
Cdd:cd07141 256 LGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 962 AKAGIEKHIQAMRDKGRnvyQMAIADGEECKRGTFVMPTLielesFDELQ-------REIFGPVLHVVRYkrKEIDQLIA 1034
Cdd:cd07141 336 QFKKILELIESGKKEGA---KLECGGKRHGDKGYFIQPTV-----FSDVTddmriakEEIFGPVQQIFKF--KTIDEVIE 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1035 QINASGYGLTLGVHTR-IDETIaKVVDNVHAGNVYVNrniVGAVVGVQ-PFGGEGLSGTGPKAG 1096
Cdd:cd07141 406 RANNTTYGLAAAVFTKdIDKAI-TFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
660-1092 |
7.92e-65 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 229.19 E-value: 7.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:PLN02278 43 PVYNPATG-EVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQARNDF-----SNDA-------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKRVYgdiipSPFPdrrllvlKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 808 VAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGGQNA 887
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKR------VSLELGGNAP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 888 MIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGI 966
Cdd:PLN02278 276 FIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 967 EKHIQAMRDKGRNVyqmaIADGEECKRG-TFVMPTLIELESFDEL--QREIFGPVLHVVRYKRKEidQLIAQINASGYGL 1043
Cdd:PLN02278 355 ESHVQDAVSKGAKV----LLGGKRHSLGgTFYEPTVLGDVTEDMLifREEVFGPVAPLTRFKTEE--EAIAIANDTEAGL 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 68348298 1044 TLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGvqPFGGEGLSGTG 1092
Cdd:PLN02278 429 AAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
661-1092 |
1.21e-64 |
|
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: 226.82 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA- 739
Cdd:cd07092 1 VVDPATGE-EIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQARN-----------DFSNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTlegpaageylpGHTSMIRRePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 808 VAAQAVRLLLEaGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGGQNA 887
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR------VHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 888 MIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGI 966
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 967 EKHIQAMRDKGRNVYQMAIADGeeckRGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYkrKEIDQLIAQINASGYGLT 1044
Cdd:cd07092 312 AGFVERAPAHARVLTGGRRAEG----PGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPF--DDEDEAIELANDVEYGLA 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 68348298 1045 LGVHTRIDETIAKVVDNVHAGNVYVNRNIVgaVVGVQPFGGEGLSGTG 1092
Cdd:cd07092 386 SSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
682-1092 |
1.33e-64 |
|
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: 226.19 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 682 VDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQA------ 755
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAeaflad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 756 --RNDFSNDA---HRPLGPVVCISPWNFPLAifsgQV----AAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVL 826
Cdd:cd07100 81 epIETDAGKAyvrYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 827 QLLPGQGESVgARLVGDERVKGVMFTGST----EVARLLQRNIAgrldnqgrpiPLIAETGGQNAMIVDSSALTEQVVID 902
Cdd:cd07100 157 QNLLIDSDQV-EAIIADPRVRGVTLTGSEragrAVAAEAGKNLK----------KSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 903 VVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKG-RNV 980
Cdd:cd07100 226 AVKGRLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 981 YQMAIADGEeckrGTFVMPTLI-----ELESFDElqrEIFGPVLHVvrYKRKEIDQLIAQINASGYGLTLGVHTRIDETI 1055
Cdd:cd07100 305 LGGKRPDGP----GAFYPPTVLtdvtpGMPAYDE---ELFGPVAAV--IKVKDEEEAIALANDSPFGLGGSVFTTDLERA 375
|
410 420 430
....*....|....*....|....*....|....*..
gi 68348298 1056 AKVVDNVHAGNVYVNRnIVGAVVGVqPFGGEGLSGTG 1092
Cdd:cd07100 376 ERVARRLEAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
661-1096 |
1.35e-64 |
|
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: 227.80 E-value: 1.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRdVVGHVQEATVEDVDNAIQCALNA--APIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAI 738
Cdd:cd07143 26 VYNPSTGK-LITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 739 A-EVREAVDFLRYYAVQARNDFSN-----------DAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:cd07143 105 RvDVQASADTFRYYGGWADKIHGQvietdikkltyTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 807 LVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIA-GRLDNqgrpipLIAETGGQ 885
Cdd:cd07143 185 LSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAkSNLKK------VTLELGGK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 886 NAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAG 965
Cdd:cd07143 259 SPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 966 IEKHIQAMRDKGRNVyqmaIADGEEC-KRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYG 1042
Cdd:cd07143 339 IMSYIESGKAEGATV----ETGGKRHgNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKF--KTEEEAIKRANDSTYG 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 68348298 1043 LTLGVHTRIDETIAKVVDNVHAGNVYVN-RNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07143 413 LAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
661-1092 |
5.23e-64 |
|
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: 225.31 E-value: 5.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:cd07110 1 VINPATEA-TIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRYYAVQAR--------------NDFSNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQT 805
Cdd:cd07110 80 VDDVAGCFEYYADLAEqldakaeravplpsEDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 806 PLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAgrldNQGRPIPLiaETGGQ 885
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA----QDIKPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 886 NAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAG 965
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 966 IEKHIQAMRDKGRNVyqmaIADG---EECKRGTFVMPTLI-ELESFDELQR-EIFGPVLHVVRYKRKeiDQLIAQINASG 1040
Cdd:cd07110 314 VLSFIARGKEEGARL----LCGGrrpAHLEKGYFIAPTVFaDVPTDSRIWReEIFGPVLCVRSFATE--DEAIALANDSE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 68348298 1041 YGLTLGVHTRIDETIAKVVDNVHAGNVYVnrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07110 388 YGLAAAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
661-1092 |
8.14e-64 |
|
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: 224.95 E-value: 8.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:cd07107 1 VINPATGQ-VLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRYYAVQA-----------RNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:cd07107 80 VMVAAALLDYFAGLVtelkgetipvgGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 810 AQAVRLLLEAgIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrpiPLIAETGGQNAMI 889
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 890 VDSSALTEQVVIDVVSSA-FDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07107 233 VFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 969 HIQAMRDKG-RNVYQMAIADGEECKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTL 1045
Cdd:cd07107 313 YIDSAKREGaRLVTGGGRPEGPALEGGFYVEPTVFAdvTPGMRIAREEIFGPVLSVLRW--RDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 68348298 1046 GVHTRIDETIAKVVDNVHAGNVYVN---RNIVGAvvgvqPFGGEGLSGTG 1092
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
662-1071 |
2.84e-63 |
|
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: 222.89 E-value: 2.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 662 LNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEV 741
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 742 REAVDFLRYYAvqarnDFSNDA-----------------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07102 80 RGMLERARYMI-----SIAEEAladirvpekdgferyirREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 805 TPLVAAQAVRLLLEAGIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGG 884
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRF------IKVGLELGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07102 228 KDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 965 GIEKHIQAMRDKGRnvyQMAIADGEE---CKRGTFVMPT-LIELE-SFDELQREIFGPVLHVvrYKRKEIDQLIAQINAS 1039
Cdd:cd07102 308 FVRAQIADAIAKGA---RALIDGALFpedKAGGAYLAPTvLTNVDhSMRVMREETFGPVVGI--MKVKSDAEAIALMNDS 382
|
410 420 430
....*....|....*....|....*....|..
gi 68348298 1040 GYGLTLGVHTRIDETIAKVVDNVHAGNVYVNR 1071
Cdd:cd07102 383 EYGLTASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
669-1092 |
6.49e-63 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 224.37 E-value: 6.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 669 DVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFL 748
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 749 RYYAVQARNDF--------------SNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVR 814
Cdd:PRK09407 123 RYYARRAPKLLaprrragalpvltkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 815 LLLEAGIPEGVLQLLPGQGESVGARLVgdERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:PRK09407 203 LLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRL------IGFSLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMR 974
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 975 DKGRNVyqmaIADGEecKR---GT-FVMPTLI-----ELESFDElqrEIFGPVLHVVRYKRkeIDQLIAQINASGYGLTL 1045
Cdd:PRK09407 355 AKGATV----LAGGK--ARpdlGPlFYEPTVLtgvtpDMELARE---ETFGPVVSVYPVAD--VDEAVERANDTPYGLNA 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 68348298 1046 GVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQ-PFGGEGLSGTG 1092
Cdd:PRK09407 424 SVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
653-1092 |
6.67e-63 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 222.86 E-value: 6.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 653 ASSETPAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGK 732
Cdd:PRK13473 13 AGEGEKQPVYNPATG-EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 733 TFANAIA-EVREAVDFLRYYAVQARN-----------DFSNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:PRK13473 92 PLHLALNdEIPAIVDVFRFFAGAARClegkaageyleGHTSMIRRdPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 800 KPAEQTPLVAAQAVRLLLEAgIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLI 879
Cdd:PRK13473 172 KPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKR------TH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVID 959
Cdd:PRK13473 245 LELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 960 AEAKAGIEKHIQAMRDKG--RNVYQMAIADGeeckRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQ 1035
Cdd:PRK13473 325 AAHRDRVAGFVERAKALGhiRVVTGGEAPDG----KGYYYEPTLLAgaRQDDEIVQREVFGPVVSVTPF--DDEDQAVRW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 68348298 1036 INASGYGLTLGVHTRiDETIA-KVVDNVHAGNVYVNRNIVgaVVGVQPFGGEGLSGTG 1092
Cdd:PRK13473 399 ANDSDYGLASSVWTR-DVGRAhRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
662-1092 |
1.27e-62 |
|
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: 221.45 E-value: 1.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 662 LNPSDHrDVVGHVQEATVEDVDNAIQCALNA--APIWqATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:cd07120 2 IDPATG-EVIGTYADGGVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQARND-----------FSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:cd07120 80 EISGAISELRYYAGLARTEagrmiepepgsFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEA-GIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGrpipliAETGGQNA 887
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 968 KHIQAMRDKGRNVYQMAIADGEECKRGTFVMPTLIELE--SFDELQREIFGPVLHVVRYKRKeiDQLIAQINASGYGLTL 1045
Cdd:cd07120 314 RMVERAIAAGAEVVLRGGPVTEGLAKGAFLRPTLLEVDdpDADIVQEEIFGPVLTLETFDDE--AEAVALANDTDYGLAA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 68348298 1046 GVHTRIDETIAKVVDNVHAGNVYVN---RNIVGAvvgvqPFGGEGLSGTG 1092
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINdwnKLFAEA-----EEGGYRQSGLG 436
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
653-1092 |
2.65e-62 |
|
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: 220.64 E-value: 2.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 653 ASSETPAPVLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGK 732
Cdd:cd07151 6 GTSERTIDVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 733 TFANAIAEVREAVDFLRYYA-----VQAR---NDFSNDAHR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAK 800
Cdd:cd07151 85 TRIKANIEWGAAMAITREAAtfplrMEGRilpSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 801 PAEQTPLVAAQAV-RLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVArllqRNIaGRLdnQGRPIPLI 879
Cdd:cd07151 165 PASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG----RHI-GEL--AGRHLKKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 A-ETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVI 958
Cdd:cd07151 238 AlELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 959 DAEAKAGIEKHIQAMRDKGRNVYQMAIADgeeckrGTFVMPT-LIELESFDELQR-EIFGPVLHVVRYKRKEidQLIAQI 1036
Cdd:cd07151 318 NESQVDGLLDKIEQAVEEGATLLVGGEAE------GNVLEPTvLSDVTNDMEIAReEIFGPVAPIIKADDEE--EALELA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 68348298 1037 NASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVqPFGGEGLSGTG 1092
Cdd:cd07151 390 NDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
662-1090 |
3.28e-62 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 220.99 E-value: 3.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 662 LNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEV 741
Cdd:PRK09457 20 RNPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 742 REAVD----FLRYYAV---QARNDFSNDA----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAA 810
Cdd:PRK09457 99 TAMINkiaiSIQAYHErtgEKRSEMADGAavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 811 QAVRLLLEAGIPEGVLQLLPGQGESvGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrpIPLIAETGGQNAMIV 890
Cdd:PRK09457 179 LTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPE-----KILALEMGGNNPLVI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 891 DSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDS-ADRVIEMLKGAMAENRLGNPerlsvD------IGPVIDAEAK 963
Cdd:PRK09457 253 DEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRW-----DaepqpfMGAVISEQAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 964 AGIEK---HIQAMrdKGRNVYQMAIADGEeckrGTFVMPTLIELESFDEL-QREIFGPVLHVVRYkrKEIDQLIAQINAS 1039
Cdd:PRK09457 328 QGLVAaqaQLLAL--GGKSLLEMTQLQAG----TGLLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDFDEAIRLANNT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 68348298 1040 GYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAvVGVQPFGGEGLSG 1090
Cdd:PRK09457 400 RFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
146-257 |
1.04e-61 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 205.82 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 146 VQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAG 225
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 68348298 226 LTSSLSRIIGKSGEPMIRKGVDMAMRLMGEQF 257
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
660-1105 |
4.79e-61 |
|
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: 217.65 E-value: 4.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKtfanAIA 739
Cdd:cd07111 40 PTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK----PIR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVRE-----AVDFLRYYAVQAR-NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV 813
Cdd:cd07111 115 ESRDcdiplVARHFYHHAGWAQlLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 814 RLLLEAGIPEGVLQLLPGQGeSVGARLVGDERVKGVMFTGSTEVARLLQRNIAGrldnQGRPIPLiaETGGQNAMIVDSS 893
Cdd:cd07111 195 EICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAG----TGKKLSL--ELGGKSPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 894 ALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAM 973
Cdd:cd07111 268 ADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 974 RDKGRNVYQmaiADGEECKRGTFVMPTLIE-LESFDEL-QREIFGPVLHVVRYKRKEidQLIAQINASGYGLTLGVHTRI 1051
Cdd:cd07111 348 RAEGADVFQ---PGADLPSKGPFYPPTLFTnVPPASRIaQEEIFGPVLVVLTFRTAK--EAVALANNTPYGLAASVWSEN 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 68348298 1052 DETIAKVVDNVHAGNVYVN-RNIVGAVVgvqPFGGEGLSGTGpKAGGPLYLYRLL 1105
Cdd:cd07111 423 LSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEYL 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
652-1092 |
6.19e-61 |
|
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: 216.92 E-value: 6.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETPAPVLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQA-TPPAERAAILERAADLMEGEIQPLMGLLAREA 730
Cdd:cd07113 10 AGQSEKRLDITNPAT-EQVIASVASATEADVDAAVASAWRAFVSAWAkTTPAERGRILLRLADLIEQHGEELAQLETLCS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 731 GKTFANAIA-EVREAVDFLRYYA-----------------VQARNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALA 792
Cdd:cd07113 89 GKSIHLSRAfEVGQSANFLRYFAgwatkingetlapsipsMQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 793 AGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNq 872
Cdd:cd07113 169 TGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTR- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 873 grpipLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSV 952
Cdd:cd07113 247 -----VTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 953 DIGPVIDAEAKAGIEKHIQAMRDKGRNVyqmaIADGEECKR-GTFVMPTLIELESFDE--LQREIFGPVLHVVRYKRKEi 1029
Cdd:cd07113 322 MFGPLANQPHFDKVCSYLDDARAEGDEI----VRGGEALAGeGYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDEE- 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1030 dQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVN-RNIVGAVVgvqPFGGEGLSGTG 1092
Cdd:cd07113 397 -ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
660-1092 |
4.26e-60 |
|
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: 214.52 E-value: 4.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGK----TFA 735
Cdd:cd07559 19 DNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKpireTLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 736 naiAEVREAVDFLRYYAVQAR------NDFSNDA-----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07559 98 ---ADIPLAIDHFRYFAGVIRaqegslSEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 805 TPLVAAQAVRLLLEAgIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGG 884
Cdd:cd07559 175 TPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------IPVTLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 885 QNAMIVDSSALTEQVVID------VVSSAFDSaGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVI 958
Cdd:cd07559 248 KSPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 959 DAEAKAGIEKHIQAMRDKGRNVyqmaIADGEE-----CKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYkrKEIDQ 1031
Cdd:cd07559 327 SKDQLEKILSYVDIGKEEGAEV----LTGGERltlggLDKGYFYEPTLIKGGNNDMriFQEEIFGPVLAVITF--KDEEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68348298 1032 LIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVN-RNIVGAVVgvqPFGGEGLSGTG 1092
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
661-1092 |
4.69e-60 |
|
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: 213.70 E-value: 4.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRYYA----------VQARND-FSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:cd07090 80 IDSSADCLEYYAglaptlsgehVPLPGGsFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 810 AQAVRLLLEAGIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNAMI 889
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 890 VDSSALTEQVVIDVVSSAFDSAGQRCS-ALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 969 HIQAMRDKGRNVYQ--MAIADGEECKRGTFVMPTLIElESFDEL---QREIFGPVLHVVRYkrKEIDQLIAQINASGYGL 1043
Cdd:cd07090 312 YIESAKQEGAKVLCggERVVPEDGLENGFYVSPCVLT-DCTDDMtivREEIFGPVMSILPF--DTEEEVIRRANDTTYGL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 68348298 1044 TLGVHTRIDETIAKVVDNVHAGNVYVNR-NIVGAVVgvqPFGGEGLSGTG 1092
Cdd:cd07090 389 AAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
652-1096 |
5.73e-60 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 216.21 E-value: 5.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETpAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNA---APiWQATPPAERAAILERAADLMEGEIQPLMGLLAR 728
Cdd:PLN02466 69 AASGKT-FPTLDPRTG-EVIAHVAEGDAEDVNRAVAAARKAfdeGP-WPKMTAYERSRILLRFADLLEKHNDELAALETW 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 729 EAGKTFANAI-AEVREAVDFLRYYA----------VQAR-NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:PLN02466 146 DNGKPYEQSAkAELPMFARLFRYYAgwadkihgltVPADgPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 797 VLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQrNIAGRldNQGRPI 876
Cdd:PLN02466 226 IVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVL-ELAAK--SNLKPV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 877 PLiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGP 956
Cdd:PLN02466 303 TL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGP 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 957 VIDAEAKAGIEKHIQAMRDKGRNVyqmaIADGEEC-KRGTFVMPTLIELESFDEL--QREIFGPVLHVVRYkrKEIDQLI 1033
Cdd:PLN02466 381 QIDSEQFEKILRYIKSGVESGATL----ECGGDRFgSKGYYIQPTVFSNVQDDMLiaQDEIFGPVQSILKF--KDLDEVI 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1034 AQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVN-RNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
669-1096 |
4.57e-58 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 209.29 E-value: 4.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 669 DVVGHVQEATVEDVDNAIQCALNA---APiWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFA-NAIAEVREA 744
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAAREAfdhGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 745 VDFLRYYAVQA-----------RNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAV 813
Cdd:PLN02766 126 AGLLRYYAGAAdkihgetlkmsRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 814 RLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPIPLiaETGGQNAMIVDSS 893
Cdd:PLN02766 206 HLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAA---TSNLKQVSL--ELGGKSPLLIFDD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 894 ALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIqam 973
Cdd:PLN02766 281 ADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYI--- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 974 rDKGRNVYQMAIADGEEC-KRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTR 1050
Cdd:PLN02766 358 -EHGKREGATLLTGGKPCgDKGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAGIVTK 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 68348298 1051 IDETIAKVVDNVHAGNVYVNRNIvgAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:PLN02766 435 DLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
662-1090 |
9.55e-58 |
|
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: 208.03 E-value: 9.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 662 LNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEV 741
Cdd:TIGR03240 18 RNPATQ-EVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVIARETGKPLWETRTEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 742 REAVD----FLRYYAVQ---ARNDFSNDA----HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAA 810
Cdd:TIGR03240 97 ASMIGkvaiSIKAYHERtgeSENPMPDGRavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPSELTPWVAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 811 QAVRLLLEAGIPEGVLQLLPGqGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrpIPLIAETGGQNAMIV 890
Cdd:TIGR03240 177 ETVKLWEKAGLPAGVLNLVQG-ARETGVALAAHPQIDGLLFTGSSNTGTLLHRQFGGRPE-----KILALEMGGNNPLIV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 891 DSSALTEQVVIDVVSSAFDSAGQRCS-ALRVLCLQEDSADRVIEMLKGAMAENRLGN----PERLsvdIGPVIDAEA-KA 964
Cdd:TIGR03240 251 DEVADIDAAVHHIIQSAFISAGQRCTcARRLLVPDGAQGDAFLARLVEVAERLTVGAwdaePQPF---MGAVISLRAaQR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 965 GIEKHIQAMRDKGRNVYQMAIADGEEckrgTFVMPTLIELESFDEL-QREIFGPVLHVVRYkrKEIDQLIAQINASGYGL 1043
Cdd:TIGR03240 328 LLAAQAKLLALGGKSLLEMRQLDPGA----AFLTPGIIDVTGVAELpDEEHFGPLLQVIRY--TDFDEAIAIANNTRFGL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 68348298 1044 TLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAvVGVQPFGGEGLSG 1090
Cdd:TIGR03240 402 SAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
660-1101 |
1.98e-55 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 201.29 E-value: 1.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIA 739
Cdd:PRK11241 29 DVTNPANG-DKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 740 EVREAVDFLRYYAVQARNDFSN--DAHR----------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:PRK11241 108 EISYAASFIEWFAEEGKRIYGDtiPGHQadkrlivikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 808 VAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNA 887
Cdd:PRK11241 188 SALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI----KKVSL--ELGGNAP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:PRK11241 262 FIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 968 KHIQAMRDKGRNVyqmaIADGEECKR-GTFVMPT-LIELESFDELQR-EIFGPVLHVVRYKRKeiDQLIAQINASGYGLT 1044
Cdd:PRK11241 342 EHIADALEKGARV----VCGGKAHELgGNFFQPTiLVDVPANAKVAKeETFGPLAPLFRFKDE--ADVIAQANDTEFGLA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1045 LGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGvqPFGG---EGLSGTGPKAGGPLYL 1101
Cdd:PRK11241 416 AYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
681-1092 |
2.86e-55 |
|
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: 198.96 E-value: 2.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 681 DVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFS 760
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 761 N----DAH--------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQL 828
Cdd:cd07105 81 GsipsDKPgtlamvvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 829 L---PGQGESVGARLVGDERVKGVMFTGSTEVARLLQRnIAGR-LdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVV 904
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAE-TAAKhL------KPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 905 SSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAENRLGnperlSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQM 983
Cdd:cd07105 234 FGAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 984 AIADGEEckRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRiDETIA-KVVD 1060
Cdd:cd07105 308 GLADESP--SGTSMPPTILDnvTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR-DLARAlAVAK 382
|
410 420 430
....*....|....*....|....*....|....*
gi 68348298 1061 NVHAGNVYVNrnivGAVVGVQ---PFGGEGLSGTG 1092
Cdd:cd07105 383 RIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
653-1092 |
7.41e-54 |
|
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: 196.14 E-value: 7.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 653 ASSETPAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGK 732
Cdd:cd07117 12 GSSGETIDSYNPANG-ETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 733 TFANAIA-EVREAVDFLRYYA--VQARNDFSND---------AHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAK 800
Cdd:cd07117 91 PIRETRAvDIPLAADHFRYFAgvIRAEEGSANMidedtlsivLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 801 PAEQTPLVAAQAVRLLLEAgIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIA 880
Cdd:cd07117 171 PSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------IPATL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 881 ETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDA 960
Cdd:cd07117 244 ELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 961 EAKAGIEKHIQAMRDKGRNVyqmaIADGEE-----CKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYkrKEIDQLI 1033
Cdd:cd07117 324 DQLDKILSYVDIAKEEGAKI----LTGGHRltengLDKGFFIEPTLIVNVTNDMrvAQEEIFGPVATVIKF--KTEDEVI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 68348298 1034 AQINASGYGLTLGVHTRiDETIA-KVVDNVHAGNVYVNR-NIVGAVVgvqPFGGEGLSGTG 1092
Cdd:cd07117 398 DMANDSEYGLGGGVFTK-DINRAlRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
662-1096 |
1.08e-53 |
|
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: 196.18 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 662 LNPSDHRdVVGHVQEATVEDVDNAIQCALNA--APIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAI- 738
Cdd:cd07140 26 INPTDGS-VICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 739 AEVREAVDFLRYYA-----VQARNDFSNDAH----------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07140 105 THVGMSIQTFRYFAgwcdkIQGKTIPINQARpnrnltltkrEPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 804 QTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPIPLiaETG 883
Cdd:cd07140 185 VTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA---VSNLKKVSL--ELG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSAD----RVIEMLKgamaENRLGNPERLSVDIGPvid 959
Cdd:cd07140 260 GKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDefvrRVVEEVK----KMKIGDPLDRSTDHGP--- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 960 AEAKAGIEKHI----QAMRDKGRNVYqmaiaDGEECKR-GTFVMPTL---IELESFDElQREIFGPVLHVVRYKRKEIDQ 1031
Cdd:cd07140 333 QNHKAHLDKLVeyceRGVKEGATLVY-----GGKQVDRpGFFFEPTVftdVEDHMFIA-KEESFGPIMIISKFDDGDVDG 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68348298 1032 LIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVN---RNIVGAvvgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynKTDVAA-----PFGGFKQSGFGKDLG 469
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
652-1092 |
1.11e-51 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 190.09 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 652 AASSETPAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAG 731
Cdd:PRK13252 17 EATSGETFEVINPATG-EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 732 KTFANAI-AEVREAVDFLRYYA----------VQAR-NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:PRK13252 96 KPIQETSvVDIVTGADVLEYYAglapalegeqIPLRgGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 800 KPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrpiPLI 879
Cdd:PRK13252 176 KPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK------EVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCS-ALRVLcLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVI 958
Cdd:PRK13252 249 MELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 959 DAEAKAGIEKHIQAMRDKG-RNVYQMAIADGEECKRGTFVMPTLielesF----DEL---QREIFGPVLHVVRYKRKeiD 1030
Cdd:PRK13252 328 SFAHRDKVLGYIEKGKAEGaRLLCGGERLTEGGFANGAFVAPTV-----FtdctDDMtivREEIFGPVMSVLTFDDE--D 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68348298 1031 QLIAQINASGYGLTLGVHTRiDETIA-KVVDNVHAGNVYVNRniVGAVVGVQPFGGEGLSGTG 1092
Cdd:PRK13252 401 EVIARANDTEYGLAAGVFTA-DLSRAhRVIHQLEAGICWINT--WGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
661-1092 |
5.17e-51 |
|
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: 187.24 E-value: 5.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDhRDVVGHVQEATVEDVDNAIQCA----LNAApiwQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFAN 736
Cdd:cd07148 3 VVNPFD-LKPIGEVPTVDWAAIDKALDTAhalfLDRN---NWLPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 737 AIAEVREAVDFLRYyAVQARNDFSN----------DAHR-------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:cd07148 79 AKVEVTRAIDGVEL-AADELGQLGGreipmgltpaSAGRiafttrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 800 KPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAgrldnQGRPIPLi 879
Cdd:cd07148 158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-----PGTRCAL- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 aETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVID 959
Cdd:cd07148 231 -EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 960 AEAKAGIEKHIQAMRDKGRNVyqmaIADGEECKRGTFvMPTLIELESFDEL--QREIFGPVlhVVRYKRKEIDQLIAQIN 1037
Cdd:cd07148 310 PREVDRVEEWVNEAVAAGARL----LCGGKRLSDTTY-APTVLLDPPRDAKvsTQEIFGPV--VCVYSYDDLDEAIAQAN 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 68348298 1038 ASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNiVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07148 383 SLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
655-1085 |
5.62e-51 |
|
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: 187.78 E-value: 5.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 655 SETPAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTF 734
Cdd:TIGR01722 14 SGTYIPVTNPATN-EVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 735 ANAIAEVR---EAVDFLRYYAVQARNDFSNDAHR---------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:TIGR01722 93 SDALGDVArglEVVEHACGVNSLLKGETSTQVATrvdvysirqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 803 EQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGaRLVGDERVKGVMFTGSTEVARLlqrnIAGRLDNQGRPIPliAET 882
Cdd:TIGR01722 173 EKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRY----IHTTGSAHGKRVQ--ALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQeDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEA 962
Cdd:TIGR01722 246 GAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 963 KAGIEKHIQAMRDKGRNVyqmaIADGEECK-----RGTFVMPTLIELESFDE--LQREIFGPVLHVVRYkrKEIDQLIAQ 1035
Cdd:TIGR01722 325 KDRVASLIAGGAAEGAEV----LLDGRGYKvdgyeEGNWVGPTLLERVPPTMkaYQEEIFGPVLCVLEA--DTLEEAIAL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 68348298 1036 INASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIvGAVVGVQPFGG 1085
Cdd:TIGR01722 399 INASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPI-PVPLPYFSFTG 447
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
662-1096 |
9.54e-49 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 182.34 E-value: 9.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 662 LNPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEV 741
Cdd:PLN02315 39 VNPANNQ-PIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 742 REAVDFLRYYAVQAR------------NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVA 809
Cdd:PLN02315 118 QEIIDMCDFAVGLSRqlngsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 810 AQAVRLLLEA----GIPEGVLQLLPGqGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGGQ 885
Cdd:PLN02315 198 IAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGK------CLLELSGN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 886 NAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAG 965
Cdd:PLN02315 271 NAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 966 IEKHIQAMRDKGRNV-YQMAIADGEeckrGTFVMPTLIELE-SFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGL 1043
Cdd:PLN02315 351 FEKGIEIIKSQGGKIlTGGSAIESE----GNFVQPTIVEISpDADVVKEELFGPVLYVMKF--KTLEEAIEINNSVPQGL 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 68348298 1044 TLGVHTRIDETIAKVVDNVHAGNVYVNRNIV--GAVVGvQPFGGEGLSGTGPKAG 1096
Cdd:PLN02315 425 SSSIFTRNPETIFKWIGPLGSDCGIVNVNIPtnGAEIG-GAFGGEKATGGGREAG 478
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
653-1070 |
7.00e-48 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 179.18 E-value: 7.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 653 ASSETPAPVLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGK 732
Cdd:PLN00412 27 SSSGKSVAITNPST-RKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 733 TFANAIAEVREAVDFLRYYAVQ-------------------ARNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAA 793
Cdd:PLN00412 106 PAKDAVTEVVRSGDLISYTAEEgvrilgegkflvsdsfpgnERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 794 GNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFT-GSTEVArllqrniagrLDNQ 872
Cdd:PLN00412 186 GNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA----------ISKK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 873 GRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERlSV 952
Cdd:PLN00412 256 AGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DC 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 953 DIGPVIDAEAKAGIEKHIQAMRDKGRNVYQmaiadgeECKR-GTFVMPTLIELESFDE--LQREIFGPVLHVVRYKRKEi 1029
Cdd:PLN00412 335 DITPVVSESSANFIEGLVMDAKEKGATFCQ-------EWKReGNLIWPLLLDNVRPDMriAWEEPFGPVLPVIRINSVE- 406
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 68348298 1030 dQLIAQINASGYGLTLGVHTR-IDETIAkVVDNVHAGNVYVN 1070
Cdd:PLN00412 407 -EGIHHCNASNFGLQGCVFTRdINKAIL-ISDAMETGTVQIN 446
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
674-1092 |
3.99e-47 |
|
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: 176.49 E-value: 3.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 674 VQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAI-AEVREAVDFLRYYA 752
Cdd:cd07116 32 VPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 753 VQAR-----------NDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLvaaqAVRLLLEA-- 819
Cdd:cd07116 112 GCIRaqegsiseideNTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPA----SILVLMELig 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 820 -GIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQ 898
Cdd:cd07116 188 dLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI------IPVTLELGGKSPNIFFADVMDAD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 899 vvidvvSSAFDSA-----------GQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07116 262 ------DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKIL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 968 KHIQAMRDKGRNVyqmaIADGEECKR-----GTFVMPTLI----ELESFdelQREIFGPVLHVVRYkrKEIDQLIAQINA 1038
Cdd:cd07116 336 SYIDIGKEEGAEV----LTGGERNELggllgGGYYVPTTFkggnKMRIF---QEEIFGPVLAVTTF--KDEEEALEIAND 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 68348298 1039 SGYGLTLGVHTRIDETIAKVVDNVHAGNVYVnrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07116 407 TLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
651-1092 |
1.17e-46 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 175.85 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 651 CAASSETPAPVLNPSDHRDVvGHVQEATVEDVDNAIQCALNA--APIWQATPPAERAAILERAADLMEGEIQPLMGLLAR 728
Cdd:PRK09847 29 TAAAENETFETVDPVTQAPL-AKIARGKSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 729 EAGKTFANAIAE-VREAVDFLRYYAVQARNDFSNDA-----------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:PRK09847 108 DTGKPIRHSLRDdIPGAARAIRWYAEAIDKVYGEVAttsshelamivREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 797 VLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNiAGRlDNQGRpi 876
Cdd:PRK09847 188 VILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKD-AGD-SNMKR-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 877 pLIAETGGQNAMIV--DSSALtEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDI 954
Cdd:PRK09847 264 -VWLEAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 955 GPVIDAEAKAGIEKHIQAMRDKGRnvyqmAIADGEECKRGTFVMPT-LIELESFDELQR-EIFGPVLHVVRYKRKEidQL 1032
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKGQ-----LLLDGRNAGLAAAIGPTiFVDVDPNASLSReEIFGPVLVVTRFTSEE--QA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1033 IAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVvgVQPFGGEGLSGTG 1092
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
677-1092 |
2.84e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 173.39 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 677 ATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQAR 756
Cdd:PRK09406 20 LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 757 N---DFSNDA-----------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIP 822
Cdd:PRK09406 100 AllaDEPADAaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 823 EGVLQ-LLPGQGESvgARLVGDERVKGVMFTGSTEVARLLQrNIAGRLDNqgrpiPLIAETGGQNAMIVDSSALTEQVVI 901
Cdd:PRK09406 180 DGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVA-AIAGDEIK-----KTVLELGGSDPFIVMPSADLDRAAE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 902 DVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVy 981
Cdd:PRK09406 252 TAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATI- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 982 qmaIADGEECKR-GTFVMPTLI-----ELESFDElqrEIFGPVLHVvrYKRKEIDQLIAQINASGYGLTLGVHTRIDETI 1055
Cdd:PRK09406 331 ---LCGGKRPDGpGWFYPPTVItditpDMRLYTE---EVFGPVASL--YRVADIDEAIEIANATTFGLGSNAWTRDEAEQ 402
|
410 420 430
....*....|....*....|....*....|....*....
gi 68348298 1056 AKVVDNVHAGNVYVNrnivGAVVGVQ--PFGGEGLSGTG 1092
Cdd:PRK09406 403 ERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
705-1071 |
6.38e-45 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 168.38 E-value: 6.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 705 AAILERAADLMEgeiqplmgLLAREAGKTFANAIAEVREAVDFLRYYAVQAR--------NDFSNDA----HRPLGPVVC 772
Cdd:PRK10090 6 AGIRERASEISA--------LIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegeiiqSDRPGENillfKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 773 ISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFT 852
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 853 GSTEV-ARLLQ---RNIagrldnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSA 928
Cdd:PRK10090 158 GSVSAgEKIMAaaaKNI----------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 929 DRVIEMLKGAMAENRLGNP-ERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQMAIADGEeckRGTFVMPTLIE--LE 1005
Cdd:PRK10090 228 DQFVNRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEG---KGYYYPPTLLLdvRQ 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68348298 1006 SFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNR 1071
Cdd:PRK10090 305 EMSIMHEETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR 368
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
660-1070 |
8.35e-45 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 170.30 E-value: 8.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 660 PVLNPSDHrDVVGHVQEATVEDVDNAIQCALNA-----APIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTF 734
Cdd:PLN02467 26 PVVNPATE-ETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 735 ANAIAEVREAVDFLRYYAVQARN-DFSNDA--------------HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:PLN02467 105 DEAAWDMDDVAGCFEYYADLAEAlDAKQKApvslpmetfkgyvlKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 800 KPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLi 879
Cdd:PLN02467 185 KPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMV----KPVSL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 aETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVID 959
Cdd:PLN02467 260 -ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 960 AEAKAGIEKHIQAMRDKGRNVYQMAIAdGEECKRGTFVMPTLI-ELESFDELQR-EIFGPVLHVVRYKRKeiDQLIAQIN 1037
Cdd:PLN02467 339 EGQYEKVLKFISTAKSEGATILCGGKR-PEHLKKGFFIEPTIItDVTTSMQIWReEVFGPVLCVKTFSTE--DEAIELAN 415
|
410 420 430
....*....|....*....|....*....|...
gi 68348298 1038 ASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVN 1070
Cdd:PLN02467 416 DSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
764-1092 |
2.18e-43 |
|
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: 164.24 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAgIPEGVLQLLPGQGEsVGARLVgD 843
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-VATALL-A 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 844 ERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCL 923
Cdd:cd07087 175 EPFDHIFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 924 QEDSADRVIEMLKGAMAEnRLGNPERLSVDIGPVIDaeakagiEKHIQAMRD--KGRNVYQMAIADGEECkrgtFVMPTL 1001
Cdd:cd07087 249 HESIKDELIEELKKAIKE-FYGEDPKESPDYGRIIN-------ERHFDRLASllDDGKVVIGGQVDKEER----YIAPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1002 IELESFDE--LQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVG 1079
Cdd:cd07087 317 LDDVSPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIP 394
|
330
....*....|...
gi 68348298 1080 VQPFGGEGLSGTG 1092
Cdd:cd07087 395 NLPFGGVGNSGMG 407
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
663-1096 |
1.93e-42 |
|
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: 162.47 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 663 NPSDHRdVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILeraADLMEGEI--QPLMGLLA-REAGKTFANA-I 738
Cdd:cd07098 2 DPATGQ-HLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVL---RSLLKYILenQEEICRVAcRDTGKTMVDAsL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 739 AEVREAVDFLRY--------YAVQARNDFSNDAHR-------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07098 78 GEILVTCEKIRWtlkhgekaLRPESRPGGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 804 QTPLVAAQAVRLLLEA----GIPEGVLQLLPGQGEsVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLI 879
Cdd:cd07098 158 QVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVID 959
Cdd:cd07098 231 LELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 960 AEAKAGIEKHIQAMRDKG-RNVYQMAIADGEECKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQI 1036
Cdd:cd07098 311 PARFDRLEELVADAVEKGaRLLAGGKRYPHPEYPQGHYFPPTLLVdvTPDMKIAQEEVFGPVMVVMKA--SDDEEAVEIA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1037 NASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:cd07098 389 NSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
682-1054 |
2.68e-37 |
|
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: 146.92 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 682 VDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYA--------V 753
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFAdlvregswL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 754 QARNDFSNDA------------HRPLGPVVCISPWNFPLAiFS---GQVAAALAAGNPVLAK--PA--EQTPLVAAQAVR 814
Cdd:cd07129 81 DARIDPADPDrqplprpdlrrmLVPLGPVAVFGASNFPLA-FSvagGDTASALAAGCPVVVKahPAhpGTSELVARAIRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 815 LLLEAGIPEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrPIPLIAETGGQNAMIVDSSA 894
Cdd:cd07129 160 ALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGSVNPVFILPGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 895 LTE---QVVIDVVSSAFDSAGQRCSALRVLCLQEDSA-DRVIEMLKGAMAEnrlgnperlsVDIGPVIDAEAKAGIEKHI 970
Cdd:cd07129 236 LAErgeAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAA----------APAQTMLTPGIAEAYRQGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 971 QAMRD--KGRNVYQMAIADGEECKRGTFVMPTLIELESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVH 1048
Cdd:cd07129 306 EALAAapGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLADPALQEEVFGPASLVVRY--DDAAELLAVAEALEGQLTATIH 383
|
....*.
gi 68348298 1049 TRIDET 1054
Cdd:cd07129 384 GEEDDL 389
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
661-1070 |
4.21e-37 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 149.13 E-value: 4.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 661 VLNPSDhRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAE 740
Cdd:PLN02419 133 VINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 741 VREAVDFLRY-----------YAVQARNDFSNDAHR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLV 808
Cdd:PLN02419 212 IFRGLEVVEHacgmatlqmgeYLPNVSNGVDTYSIRePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 809 AAQAVRLLLEAGIPEGVLQLLPGQGESVGArLVGDERVKGVMFTGSTEVArllqRNIAGRLDNQGRPIPliAETGGQNAM 888
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAG----MHIYARAAAKGKRIQ--SNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSA---DRVIEMLKgAMAENRLGNPErlsVDIGPVIDAEAKAG 965
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVERAK-ALKVTCGSEPD---ADLGPVISKQAKER 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 966 IEKHIQAMRDKGRNVyqmaIADGEEC-----KRGTFVMPTLI-----ELESFDElqrEIFGPVLhvVRYKRKEIDQLIAQ 1035
Cdd:PLN02419 441 ICRLIQSGVDDGAKL----LLDGRDIvvpgyEKGNFIGPTILsgvtpDMECYKE---EIFGPVL--VCMQANSFDEAISI 511
|
410 420 430
....*....|....*....|....*....|....*
gi 68348298 1036 INASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVN 1070
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
764-1097 |
1.34e-36 |
|
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: 144.29 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVlQLLPGQGESVGARLvgD 843
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEGDAEVAQALL--E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 844 ERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCL 923
Cdd:cd07134 175 LPFDHIFFTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 924 QEDSADRVIEMLKGAMAENRLGNPERL-SVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQMAIADGEECkrgtFVMPTLI 1002
Cdd:cd07134 249 HESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR----YIAPTVL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1003 E--LESFDELQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGV 1080
Cdd:cd07134 325 TnvTPDMKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPN 402
|
330
....*....|....*..
gi 68348298 1081 QPFGGEGLSGTGpKAGG 1097
Cdd:cd07134 403 LPFGGVNNSGIG-SYHG 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
766-1092 |
3.48e-35 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 141.32 E-value: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVaAQAVRLLLEAGIPEGVLQLLPGQGESVGARLvgDER 845
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT-SKLMAKLLTKYLDPSYVRVIEGGVEVTTELL--KEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 846 VKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQE 925
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 926 DSADRVIEMLKGAMAENRLGNPERlSVDIGPVIDAEAkagIEKHIQAMRDKGRNVYQMAIADGEEckrgTFVMPTLIELE 1005
Cdd:PTZ00381 260 SIKDKFIEALKEAIKEFFGEDPKK-SEDYSRIVNEFH---TKRLAELIKDHGGKVVYGGEVDIEN----KYVAPTIIVNP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1006 SFDE--LQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQPF 1083
Cdd:PTZ00381 332 DLDSplMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPF 409
|
....*....
gi 68348298 1084 GGEGLSGTG 1092
Cdd:PTZ00381 410 GGVGNSGMG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
764-1092 |
3.33e-34 |
|
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: 137.23 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAqAVRLLLEAGIPEGVLQLLPGQGEsVGA---RL 840
Cdd:cd07133 99 YQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSA-LLAELLAEYFDEDEVAVVTGGAD-VAAafsSL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 841 VGDErvkgVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRV 920
Cdd:cd07133 177 PFDH----LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 921 LCLQEDSADRVIEMLKGAMAE---NRLGNPerlsvDIGPVIDAEAKAGIEKHIQAMRDKGRNVYQmaIADGEECKRGTFV 997
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKmypTLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIE--LNPAGEDFAATRK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 998 MPTLIELESFDE---LQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIV 1074
Cdd:cd07133 320 LPPTLVLNVTDDmrvMQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
330
....*....|....*...
gi 68348298 1075 GAVVGVQPFGGEGLSGTG 1092
Cdd:cd07133 398 HVAQDDLPFGGVGASGMG 415
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
654-1070 |
2.88e-33 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 134.99 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 654 SSETPAPVLNPSDHrDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKT 733
Cdd:PRK13968 4 TPATHAISVNPATG-EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 734 FANAIAEVREAVDFLRYYAVQA-----------RNDFSNDAHRPLGPVVCISPWNFPL-AIFSGQVAAALaAGNPVLAKP 801
Cdd:PRK13968 83 INQARAEVAKSANLCDWYAEHGpamlkaeptlvENQQAVIEYRPLGTILAIMPWNFPLwQVMRGAVPILL-AGNGYLLKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 802 AEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVgARLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAE 881
Cdd:PRK13968 162 APNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAE 961
Cdd:PRK13968 235 LGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 962 AKAGIEKHIQAMRDKGRNVyqmaIADGEECK-RGTFVMPTLI-----ELESFDElqrEIFGPVLHVVryKRKEIDQLIAQ 1035
Cdd:PRK13968 315 LRDELHHQVEATLAEGARL----LLGGEKIAgAGNYYAPTVLanvtpEMTAFRE---ELFGPVAAIT--VAKDAEHALEL 385
|
410 420 430
....*....|....*....|....*....|....*
gi 68348298 1036 INASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVN 1070
Cdd:PRK13968 386 ANDSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
764-1092 |
3.48e-33 |
|
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: 134.27 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAgIPEGVLQLLPGQGESVGARLvgD 843
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 844 ERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALR-VLC 922
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIAEAAAKHL------TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDyVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 923 lQEDSADRVIEMLKGAMAENRLGNPERLSvDIGPVIDAEAKAGIEKHIQamRDKGRNVYQmAIADGEECkrgtFVMPTLI 1002
Cdd:cd07135 257 -DPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLD--TTKGKVVIG-GEMDEATR----FIPPTIV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1003 ELESFDE--LQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGV 1080
Cdd:cd07135 328 SDVSWDDslMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDN 405
|
330
....*....|..
gi 68348298 1081 QPFGGEGLSGTG 1092
Cdd:cd07135 406 APFGGVGDSGYG 417
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
682-1112 |
7.60e-31 |
|
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: 127.35 E-value: 7.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 682 VDNAIQCALNAAPIWQATPPAERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQAR----- 756
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSyriph 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 757 -------NDFSNDAHR---PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGI-PEGV 825
Cdd:cd07084 81 epgnhlgQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 826 LQLLPGQGESvGARLVGDERVKGVMFTGSTEVARLLQRNIAgrldnqgrPIPLIAETGGQNAMIVDSSALTEQVVID-VV 904
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAK--------QARIYLELAGFNWKVLGPDAQAVDYVAWqCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 905 SSAFDSAGQRCSALRVLCLQEDSADR-VIEMLKGAMAENRLGnperlSVDIGPVIDAEAKAGIEkhiqAMRDKGRNVyqm 983
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQTFTTLAMIA----HMENLLGSV--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 984 AIADGEE------------CKRGTFVMPTLIELESFDELQREIFGPVLHVVRYKRKEIDQLIAQINASGYGLTLGVHTRI 1051
Cdd:cd07084 300 LLFSGKElknhsipsiygaCVASALFVPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSND 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68348298 1052 DETIAKVVDN--VHAGNVYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPVDA 1112
Cdd:cd07084 380 PIFLQELIGNlwVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAEQA 442
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
764-1092 |
1.38e-27 |
|
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: 117.71 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 764 HRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLL-----------LEAGIPEgVLQLLpgq 832
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyldkecypvVLGGVEE-TTELL--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 833 gesvgarlvgDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAG 912
Cdd:cd07132 174 ----------KQRFDYIFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 913 QRCSALR-VLCLQEdSADRVIEMLKGAMAEnRLGNPERLSVDIGPVIDaeakagiEKH---IQAMRDKGRnvyqmaIADG 988
Cdd:cd07132 238 QTCIAPDyVLCTPE-VQEKFVEALKKTLKE-FYGEDPKESPDYGRIIN-------DRHfqrLKKLLSGGK------VAIG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 989 EECKRGT-FVMPT-LIELESFDEL-QREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAG 1065
Cdd:cd07132 303 GQTDEKErYIAPTvLTDVKPSDPVmQEEIFGPILPIVTV--NNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSG 380
|
330 340
....*....|....*....|....*..
gi 68348298 1066 NVYVNRNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07132 381 GVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
766-1092 |
1.42e-27 |
|
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: 117.61 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 766 PLGPVVCISPWNFP--LAIfsGQVAAALAAGNPVLAKPAEQTPLVAAqAVRLLLEAGIPEGVLQLLPGQGESVGARLvgD 843
Cdd:cd07136 100 PYGVVLIIAPWNYPfqLAL--APLIGAIAAGNTAVLKPSELTPNTSK-VIAKIIEETFDEEYVAVVEGGVEENQELL--D 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 844 ERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCL 923
Cdd:cd07136 175 QKFDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 924 QEDSADRVIEMLKGAmAENRLGNPERLSVDIGPVIDaeakagiEKH---IQAMRDKGRNVYQmaiadGEECKRGTFVMPT 1000
Cdd:cd07136 249 HESVKEKFIKELKEE-IKKFYGEDPLESPDYGRIIN-------EKHfdrLAGLLDNGKIVFG-----GNTDRETLYIEPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1001 LIELESFDE--LQREIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVV 1078
Cdd:cd07136 316 ILDNVTWDDpvMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLAN 393
|
330
....*....|....
gi 68348298 1079 GVQPFGGEGLSGTG 1092
Cdd:cd07136 394 PYLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
766-1092 |
2.41e-26 |
|
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: 113.66 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLL-----------LEAGIPEGVlQLLpgqge 834
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIpeyldtkaikvIEGGVPETT-ALL----- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 835 svgarlvgDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDS-AGQ 913
Cdd:cd07137 175 --------EQKWDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 914 RCSALRVLCLQEDSADRVIEMLKgAMAENRLGNPERLSVDIGPVIDAeakagieKHIQ--AMRDKGRNVYQMAIADGEEC 991
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALK-NTLEKFFGENPKESKDLSRIVNS-------HHFQrlSRLLDDPSVADKIVHGGERD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 992 KRGTFVMPTLIELESFDEL--QREIFGPVLHVVryKRKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYV 1069
Cdd:cd07137 313 EKNLYIEPTILLDPPLDSSimTEEIFGPLLPII--TVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTF 390
|
330 340
....*....|....*....|...
gi 68348298 1070 NRNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07137 391 NDTVVQYAIDTLPFGGVGESGFG 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
766-1097 |
5.53e-26 |
|
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: 113.90 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 766 PLGPV-VCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGI-PEGVLQLLPGQGESVGARLvGD 843
Cdd:cd07128 143 PRRGVaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHL-GE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 844 ERVkgVMFTGSTEVARLLQRNiagrlDN-QGRPIPLIAETGGQNAMIV--DSSALTEQ---VVIDVVSSAFDSAGQRCSA 917
Cdd:cd07128 222 QDV--VAFTGSAATAAKLRAH-----PNiVARSIRFNAEADSLNAAILgpDATPGTPEfdlFVKEVAREMTVKAGQKCTA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 918 LRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVY---QMAIADGEECKRG 994
Cdd:cd07128 295 IRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFggpDRFEVVGADAEKG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 995 TFVMPTLIELESFDELQR----EIFGPVLHVVRYkrKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNV--HAGNVY 1068
Cdd:cd07128 375 AFFPPTLLLCDDPDAATAvhdvEAFGPVATLMPY--DSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAapYHGRLL 452
|
330 340 350
....*....|....*....|....*....|....*.
gi 68348298 1069 V-NRNIVGAVVG---VQP---FGGEGLSGTGPKAGG 1097
Cdd:cd07128 453 VlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGG 488
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
766-1092 |
1.82e-25 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 111.74 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAqavrlLLEAGIPE----GVLQLLPGqGESVGARLV 841
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPKyldsKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 842 gDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVD--SSALTEQVVID-VVSSAFDS-AGQRCSA 917
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDslSSSRDTKVAVNrIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 918 LRVLCLQEDSADRVIEMLKgAMAENRLGNPERLSVDIGPVIDaeakagiEKHIQAMRD--KGRNVYQMAIADGEECKRGT 995
Cdd:PLN02203 255 IDYVLVEERFAPILIELLK-STIKKFFGENPRESKSMARILN-------KKHFQRLSNllKDPRVAASIVHGGSIDEKKL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 996 FVMPTLIELESFDE--LQREIFGPVLHVVRYKRkeIDQLIAQINASGYGLTLGVHTRiDETIAK-VVDNVHAGNVYVNRN 1072
Cdd:PLN02203 327 FIEPTILLNPPLDSdiMTEEIFGPLLPIITVKK--IEDSIAFINSKPKPLAIYAFTN-NEKLKRrILSETSSGSVTFNDA 403
|
330 340
....*....|....*....|
gi 68348298 1073 IVGAVVGVQPFGGEGLSGTG 1092
Cdd:PLN02203 404 IIQYACDSLPFGGVGESGFG 423
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
702-1097 |
4.16e-20 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 95.54 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 702 AERAAILERAADLMEGEIQPLMGLLAREAGKTFANAIAEVREAVDFLRYYA--------VQARND------------FSN 761
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalgdARLLRDgeavqlgkdpafQGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 762 DAHRPL-GPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEAGI-PEGVLQLLPGQGESVGAR 839
Cdd:PRK11903 143 HVLVPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 840 LVGDERVKgvmFTGSTEVARLLqRNIAGRLDNQGRpipLIAETGGQNAMI-----VDSSALTEQVVIDVVSSAFDSAGQR 914
Cdd:PRK11903 223 LQPFDVVS---FTGSAETAAVL-RSHPAVVQRSVR---VNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 915 CSALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVY---QMAIADGEEC 991
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFdggGFALVDADPA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 992 KrGTFVMPTLIELESFDELQR----EIFGPVLHVVRYKRKEidQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHA--G 1065
Cdd:PRK11903 376 V-AACVGPTLLGASDPDAATAvhdvEVFGPVATLLPYRDAA--HALALARRGQGSLVASVYSDDAAFLAAAALELADshG 452
|
410 420 430
....*....|....*....|....*....|....*....
gi 68348298 1066 NVYVNRNIVGA-------VVGVQPFGGEGLSGTGPKAGG 1097
Cdd:PRK11903 453 RVHVISPDVAAlhtghgnVMPQSLHGGPGRAGGGEELGG 491
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
725-1068 |
1.65e-19 |
|
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: 93.71 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 725 LLAREAGKTFANAIAEVREAVDFL------------RYYAVQA--RNDFSNDAHRPLGPVVCISPWNFPLAIFSGQVAAA 790
Cdd:cd07126 87 LIQRVAPKSDAQALGEVVVTRKFLenfagdqvrflaRSFNVPGdhQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 791 LAAGNPVLAKPAEQTPLVAAQAVRLLLEAGIPEGVLQLLPGQGESVGaRLVGDERVKGVMFTGSTEVARLLQRNIAGRLD 870
Cdd:cd07126 167 LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPRMTLFTGSSKVAERLALELHGKVK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 871 nqgrpiplIAETGgqnamiVDSSALTEQVV-IDVVS-----SAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAENRl 944
Cdd:cd07126 246 --------LEDAG------FDWKILGPDVSdVDYVAwqcdqDAYACSGQKCSAQSILFAHENWVQAGILDKLKALAEQR- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 945 gNPERLSvdIGPVIDAEAkagiekhiQAMRDKGRNVYQMAIAD----GEECKRGTF------VMPTLIEL--------ES 1006
Cdd:cd07126 311 -KLEDLT--IGPVLTWTT--------ERILDHVDKLLAIPGAKvlfgGKPLTNHSIpsiygaYEPTAVFVpleeiaieEN 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68348298 1007 FDELQREIFGPVLHVVRYKRKEIDQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVY 1068
Cdd:cd07126 380 FELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
766-1096 |
7.01e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 88.56 E-value: 7.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRlLLEAGIPEGVLQLLPGQGESVGARLvgDER 845
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAK-LLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 846 VKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFD-SAGQRCSALRVLCLQ 924
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 925 EDSADRVIEMLKGAMAENRLGNPERlSVDIGPVIDAEAKAGIEKHIQAMRDKGRNVYqmaiaDGEECKRGTFVMPTLIEL 1004
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVY-----GGEKDRENLKIAPTILLD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 1005 ESFDEL--QREIFGPVLHVVRYKRKEidQLIAQINASGYGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAVVGVQP 1082
Cdd:PLN02174 337 VPLDSLimSEEIFGPLLPILTLNNLE--ESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLP 414
|
330
....*....|....
gi 68348298 1083 FGGEGLSGTGPKAG 1096
Cdd:PLN02174 415 FGGVGESGMGAYHG 428
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
87-134 |
1.66e-17 |
|
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: 77.12 E-value: 1.66e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 68348298 87 SVLRASITAAYRRPEPEVVPMLLEQARLPAATAEAANKLAASIAEKLR 134
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-68 |
1.16e-14 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 69.85 E-value: 1.16e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68348298 2 ATTTLGVKLDDPTRERLKAAAASIDRTPHWLIKQAIFNYLEKLEGGATLTELSSATAKDGE--DAGEVQ 68
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQEGLAAADAGEfvSHEEVE 69
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
681-1077 |
1.86e-13 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 74.82 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 681 DVDNAIQCALNAAPIWQATPPAERAA----ILERAADL---MEGEIQPLMG---LLAREAGKTFA-----NAIAEVREAV 745
Cdd:cd07127 85 DPDALLAAARAAMPGWRDAGARARAGvcleILQRLNARsfeMAHAVMHTTGqafMMAFQAGGPHAqdrglEAVAYAWREM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 746 DFL----RYYAVQARND-FSNDAH-----RPLGPVVCISP---WNFPLAIFsgqvaAALAAGNPVLAKPAEQTPLVAAQA 812
Cdd:cd07127 165 SRIpptaEWEKPQGKHDpLAMEKTftvvpRGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAIT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 813 VR----LLLEAGI-PEGVLQLLPGQGESVGARLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpipLIAETGGQNA 887
Cdd:cd07127 240 VQvareVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--------VYTEKAGVNT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 888 MIVDSsalTEQVVIDVVSSAFDSA---GQRCSALRVLCLQED---------SADRVIEMLkGAMAENRLGNPERLSVDIG 955
Cdd:cd07127 312 VVVDS---TDDLKAMLRNLAFSLSlysGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADL-AAAIDGLLADPARAAALLG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 956 PVIDAEAKAGIEKHIQAMRdkgrnvyqmAIADGEECKRGTFV-----MPTLIELESFDE--LQREIFGPVLHVVRYKRKE 1028
Cdd:cd07127 388 AIQSPDTLARIAEARQLGE---------VLLASEAVAHPEFPdarvrTPLLLKLDASDEaaYAEERFGPIAFVVATDSTD 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 68348298 1029 --IDQLIAQINASGyGLTLGVHTRIDETIAKVVDNVHAGNVYVNRNIVGAV 1077
Cdd:cd07127 459 hsIELARESVREHG-AMTVGVYSTDPEVVERVQEAALDAGVALSINLTGGV 508
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
199-558 |
4.03e-10 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 63.57 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 199 SPSLFVNAATWGLLLTGKLVsTHNEAGLTSSLSRIIGKSGEPMIRKGVdmamrlmGEQFVTGETIAEALANASKFEAKGF 278
Cdd:PLN02681 38 TSELLRSLLVLQLCAIGPLV-DLGEWLLTSPLMVLGRAIVLALVKATF-------YSHFCAGEDAEEAARTVRRLWELGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 279 R----YSYDMLGEAALTEHDAQKYLASYEQAIHSIGKAS-------------------------HGRGIYEGPGI--SIK 327
Cdd:PLN02681 110 GgildYAAEDAGDNAACDRNLEKFLAAIRAAATLPPSSSsaavkitalcppsllervsdllrwqDRDPNGKLPWKqwSFP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 328 LSALH-PRYS--------RAQYERVMEELYPRLLSLTLLAKQYDIGLNIDAEEAdRLELSLDlleRLCFEPQLTGWNGIG 398
Cdd:PLN02681 190 LFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYT-SLQPAID---YITYDLAREFNKGKD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 399 F-----VIQAYQKRCPYVIDYVIDLARRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGyPVYTRKVYTDVSYIACARKLL- 472
Cdd:PLN02681 266 RpivygTYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAEFLLe 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 473 ----SVPEVIypqFATHNAHTLSAIYHIA---GQNYYPGQYEFQCLHGMGEPLyeqvvgkvAEGKLNRPCRV--YAPVGT 543
Cdd:PLN02681 345 kasnGDGEVM---LATHNVESGELAAAKMnelGLHKGDPRVQFAQLLGMSDNL--------SFGLGNAGFRVskYLPYGP 413
|
410
....*....|....*
gi 68348298 544 HETLLAYLVRRLLEN 558
Cdd:PLN02681 414 VEEVIPYLLRRAEEN 428
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-45 |
1.84e-09 |
|
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar proteins; This family includes the N-terminal ribbon-helix-helix (RHH) domain of Shewanella oneidensis CopA(SO), a newly identified type II antitoxin, as well as the N-terminal RHH domain of Escherichia coli PutA flavoprotein, among other similar proteins, many of which are as yet uncharacterized. CopA(SO) is a typical RHH antitoxin that includes an ordered N-terminal domain (CopA(SO)-N) and a disordered C-terminal domain (CopA(SO)-C). Biophysical investigation indicates allosteric effects of CopA(SO)-N on CopA(SO)-C; DNA binding of CopA(SO)-N appears to induce CopA(SO)-C to fold and self-associate the C-terminal domain. The multifunctional E. coli proline utilization A (PutA) flavoprotein functions as a membrane-associated proline catabolic enzyme as well as a transcriptional repressor of the proline utilization genes putA and putP. The N-terminal domain of PutA is a transcriptional regulator with an RHH fold; structure studies show that it forms a homodimer to bind one DNA duplex. This family also includes orphan antitoxin ParD2, an antitoxin component of a non-functional type II toxin-antitoxin (TA system); it does not neutralize the effect of any of the RelE or ParE toxins.
Pssm-ID: 409023 Cd Length: 44 Bit Score: 54.30 E-value: 1.84e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 68348298 4 TTLGVKLDDPTRERLKAAAASIDRTPHWLIKQAIFNYLEKLE 45
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREE 42
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
701-968 |
1.79e-07 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 54.92 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 701 PAERAAILERAADLMEGEIQPLMGLLAREAG----KTFANAIAEVREAVDFLRYYAVQARNDFSNDAHRP-------LGP 769
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGayirSLIANWIAMMGCSESKLYKNIDTERGITASVGHIQdvllpdnGET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 770 VVCISPWNFPLAIFSGQV--------AAALAAGNPVLAKPAEQTPlVAAQAVRLLLEAGIPEG----VLQLLPGQGESVG 837
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNplsgitsaLRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkiLVLYVPHPSDELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 838 ARLVGDERVKGVMFTGSTEVARLLQRNiagrldnqGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSA-FDSAGqrCS 916
Cdd:cd07077 174 EELLSHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA--CA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 68348298 917 ALRVLCLQEDSADRVIEMLKGAMAENRLGNPERLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07077 244 SEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFDDEALES 295
|
|
| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-45 |
5.74e-07 |
|
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins; This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.
Pssm-ID: 409020 Cd Length: 42 Bit Score: 47.12 E-value: 5.74e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 68348298 4 TTLGVKLDDPTRERLKAAAASIDRTPHWLIKQAIFNYLEKLE 45
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLERLE 42
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
766-1058 |
1.96e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 48.80 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLLLEA----GIPEGVLQLLPGQGESVGARLV 841
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 842 GDERVKGVMFTGSTEVARllqrniAGRLDNQgrpiPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVL 921
Cdd:cd07081 175 KFPGIGLLLATGGPAVVK------AAYSSGK----PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68348298 922 CLQEDSADRVIEMLKGAMAENRLGNPERLSVDIgpvidaeakagIEKHIQAMRD-KGRNVYQMAIADGEECKRGTFVMpt 1000
Cdd:cd07081 245 IVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPV-----------ILKNGDVNRDiVGQDAYKIAAAAGLKVPQETRIL-- 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68348298 1001 LIELESFDE---LQREIFGPVLHVVRYKRKEIDQLIAQ--INASGYGLTLGVHTRIDETIAKV 1058
Cdd:cd07081 312 IGEVTSLAEhepFAHEKLSPVLAMYRAANFADADAKALalKLEGGCGHTSAMYSDNIKAIENM 374
|
|
| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
1-45 |
4.31e-04 |
|
Predicted DNA-binding protein with an HTH domain [General function prediction only];
Pssm-ID: 443745 Cd Length: 76 Bit Score: 40.27 E-value: 4.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 68348298 1 MATTTlgVKLDDPTRERLKAAAASIDRTPHWLIKQAIFNYLEKLE 45
Cdd:COG4710 1 MKMLS--IRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
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