|
Name |
Accession |
Description |
Interval |
E-value |
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
1-1262 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 2210.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1 MATVTLGVKVDEALRERLRVLAESLGCTPHWLHKQALLSYIEAIERGQVPAEIDRRADADSTEASAVEP---EPLAPFHE 77
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADTpaeEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 78 FAQEVLPQSVLRAAITAAYRRPEPECVAMLVDQAESSQP--ERVETLARRLVQTLRDKRKGGG----VEGLIQEFSLSSQ 151
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPlaEAAHKLAYQLAEKLRNQKSAGGragmVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 152 EGVALMCLAEALLRIPDQATRDALIRDKISHGDWRAHVGESRSLFVNAATWGLLVTGKLVSVNSEQNLSQALTRLIAKGG 231
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 232 EPLIRRGVNMAMRLMGEQFVTGQTISSALANSRKFEDIGFRYSYDMLGEAATTAEDAARYYQSYEQAIHAIGKASQGRGI 311
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 312 YEGPGISIKLSALHPRYSRAQRDRVMEELLPRMVGLAALARRYDIGLNIDAEEADRLELSLDLLEALCFDERLRGWNGIG 391
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 392 FVIQAYQKRAPFVIDFVIDLARRSKHRLMVRLVKGAYWDSEVKRAQVDGLEGYPVYTRKIHTDVSYLACARKLLSAPEAV 471
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 472 FPQFATHNAQTLASIYYMAGENYYPGQYEFQCLHGMGEPLYEEVVGPVSKGRLNRPCRVYAPVGTHETLLAYLVRRLLEN 551
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 552 GANTSFVNQIGDRDLPIDALVADPVRKARAIQ----PLGAPHERIPLPRDLYRAheDRANSAGLDLSNEHRLGSLAAALL 627
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAqqegQLGLPHPKIPLPRDLYGK--GRANSAGLDLANEHRLASLSSALL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 628 GAAAQDWRAAP--PGEWRGERARPVPNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLME 705
Cdd:PRK11809 639 ASAHQKWQAAPmlEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLME 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 706 DEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNV 785
Cdd:PRK11809 719 AQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNS 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 786 VLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAGHPV 865
Cdd:PRK11809 799 VLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPI 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 866 PLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGP 945
Cdd:PRK11809 879 PLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGP 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 946 VIDAEARAVIERHVQAMQAAGHAVDRYPLDEAQT-RHGTFVAPTLIEIADIAELEREVFGPVLHVLRYRRQDLDAVIDAI 1024
Cdd:PRK11809 959 VIDAEAKANIERHIQAMRAKGRPVFQAARENSEDwQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQI 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1025 NGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYLHRLLADAP-GTLPVE 1103
Cdd:PRK11809 1039 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPeDALAVT 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1104 GVVGKGARPL-------------------------------------------TLPGPTGETNQYHLKPRGTVLCHAASA 1140
Cdd:PRK11809 1119 LARQDAEYPVdaqlraallapltalrewaaerepelaalcdqyaelaqagttrLLPGPTGERNTYTLLPRERVLCLADTE 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1141 AGAQAQMEACHRTGNEMLWVDHPEVRAFHAARPAG--AAVRWVAPEAVATADFQAVLYEGDSDGLQALSRAIVGRPGPIV 1218
Cdd:PRK11809 1199 QDALTQLAAVLAVGSQALWPDDALHRALVAALPAAvqARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPIV 1278
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....
gi 589266809 1219 PVLARRvdelSAGKTYPLEMLVREVSVCVNTAAAGGNASLMMVG 1262
Cdd:PRK11809 1279 SVQGFA----RGETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
74-1262 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1951.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 74 PFHEFAQEVLPQSVLRAAITAAYRRPEPECVAMLVDQAESSQPER--VETLARRLVQTLRDKRKGGGVEGLIQEFSLSSQ 151
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARaaIRERARKLVEALRAKRKGTGVEALLQEYSLSSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 152 EGVALMCLAEALLRIPDQATRDALIRDKISHGDWRAHVGESRSLFVNAATWGLLVTGKLVSVNSEQNLSQALTRLIAKGG 231
Cdd:PRK11905 81 EGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIARLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 232 EPLIRRGVNMAMRLMGEQFVTGQTISSALANSRKFEDIGFRYSYDMLGEAATTAEDAARYYQSYEQAIHAIGKASQGRGI 311
Cdd:PRK11905 161 EPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 312 YEGPGISIKLSALHPRYSRAQRDRVMEELLPRMVGLAALARRYDIGLNIDAEEADRLELSLDLLEALCFDERLRGWNGIG 391
Cdd:PRK11905 241 YDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 392 FVIQAYQKRAPFVIDFVIDLARRSKHRLMVRLVKGAYWDSEVKRAQVDGLEGYPVYTRKIHTDVSYLACARKLLSAPEAV 471
Cdd:PRK11905 321 FVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 472 FPQFATHNAQTLASIYYMAGENYypgQYEFQCLHGMGEPLYEEVVGpvsKGRLNRPCRVYAPVGTHETLLAYLVRRLLEN 551
Cdd:PRK11905 401 YPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVG---KEKLGRPCRIYAPVGTHETLLAYLVRRLLEN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 552 GANTSFVNQIGDRDLPIDALVADPVRKARAIQplGAPHERIPLPRDLYraHEDRANSAGLDLSNEHRLGSLAAALLGAAA 631
Cdd:PRK11905 475 GANSSFVNRIVDENVPVEELIADPVEKVAAMG--VAPHPQIPLPRDLY--GPERRNSKGLDLSDEATLAALDEALNAFAA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 632 QDWRAAPP--GEWRGERARPVPNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQ 709
Cdd:PRK11905 551 KTWHAAPLlaGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMP 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 710 SAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAK 789
Cdd:PRK11905 631 ELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAK 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 790 PAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaGHPVPLIA 869
Cdd:PRK11905 711 PAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GPPVPLIA 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 870 ETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDA 949
Cdd:PRK11905 788 ETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDA 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 950 EARAVIERHVQAMQAAGHAVDRYPLDEAqTRHGTFVAPTLIEIADIAELEREVFGPVLHVLRYRRQDLDAVIDAINGRGY 1029
Cdd:PRK11905 868 EAQANIEAHIEAMRAAGRLVHQLPLPAE-TEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGY 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1030 GLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYLHRLLADAPGTLPVE------ 1103
Cdd:PRK11905 947 GLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPIPPAhesvdt 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1104 --------------------------GVVGKGARPLTLPGPTGETNQYHLKPRGTVLCHAASAAGAQAQMEACHRTGNEM 1157
Cdd:PRK11905 1027 daaardflawldkegkaalaaaardaRARSALGLEQELPGPTGESNLLSLHPRGRVLCVADTEEALLRQLAAALATGNVA 1106
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1158 LWVDHPEVRAFHAARPAGAAVR-WVAPEAVATADFQAVLYEGDSDGLQALSRAIVGRPGPIVPVLARRVDELsagktYPL 1236
Cdd:PRK11905 1107 VVAADSGLAAALADLPGLVAARiDWTQDWEADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEPTDA-----YDL 1181
|
1210 1220
....*....|....*....|....*.
gi 589266809 1237 EMLVREVSVCVNTAAAGGNASLMMVG 1262
Cdd:PRK11905 1182 ARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
84-1092 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1534.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 84 PQSVLRAAITAAYRRPEPECVAMLVDQAESSQPE--RVETLARRLVQTLRDKRKG-GGVEGLIQEFSLSSQEGVALMCLA 160
Cdd:PRK11904 9 SLDELRAAISALYRVDEAAYLRELLELAPLSPEEkaRVTARATQLVEAVRAKKKKlGGIDAFLQEYSLSTEEGIALMCLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 161 EALLRIPDQATRDALIRDKISHGDWRAHVGESRSLFVNAATWGLLVTGKLVSVNSE--QNLSQALTRLIAKGGEPLIRRG 238
Cdd:PRK11904 89 EALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKadGTPSGVLKRLVNRLGEPVIRKA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 239 VNMAMRLMGEQFVTGQTISSALANSRKFEDIGFRYSYDMLGEAATTAEDAARYYQSYEQAIHAIGKASQGRGIYEGPGIS 318
Cdd:PRK11904 169 MRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADLPARPGIS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 319 IKLSALHPRYSRAQRDRVMEELLPRMVGLAALARRYDIGLNIDAEEADRLELSLDLLEALCFDERLRGWNGIGFVIQAYQ 398
Cdd:PRK11904 249 IKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLAVQAYQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 399 KRAPFVIDFVIDLARRSKHRLMVRLVKGAYWDSEVKRAQVDGLEGYPVYTRKIHTDVSYLACARKLLSAPEAVFPQFATH 478
Cdd:PRK11904 329 KRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAIYPQFATH 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 479 NAQTLASIYYMAGEnyypGQYEFQCLHGMGEPLYEEVVgpvskGRLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFV 558
Cdd:PRK11904 409 NAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSFV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 559 NQIGDRDLPIDALVADPVRKARAiqPLGAPHERIPLPRDLYRahEDRANSAGLDLSNEHRLGSLAAALLGAAAQDWRAAP 638
Cdd:PRK11904 480 HRLVDPDVPIEELVADPVEKLRS--FETLPNPKIPLPRDIFG--PERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGP 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 639 PGEWRGErARPVPNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVRE 718
Cdd:PRK11904 556 IINGEGE-ARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVRE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 719 AGKSFPNAIAEVREAVDFLRYYAVRIEESFSND-------------SHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNV 785
Cdd:PRK11904 635 AGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPeklpgptgesnelRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNT 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 786 VLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERlDGAghPV 865
Cdd:PRK11904 715 VIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAAR-DGP--IV 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 866 PLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGP 945
Cdd:PRK11904 792 PLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGP 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 946 VIDAEARAVIERHVQAMQAAGHAVDRYPLDEAqTRHGTFVAPTLIEIADIAELEREVFGPVLHVLRYRRQDLDAVIDAIN 1025
Cdd:PRK11904 872 VIDAEAKANLDAHIERMKREARLLAQLPLPAG-TENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAIN 950
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589266809 1026 GRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYLHRL 1092
Cdd:PRK11904 951 ATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRF 1017
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
73-1259 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1484.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 73 APFHEFAQEVLPQSVLRAAITAAYRRPEPECVAMLVDQAESSQP--ERVETLARRLVQTLRDKRKGGGVEGLIQEFSLSS 150
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAaaAAAAAAALAARERVRARRGGGGGLLLLLELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 151 QEGVALMCLAEALLRIPDQATRDALIRDKISHGDWRAHVGESRSLFVNAATWGLLVTGKLVSVNSEQNLSQALTRLIAKG 230
Cdd:COG4230 81 SEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 231 GEPLIRRGVNMAMRLMGEQFVTGQTISSALANSRKFEDIGFRYSYDMLGEAATTAEDAARYYQSYEQAIHAIGKASQGRG 310
Cdd:COG4230 161 GRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 311 IYEGPGISIKLSALHPRYSRAQRDRVMEELLPRMVGLAALARRYDIGLNIDAEEADRLELSLDLLEALCFDERLRGWNGI 390
Cdd:COG4230 241 GGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 391 GFVIQAYQKRAPFVIDFVIDLARRSKHRLMVRLVKGAYWDSEVKRAQVDGLEGYPVYTRKIHTDVSYLACARKLLSAPEA 470
Cdd:COG4230 321 GGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 471 VFPQFATHNAQTLASIYYMAGENYYPGQYEFQCLHGMGEPLYEEVVgpvsKGRLNRPCRVYAPVGTHETLLAYLVRRLLE 550
Cdd:COG4230 401 AQPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVG----RGKLGRPCRIYAPVGSHEDLLAYLVRRLLE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 551 NGANTSFVNQIGDRDLPIDALVADPVRKARAIQplGAPHERIPLPRDLYRAheDRANSAGLDLSNEHRLGSLAAALLGAA 630
Cdd:COG4230 477 NGANSSFVNRIADEDVPVEELIADPVEKARALG--GAPHPRIPLPRDLYGP--ERRNSAGLDLSDEAVLAALSAALAAAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 631 AQDWRAAP--PGEWRGERARPVPNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEM 708
Cdd:COG4230 553 EKQWQAAPliAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHR 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 709 QSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESFSNDS-HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVL 787
Cdd:COG4230 633 AELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVL 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 788 AKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERldgAGHPVPL 867
Cdd:COG4230 713 AKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR---DGPIVPL 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 868 IAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVI 947
Cdd:COG4230 790 IAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVI 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 948 DAEARAVIERHVQAMQAAGHAVDRYPLDEAqTRHGTFVAPTLIEIADIAELEREVFGPVLHVLRYRRQDLDAVIDAINGR 1027
Cdd:COG4230 870 DAEARANLEAHIERMRAEGRLVHQLPLPEE-CANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINAT 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1028 GYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYLHRLLADAPGTLPVEGVVG 1107
Cdd:COG4230 949 GYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTAAGG 1028
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1108 ------------KGARPLTLPGPTGETNQYHLKPRGTVLCHAASAAGAQAQMEACHRTGNEMLWVDHPEVRAFhaarpag 1175
Cdd:COG4230 1029 nasllalgdwlaSLLGALTLPGPTGERNTLTLRPRGRVLCLADSLEALLAQLAAALATGNRAVVAADLALAGL------- 1101
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1176 aavrwvaPEAVAtADFQAVLYEGDsdgLQALSRAIVGRPGPIVPVLARrvdelsagkTYPLEMLVREvsvcvntaaAGGN 1255
Cdd:COG4230 1102 -------PAVLL-PPFDAVLFEGR---LRALRQALAARDGAIVPVIDA---------GYDLERLLEE---------AGGN 1152
|
....
gi 589266809 1256 ASLM 1259
Cdd:COG4230 1153 ASLM 1156
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
597-1097 |
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: 694.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 597 DLYraHEDRANSAGLDLSNEHRLGSLAAALLGAAAQDWRAAP--PGEWRGE-RARPVPNPADRRDVVGQVIEADEADVRA 673
Cdd:TIGR01238 1 DLY--GEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPiiGHSYKADgEAQPVTNPADRRDIVGQVFHANLAHVQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 674 ALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESFSNDSH 753
Cdd:TIGR01238 79 AIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 754 RPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASP 833
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 834 AVRGVLFTGSTEVARLIAATLAERLDGaghPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQ 913
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 914 EDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGHAVDRYPLDEA-QTRHGTFVAPTLIEI 992
Cdd:TIGR01238 316 EDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSrACQHGTFVAPTLFEL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 993 ADIAELEREVFGPVLHVLRYRRQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFG 1072
Cdd:TIGR01238 396 DDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFG 475
|
490 500
....*....|....*....|....*
gi 589266809 1073 GEGLSGTGPKAGGPLYLHRLLADAP 1097
Cdd:TIGR01238 476 GQGLSGTGPKAGGPHYLYRLTQVQY 500
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
553-1092 |
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: 670.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 553 ANTSFVNQIGDRDLPIDALVADpvrkaraiqpLGAPHEriplprdlyrahedransagldlsnehrlgslaaallgaaaQ 632
Cdd:cd07125 1 ANSSFVNRIFDLEVPLEALADA----------LKAFDE-----------------------------------------K 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 633 DWRAAP--PG-EWRGERARPVPNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQ 709
Cdd:cd07125 30 EWEAIPiiNGeETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 710 SAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESFS-----------NDSH-RPLGPVLCISPWNFPLAIFTGQVA 777
Cdd:cd07125 110 ELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFVCISPWNFPLAIFTGQIA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 778 AALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAER 857
Cdd:cd07125 190 AALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAER 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 858 ldgAGHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPE 937
Cdd:cd07125 270 ---DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPW 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 938 LLSTDIGPVIDAEARAVIERHVQAMQAAGHAVDRYPLDEAQtrhGTFVAPTLIEIADIAELEREVFGPVLHVLRYRRQDL 1017
Cdd:cd07125 347 DLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGN---GYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDL 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589266809 1018 DAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYLHRL 1092
Cdd:cd07125 424 DEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRF 498
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
115-1099 |
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: 634.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 115 QPERVETLARRLVQTLRdKRKGGGVEGLIQEFSLSSQEGVALMCLAEALLRIPDQATRDALIRDKISHgdwrahvgeSRS 194
Cdd:COG0506 9 LRARAVALARRLVEAIR-AAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAK---------SPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 195 LFVNAATWGLLVTgklvsvnseqnlsqaltrLIAKGGEPLIRRGVNMAMRLMGEQFVTGQTISSALANSRKFEDIGFRYS 274
Cdd:COG0506 79 FLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 275 YDMLGEAATTAEDAARYYQSYEQAIHAIGKASqgrgiYEGPGISIKLSALHPRYSRAQRDRVMEELLPRMVGLAALARRY 354
Cdd:COG0506 141 LDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 355 DIGLNIDAEEADRLELSLDLLEALCFDERLRGWNGIGFVIQAYQKRAPFVIDFVIDLARRSKHRLMVRLVKGAYWDSEVK 434
Cdd:COG0506 216 GIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAYWDPEIV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 435 RAQVDGLeGYPVYTRKIHTDVSYLACARKLLSAPEAVFPQFATHNAQTLASIYYMAGE-NYYPGQYEFQCLHGMGEPLYE 513
Cdd:COG0506 296 RAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQMLYGMGEDLQR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 514 EVVGpVSKGRLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNQIGDRDLPIDALVADPVRKARAIQPLGAPHerIP 593
Cdd:COG0506 375 ALAA-VDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPP--PP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 594 LPRDLYRAHEDRANSAGLDLSNEHRLGSLAAALLGAAAQDWRAAPPGEWRGERARPVPNPADRRDVVGQVIEADEADVRA 673
Cdd:COG0506 452 LRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 674 ALGRAEYAAPIWQATPPAERAQ-CLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESF---- 748
Cdd:COG0506 532 AAAAAAAAAAAAAAAAAAAAAAaAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAApppp 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 749 ---SNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETV 825
Cdd:COG0506 612 ppgGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGG 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 826 GAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAGHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCS 905
Cdd:COG0506 692 GAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLL 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 906 ALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGHAVDRYPLDEAQTRHGTFV 985
Cdd:COG0506 772 SLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPL 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 986 APTLIEIADIAELEREVFGPVLHVLRYRRQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGAT 1065
Cdd:COG0506 852 LVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGG 931
|
970 980 990
....*....|....*....|....*....|....
gi 589266809 1066 VGVQPFGGEGLSGTGPKAGGPLYLHRLLADAPGT 1099
Cdd:COG0506 932 GGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAAT 965
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
634-1093 |
7.62e-146 |
|
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: 450.49 E-value: 7.62e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 634 WRAAP-----PGEWRGERARPVpNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEM 708
Cdd:cd07083 16 GRAYPlviggEWVDTKERMVSV-SPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 709 QSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESFS------------NDS-HRPLGPVLCISPWNFPLAIFTGQ 775
Cdd:cd07083 95 RELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpavevvpypgedNESfYVGLGAGVVISPWNFPVAIFTGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 776 VAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLA 855
Cdd:cd07083 175 IVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 856 ERLDGAGHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGR 935
Cdd:cd07083 255 RLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 936 PELLSTDIGPVIDAEARAVIERHVQAMQAAGHAVDRYPLDEAQtrhGTFVAPTLIEIADIAE--LEREVFGPVLHVLRYR 1013
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGE---GYFVAPTVVEEVPPKAriAQEEIFGPVLSVIRYK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1014 RQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYLHRLL 1093
Cdd:cd07083 412 DDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFL 491
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
259-560 |
5.24e-142 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 432.30 E-value: 5.24e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 259 ALANSRKFEDIGFRYSYDMLGEAATTAEDAARYYQSYEQAIHAIGKASQGRGIYEGPGISIKLSALHPRYSRAQRDRVME 338
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 339 ELLPRMVGLAALARRYDIGLNIDAEEADRLELSLDLLEALCFDERLRGWNGIGFVIQAYQKRAPFVIDFVIDLARRSKHR 418
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 419 LMVRLVKGAYWDSEVKRAQVdGLEGYPVYTRKIHTDVSYLACARKLLSAPEAVFPQFATHNAQTLASIYYMAGE-NYYPG 497
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589266809 498 QYEFQCLHGMGEPLYEEVVGpvskgrLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNQ 560
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVA------AGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
640-1089 |
1.23e-126 |
|
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: 400.06 E-value: 1.23e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEW-RGERARPVPNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVRE 718
Cdd:cd07124 39 GKEvRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 719 AGKSFPNAIAEVREAVDFLRYYAVRIEE----------SFSNDSH-RPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVL 787
Cdd:cd07124 119 VGKNWAEADADVAEAIDFLEYYAREMLRlrgfpvemvpGEDNRYVyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 788 AKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAGHPVPL 867
Cdd:cd07124 199 LKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 868 IAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVI 947
Cdd:cd07124 279 IAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 948 DAEARAVIERHVQAMQAAGHAVDRYPLDEAQTRhGTFVAPTLieIADIAELER----EVFGPVLHVLRYRrqDLDAVIDA 1023
Cdd:cd07124 359 DKGARDRIRRYIEIGKSEGRLLLGGEVLELAAE-GYFVQPTI--FADVPPDHRlaqeEIFGPVLAVIKAK--DFDEALEI 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589266809 1024 INGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYL 1089
Cdd:cd07124 434 ANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYL 499
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
640-1085 |
2.32e-126 |
|
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: 397.96 E-value: 2.32e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIV 716
Cdd:COG1012 12 GEWVaaaSGETFDVINPATGE-VLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKSFPNAIAEVREAVDFLRYYA---VRIE-ESFSNDS--------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGN 784
Cdd:COG1012 91 LETGKPLAEARGEVDRAADFLRYYAgeaRRLYgETIPSDApgtrayvrREPLGVVGAITPWNFPLALAAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 785 VVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghp 864
Cdd:COG1012 171 TVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 865 VPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIG 944
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 945 PVIDAEARAVIERHVQAMQAAGH--AVDRYPLDEAQtrhGTFVAPTLIEIAD----IAelEREVFGPVLHVLRYRrqDLD 1018
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAelLTGGRRPDGEG---GYFVEPTVLADVTpdmrIA--REEIFGPVLSVIPFD--DEE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589266809 1019 AVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGAtVGVQPFGGEGLSGTGPKAGG 1085
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGA-VPQAPFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
649-1090 |
3.24e-117 |
|
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: 373.02 E-value: 3.24e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 649 PVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA 728
Cdd:pfam00171 10 EVINPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 EVREAVDFLRYYAVRIE----ESFSNDS-------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALI 797
Cdd:pfam00171 89 EVDRAIDVLRYYAGLARrldgETLPSDPgrlaytrREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 798 AAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNAL 877
Cdd:pfam00171 169 ALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 878 IVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIER 957
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 958 HVQAMQAAGHAVdryPLD-EAQTRHGTFVAPTLieIADIAELER----EVFGPVLHVLRYRrqDLDAVIDAINGRGYGLT 1032
Cdd:pfam00171 323 YVEDAKEEGAKL---LTGgEAGLDNGYFVEPTV--LANVTPDMRiaqeEIFGPVLSVIRFK--DEEEAIEIANDTEYGLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 589266809 1033 FGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVqPFGGEGLSGTGpKAGGPLYLH 1090
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLE 451
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
673-1091 |
2.88e-112 |
|
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: 358.44 E-value: 2.88e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 673 AALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIE----ESF 748
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARrlhgEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 749 SNDS--------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPG 820
Cdd:cd07078 82 PSPDpgelaivrREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 821 RGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSA 900
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 901 GQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGhAVDRYPLDEAQTR 980
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEG-AKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 981 HGTFVAPTLIE-IADIAELER-EVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVN 1058
Cdd:cd07078 315 KGYFVPPTVLTdVDPDMPIAQeEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430
....*....|....*....|....*....|...
gi 589266809 1059 RNIVGATVGvQPFGGEGLSGTGpKAGGPLYLHR 1091
Cdd:cd07078 393 DYSVGAEPS-APFGGVKQSGIG-REGGPYGLEE 423
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
652-1089 |
3.91e-102 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 334.14 E-value: 3.91e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVR 731
Cdd:TIGR01237 52 NPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 732 EAVDFLRYYAVRIEE--------SFSNDSHR----PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAA 799
Cdd:TIGR01237 132 EAIDFMEYYARQMIElakgkpvnSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 800 YGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAGHPVPLIAETGGQNALIV 879
Cdd:TIGR01237 212 KFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 880 DSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHV 959
Cdd:TIGR01237 292 DEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYI 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 960 QAMQAAGHAVDRYPLDEAQtrhGTFVAPTLIEIADIAE--LEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHT 1037
Cdd:TIGR01237 372 EIGKAEGRLVSGGCGDDSK---GYFIGPTIFADVDRKArlAQEEIFGPVVAFIRAS--DFDEALEIANNTEYGLTGGVIS 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 589266809 1038 RLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYL 1089
Cdd:TIGR01237 447 NNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYL 498
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
652-1089 |
4.67e-101 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 331.13 E-value: 4.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVR 731
Cdd:PRK03137 56 NPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 732 EAVDFLRYYA------------VRIEESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAA 799
Cdd:PRK03137 136 EAIDFLEYYArqmlkladgkpvESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 800 YGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAGHPVPLIAETGGQNALIV 879
Cdd:PRK03137 216 KFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 880 DSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPElLSTDIGPVIDAEARAVIERHV 959
Cdd:PRK03137 296 DEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPE-DNAYMGPVINQASFDKIMSYI 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 960 QAMQAAGHAVDRYPLDEAQtrhGTFVAPTLieIADIAELER----EVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGV 1035
Cdd:PRK03137 375 EIGKEEGRLVLGGEGDDSK---GYFIQPTI--FADVDPKARimqeEIFGPVVAFIKAK--DFDHALEIANNTEYGLTGAV 447
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 589266809 1036 HTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYL 1089
Cdd:PRK03137 448 ISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYL 501
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
640-1086 |
1.38e-92 |
|
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: 306.48 E-value: 1.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWRGERAR-PVPNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVRE 718
Cdd:cd07097 7 GEWVAGGDGeENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 719 AGKSFPNAIAEVREAVDFLRYYA---VRIE-ESFSN-------DSHR-PLGPVLCISPWNFPLAIFTGQVAAALAAGNVV 786
Cdd:cd07097 87 EGKTLPEARGEVTRAGQIFRYYAgeaLRLSgETLPStrpgvevETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 787 LAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVP 866
Cdd:cd07097 167 VFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG------AR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 867 LIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPV 946
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 947 IDAEARAVIERHVQAMQA--AGHAVDRYPLDEAQtrHGTFVAPTLIEIAD----IAelEREVFGPVLHVLRYRrqDLDAV 1020
Cdd:cd07097 321 VSERQLEKDLRYIEIARSegAKLVYGGERLKRPD--EGYYLAPALFAGVTndmrIA--REEIFGPVAAVIRVR--DYDEA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589266809 1021 IDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRnivgATVGVQ---PFGGEGLSGTGPKAGGP 1086
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNL----PTAGVDyhvPFGGRKGSSYGPREQGE 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
677-1093 |
3.68e-87 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 287.59 E-value: 3.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 677 RAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESFSNDS---- 752
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELpspd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 753 --------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGET 824
Cdd:cd06534 82 pggeayvrREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 825 VGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRC 904
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 905 SALRVLCVQEDCADRTLAMLRGamnelrvgrpelLSTDIGPvidaearavierhvqamqaaghavdrypldeaqtrhgtf 984
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLVT------------VLVDVDP--------------------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 985 vaptlieiaDIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGA 1064
Cdd:cd06534 265 ---------DMPIAQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV 333
|
410 420
....*....|....*....|....*....
gi 589266809 1065 TVGvQPFGGEGLSGTGpKAGGPLYLHRLL 1093
Cdd:cd06534 334 GPE-APFGGVKNSGIG-REGGPYGLEEYT 360
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
633-1086 |
4.68e-85 |
|
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: 285.78 E-value: 4.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 633 DWRAAPPGEwRGERArpvpNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAI 712
Cdd:cd07131 6 EWVDSASGE-TFDSR----NPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 713 GLIVREAGKSFPNAIAEVREAVDFLRYYA------------VRIEESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAAL 780
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAgegrrlfgetvpSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 781 AAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERldg 860
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 861 aGHPVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLS 940
Cdd:cd07131 238 -NKRVAL--EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 941 TDIGPVIDAEARAVIERHVQAMQAAGHAV--DRYPLDEAQTRHGTFVAPTLIEIA--DIAELEREVFGPVLHVLRYrrQD 1016
Cdd:cd07131 315 TDMGPLINEAQLEKVLNYNEIGKEEGATLllGGERLTGGGYEKGYFVEPTVFTDVtpDMRIAQEEIFGPVVALIEV--SS 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1017 LDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVqPFGGEGLSGTGPKAGGP 1086
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
650-1080 |
1.02e-83 |
|
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: 281.24 E-value: 1.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:cd07103 1 VINPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLRYYA---VRIE----ESFSNDS-----HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALI 797
Cdd:cd07103 80 VDYAASFLEWFAeeaRRIYgrtiPSPAPGKrilviKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 798 AAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAAtlaerlDGAGHPVPLIAETGGQNAL 877
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMA------QAADTVKRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 878 IVDSSALTEQVVYDVLSSAFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIE 956
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCvCANRIY-VHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 957 RHVQAMQAAGHAVdrypL--DEAQTRHGTFVAPTLIEI----ADIAelEREVFGPVLHVLRYRrqDLDAVIDAINGRGYG 1030
Cdd:cd07103 313 ALVEDAVAKGAKV----LtgGKRLGLGGYFYEPTVLTDvtddMLIM--NEETFGPVAPIIPFD--TEDEVIARANDTPYG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 589266809 1031 LTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATvgVQPFGGEGLSGTG 1080
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
640-1084 |
7.60e-79 |
|
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: 268.28 E-value: 7.60e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWRGERARPVP--NPADRRDVVGqVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQsAIG-LIV 716
Cdd:cd07086 5 GEWVGSGGETFTsrNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKE-ALGrLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKSFPNAIAEVREAVDfLRYYAVRIEESFSNDS-------HR------PLGPVLCISPWNFPLAIFTGQVAAALAAG 783
Cdd:cd07086 83 LEMGKILPEGLGEVQEMID-ICDYAVGLSRMLYGLTipserpgHRlmeqwnPLGVVGVITAFNFPVAVPGWNAAIALVCG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 784 NVVLAKPAEQTALIA----AYGVSVLHRAGIPADAVQLLPGRGEtVGAALVASPAVRGVLFTGSTEVARLIAATLAERLd 859
Cdd:cd07086 162 NTVVWKPSETTPLTAiavtKILAEVLEKNGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 860 gaGHPvplIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELL 939
Cdd:cd07086 240 --GRV---LLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 940 STDIGPVIDaearaviERHVQAMQAA--------------GHAVDRYPldeaqtrHGTFVAPTLIEI-ADIAEL-EREVF 1003
Cdd:cd07086 315 GTLVGPLIN-------QAAVEKYLNAieiaksqggtvltgGKRIDGGE-------PGNYVEPTIVTGvTDDARIvQEETF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1004 GPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIER--IHAGNVYVNRNIVGATVGVqPFGGEGLSGTGP 1081
Cdd:cd07086 381 APILYVIKFD--SLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGR 457
|
...
gi 589266809 1082 KAG 1084
Cdd:cd07086 458 ESG 460
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
649-1080 |
9.36e-76 |
|
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: 258.68 E-value: 9.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 649 PVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA 728
Cdd:cd07149 2 EVISPYDGE-VIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 EVREAVDFLRYY---AVRIE-ESFSNDSH------------RPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAE 792
Cdd:cd07149 81 EVDRAIETLRLSaeeAKRLAgETIPFDASpggegrigftirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 793 QTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERldgaghpvPLIAETG 872
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--------KVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 873 GQNALIVDSSALTEQVVYDVLSSAFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEA 951
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 952 RAVIERHVQAMQAAGHAVDRYPldeaqTRHGTFVAPTLIEiaDIAELER----EVFGPVLHVLRYRrqDLDAVIDAINGR 1027
Cdd:cd07149 312 AERIEEWVEEAVEGGARLLTGG-----KRDGAILEPTVLT--DVPPDMKvvceEVFAPVVSLNPFD--TLDEAIAMANDS 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 589266809 1028 GYGLTFGVHTRLDETVRHVIERIHAGNVYVNrNIVGATVGVQPFGGEGLSGTG 1080
Cdd:cd07149 383 PYGLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
641-1059 |
3.11e-74 |
|
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: 254.88 E-value: 3.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 641 EWRGERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAG 720
Cdd:cd07088 8 PSSSGETIDVLNPATG-EVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 721 KSFPNAIAEVREAVDFLRYY---AVRIE-ESFSNDS--------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLA 788
Cdd:cd07088 87 KTLSLARVEVEFTADYIDYMaewARRIEgEIIPSDRpnenififKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 789 KPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLI 868
Cdd:cd07088 167 KPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 869 AETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVID 948
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 949 AEARAVIERHVQAMQAAGHAVdRYPLDEAQTRHGTFVAPTLIEIAD----IAelEREVFGPVLHVLRYRrqDLDAVIDAI 1024
Cdd:cd07088 321 EAALDKVEEMVERAVEAGATL-LTGGKRPEGEKGYFYEPTVLTNVRqdmeIV--QEEIFGPVLPVVKFS--SLDEAIELA 395
|
410 420 430
....*....|....*....|....*....|....*
gi 589266809 1025 NGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNR 1059
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
652-1091 |
4.50e-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: 250.99 E-value: 4.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRDVvGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVR 731
Cdd:cd07099 2 NPATGEVL-GEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 732 EAVDFLRYYAVRIEE-----------SFSNDS----HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTAL 796
Cdd:cd07099 81 LALEAIDWAARNAPRvlaprkvptglLMPNKKatveYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 797 IAAYGVSVLHRAGIPADAVQLLPGRGETvGAALVASPaVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNA 876
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAERL------IPVVLELGGKDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 877 LIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIE 956
Cdd:cd07099 233 MIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 957 RHVQAMQAAGhAVDRYPLDEAQTRhGTFVAPT-LIEIADIAELER-EVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFG 1034
Cdd:cd07099 313 RHVDDAVAKG-AKALTGGARSNGG-GPFYEPTvLTDVPHDMDVMReETFGPVLPVMPVA--DEDEAIALANDSRYGLSAS 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 589266809 1035 VHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGpKAGGPLYLHR 1091
Cdd:cd07099 389 VFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLRE 444
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
641-1080 |
5.35e-73 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 251.72 E-value: 5.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 641 EWRGERArPVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQAT-PPAERAQCLRHAAQLMEDEMQSAIGLIVREA 719
Cdd:cd07082 12 ESSGKTI-EVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 720 GKSFPNAIAEVREAVDFLRYYA---VRIEESFSN-DSHR------------PLGPVLCISPWNFPLAIFTGQVAAALAAG 783
Cdd:cd07082 90 GKTLKDALKEVDRTIDYIRDTIeelKRLDGDSLPgDWFPgtkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 784 NVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATlaerldgagH 863
Cdd:cd07082 170 NTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ---------H 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 864 PV-PLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTD 942
Cdd:cd07082 241 PMkRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 943 IGPVIDAEARAVIERHVQAMQAAGHAVdrypLDEAQTRHGTFVAPTLIEI--ADIAELEREVFGPVLHVLRYRrqDLDAV 1020
Cdd:cd07082 321 ITPLIDPKSADFVEGLIDDAVAKGATV----LNGGGREGGNLIYPTLLDPvtPDMRLAWEEPFGPVLPIIRVN--DIEEA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589266809 1021 IDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVN----RNIvgatvGVQPFGGEGLSGTG 1080
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIG 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
652-1080 |
1.32e-72 |
|
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: 249.79 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA-EV 730
Cdd:cd07093 3 NPATGE-VLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 731 REAVDFLRYYAVRI----EESFSND-------SHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAA 799
Cdd:cd07093 82 PRAAANFRFFADYIlqldGESYPQDggalnyvLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 800 YGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIV 879
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPNIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 880 DSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHV 959
Cdd:cd07093 236 FADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 960 QAMQAAGHAVDR--YPLDEAQTRHGTFVAPTLIE-IADIAEL-EREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGV 1035
Cdd:cd07093 316 ELARAEGATILTggGRPELPDLEGGYFVEPTVITgLDNDSRVaQEEIFGPVVTVIPFD--DEEEAIELANDTPYGLAAYV 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 589266809 1036 HTRLDETVRHVIERIHAGNVYVNRNIV---GAtvgvqPFGGEGLSGTG 1080
Cdd:cd07093 394 WTRDLGRAHRVARRLEAGTVWVNCWLVrdlRT-----PFGGVKASGIG 436
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
650-1080 |
1.16e-71 |
|
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: 247.15 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRRdVVGQVIEADEADVRAALGRAEYAAPI-WQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA 728
Cdd:cd07109 1 VFDPSTGE-VFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 EVREAVDFLRYYAVRIEeSFSNDS------------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTAL 796
Cdd:cd07109 80 DVEAAARYFEYYGGAAD-KLHGETiplgpgyfvytvREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 797 IAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNA 876
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 877 LIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGrPELLSTDIGPVIDAEARAVIE 956
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 957 RHVQ-------AMQAAGHAVdrypldEAQTRHGTFVAPTLIEIADIA-ELER-EVFGPVLHVLRYRrqDLDAVIDAINGR 1027
Cdd:cd07109 312 GFVArarargaRIVAGGRIA------EGAPAGGYFVAPTLLDDVPPDsRLAQeEIFGPVLAVMPFD--DEAEAIALANGT 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 589266809 1028 GYGLTFGVHTRLDETVRHVIERIHAGNVYVNRniVGATVGVQ-PFGGEGLSGTG 1080
Cdd:cd07109 384 DYGLVAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
652-1084 |
1.24e-71 |
|
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: 247.08 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRdVVGQVIEADEADVRAALGRAEYA--APIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:cd07114 3 NPATGE-PWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLRYYA------------VRIEESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALI 797
Cdd:cd07114 82 VRYLAEWYRYYAgladkiegavipVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 798 AAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNAL 877
Cdd:cd07114 162 TLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 878 IVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIER 957
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 958 HVQAMQAAGHAVDR--YPLDEAQTRHGTFVAPTLIEIA--DIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTF 1033
Cdd:cd07114 316 YVARAREEGARVLTggERPSGADLGAGYFFEPTILADVtnDMRIAQEEVFGPVLSVIPFD--DEEEAIALANDSEYGLAA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 589266809 1034 GVHTR-LDETVRhVIERIHAGNVYVN--RNIVGATvgvqPFGGEGLSGTGPKAG 1084
Cdd:cd07114 394 GIWTRdLARAHR-VARAIEAGTVWVNtyRALSPSS----PFGGFKDSGIGRENG 442
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
640-1080 |
1.98e-70 |
|
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: 243.95 E-value: 1.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLME---DEMQSAIg 713
Cdd:cd07138 5 GAWVapaGTETIDVINPATE-EVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEaraDELAQAI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 714 liVREAG--KSF------PNAIAEVREAVDFLRYYAvrIEESFSND--SHRPLGPVLCISPWNFPLAIFTGQVAAALAAG 783
Cdd:cd07138 83 --TLEMGapITLaraaqvGLGIGHLRAAADALKDFE--FEERRGNSlvVREPIGVCGLITPWNWPLNQIVLKVAPALAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 784 NVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgagh 863
Cdd:cd07138 159 CTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 864 PVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSAL-RVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTD 942
Cdd:cd07138 235 RVAL--ELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 943 IGPVIDAEARavieRHVQAMQAAGhavdrypLDEAQT------------RHGTFVAPTLieIADIA---ELER-EVFGPV 1006
Cdd:cd07138 312 LGPLASAAQF----DRVQGYIQKG-------IEEGARlvaggpgrpeglERGYFVKPTV--FADVTpdmTIAReEIFGPV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589266809 1007 LHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNrnivGATVGVQ-PFGGEGLSGTG 1080
Cdd:cd07138 379 LSIIPYD--DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
670-1086 |
3.12e-70 |
|
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: 242.44 E-value: 3.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 670 DVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNA-------IAEVREAVDFLRYYAV 742
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAafevgaaIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 743 RIEES-----FSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTA-----LIAaygvSVLHRAGIPA 812
Cdd:cd07104 81 EILPSdvpgkESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 813 DAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATlaerldgAGHPVPLIA-ETGGQNALIVDSSALTEQVVYD 891
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGEL-------AGRHLKKVAlELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 892 VLSSAFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGHAVd 970
Cdd:cd07104 230 AAFGAFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 971 rypldEAQ-TRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVI 1047
Cdd:cd07104 308 -----LTGgTYEGLFYQPTVLSdvTPDMPIFREEIFGPVAPVIPFD--DDEEAVELANDTEYGLSAAVFTRDLERAMAFA 380
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 589266809 1048 ERIHAGNVYVNrnivGATVG---VQPFGGEGLSGTGpKAGGP 1086
Cdd:cd07104 381 ERLETGMVHIN----DQTVNdepHVPFGGVKASGGG-RFGGP 417
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
649-1080 |
5.26e-70 |
|
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: 242.64 E-value: 5.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 649 PVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA 728
Cdd:cd07145 2 EVRNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 EVREAVDFLR---YYAVRIE------ESFSNDSHR-------PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAE 792
Cdd:cd07145 81 EVERTIRLFKlaaEEAKVLRgetipvDAYEYNERRiaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 793 QTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgaghpvPLIAETG 872
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGK------KVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 873 GQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEAR 952
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 953 AVIERHV-QAMQAAGHAVDRYPLDEaqtrhGTFVAPTLIEIA--DIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGY 1029
Cdd:cd07145 315 ERMENLVnDAVEKGGKILYGGKRDE-----GSFFPPTVLENDtpDMIVMKEEVFGPVLPIAKVK--DDEEAVEIANSTEY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 589266809 1030 GLTFGVHTRLDETVRHVIERIHAGNVYVNR-------NIvgatvgvqPFGGEGLSGTG 1080
Cdd:cd07145 388 GLQASVFTNDINRALKVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG 437
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
641-1091 |
1.43e-69 |
|
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: 243.26 E-value: 1.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 641 EWRGERARPVPNPADRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLME----DEMQSAIGLIv 716
Cdd:cd07123 41 EVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSgkyrYELNAATMLG- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 reAGKSFPNA-IAEVREAVDFLR---YYAVRIEES--FSNDS-------HRPL-GPVLCISPWNFPlAIFTGQVAAALAA 782
Cdd:cd07123 120 --QGKNVWQAeIDAACELIDFLRfnvKYAEELYAQqpLSSPAgvwnrleYRPLeGFVYAVSPFNFT-AIGGNLAGAPALM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 783 GNVVLAKPAEqTALIAAYGV-SVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgA 861
Cdd:cd07123 197 GNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLD-R 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 862 GHPVP-LIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLS 940
Cdd:cd07123 275 YRTYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 941 TDIGPVIDAEARAVIERHVQAMQA-------AGHAVDRypldeaqtRHGTFVAPTLIEIADIAE--LEREVFGPVLHVLR 1011
Cdd:cd07123 355 NFMGAVIDEKAFDRIKGYIDHAKSdpeaeiiAGGKCDD--------SVGYFVEPTVIETTDPKHklMTEEIFGPVLTVYV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1012 YRRQDLDAVIDAIN-GRGYGLTFGVHTRlDetvRHVIE------RIHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAG 1084
Cdd:cd07123 427 YPDSDFEETLELVDtTSPYALTGAIFAQ-D---RKAIReatdalRNAAGNFYINDKPTGAVVGQQPFGGARASGTNDKAG 502
|
....*..
gi 589266809 1085 GPLYLHR 1091
Cdd:cd07123 503 SPLNLLR 509
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
670-1078 |
2.62e-69 |
|
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: 239.48 E-value: 2.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 670 DVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLME---DEMQSAIGlivREAGKSFPNAIAEVREA---VDF-LRYYAV 742
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKankEELARLIS---RETGKPLWEAQTEVAAMagkIDIsIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 743 RI-EESFSND------SHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAV 815
Cdd:cd07095 78 RTgERATPMAqgravlRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 816 QLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAATLaerldgAGHPVPLIA-ETGGQNALIVDSSALTEQVVYDVLS 894
Cdd:cd07095 158 NLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQF------AGRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 895 SAFDSAGQRCSALRVLCVQEDC-ADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAG----HAV 969
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGAvGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGgeplLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 970 DRYPLDeaqtrhGTFVAPTLIEIADIAEL-EREVFGPVLHVLRYrrQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIE 1048
Cdd:cd07095 311 ERLVAG------TAFLSPGIIDVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLA 382
|
410 420 430
....*....|....*....|....*....|
gi 589266809 1049 RIHAGNVYVNRNIVGATvGVQPFGGEGLSG 1078
Cdd:cd07095 383 RIRAGIVNWNRPTTGAS-STAPFGGVGLSG 411
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
650-1080 |
1.24e-68 |
|
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: 238.20 E-value: 1.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:cd07106 1 VINPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLRYYA------VRIEESFSNDS---HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAY 800
Cdd:cd07106 80 VGGAVAWLRYTAsldlpdEVIEDDDTRRVelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 801 GVSVLHRAgIPADAVQLLPGRGEtVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgaghPVPLiaETGGQNALIVD 880
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLK----RVTL--ELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 881 SSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQ 960
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 961 AMQAAGHAVdrYPLDEAQTRHGTFVAPTLieIADIAELER----EVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVH 1036
Cdd:cd07106 312 DAKAKGAKV--LAGGEPLDGPGYFIPPTI--VDDPPEGSRivdeEQFGPVLPVLKYS--DEDEVIARANDSEYGLGASVW 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 589266809 1037 TRLDETVRHVIERIHAGNVYVNRN-IVGATVgvqPFGGEGLSGTG 1080
Cdd:cd07106 386 SSDLERAEAVARRLEAGTVWINTHgALDPDA---PFGGHKQSGIG 427
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
650-1084 |
2.00e-68 |
|
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: 237.64 E-value: 2.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRrDVVGQVIEADEADVRAALgraEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:cd07146 3 VRNPYTG-EVVGTVPAGTEEALREAL---ALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLRYYAVRIE----ESFSND-----------SHR-PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQ 793
Cdd:cd07146 79 VGRAADVLRFAAAEALrddgESFSCDltangkarkifTLRePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 794 TALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERldgaghpvPLIAETGG 873
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 874 QNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARA 953
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 954 VIERHVQAMQAAGHAVdrypLDEAQtRHGTFVAPTLIEIAD-IAEL-EREVFGPVLHVLRYRrqDLDAVIDAINGRGYGL 1031
Cdd:cd07146 311 QIENRVEEAIAQGARV----LLGNQ-RQGALYAPTVLDHVPpDAELvTEETFGPVAPVIRVK--DLDEAIAISNSTAYGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 589266809 1032 TFGVHTRLDETVRHVIERIHAGNVYVNrNIVGATVGVQPFGGEGLSGTGPKAG 1084
Cdd:cd07146 384 SSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
658-1084 |
2.97e-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: 234.51 E-value: 2.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 658 DVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFL 737
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 738 RYYAVRIEE--------------SFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVS 803
Cdd:cd07101 87 RYYARRAERllkprrrrgaipvlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 804 VLHRAGIPADAVQLLPGRGETVGAALVASpaVRGVLFTGSTEVARLIAATLAERLDGAGhpvpliAETGGQNALIVDSSA 883
Cdd:cd07101 167 LLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCS------LELGGKNPMIVLEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 884 LTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQ 963
Cdd:cd07101 239 DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 964 AAGHAV--------DRYPLdeaqtrhgtFVAPT-LIEIADIAELER-EVFGPVLHVlrYRRQDLDAVIDAINGRGYGLTF 1033
Cdd:cd07101 319 AKGATVlaggrarpDLGPY---------FYEPTvLTGVTEDMELFAeETFGPVVSI--YRVADDDEAIELANDTDYGLNA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 589266809 1034 GVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQ-PFGGEGLSGTGPKAG 1084
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
640-1084 |
4.21e-67 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 234.80 E-value: 4.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWRGERAR---PVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPI--WQATPPAERAQCLRHAAQLMEDEMQSAIGL 714
Cdd:cd07091 10 NEFVDSVSGktfPTINPATE-EVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 715 IVREAGKSFP-NAIAEVREAVDFLRYYA----------VRIEESFSNDSHR-PLGPVLCISPWNFPLAIFTGQVAAALAA 782
Cdd:cd07091 89 ESLDNGKPLEeSAKGDVALSIKCLRYYAgwadkiqgktIPIDGNFLAYTRRePIGVCGQIIPWNFPLLMLAWKLAPALAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 783 GNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAER-LDga 861
Cdd:cd07091 169 GNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnLK-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 862 ghPVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLST 941
Cdd:cd07091 247 --KVTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 942 DIGPVIDAEARAVIERHVQAMQAAG----HAVDRYPldeaqtRHGTFVAPTLieIADIAELER----EVFGPVLHVLRYR 1013
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGatllTGGERHG------SKGYFIQPTV--FTDVKDDMKiakeEIFGPVVTILKFK 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 589266809 1014 rqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNR-NIVGATVgvqPFGGEGLSGTGPKAG 1084
Cdd:cd07091 395 --TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
652-1090 |
2.98e-66 |
|
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: 231.45 E-value: 2.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVR 731
Cdd:cd07150 5 NPADG-SVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 732 EAVDFLRY-----YAVRIE-------ESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAA 799
Cdd:cd07150 84 FTPELLRAaagecRRVRGEtlpsdspGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 800 YGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATlaerldGAGHPVPLIAETGGQNALIV 879
Cdd:cd07150 164 KIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEK------AGRHLKKITLELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 880 DSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHV 959
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 960 QAMQAAGHAvdrypLDEAQTRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYrrQDLDAVIDAINGRGYGLTFGVHT 1037
Cdd:cd07150 318 EDAVAKGAK-----LLTGGKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPA--KDAEEALELANDTEYGLSAAILT 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 589266809 1038 RLDETVRHVIERIHAGNVYVNRNIV--GATVgvqPFGGEGLSGTGpKAGGPLYLH 1090
Cdd:cd07150 391 NDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSME 441
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
650-1083 |
5.56e-66 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 231.10 E-value: 5.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPAdRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSF-PNAIA 728
Cdd:cd07108 1 VINPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 EVREAVDFLRYYAVRIEE-----------SFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQtALI 797
Cdd:cd07108 80 EAAVLADLFRYFGGLAGElkgetlpfgpdVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED-APL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 798 AAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNAL 877
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 878 IVDSSALTEQVVYDVLSSA-FDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIE 956
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 957 RHVQ---AMQAAGHAVDRYPLDEAQTRHGTFVAPTLIEIADIA-ELER-EVFGPVLHVLRYRrqDLDAVIDAINGRGYGL 1031
Cdd:cd07108 313 GYIDlglSTSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEwRLAReEIFGPVLCAIPWK--DEDEVIAMANDSHYGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 589266809 1032 TFGVHTR-LDETVRHViERIHAGNVYVNRNiVGATVGvQPFGGEGLSGTGPKA 1083
Cdd:cd07108 391 AAYVWTRdLGRALRAA-HALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
658-1086 |
1.47e-65 |
|
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: 229.10 E-value: 1.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 658 DVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFL 737
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 738 RYYAVRIEES-----------FSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVS-VL 805
Cdd:cd07152 82 HEAAGLPTQPqgeilpsapgrLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIArLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 806 HRAGIPADAVQLLPGRGEtVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgaghPVPLiaETGGQNALIVDSSALT 885
Cdd:cd07152 162 EEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLK----KVSL--ELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 886 EQVVYDVLSSAFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQA 964
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 965 AGHAVdrypldEA-QTRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDE 1041
Cdd:cd07152 314 AGARL------EAgGTYDGLFYRPTVLSgvKPGMPAFDEEIFGPVAPVTVFD--SDEEAVALANDTEYGLSAGIISRDVG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 589266809 1042 TVRHVIERIHAGNVYVNRNIVGATVgVQPFGGEGLSGTGPKAGGP 1086
Cdd:cd07152 386 RAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
640-1080 |
4.92e-65 |
|
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: 228.94 E-value: 4.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIV 716
Cdd:cd07085 7 GEWVeskTTEWLDVYNPATGE-VIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKSFPNAIAEVR---EAVDFlryyAVRIE--------ESFSND-----SHRPLGPVLCISPWNFPLAIFTGQVAAAL 780
Cdd:cd07085 86 LEHGKTLADARGDVLrglEVVEF----ACSIPhllkgeylENVARGidtysYRQPLGVVAGITPFNFPAMIPLWMFPMAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 781 AAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAaLVASPAVRGVLFTGSTEVARLIAATlaerldG 860
Cdd:cd07085 162 ACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYER------A 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 861 AGHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLS 940
Cdd:cd07085 235 AANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 941 TDIGPVIDAEARAVIERHVQAMQAAG---------HAVDRYPldeaqtrHGTFVAPTLIE--IADIAELEREVFGPVLHV 1009
Cdd:cd07085 315 ADMGPVISPAAKERIEGLIESGVEEGaklvldgrgVKVPGYE-------NGNFVGPTILDnvTPDMKIYKEEIFGPVLSI 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589266809 1010 LRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNrniVG--ATVGVQPFGGEGLSGTG 1080
Cdd:cd07085 388 VRVD--TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPipVPLAFFSFGGWKGSFFG 455
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
650-1080 |
7.38e-65 |
|
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: 227.70 E-value: 7.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:cd07094 3 VHNPYDG-EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLR---YYAVRIE-ESFSNDSHR------------PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQ 793
Cdd:cd07094 82 VDRAIDTLRlaaEEAERIRgEEIPLDATQgsdnrlawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 794 TALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLaerldgaghPVPLIA-ETG 872
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA---------GGKRIAlELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 873 GQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEAR 952
Cdd:cd07094 233 GNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 953 AVIERHV-QAMQAAGHAVDrypldeAQTRHGTFVAPTLIEIA--DIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGY 1029
Cdd:cd07094 313 ERVERWVeEAVEAGARLLC------GGERDGALFKPTVLEDVprDTKLSTEETFGPVVPIIRYD--DFEEAIRIANSTDY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 589266809 1030 GLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVgATVGVQPFGGEGLSGTG 1080
Cdd:cd07094 385 GLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
644-1080 |
3.12e-64 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 227.84 E-value: 3.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 644 GERARPVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSF 723
Cdd:PRK09407 30 AGPTREVTAPFTGE-PLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 724 PNAIAEVREAVDFLRYYAVRIEESFSNDSHR--------------PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAK 789
Cdd:PRK09407 109 RHAFEEVLDVALTARYYARRAPKLLAPRRRAgalpvltkttelrqPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 790 PAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVAspAVRGVLFTGSTEVARLIAATLAERLDGAGhpvpliA 869
Cdd:PRK09407 189 PDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAGRRLIGFS------L 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 870 ETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDA 949
Cdd:PRK09407 261 ELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 950 EARAVIERHVQAMQAAGHAV--------DRYPLdeaqtrhgtFVAPT-LIEIADIAELER-EVFGPVLHVlrYRRQDLDA 1019
Cdd:PRK09407 341 AQLETVSAHVDDAVAKGATVlaggkarpDLGPL---------FYEPTvLTGVTPDMELAReETFGPVVSV--YPVADVDE 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 589266809 1020 VIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVQ-PFGGEGLSGTG 1080
Cdd:PRK09407 410 AVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
640-1080 |
5.26e-64 |
|
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: 226.04 E-value: 5.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVPNPADRrDVVGQVIEADEADVRAAL--GRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGL 714
Cdd:cd07119 4 GEWVeaaSGKTRDIINPANG-EVIATVPEGTAEDAKRAIaaARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 715 IVREAGKSFPNAIAEVREAVDFLRYYAVRI-----------EESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAG 783
Cdd:cd07119 83 ETLNTGKTLRESEIDIDDVANCFRYYAGLAtketgevydvpPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 784 NVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAGh 863
Cdd:cd07119 163 NTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 864 pvpliAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDI 943
Cdd:cd07119 242 -----LELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 944 GPVIDAEARAVIERHVQAMQAAGhAVDRY---PLDEAQTRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYRRQDlD 1018
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEG-ARLVCggkRPTGDELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERFDTEE-E 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 589266809 1019 AVIDAiNGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRniVGATVGVQPFGGEGLSGTG 1080
Cdd:cd07119 395 AIRLA-NDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
139-250 |
6.46e-64 |
|
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: 211.98 E-value: 6.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 139 VEGLIQEFSLSSQEGVALMCLAEALLRIPDQATRDALIRDKISHGDWRAHVGESRSLFVNAATWGLLVTGKLVSVNSEQN 218
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 589266809 219 LSQALTRLIAKGGEPLIRRGVNMAMRLMGEQF 250
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
652-1084 |
7.27e-64 |
|
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: 224.63 E-value: 7.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNA-IAEV 730
Cdd:cd07115 3 NPATG-ELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 731 REAVDFLRYYA----------VRIEESFSNDSHR-PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAA 799
Cdd:cd07115 82 PRAADTFRYYAgwadkiegevIPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 800 YGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgaghPVPLiaETGGQNALIV 879
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLK----RVSL--ELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 880 DSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHV 959
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 960 QAMQAAGHAVdrYPLDEAQTRHGTFVAPTLIEIAD----IAelEREVFGPVLHVLRYRRQDlDAVIDAiNGRGYGLTFGV 1035
Cdd:cd07115 316 DVGREEGARL--LTGGKRPGARGFFVEPTIFAAVPpemrIA--QEEIFGPVVSVMRFRDEE-EALRIA-NGTEYGLAAGV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 589266809 1036 HTRLDETVRHVIERIHAGNVYVnrNIVGATVGVQPFGGEGLSGTGPKAG 1084
Cdd:cd07115 390 WTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
640-1093 |
1.96e-63 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 224.95 E-value: 1.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEW---RGERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIV 716
Cdd:PLN02278 31 GKWtdaYDGKTFPVYNPATG-EVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKSFPNAIAEVREAVDFLRYYA---VR-----IEESFSNDS----HRPLGPVLCISPWNFPLAIFTGQVAAALAAGN 784
Cdd:PLN02278 110 LEQGKPLKEAIGEVAYGASFLEYFAeeaKRvygdiIPSPFPDRRllvlKQPVGVVGAITPWNFPLAMITRKVGPALAAGC 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 785 VVLAKPAEQTALIA-AYGVSVLhRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAAtlaerldGAGH 863
Cdd:PLN02278 190 TVVVKPSELTPLTAlAAAELAL-QAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMA-------GAAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 864 PVPLIA-ETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLST 941
Cdd:PLN02278 262 TVKRVSlELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 942 DIGPVIDAEARAVIERHVQAMQAAGHAVdrypL--DEAQTRHGTFVAPTLIEIADIAEL--EREVFGPVLHVLRYrRQDL 1017
Cdd:PLN02278 341 TQGPLINEAAVQKVESHVQDAVSKGAKV----LlgGKRHSLGGTFYEPTVLGDVTEDMLifREEVFGPVAPLTRF-KTEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589266809 1018 DAVIDAiNGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGvqPFGGEGLSGTGpKAGGPLYLHRLL 1093
Cdd:PLN02278 416 EAIAIA-NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKYGIDEYL 487
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
640-1078 |
1.38e-62 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 222.14 E-value: 1.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVpNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQ-CLRHAAQLME--DEMQSAIG 713
Cdd:PRK09457 7 GDWIagqGEAFESR-NPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAiVERFAALLEEnkEELAEVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 714 livREAGKSFPNAIAEVREAVD----FLRYYAVRIEESfSND--------SHRPLGPVLCISPWNFPLAIFTGQVAAALA 781
Cdd:PRK09457 85 ---RETGKPLWEAATEVTAMINkiaiSIQAYHERTGEK-RSEmadgaavlRHRPHGVVAVFGPYNFPGHLPNGHIVPALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 782 AGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAATLaerldgA 861
Cdd:PRK09457 161 AGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQF------A 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 862 GHPVPLIA-ETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDC-ADRTLAMLRGAMNELRVGRPELL 939
Cdd:PRK09457 234 GQPEKILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 940 STD-IGPVIDAEARAVIERHVQAMQAAGhAVDRYPLDEAQTRHGtFVAPTLIEIADIAEL-EREVFGPVLHVLRYrrQDL 1017
Cdd:PRK09457 314 PQPfMGAVISEQAAQGLVAAQAQLLALG-GKSLLEMTQLQAGTG-LLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDF 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589266809 1018 DAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATvGVQPFGGEGLSG 1078
Cdd:PRK09457 390 DEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGAS-SAAPFGGVGASG 449
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
650-1080 |
4.21e-62 |
|
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: 219.81 E-value: 4.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIW-QATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA 728
Cdd:cd07089 1 VINPATE-EVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 -EVREAVDFLRYYAVRI-----EESFSNDS-----------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPA 791
Cdd:cd07089 80 mQVDGPIGHLRYFADLAdsfpwEFDLPVPAlrggpgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 792 EQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgagHPVPLiaET 871
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 872 GGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEA 951
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 952 RAVIERHVQAMQAAG----HAVDRyPLDEAQtrhGTFVAPTLIEIAD----IAelEREVFGPVLHVLRYRrqDLDAVIDA 1023
Cdd:cd07089 314 RDRVEGYIARGRDEGarlvTGGGR-PAGLDK---GFYVEPTLFADVDndmrIA--QEEIFGPVLVVIPYD--DDDEAVRI 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 589266809 1024 INGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRnivGATVGVQ-PFGGEGLSGTG 1080
Cdd:cd07089 386 ANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGING---GGGYGPDaPFGGYKQSGLG 440
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
671-1080 |
8.75e-62 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 217.71 E-value: 8.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 671 VRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIE----- 745
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEaflad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 746 ---ESFSNDS---HRPLGPVLCISPWNFPLAiftgQV----AAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAV 815
Cdd:cd07100 81 epiETDAGKAyvrYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 816 QLLPGRGETVgAALVASPAVRGVLFTGSTEVARLIAATLAERLDgaghPVPLiaETGGQNALIVDSSALTEQVVYDVLSS 895
Cdd:cd07100 157 QNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLK----KSVL--ELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 896 AFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGhAVDRYPl 974
Cdd:cd07100 230 RLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAG-ATLLLG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 975 DEAQTRHGTFVAPTLIEiaDIAE----LEREVFGPVLHVlrYRRQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERI 1050
Cdd:cd07100 307 GKRPDGPGAFYPPTVLT--DVTPgmpaYDEELFGPVAAV--IKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL 382
|
410 420 430
....*....|....*....|....*....|
gi 589266809 1051 HAGNVYVNRnIVGATVGVqPFGGEGLSGTG 1080
Cdd:cd07100 383 EAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
640-1093 |
4.12e-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: 4.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIV 716
Cdd:cd07111 28 GKWVkpeNRKSFPTINPATG-EVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLES 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKsfpnAIAEVRE-----AVDFLRYYAV---RIEESFSNdsHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLA 788
Cdd:cd07111 107 LDNGK----PIRESRDcdiplVARHFYHHAGwaqLLDTELAG--WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 789 KPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAATLAerldGAGHPVPLi 868
Cdd:cd07111 181 KPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA----GTGKKLSL- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 869 aETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVID 948
Cdd:cd07111 255 -ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 949 AEARAVIERHVQAMQAAGhaVDRYPLDEAQTRHGTFVAPTLIEiaDIAELER----EVFGPVLHVLRYRRQDlDAVIDAi 1024
Cdd:cd07111 334 PAQLKRIRELVEEGRAEG--ADVFQPGADLPSKGPFYPPTLFT--NVPPASRiaqeEIFGPVLVVLTFRTAK-EAVALA- 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1025 NGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVN-RNIVGATVgvqPFGGEGLSGTGpKAGGPLYLHRLL 1093
Cdd:cd07111 408 NNTPYGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEYL 473
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
652-1080 |
3.70e-60 |
|
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: 214.39 E-value: 3.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRdVVGQVIEADEADVRAAL--GRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA- 728
Cdd:cd07112 8 NPATGR-VLAEVAACDAADVDRAVaaARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 EVREAVDFLRYYAVRI-----------EESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALI 797
Cdd:cd07112 87 DVPSAANTFRWYAEAIdkvygevaptgPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 798 AAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIaatLAERLDGAGHPVPLiaETGGQNAL 877
Cdd:cd07112 167 ALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRF---LEYSGQSNLKRVWL--ECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 878 IV-DSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIE 956
Cdd:cd07112 242 IVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 957 RHVQAMQAAGHAVDRYPLDEAQTRHGTFVAPTLIE-IADIAELER-EVFGPVLHVLRYRRQDlDAVIDAiNGRGYGLTFG 1034
Cdd:cd07112 322 GYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDgVTPDMRIAReEIFGPVLSVITFDSEE-EAVALA-NDSVYGLAAS 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 589266809 1035 VHTRLDETVRHVIERIHAGNVYVNR-NIVGATVgvqPFGGEGLSGTG 1080
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCfDEGDITT---PFGGFKQSGNG 443
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
658-1084 |
3.03e-59 |
|
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: 211.43 E-value: 3.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 658 DVVGQVIEADEADVRAALGRAEYA--APIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVD 735
Cdd:cd07118 8 VVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 736 FLRYYAVRIE----ESFSN--------DSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVS 803
Cdd:cd07118 88 LWRYAASLARtlhgDSYNNlgddmlglVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 804 VLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAGhpvpliAETGGQNALIVDSSA 883
Cdd:cd07118 168 LLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 884 LTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQ 963
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 964 AAGHAVdRYPLDEAQTRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYrrQDLDAVIDAINGRGYGLTFGVHTRLDE 1041
Cdd:cd07118 322 AEGATL-LLGGERLASAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 589266809 1042 TVRHVIERIHAGNVYVNRNIVGatvGVQ-PFGGEGLSGTGPKAG 1084
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDG---SPElPFGGFKQSGIGRELG 439
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
650-1080 |
1.19e-58 |
|
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: 209.54 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:cd07107 1 VINPATGQ-VLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLRYYAVRIEE-----------SFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALiA 798
Cdd:cd07107 80 VMVAAALLDYFAGLVTElkgetipvggrNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL-S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 799 AYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgaghpvPLIAETGGQNALI 878
Cdd:cd07107 159 ALRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 879 VDSSALTEQVVYD-VLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIER 957
Cdd:cd07107 233 VFPDADPEAAADAaVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 958 HVQAMQAAGHAV---DRYPLDEAqTRHGTFVAPTLieIADIA---ELER-EVFGPVLHVLRYRrqDLDAVIDAINGRGYG 1030
Cdd:cd07107 313 YIDSAKREGARLvtgGGRPEGPA-LEGGFYVEPTV--FADVTpgmRIAReEIFGPVLSVLRWR--DEAEMVAQANGVEYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 589266809 1031 LTFGVHTRLDETVRHVIERIHAGNVYVN---RNIVGAtvgvqPFGGEGLSGTG 1080
Cdd:cd07107 388 LTAAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
640-1080 |
1.86e-58 |
|
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: 209.47 E-value: 1.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIV 716
Cdd:cd07151 1 GEWRdgtSERTIDVLNPYTG-ETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKSFPNAIAEV-------REAVDFLRYYAVRIEES-FSNDSHR----PLGPVLCISPWNFPLAIFTGQVAAALAAGN 784
Cdd:cd07151 80 RESGSTRIKANIEWgaamaitREAATFPLRMEGRILPSdVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 785 VVLAKPAEQTA-----LIAaygvSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATlaerld 859
Cdd:cd07151 160 AVVLKPASDTPitgglLLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGEL------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 860 gAGHPVPLIA-ETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPEL 938
Cdd:cd07151 230 -AGRHLKKVAlELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 939 LSTDIGPVIDAEARAVIERHVQAMQAAGHAVdrypLDEAQtRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYRrqD 1016
Cdd:cd07151 309 PDTVVGPLINESQVDGLLDKIEQAVEEGATL----LVGGE-AEGNVLEPTVLSdvTNDMEIAREEIFGPVAPIIKAD--D 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589266809 1017 LDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGVqPFGGEGLSGTG 1080
Cdd:cd07151 382 EEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
640-1086 |
3.46e-58 |
|
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: 208.58 E-value: 3.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVPNPADRRdVVGQVIEADEADVRAAL--GRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGL 714
Cdd:cd07139 5 GRWVapsGSETIDVVSPATEE-VVGRVPEATPADVDAAVaaARRAFDNGPWPRLSPAERAAVLRRLADALEARADELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 715 IVREAGKsfPNAIAEVRE---AVDFLRYYAvRIEESFSNDSHR-------------PLGPVLCISPWNFPLAIFTGQVAA 778
Cdd:cd07139 84 WTAENGM--PISWSRRAQgpgPAALLRYYA-ALARDFPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 779 ALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGrGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERL 858
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 859 dgagHPVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSAL-RVLcVQEDCADRTLAMLRGAMNELRVGRPE 937
Cdd:cd07139 240 ----ARVTL--ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVEALAAAVAALKVGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 938 LLSTDIGPVIDAEARAVIERHVQAMQAAGHAVDRYPLDEAQTRHGTFVAPTLIEIAD----IAelEREVFGPVLHVLRYR 1013
Cdd:cd07139 313 DPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDndmrIA--QEEIFGPVLSVIPYD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589266809 1014 RQDlDAVidAI-NGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNrnivGATVGVQ-PFGGEGLSGTGpKAGGP 1086
Cdd:cd07139 391 DED-DAV--RIaNDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGP 457
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
640-1080 |
2.34e-57 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 206.30 E-value: 2.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR--GERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVR 717
Cdd:PRK13473 9 GELVagEGEKQPVYNPATG-EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 718 EAGKSFPNAIA-EVREAVDFLRYYA--VRIEESFS--------NDSHR--PLGPVLCISPWNFPLAIFTGQVAAALAAGN 784
Cdd:PRK13473 88 NCGKPLHLALNdEIPAIVDVFRFFAgaARCLEGKAageyleghTSMIRrdPVGVVASIAPWNYPLMMAAWKLAPALAAGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 785 VVLAKPAEQTALIAAYGVSVLHRAgIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAerldGAGHP 864
Cdd:PRK13473 168 TVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA----DSVKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 865 VPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIG 944
Cdd:PRK13473 243 THL--ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 945 PVIDAEARAVIERHVQAMQAAGHAvDRYPLDEAQTRHGTFVAPTLieIADIAE----LEREVFGPVLHVLRYRrqDLDAV 1020
Cdd:PRK13473 321 PLISAAHRDRVAGFVERAKALGHI-RVVTGGEAPDGKGYYYEPTL--LAGARQddeiVQREVFGPVVSVTPFD--DEDQA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1021 IDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVgaTVGVQPFGGEGLSGTG 1080
Cdd:PRK13473 396 VRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
652-1080 |
2.77e-57 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 205.66 E-value: 2.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRrDVVGQVIEADEADVRAALGRAEYA--APIWqATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:cd07120 3 DPATG-EVIGTYADGGVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLRYYAV-------RIEE----SFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIA 798
Cdd:cd07120 81 ISGAISELRYYAGlarteagRMIEpepgSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 799 AYGVSVLHRA-GIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAGhpvpliAETGGQNAL 877
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 878 IVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIER 957
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 958 HV-QAMQAAGHAVDR-YPLDEAQTRhGTFVAPTLIEIADIAE--LEREVFGPVLHVLRYRRQDlDAVIDAiNGRGYGLTF 1033
Cdd:cd07120 315 MVeRAIAAGAEVVLRgGPVTEGLAK-GAFLRPTLLEVDDPDAdiVQEEIFGPVLTLETFDDEA-EAVALA-NDTDYGLAA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 589266809 1034 GVHTR-LDETVRhVIERIHAGNVYVN---RNIVGATvgvqpFGGEGLSGTG 1080
Cdd:cd07120 392 SVWTRdLARAMR-VARAIRAGTVWINdwnKLFAEAE-----EGGYRQSGLG 436
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
658-1080 |
3.37e-57 |
|
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: 205.25 E-value: 3.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 658 DVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA-EVREAVDF 736
Cdd:cd07092 8 EEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdELPGAVDN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 737 LRYYA--VRIEESFSNDSH----------RPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSV 804
Cdd:cd07092 88 FRFFAgaARTLEGPAAGEYlpghtsmirrEPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 805 LHRaGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAghpvplIAETGGQNALIVDSSAL 884
Cdd:cd07092 168 AAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRV------HLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 885 TEQVVYDVLSSAFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQamQ 963
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE--R 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 964 AAGHAvdrypldEAQT------RHGTFVAPTLI-EIADIAEL-EREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGV 1035
Cdd:cd07092 318 APAHA-------RVLTggrraeGPGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 589266809 1036 HTRLDETVRHVIERIHAGNVYVNRNIVGATvgVQPFGGEGLSGTG 1080
Cdd:cd07092 389 WTRDVGRAMRLSARLDFGTVWVNTHIPLAA--EMPHGGFKQSGYG 431
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
640-1078 |
4.01e-57 |
|
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: 206.10 E-value: 4.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GErARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIV 716
Cdd:TIGR03240 5 GKWRagqGE-SFASRNPATQ-EVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKSFPNAIAEVREAVD----FLRYYAVRIEESfSND--------SHRPLGPVLCISPWNFPLAIFTGQVAAALAAGN 784
Cdd:TIGR03240 83 RETGKPLWETRTEVASMIGkvaiSIKAYHERTGES-ENPmpdgravlRHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 785 VVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgaghp 864
Cdd:TIGR03240 162 TVVFKPSELTPWVAEETVKLWEKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFGGRPE----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 865 VPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDC-ADRTLAMLRGAMNELRVGR----PELL 939
Cdd:TIGR03240 236 KILALEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRLLVPDGAqGDAFLARLVEVAERLTVGAwdaePQPF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 940 stdIGPVIDAEARaviERHVQAMQAAGHAVDRYPLDEAQTRHGT-FVAPTLIEIADIAEL-EREVFGPVLHVLRYRrqDL 1017
Cdd:TIGR03240 316 ---MGAVISLRAA---QRLLAAQAKLLALGGKSLLEMRQLDPGAaFLTPGIIDVTGVAELpDEEHFGPLLQVIRYT--DF 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589266809 1018 DAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATvGVQPFGGEGLSG 1078
Cdd:TIGR03240 388 DEAIAIANNTRFGLSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGAS-SAAPFGGIGASG 447
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
652-1080 |
5.98e-57 |
|
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: 204.85 E-value: 5.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEdEMQSAIGLI-VREAGKSFPNAIAEV 730
Cdd:cd07090 3 EPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLR-ERNDEIARLeTIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 731 REAVDFLRYYAVRI-----------EESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAA 799
Cdd:cd07090 81 DSSADCLEYYAGLAptlsgehvplpGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 800 YGVSVLHRAGIPADAVQLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgagHPVPLiaETGGQNALIV 879
Cdd:cd07090 161 LLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 880 DSSALTEQVVYDVLSSAFDSAGQRCS-ALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERH 958
Cdd:cd07090 234 FDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 959 VQAMQAAGHAV----DRYPLDEAQTRhGTFVAPTLI-EIADIAELER-EVFGPVLHVLRYrrQDLDAVIDAINGRGYGLT 1032
Cdd:cd07090 313 IESAKQEGAKVlcggERVVPEDGLEN-GFYVSPCVLtDCTDDMTIVReEIFGPVMSILPF--DTEEEVIRRANDTTYGLA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 589266809 1033 FGVHTRLDETVRHVIERIHAGNVYVNR-NIVGATVgvqPFGGEGLSGTG 1080
Cdd:cd07090 390 AGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
650-1084 |
6.82e-57 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 205.46 E-value: 6.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRRdVVGQVIEADEADVRAAL--GRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAI 727
Cdd:cd07143 26 VYNPSTGK-LITKIAEATEADVDIAVevAHAAFETDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 728 A-EVREAVDFLRYYA--------VRIE---ESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTA 795
Cdd:cd07143 105 RvDVQASADTFRYYGgwadkihgQVIEtdiKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 796 LIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAErldgaGHPVPLIAETGGQN 875
Cdd:cd07143 185 LSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK-----SNLKKVTLELGGKS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 876 ALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVI 955
Cdd:cd07143 260 PNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 956 ERHVQAMQAAGHAVdryplDEAQTRHGT---FVAPTLIE--IADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYG 1030
Cdd:cd07143 340 MSYIESGKAEGATV-----ETGGKRHGNegyFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKFK--TEEEAIKRANDSTYG 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 589266809 1031 LTFGVHTRLDETVRHVIERIHAGNVYVN-RNIVGATVgvqPFGGEGLSGTGPKAG 1084
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 ... |
650-1080 |
8.59e-57 |
|
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: 204.12 E-value: 8.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:cd07110 1 VINPATEA-TIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLRYYAVRIE--------------ESFSNDSHR-PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQT 794
Cdd:cd07110 80 VDDVAGCFEYYADLAEqldakaeravplpsEDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 795 ALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgagHPVPLiaETGGQ 874
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDI----KPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 875 NALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAV 954
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 955 IERHVQAMQAAGHAVDRYPLDEAQTRHGTFVAPTLieIADIAELER----EVFGPVLHVLRYRRQdlDAVIDAINGRGYG 1030
Cdd:cd07110 314 VLSFIARGKEEGARLLCGGRRPAHLEKGYFIAPTV--FADVPTDSRiwreEIFGPVLCVRSFATE--DEAIALANDSEYG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 589266809 1031 LTFGVHTRLDETVRHVIERIHAGNVYVnrNIVGATVGVQPFGGEGLSGTG 1080
Cdd:cd07110 390 LAAAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
649-1084 |
9.89e-57 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 204.89 E-value: 9.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 649 PVPNPADRrDVVGQVIEADEADVRAALGRAEYA----APiWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSF- 723
Cdd:cd07141 25 PTINPATG-EKICEVQEGDKADVDKAVKAARAAfklgSP-WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFs 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 724 PNAIAEVREAVDFLRYYAV---RIE--------ESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAE 792
Cdd:cd07141 103 KSYLVDLPGAIKVLRYYAGwadKIHgktipmdgDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 793 QTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIaatlaerLDGAGHP----VPLi 868
Cdd:cd07141 183 QTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI-------QQAAGKSnlkrVTL- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 869 aETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVID 948
Cdd:cd07141 255 -ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 949 AEARAVIERHVQAMQAAGHAvdrypLDEAQTRHGT---FVAPTLieIADIAELER----EVFGPVLHVLRYRrqDLDAVI 1021
Cdd:cd07141 334 EEQFKKILELIESGKKEGAK-----LECGGKRHGDkgyFIQPTV--FSDVTDDMRiakeEIFGPVQQIFKFK--TIDEVI 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589266809 1022 DAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNR-NIVGATVgvqPFGGEGLSGTGPKAG 1084
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCyNVVSPQA---PFGGYKMSGNGRELG 465
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
670-1080 |
2.41e-56 |
|
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: 202.04 E-value: 2.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 670 DVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAVRI----E 745
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLItqiiG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 746 ESFSNDSH--------RPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQL 817
Cdd:cd07105 81 GSIPSDKPgtlamvvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 818 L---PGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIVDSSALTEQVVYDVLS 894
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHL------KPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 895 SAFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGrpellSTDIGPVIDAEARAVIERHVQAMQAAGhAVDRYP 973
Cdd:cd07105 235 GAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKG-AKLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 974 LDEAQTRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIH 1051
Cdd:cd07105 308 GLADESPSGTSMPPTILDnvTPDMDIYSEESFGPVVSIIRVK--DEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIE 385
|
410 420 430
....*....|....*....|....*....|..
gi 589266809 1052 AGNVYVNrnivGATVGVQ---PFGGEGLSGTG 1080
Cdd:cd07105 386 SGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
652-1059 |
2.92e-56 |
|
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: 202.48 E-value: 2.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVR 731
Cdd:cd07102 2 SPIDGS-VIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 732 EAVDFLRYYAVRIEESFSND------------SHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAA 799
Cdd:cd07102 81 GMLERARYMISIAEEALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 800 YGVSVLHRAGIPADAVQLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIV 879
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRF------IKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 880 DSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHV 959
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 960 QAMQAAG--HAVD--RYPLDEAqtrHGTFVAPT-LIEIADIAELER-EVFGPVLHVlrYRRQDLDAVIDAINGRGYGLTF 1033
Cdd:cd07102 314 ADAIAKGarALIDgaLFPEDKA---GGAYLAPTvLTNVDHSMRVMReETFGPVVGI--MKVKSDAEAIALMNDSEYGLTA 388
|
410 420
....*....|....*....|....*.
gi 589266809 1034 GVHTRLDETVRHVIERIHAGNVYVNR 1059
Cdd:cd07102 389 SVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
640-1085 |
3.28e-56 |
|
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: 203.21 E-value: 3.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWRGERAR-PVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVRE 718
Cdd:cd07130 5 GEWGGGGGVvTSISPANGE-PIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 719 AGKSFPNAIAEVREAVDFLRYyAVRIEESFSND-------SHR------PLGPVLCISPWNFPLAIFTGQVAAALAAGNV 785
Cdd:cd07130 84 MGKILPEGLGEVQEMIDICDF-AVGLSRQLYGLtipserpGHRmmeqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 786 VLAKPAEQTAL--IAAYGV--SVLHRAGIPADAVQLLPGRGEtVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGA 861
Cdd:cd07130 163 VVWKPSPTTPLtaIAVTKIvaRVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 862 ghpvplIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLST 941
Cdd:cd07130 242 ------LLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 942 DIGPVIDAEAravierhVQAMQAAghavdrypLDEAQ-------------TRHGTFVAPTLIEI-ADIAELEREVFGPVL 1007
Cdd:cd07130 316 LVGPLHTKAA-------VDNYLAA--------IEEAKsqggtvlfggkviDGPGNYVEPTIVEGlSDAPIVKEETFAPIL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1008 HVLRYRrqDLDAVIDAINGRGYGLTFGVHTRldeTVRHVIERIHA-----GNVYVNRNIVGATVGvQPFGGEGLSGTGPK 1082
Cdd:cd07130 381 YVLKFD--TLEEAIAWNNEVPQGLSSSIFTT---DLRNAFRWLGPkgsdcGIVNVNIGTSGAEIG-GAFGGEKETGGGRE 454
|
...
gi 589266809 1083 AGG 1085
Cdd:cd07130 455 SGS 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
658-1084 |
8.53e-55 |
|
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: 198.87 E-value: 8.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 658 DVVGQVIEADEADVRAALGRAEYA---APiWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNA-IAEVREA 733
Cdd:cd07142 30 EVIAHVAEGDAEDVDRAVKAARKAfdeGP-WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 734 VDFLRYYAVRIEES-----------FSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGV 802
Cdd:cd07142 109 ARLFRYYAGWADKIhgmtlpadgphHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 803 SVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAErldGAGHPVPLiaETGGQNALIVDSS 882
Cdd:cd07142 189 KLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAK---SNLKPVTL--ELGGKSPFIVCED 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 883 ALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAM 962
Cdd:cd07142 264 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 963 QAAGHAvdrypLDEAQTRHGT---FVAPTLI-EIADIAELER-EVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHT 1037
Cdd:cd07142 344 KEEGAT-----LITGGDRIGSkgyYIQPTIFsDVKDDMKIARdEIFGPVQSILKFK--TVDEVIKRANNSKYGLAAGVFS 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 589266809 1038 RLDETVRHVIERIHAGNVYVN-RNIVGATVgvqPFGGEGLSGTGPKAG 1084
Cdd:cd07142 417 KNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
649-1084 |
4.04e-54 |
|
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: 197.24 E-value: 4.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 649 PVPNPADRrDVVGQVIEADEADVRAALGRAEYA-APIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSF-PNA 726
Cdd:cd07144 26 KTVNPSTG-EVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 727 IAEVREAVDFLRYYAVRIE----ESFSNDS-------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTA 795
Cdd:cd07144 105 LGDLDEIIAVIRYYAGWADkiqgKTIPTSPnklaytlHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 796 LIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGaghpVPLiaETGGQN 875
Cdd:cd07144 185 LSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA----VTL--ECGGKS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 876 ALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNE-LRVGRPELLSTDIGPVIDAEARAV 954
Cdd:cd07144 259 PALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKTQYDR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 955 IERHVQAMQAAGHAVDR----YPLDEAQtrhGTFVAPTLieIADIAE----LEREVFGPVLHVLRYRrqDLDAVIDAING 1026
Cdd:cd07144 339 VLSYIEKGKKEGAKLVYggekAPEGLGK---GYFIPPTI--FTDVPQdmriVKEEIFGPVVVISKFK--TYEEAIKKAND 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 589266809 1027 RGYGLTFGVHTRlDETVRH-VIERIHAGNVYVNRNIVGaTVGVqPFGGEGLSGTGPKAG 1084
Cdd:cd07144 412 TTYGLAAAVFTK-DIRRAHrVARELEAGMVWINSSNDS-DVGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
640-1080 |
6.08e-54 |
|
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: 196.80 E-value: 6.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWR---GERARPVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMED--EMQSAI-- 712
Cdd:cd07559 7 GEWVapsKGEYFDNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEEnlELLAVAet 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 713 ---GLIVREAgksfpnAIAEVREAVDFLRYYA--VRIEESFSND---------SHRPLGPVLCISPWNFPLAIFTGQVAA 778
Cdd:cd07559 86 ldnGKPIRET------LAADIPLAIDHFRYFAgvIRAQEGSLSEidedtlsyhFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 779 ALAAGNVVLAKPAEQTALiaaygvSVLHRAGI-----PADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAAT 853
Cdd:cd07559 160 ALAAGNTVVLKPASQTPL------SILVLMELigdllPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 854 LAERLdgaghpVPLIAETGGQNALIVDSSALTEQVVYD------VLSSAFDSaGQRCSALRVLCVQEDCADRTLAMLRGA 927
Cdd:cd07559 234 AAENL------IPVTLELGGKSPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 928 MNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGHAV----DRYPLDEAQTrhGTFVAPTLIEIAD----IAelE 999
Cdd:cd07559 307 FEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVltggERLTLGGLDK--GYFYEPTLIKGGNndmrIF--Q 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 1000 REVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRlDETVRHVIER-IHAGNVYVN-RNIVGATVgvqPFGGEGLS 1077
Cdd:cd07559 383 EEIFGPVLAVITFK--DEEEAIAIANDTEYGLGGGVWTR-DINRALRVARgIQTGRVWVNcYHQYPAHA---PFGGYKKS 456
|
...
gi 589266809 1078 GTG 1080
Cdd:cd07559 457 GIG 459
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
639-1080 |
7.37e-53 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 193.43 E-value: 7.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 639 PGEWRGERARPVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQA-TPPAERAQCLRHAAQLMEDEMQSAIGLIVR 717
Cdd:cd07113 8 PVAGQSEKRLDITNPATEQ-VIASVASATEADVDAAVASAWRAFVSAWAkTTPAERGRILLRLADLIEQHGEELAQLETL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 718 EAGKSFPNAIA-EVREAVDFLRYYA----------------VRIEESFSNDSHR-PLGPVLCISPWNFPLAIFTGQVAAA 779
Cdd:cd07113 87 CSGKSIHLSRAfEVGQSANFLRYFAgwatkingetlapsipSMQGERYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 780 LAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGEtVGAALVASPAVRGVLFTGSTEVARLIAATlaerld 859
Cdd:cd07113 167 LATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 860 GAGHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELL 939
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 940 STDIGPVIDAEARAVIERHVQAMQAAGHAVDRYplDEAQTRHGTFVAPTLIEI--ADIAELEREVFGPVLHVLRYrrQDL 1017
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRG--GEALAGEGYFVQPTLVLArsADSRLMREETFGPVVSFVPY--EDE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589266809 1018 DAVIDAINGRGYGLTFGVHTR-LDETVRHvIERIHAGNVYVN-RNIVGATVgvqPFGGEGLSGTG 1080
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNnLSKALRY-IPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
633-1089 |
9.70e-53 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 193.20 E-value: 9.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 633 DWRAAPPGEwrgerARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAI 712
Cdd:PRK11241 18 EWLDANNGE-----VIDVTNPANG-DKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 713 GLIVREAGKSFPNAIAEVREAVDFLRYYAVRIEESFSN--DSHR----------PLGPVLCISPWNFPLAIFTGQVAAAL 780
Cdd:PRK11241 92 RLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDtiPGHQadkrlivikqPIGVTAAITPWNFPAAMITRKAGPAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 781 AAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDg 860
Cdd:PRK11241 172 AAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 861 aghPVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLS 940
Cdd:PRK11241 251 ---KVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 941 TDIGPVIDAEARAVIERHVQAMQAAGHAVdrYPLDEAQTRHGTFVAPT-LIEIADIAELER-EVFGPVLHVLRYRrqDLD 1018
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHIADALEKGARV--VCGGKAHELGGNFFQPTiLVDVPANAKVAKeETFGPLAPLFRFK--DEA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589266809 1019 AVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATVGvqPFGG---EGLSGTGPKAGGPLYL 1089
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
649-1080 |
2.93e-52 |
|
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: 190.92 E-value: 2.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 649 PVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIA 728
Cdd:cd07147 2 EVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 EVREAVDFLRYYA---VRIE------ESFSNDSHR-------PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAE 792
Cdd:cd07147 81 EVARAIDTFRIAAeeaTRIYgevlplDISARGEGRqglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 793 QTALIAAYGVSVLHRAGIPADAVQLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAAtlaerLDGAGHPVpliAETG 872
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKA-----RAGKKKVV---LELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 873 GQNALIVDSSALTEQVVYDVLSSAFDSAGQRC-SALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEA 951
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 952 RAVIERHVQAMQAAGHAvdrypLDEAQTRHGTFVAPTLIEIADI-AELER-EVFGPVLHVLRYrrQDLDAVIDAINGRGY 1029
Cdd:cd07147 311 AERVEGWVNEAVDAGAK-----LLTGGKRDGALLEPTILEDVPPdMEVNCeEVFGPVVTVEPY--DDFDEALAAVNDSKF 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 589266809 1030 GLTFGVHTRLDETVRHVIERIHAGNVYVNrNIVGATVGVQPFGGEGLSGTG 1080
Cdd:cd07147 384 GLQAGVFTRDLEKALRAWDELEVGGVVIN-DVPTFRVDHMPYGGVKDSGIG 433
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
652-1080 |
5.67e-52 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 190.33 E-value: 5.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPAdrrdvVGQVIE----ADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAI 727
Cdd:PRK09406 7 NPA-----TGETVKtftaLTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 728 AEVREAVDFLRYYAVRIEESFSNDS--------------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAE- 792
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADEPadaaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASn 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 793 --QTALiaaYGVSVLHRAGIPADAVQ-LLPGRGETvgAALVASPAVRGVLFTGSTEVARLIAATlaerldgAGHPV-PLI 868
Cdd:PRK09406 162 vpQTAL---YLADLFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAI-------AGDEIkKTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 869 AETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVID 948
Cdd:PRK09406 230 LELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 949 AEARAVIERHVQAMQAAGHAVdrYPLDEAQTRHGTFVAPTLieIADIAELER----EVFGPVLHVlrYRRQDLDAVIDAI 1024
Cdd:PRK09406 310 EQGRDEVEKQVDDAVAAGATI--LCGGKRPDGPGWFYPPTV--ITDITPDMRlyteEVFGPVASL--YRVADIDEAIEIA 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 589266809 1025 NGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNrnivGATVGVQ--PFGGEGLSGTG 1080
Cdd:PRK09406 384 NATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
652-1084 |
3.40e-51 |
|
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: 188.28 E-value: 3.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNA-IAEV 730
Cdd:cd07098 2 DPATGQ-HLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 731 REAVDFLRYYAVRIEESFS--------NDSHR-------PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTA 795
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRpesrpgglLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 796 LIAAYGVSVLHRA----GIPADAVQLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAET 871
Cdd:cd07098 161 WSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 872 GGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVI-DAE 950
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIsPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 951 ARAVIERHVQAMQ------AAGHavdRYPLdeAQTRHGTFVAPTLI----EIADIAelEREVFGPVLHVLRYRrqDLDAV 1020
Cdd:cd07098 314 FDRLEELVADAVEkgarllAGGK---RYPH--PEYPQGHYFPPTLLvdvtPDMKIA--QEEVFGPVMVVMKAS--DDEEA 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589266809 1021 IDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRniVGATVGVQ--PFGGEGLSGTGPKAG 1084
Cdd:cd07098 385 VEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIND--FGVNYYVQqlPFGGVKGSGFGRFAG 448
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
640-1080 |
3.11e-49 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 182.65 E-value: 3.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEW---RGERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIV 716
Cdd:cd07117 7 GEWvkgSSGETIDSYNPANG-ETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKSFPNAIA-EVREAVDFLRYYA--VRIEESFSND---------SHRPLGPVLCISPWNFPLAIFTGQVAAALAAGN 784
Cdd:cd07117 86 LDNGKPIRETRAvDIPLAADHFRYFAgvIRAEEGSANMidedtlsivLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 785 VVLAKPAEQTALiaaygvSVLHRAGI-----PADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLd 859
Cdd:cd07117 166 TVVIKPSSTTSL------SLLELAKIiqdvlPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 860 gaghpVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELL 939
Cdd:cd07117 239 -----IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 940 STDIGPVIDAEARAVIERHVQAMQAAGH--AVDRYPLDEAQTRHGTFVAPTLIEIAD----IAelEREVFGPVLHVLRYR 1013
Cdd:cd07117 314 DTQMGAQVNKDQLDKILSYVDIAKEEGAkiLTGGHRLTENGLDKGFFIEPTLIVNVTndmrVA--QEEIFGPVATVIKFK 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589266809 1014 rqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNR-NIVGATVgvqPFGGEGLSGTG 1080
Cdd:cd07117 392 --TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
649-1080 |
1.59e-47 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 177.77 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 649 PVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAI- 727
Cdd:PRK13252 25 EVINPATG-EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 728 AEVREAVDFLRYYA------------VRiEESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTA 795
Cdd:PRK13252 104 VDIVTGADVLEYYAglapalegeqipLR-GGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 796 LIAAYGVSVLHRAGIPADAVQLLPGRGEtVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgagHPVPLiaETGGQN 875
Cdd:PRK13252 183 LTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL----KEVTM--ELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 876 ALIVDSSALTEQVVYDVLSSAFDSAGQRCS-ALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAV 954
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 955 IERHVQAMQAAGHAV--DRYPLDEAQTRHGTFVAPTL-IEIADIAELER-EVFGPVLHVLRYrrQDLDAVIDAINGRGYG 1030
Cdd:PRK13252 335 VLGYIEKGKAEGARLlcGGERLTEGGFANGAFVAPTVfTDCTDDMTIVReEIFGPVMSVLTF--DDEDEVIARANDTEYG 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 589266809 1031 LTFGVHTRlDETVRH-VIERIHAGNVYVNRniVGATVGVQPFGGEGLSGTG 1080
Cdd:PRK13252 413 LAAGVFTA-DLSRAHrVIHQLEAGICWINT--WGESPAEMPVGGYKQSGIG 460
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
640-1058 |
6.45e-47 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 176.46 E-value: 6.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWRG---ERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYA-----APIWQATPPAERAQCLRHAAQLMEDEMQSA 711
Cdd:PLN02467 14 GEWREpvlGKRIPVVNPATE-ETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 712 IGLIVREAGKSFPNAIAEVREAVDFLRYYAVRIE--------------ESFsnDSH---RPLGPVLCISPWNFPLAIFTG 774
Cdd:PLN02467 93 AKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEaldakqkapvslpmETF--KGYvlkEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 775 QVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATL 854
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 855 AERLdgagHPVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVG 934
Cdd:PLN02467 251 AQMV----KPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 935 RPELLSTDIGPVIDAEARAVIERHVQAMQAAGHAVDRYPLDEAQTRHGTFVAPTLI-EIADIAELER-EVFGPVLHVLRY 1012
Cdd:PLN02467 325 DPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIItDVTTSMQIWReEVFGPVLCVKTF 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 589266809 1013 RRQdlDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVN 1058
Cdd:PLN02467 405 STE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
753-1080 |
1.61e-46 |
|
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: 173.48 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 753 HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAygvsVLHR---AGIPADAVQLLPGrGETVGAAL 829
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSA----LLAKlipKYFDPEAVAVVEG-GVEVATAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 830 VASPaVRGVLFTGSTEVARLIAATLAErldgagHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRV 909
Cdd:cd07087 173 LAEP-FDHIFFTGSPAVGKIVMEAAAK------HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 910 LCVQEDCADRTLAMLRGAMNELRvGRPELLSTDIGPVIDaearaviERHVQAMQAAghavdrypLDEAQTRHG------- 982
Cdd:cd07087 246 VLVHESIKDELIEELKKAIKEFY-GEDPKESPDYGRIIN-------ERHFDRLASL--------LDDGKVVIGgqvdkee 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 983 TFVAPTLIEIADIAE--LEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRN 1060
Cdd:cd07087 310 RYIAPTILDDVSPDSplMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDV 387
|
330 340
....*....|....*....|
gi 589266809 1061 IVGATVGVQPFGGEGLSGTG 1080
Cdd:cd07087 388 LLHAAIPNLPFGGVGNSGMG 407
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
640-1058 |
5.56e-46 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 173.79 E-value: 5.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWRGERAR---PVPNPAdRRDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIV 716
Cdd:PLN00412 22 GEWRTSSSGksvAITNPS-TRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 717 REAGKSFPNAIAEVREAVDFLRYYA---VRI--------EESF-SND-------SHRPLGPVLCISPWNFPLAIFTGQVA 777
Cdd:PLN00412 101 KEIAKPAKDAVTEVVRSGDLISYTAeegVRIlgegkflvSDSFpGNErnkycltSKIPLGVVLAIPPFNYPVNLAVSKIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 778 AALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFT-GSTEVARLIAATLae 856
Cdd:PLN00412 181 PALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIAISKKAGM-- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 857 rldgaghpVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRP 936
Cdd:PLN00412 259 --------VPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 937 ElLSTDIGPVIDAEARAVIERHVQAMQAAGHAvdrypLDEAQTRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYRr 1014
Cdd:PLN00412 331 E-DDCDITPVVSESSANFIEGLVMDAKEKGAT-----FCQEWKREGNLIWPLLLDnvRPDMRIAWEEPFGPVLPVIRIN- 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 589266809 1015 qDLDAVIDAINGRGYGLTFGVHTR-LDETVRhVIERIHAGNVYVN 1058
Cdd:PLN00412 404 -SVEEGIHHCNASNFGLQGCVFTRdINKAIL-ISDAMETGTVQIN 446
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
658-1084 |
7.39e-46 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 173.47 E-value: 7.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 658 DVVGQVIEADEADVRAALGRAEYA---APiWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFP-NAIAEVREA 733
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAAREAfdhGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 734 VDFLRYYA----------VRIEESFSNDS-HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGV 802
Cdd:PLN02766 126 AGLLRYYAgaadkihgetLKMSRQLQGYTlKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 803 SVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAErldGAGHPVPLiaETGGQNALIVDSS 882
Cdd:PLN02766 206 HLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAT---SNLKQVSL--ELGGKSPLLIFDD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 883 ALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAM 962
Cdd:PLN02766 281 ADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 963 QAAGHAVdrYPLDEAQTRHGTFVAPTLieIADIAE----LEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTR 1038
Cdd:PLN02766 361 KREGATL--LTGGKPCGDKGYYIEPTI--FTDVTEdmkiAQDEIFGPVMSLMKFK--TVEEAIKKANNTKYGLAAGIVTK 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 589266809 1039 LDETVRHVIERIHAGNVYVNRNIvgATVGVQPFGGEGLSGTGPKAG 1084
Cdd:PLN02766 435 DLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
652-1084 |
3.10e-44 |
|
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: 168.06 E-value: 3.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRdVVGQVIEADEADVRAALGRAEYA--APIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAI-A 728
Cdd:cd07140 27 NPTDGS-VICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALkT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 729 EVREAVDFLRYYA----------VRIEESFSNDS-----HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQ 793
Cdd:cd07140 106 HVGMSIQTFRYFAgwcdkiqgktIPINQARPNRNltltkREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 794 TALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAerlDGAGHPVPLiaETGG 873
Cdd:cd07140 186 TPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA---VSNLKKVSL--ELGG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 874 QNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPvidAEARA 953
Cdd:cd07140 261 KSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP---QNHKA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 954 VIERHVQAMQAAghavdrypLDEAQT---------RHGTFVAPTLI-EIAD---IAelEREVFGPVLHVLRYRRQDLDAV 1020
Cdd:cd07140 338 HLDKLVEYCERG--------VKEGATlvyggkqvdRPGFFFEPTVFtDVEDhmfIA--KEESFGPIMIISKFDDGDVDGV 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589266809 1021 IDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVnrNIVGATVGVQPFGGEGLSGTGPKAG 1084
Cdd:cd07140 408 LQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFV--NTYNKTDVAAPFGGFKQSGFGKDLG 469
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
658-1084 |
3.35e-44 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 169.22 E-value: 3.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 658 DVVGQVIEADEADVRAALGRAEYA---APiWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAI-AEVREA 733
Cdd:PLN02466 84 EVIAHVAEGDAEDVNRAVAAARKAfdeGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 734 VDFLRYYAVRIEESFS----NDS-------HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGV 802
Cdd:PLN02466 163 ARLFRYYAGWADKIHGltvpADGphhvqtlHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 803 SVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAAtLAERLDgaGHPVPLiaETGGQNALIVDSS 882
Cdd:PLN02466 243 KLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLE-LAAKSN--LKPVTL--ELGGKSPFIVCED 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 883 ALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAM 962
Cdd:PLN02466 318 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 963 QAAGHAV----DRYpldeaqTRHGTFVAPTLieIADIAE----LEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFG 1034
Cdd:PLN02466 398 VESGATLecggDRF------GSKGYYIQPTV--FSNVQDdmliAQDEIFGPVQSILKFK--DLDEVIRRANNTRYGLAAG 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 589266809 1035 VHTRLDETVRHVIERIHAGNVYVN-RNIVGATVgvqPFGGEGLSGTGPKAG 1084
Cdd:PLN02466 468 VFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
640-1091 |
1.10e-43 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 166.93 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEWRGE-RARPVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVRE 718
Cdd:PLN02315 27 GEWRANgPLVSSVNPANNQ-PIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 719 AGKSFPNAIAEVREAVDFLRYyAVRIEESFSND---SHRP----------LGPVLCISPWNFPLAIFTGQVAAALAAGNV 785
Cdd:PLN02315 106 MGKILAEGIGEVQEIIDMCDF-AVGLSRQLNGSiipSERPnhmmmevwnpLGIVGVITAFNFPCAVLGWNACIALVCGNC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 786 VLAKPAEQTALIAAYGV----SVLHRAGIPADAVQLLPGrGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDGA 861
Cdd:PLN02315 185 VVWKGAPTTPLITIAMTklvaEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKC 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 862 ghpvplIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLST 941
Cdd:PLN02315 264 ------LLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 942 DIGPVIDAEARAVIERHVQAMQAAGHAVdrYPLDEAQTRHGTFVAPTLIEIADIAELER-EVFGPVLHVLRYrrQDLDAV 1020
Cdd:PLN02315 338 LLGPLHTPESKKNFEKGIEIIKSQGGKI--LTGGSAIESEGNFVQPTIVEISPDADVVKeELFGPVLYVMKF--KTLEEA 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589266809 1021 IDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIV--GATVGvQPFGGEGLSGTGPKAGG---PLYLHR 1091
Cdd:PLN02315 414 IEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPtnGAEIG-GAFGGEKATGGGREAGSdswKQYMRR 488
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
650-1080 |
3.98e-42 |
|
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: 161.05 E-value: 3.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRRdVVGQVIEADEADVRAALGRAeYAAPIWQAT--PPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAI 727
Cdd:cd07148 3 VVNPFDLK-PIGEVPTVDWAAIDKALDTA-HALFLDRNNwlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 728 AEVREAVDFLRYYAVRI----------------EESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPA 791
Cdd:cd07148 81 VEVTRAIDGVELAADELgqlggreipmgltpasAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 792 EQTALIAAYGVSVLHRAGIPADAVQLLPGRGEtVGAALVASPAVRGVLFTGSTEVARLIAATLAerldgAGHPVPLiaET 871
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-----PGTRCAL--EH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 872 GGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEA 951
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 952 RAVIERHVQAMQAAGHAVdrypLDEAQTRHGTFVAPT-LIEIADIAELER-EVFGPVLHVLRYRrqDLDAVIDAINGRGY 1029
Cdd:cd07148 313 VDRVEEWVNEAVAAGARL----LCGGKRLSDTTYAPTvLLDPPRDAKVSTqEIFGPVVCVYSYD--DLDEAIAQANSLPV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 589266809 1030 GLTFGVHTRLDETVRHVIERIHAGNVYVNRNiVGATVGVQPFGGEGLSGTG 1080
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
634-1073 |
2.25e-41 |
|
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: 159.66 E-value: 2.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 634 WRAAPPGEWRGERARPVPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIG 713
Cdd:TIGR01722 4 WIGGKFAEGASGTYIPVTNPATN-EVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 714 LIVREAGKSFPNAIAEVREAVDFLRY-----------YAVRIEESFSNDSHR-PLGPVLCISPWNFPLAIFTGQVAAALA 781
Cdd:TIGR01722 83 LITAEHGKTHSDALGDVARGLEVVEHacgvnsllkgeTSTQVATRVDVYSIRqPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 782 AGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGaALVASPAVRGVLFTGSTEVARLIAATlaerldGA 861
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTT------GS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 862 GHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLcVQEDCADRTLAMLRGAMNELRVGRPELLST 941
Cdd:TIGR01722 236 AHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAA-VLVGAADEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 942 DIGPVIDAEARAVIERHVQA---------MQAAGHAVDRYPldeaqtrHGTFVAPTLIE--IADIAELEREVFGPVLHVL 1010
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGgaaegaevlLDGRGYKVDGYE-------EGNWVGPTLLErvPPTMKAYQEEIFGPVLCVL 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589266809 1011 RYrrQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIvGATVGVQPFGG 1073
Cdd:TIGR01722 388 EA--DTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPI-PVPLPYFSFTG 447
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
697-1059 |
9.69e-39 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 149.89 E-value: 9.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 697 LRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRY---YAVRIE-ESFSNDS--------HRPLGPVLCISP 764
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYmaeWARRYEgEIIQSDRpgenillfKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 765 WNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGST 844
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 845 EVARLIAATLAERLDgaghPVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAML 924
Cdd:PRK10090 161 SAGEKIMAAAAKNIT----KVCL--ELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 925 RGAMNELRVGRP-ELLSTDIGPVIDAEARAVIERHVQAMQAAGHAVDRYplDEAQTRHGTFVAPTLIEIAD--IAELERE 1001
Cdd:PRK10090 235 GEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALG--GKAVEGKGYYYPPTLLLDVRqeMSIMHEE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 589266809 1002 VFGPVLHVLRYrrQDLDAVIDAINGRGYGLTFGVHTR-LDETVRhVIERIHAGNVYVNR 1059
Cdd:PRK10090 313 TFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQnLNVAMK-AIKGLKFGETYINR 368
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
640-1080 |
1.02e-37 |
|
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: 148.75 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 640 GEW----RGERARpVPNPADRRdVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLI 715
Cdd:cd07116 7 GEWvapvKGEYFD-NITPVTGK-VFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 716 VREAGKSFPNAI-AEVREAVDFLRYYAVRI-----------EESFSNDSHRPLGPVLCISPWNFPLAIFTGQVAAALAAG 783
Cdd:cd07116 85 TWDNGKPVRETLaADIPLAIDHFRYFAGCIraqegsiseidENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 784 NVVLAKPAEQTALIAAYGVSVLHRAgIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgagh 863
Cdd:cd07116 165 NCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 864 pVPLIAETGGQNALIVDSSALTEQvvydvlSSAFDSA-----------GQRCSALRVLCVQEDCADRTLAMLRGAMNELR 932
Cdd:cd07116 239 -IPVTLELGGKSPNIFFADVMDAD------DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 933 VGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGHAV----DRYPLDEAQTrhGTFVAPTLIEIA-DIAELEREVFGPVL 1007
Cdd:cd07116 312 QGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVltggERNELGGLLG--GGYYVPTTFKGGnKMRIFQEEIFGPVL 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589266809 1008 HVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVnrNIVGATVGVQPFGGEGLSGTG 1080
Cdd:cd07116 390 AVTTFK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
652-1080 |
1.19e-37 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 148.89 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 652 NPADRRDVvGQVIEADEADVRAAL--GRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:PRK09847 41 DPVTQAPL-AKIARGKSVDIDRAVsaARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 -VREAVDFLRYYAVRIE----ESFSNDSH-------RPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALI 797
Cdd:PRK09847 120 dIPGAARAIRWYAEAIDkvygEVATTSSHelamivrEPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 798 AAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIaatLAERLDGAGHPVPLiaETGGQNAL 877
Cdd:PRK09847 200 AIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL---LKDAGDSNMKRVWL--EAGGKSAN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 878 IV--DSSALtEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVI 955
Cdd:PRK09847 275 IVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 956 ERHVQAMQAAGHAVdrypLDEAQTRHGTFVAPT-LIEIADIAELER-EVFGPVLHVLRYRRQdlDAVIDAINGRGYGLTF 1033
Cdd:PRK09847 354 HSFIREGESKGQLL----LDGRNAGLAAAIGPTiFVDVDPNASLSReEIFGPVLVVTRFTSE--EQALQLANDSQYGLGA 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 589266809 1034 GVHTRLDETVRHVIERIHAGNVYVNR-NIVGATVgvqPFGGEGLSGTG 1080
Cdd:PRK09847 428 AVWTRDLSRAHRMSRRLKAGSVFVNNyNDGDMTV---PFGGYKQSGNG 472
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
753-1085 |
5.49e-37 |
|
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: 145.45 E-value: 5.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 753 HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYgVSVLHRAGIPADAVQLLPGrGETVGAALVAS 832
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAV-IAKIIREAFDEDEVAVFEG-DAEVAQALLEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 833 PaVRGVLFTGSTEVARLIAATLAERLDgaghPVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCV 912
Cdd:cd07134 176 P-FDHIFFTGSPAVGKIVMAAAAKHLA----SVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 913 QEDCADRTLAMLRGAMNELRVGRPELL-STDIGPVIDAEA----RAVIERHVQ--AMQAAGHAVDrypldeAQTRhgtFV 985
Cdd:cd07134 249 HESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHfdrlKGLLDDAVAkgAKVEFGGQFD------AAQR---YI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 986 APTLIE--IADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVG 1063
Cdd:cd07134 320 APTVLTnvTPDMKIMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLH 397
|
330 340
....*....|....*....|..
gi 589266809 1064 ATVGVQPFGGEGLSGTGpKAGG 1085
Cdd:cd07134 398 FLNPNLPFGGVNNSGIG-SYHG 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
755-1080 |
1.07e-36 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 145.94 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 755 PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEqtalIAAYGVSVLHR---AGIPADAVQLLPGrGETVGAALVA 831
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSE----LSPHTSKLMAKlltKYLDPSYVRVIEG-GVEVTTELLK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 832 SPaVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLC 911
Cdd:PTZ00381 184 EP-FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 912 VQEDCADRTLAMLRGAMNELrVGRPELLSTDIGpvidaeaRAVIERHVQAMQA-----AGHAVDRYPLDEAQtrhgTFVA 986
Cdd:PTZ00381 257 VHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYS-------RIVNEFHTKRLAElikdhGGKVVYGGEVDIEN----KYVA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 987 PTLIEIADIAE--LEREVFGPVLHVLRYrrQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGA 1064
Cdd:PTZ00381 325 PTIIVNPDLDSplMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHL 402
|
330
....*....|....*.
gi 589266809 1065 TVGVQPFGGEGLSGTG 1080
Cdd:PTZ00381 403 LNPNLPFGGVGNSGMG 418
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
753-1080 |
2.02e-34 |
|
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: 137.74 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 753 HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQT----ALIAAygvsvLHRAGIPADAVQLLPGRGETVGAA 828
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTphtaALLAE-----LVPKYLDPDAFQVVQGGVPETTAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 829 LvaSPAVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALR 908
Cdd:cd07135 181 L--EQKFDKIFYTGSGRVGRIIAEAAAKHL------TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 909 VLCVQEDCADRTLAMLRGAMNELrvgRPELLSTDigpviDAEARAVIERH---VQAM--QAAGHAVDRYPLDEAqTRhgt 983
Cdd:cd07135 253 YVLVDPSVYDEFVEELKKVLDEF---YPGGANAS-----PDYTRIVNPRHfnrLKSLldTTKGKVVIGGEMDEA-TR--- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 984 FVAPTLIEI--ADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNI 1061
Cdd:cd07135 321 FIPPTIVSDvsWDDSLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTL 398
|
330
....*....|....*....
gi 589266809 1062 VGATVGVQPFGGEGLSGTG 1080
Cdd:cd07135 399 IHVGVDNAPFGGVGDSGYG 417
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
753-1080 |
2.47e-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: 137.62 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 753 HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQT----ALIAAygvsvLHRAGIPADAVQLLPGRGEtVGAA 828
Cdd:cd07133 99 YQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTprtsALLAE-----LLAEYFDEDEVAVVTGGAD-VAAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 829 LVASPaVRGVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALR 908
Cdd:cd07133 173 FSSLP-FDHLLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 909 VLCVQEDCADRTLAMLRGAMNELrvgRPELL-STDIGPVIDAEARAVIERHVQAMQAAG---HAVDRYPLDEAQTRHgtf 984
Cdd:cd07133 246 YVLVPEDKLEEFVAAAKAAVAKM---YPTLAdNPDYTSIINERHYARLQGLLEDARAKGarvIELNPAGEDFAATRK--- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 985 VAPTLIEIA--DIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIV 1062
Cdd:cd07133 320 LPPTLVLNVtdDMRVMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
330
....*....|....*...
gi 589266809 1063 GATVGVQPFGGEGLSGTG 1080
Cdd:cd07133 398 HVAQDDLPFGGVGASGMG 415
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
671-1091 |
1.38e-32 |
|
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: 132.75 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 671 VRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRY----YAVRIEE 746
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARafviYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 747 SFSN--------DSHR---PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGI-PADA 814
Cdd:cd07084 81 EPGNhlgqglkqQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 815 VQLLPGRGETvGAALVASPAVRGVLFTGSTEVARLIAATLAErldgaghpVPLIAETGGQNALIVDSSA-LTEQVVYDVL 893
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKLALDAKQ--------ARIYLELAGFNWKVLGPDAqAVDYVAWQCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 894 SSAFDSAGQRCSALRVLCVQEDcaDRTLAMLRGAMNELRVGRPEllSTDIGPVID-------AEARAVIERHVQAMQAAG 966
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPEN--WSKTPLVEKLKALLARRKLE--DLLLGPVQTfttlamiAHMENLLGSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 967 HAVDRYPLDEAQTRHGTFVAptlIEIADIAEL--EREVFGPVLHVLRYRRQDLDAVIDAINgRGYG-LTFGVHTRLDETV 1043
Cdd:cd07084 308 KNHSIPSIYGACVASALFVP---IDEILKTYElvTEEIFGPFAIVVEYKKDQLALVLELLE-RMHGsLTAAIYSNDPIFL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 589266809 1044 RHVIER--IHAGNVYVNRNIVGATVGVQPFGGEGLSGTGPKAGGPLYLHR 1091
Cdd:cd07084 384 QELIGNlwVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKL 433
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
666-1080 |
3.17e-30 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 125.74 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 666 ADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYA---- 741
Cdd:PRK13968 26 AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAehgp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 742 -------VRIEESFSNDSHRPLGPVLCISPWNFPL-AIFTGQVAAALaAGNVVLAKPAEQTALIAAYGVSVLHRAGIPAD 813
Cdd:PRK13968 106 amlkaepTLVENQQAVIEYRPLGTILAIMPWNFPLwQVMRGAVPILL-AGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 814 AVQLLPGRGETVgAALVASPAVRGVLFTGSTEVARLIAATLAERLDGAghpvplIAETGGQNALIVDSSALTEQVVYDVL 893
Cdd:PRK13968 185 VYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKC------VLELGGSDPFIVLNDADLELAVKAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 894 SSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGHavdRYP 973
Cdd:PRK13968 258 AGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGA---RLL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 974 LD-EAQTRHGTFVAPTLIE--IADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERI 1050
Cdd:PRK13968 335 LGgEKIAGAGNYYAPTVLAnvTPEMTAFREELFGPVAAITVAK--DAEHALELANDSEFGLSATIFTTDETQARQMAARL 412
|
410 420 430
....*....|....*....|....*....|
gi 589266809 1051 HAGNVYVNRniVGATVGVQPFGGEGLSGTG 1080
Cdd:PRK13968 413 ECGGVFING--YCASDARVAFGGVKKSGFG 440
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
688-1080 |
3.38e-29 |
|
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: 122.33 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 688 TPPAE-RAQCLRHAAQLMEDEMQSAIGLIVREAGKS-FPNAIAEV-------REAVDFLRYYA--VRIEESFSN--DS-- 752
Cdd:cd07132 16 TRPLEfRIQQLEALLRMLEENEDEIVEALAKDLRKPkFEAVLSEIllvkneiKYAISNLPEWMkpEPVKKNLATllDDvy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 753 --HRPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAE---QTA-LIA----------AYGVsVLhrAGIPaDAVQ 816
Cdd:cd07132 96 iyKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEvspATAkLLAelipkyldkeCYPV-VL--GGVE-ETTE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 817 LLPGRGETVgaalvaspavrgvLFTGSTEVARLIAATLAERLDgaghPVPLiaETGGQNALIVDSSALTEQVVYDVLSSA 896
Cdd:cd07132 172 LLKQRFDYI-------------FYTGSTSVGKIVMQAAAKHLT----PVTL--ELGGKSPCYVDKSCDIDVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 897 FDSAGQRCSALR-VLCVQEdCADRTLAMLRGAMNELrVGRPELLSTDIGPVIDaearaviERHVQAMQ--------AAGH 967
Cdd:cd07132 233 FINAGQTCIAPDyVLCTPE-VQEKFVEALKKTLKEF-YGEDPKESPDYGRIIN-------DRHFQRLKkllsggkvAIGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 968 AVDrypldeAQTRhgtFVAPTLIeiADIAE----LEREVFGPVLHVLRYrrQDLDAVIDAINGRGYGLTFGVHTRLDETV 1043
Cdd:cd07132 304 QTD------EKER---YIAPTVL--TDVKPsdpvMQEEIFGPILPIVTV--NNLDEAIEFINSREKPLALYVFSNNKKVI 370
|
410 420 430
....*....|....*....|....*....|....*..
gi 589266809 1044 RHVIERIHAGNVYVNRNIVGATVGVQPFGGEGLSGTG 1080
Cdd:cd07132 371 NKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
755-1080 |
8.83e-28 |
|
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: 117.90 E-value: 8.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 755 PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEqtalIAAYGVSVLHRAgIP----ADAVQLLPGrGETVGAALV 830
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSE----LAPATSALLAKL-IPeyldTKAIKVIEG-GVPETTALL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 831 ASPAVRgVLFTGSTEVARLIAATLAErldgagHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFDS-AGQRCSALRV 909
Cdd:cd07137 175 EQKWDK-IFFTGSPRVGRIIMAAAAK------HLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 910 LCVQEDCADRTLAMLRGAMNELrVGRPELLSTDIGPVIDAE-----ARAVIERHVQAMQAAGHAVDRYPLdeaqtrhgtF 984
Cdd:cd07137 248 VLVEESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHhfqrlSRLLDDPSVADKIVHGGERDEKNL---------Y 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 985 VAPTLIEIA--DIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIV 1062
Cdd:cd07137 318 IEPTILLDPplDSSIMTEEIFGPLLPIITVK--KIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVV 395
|
330
....*....|....*...
gi 589266809 1063 GATVGVQPFGGEGLSGTG 1080
Cdd:cd07137 396 QYAIDTLPFGGVGESGFG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
650-1058 |
5.73e-27 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 117.93 E-value: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 650 VPNPADRrDVVGQVIEADEADVRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAE 729
Cdd:PLN02419 133 VINPATQ-EVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 730 VREAVDFLRYY----AVRIEESFSNDSH--------RPLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALI 797
Cdd:PLN02419 212 IFRGLEVVEHAcgmaTLQMGEYLPNVSNgvdtysirEPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 798 AAYGVSVLHRAGIPADAVQLLPGRGETVGaALVASPAVRGVLFTGSTEVARLIAATLAERldgaGHPVPliAETGGQNAL 877
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAK----GKRIQ--SNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 878 IVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAmNELRVGRPELLSTDIGPVIDAEARAVIER 957
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERA-KALKVTCGSEPDADLGPVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 958 HVQAM--QAAGHAVDRYPLDEAQTRHGTFVAPTLIE--IADIAELEREVFGPVLHVLryRRQDLDAVIDAINGRGYGLTF 1033
Cdd:PLN02419 444 LIQSGvdDGAKLLLDGRDIVVPGYEKGNFIGPTILSgvTPDMECYKEEIFGPVLVCM--QANSFDEAISIINKNKYGNGA 521
|
410 420
....*....|....*....|....*
gi 589266809 1034 GVHTRLDETVRHVIERIHAGNVYVN 1058
Cdd:PLN02419 522 AIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
671-1037 |
3.99e-26 |
|
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: 113.41 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 671 VRAALGRAEYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGksFPNAIAEV---------REAVDFLR--- 738
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQGelgrttgqlRLFADLVRegs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 739 YYAVRIEESfsnDSHR-------------PLGPVLCISPWNFPLAIFT--GQVAAALAAGNVVLAK--PA--EQTALIAA 799
Cdd:cd07129 79 WLDARIDPA---DPDRqplprpdlrrmlvPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhpGTSELVAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 800 YGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLDgaghPVPLIAETGGQNALIV 879
Cdd:cd07129 156 AIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGSVNPVFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 880 DSSALTEQVvyDVLSSAFD-----SAGQRCSALRVLCVQEDCA-DRTLAMLRGAMNELRVGRpeLLSTDIgpvidaeARA 953
Cdd:cd07129 232 LPGALAERG--EAIAQGFVgsltlGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQT--MLTPGI-------AEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 954 VIERhVQAMQAAGHAvdRYPLDEAQTRHGTFVAPTLIEI-----ADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRG 1028
Cdd:cd07129 301 YRQG-VEALAAAPGV--RVLAGGAAAEGGNQAAPTLFKVdaaafLADPALQEEVFGPASLVVRYD--DAAELLAVAEALE 375
|
....*....
gi 589266809 1029 YGLTFGVHT 1037
Cdd:cd07129 376 GQLTATIHG 384
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
755-1080 |
1.30e-23 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 105.96 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 755 PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAgIPADAVQLLPGrGETVGAALVASPA 834
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVIEG-GPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 835 VRgVLFTGSTEVARLIAATLAErldgagHPVPLIAETGGQNALIVD---SSALTEQVVYDVLSSAFDS-AGQRCSALRVL 910
Cdd:PLN02203 186 DK-IFFTGSPRVGRIIMTAAAK------HLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDYV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 911 CVQEDCADRTLAMLRGAMNELRVGRPELLstdigpviDAEARAVIERHVQAMqaagHAVDRYPLDEAQTRHG-------T 983
Cdd:PLN02203 259 LVEERFAPILIELLKSTIKKFFGENPRES--------KSMARILNKKHFQRL----SNLLKDPRVAASIVHGgsidekkL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 984 FVAPTLI--EIADIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNI 1061
Cdd:PLN02203 327 FIEPTILlnPPLDSDIMTEEIFGPLLPIITVK--KIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
330
....*....|....*....
gi 589266809 1062 VGATVGVQPFGGEGLSGTG 1080
Cdd:PLN02203 405 IQYACDSLPFGGVGESGFG 423
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
755-1080 |
4.63e-23 |
|
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: 104.12 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 755 PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAgIPADAVQLLPGrGETVGAALVASPa 834
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELLDQK- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 835 VRGVLFTGSTEVARLIAATLAERLDgaghPVPLiaETGGQNALIVDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQE 914
Cdd:cd07136 177 FDYIFFTGSVRVGKIVMEAAAKHLT----PVTL--ELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 915 DCADRTLAMLRGAMNELrVGRPELLSTDIGpvidaeaRAVIERH---VQAMqaaghavdrypLDEAQTRHG-------TF 984
Cdd:cd07136 251 SVKEKFIKELKEEIKKF-YGEDPLESPDYG-------RIINEKHfdrLAGL-----------LDNGKIVFGgntdretLY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 985 VAPTLIEIA--DIAELEREVFGPVLHVLRYRrqDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIV 1062
Cdd:cd07136 312 IEPTILDNVtwDDPVMQEEIFGPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIM 389
|
330
....*....|....*...
gi 589266809 1063 GATVGVQPFGGEGLSGTG 1080
Cdd:cd07136 390 HLANPYLPFGGVGNSGMG 407
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
696-1056 |
1.96e-20 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 96.41 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 696 CLRHAAQLMEDEMQSAIG-LIVREAGKSFPNAIAEVREAVDFLRYYA---VR-IEESFSN-------DSHR---PLGPVL 760
Cdd:cd07126 68 SHRVAHELRKPEVEDFFArLIQRVAPKSDAQALGEVVVTRKFLENFAgdqVRfLARSFNVpgdhqgqQSSGyrwPYGPVA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 761 CISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVASPAvRGVLF 840
Cdd:cd07126 148 IITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANP-RMTLF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 841 TGSTEVARLIAATLAER--LDGAGHPVPLIaetgGQNALIVDssalteQVVYDVLSSAFDSAGQRCSALRVLCVQEDCAD 918
Cdd:cd07126 227 TGSSKVAERLALELHGKvkLEDAGFDWKIL----GPDVSDVD------YVAWQCDQDAYACSGQKCSAQSILFAHENWVQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 919 rtlAMLRGAMNELrVGRPELLSTDIGPVIDAEARAVIErHVQ---AMQAAGHAVDRYPLDEAQ--TRHGTfVAPT----- 988
Cdd:cd07126 297 ---AGILDKLKAL-AEQRKLEDLTIGPVLTWTTERILD-HVDkllAIPGAKVLFGGKPLTNHSipSIYGA-YEPTavfvp 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589266809 989 LIEIADIAELE---REVFGPVLHVLRYRRQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVY 1056
Cdd:cd07126 371 LEEIAIEENFElvtTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
762-1085 |
4.07e-17 |
|
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: 86.17 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 762 ISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAGI-PADAVQLLPGrgeTVGAAL--VASPAVrgV 838
Cdd:cd07128 151 INAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICG---SVGDLLdhLGEQDV--V 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 839 LFTGStevarliAATlAERLdgAGHP------VPLIAETGGQNALIV--DSSALTEQ---VVYDVLSSAFDSAGQRCSAL 907
Cdd:cd07128 226 AFTGS-------AAT-AAKL--RAHPnivarsIRFNAEADSLNAAILgpDATPGTPEfdlFVKEVAREMTVKAGQKCTAI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 908 RVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAEARAVIERHVQAMQAAGHAV----DRYPLDEAQTRHGT 983
Cdd:cd07128 296 RRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVfggpDRFEVVGADAEKGA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 984 FVAPTLIEIAD----IAELEREVFGPVLHVLRYRRQDlDAVIDAINGRGyGLTFGVHTRLDETVRHVIERI--HAGNVYV 1057
Cdd:cd07128 376 FFPPTLLLCDDpdaaTAVHDVEAFGPVATLMPYDSLA-EAIELAARGRG-SLVASVVTNDPAFARELVLGAapYHGRLLV 453
|
330 340 350
....*....|....*....|....*....|....*
gi 589266809 1058 -NRNIVGATVG---VQP---FGGEGLSGTGPKAGG 1085
Cdd:cd07128 454 lNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGG 488
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
755-1084 |
4.93e-17 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 85.87 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 755 PLGPVLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAYGVSVLHRAgIPADAVQLLPGrGETVGAALVASPA 834
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEG-AVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 835 VRgVLFTGSTEVARLIAATLAERLdgaghpVPLIAETGGQNALIVDSSALTEQVVYDVLSSAFD-SAGQRCSALRVLCVQ 913
Cdd:PLN02174 190 DK-IFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 914 EDCADRTLAMLRGAMnELRVGRPELLSTDIGPVIDAE-----ARAVIERHVQAMQAAGHAVDRYPLDeaqtrhgtfVAPT 988
Cdd:PLN02174 263 KEYAPKVIDAMKKEL-ETFYGKNPMESKDMSRIVNSThfdrlSKLLDEKEVSDKIVYGGEKDRENLK---------IAPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 989 -LIEIA-DIAELEREVFGPVLHVLRYrrQDLDAVIDAINGRGYGLTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGATV 1066
Cdd:PLN02174 333 iLLDVPlDSLIMSEEIFGPLLPILTL--NNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAL 410
|
330
....*....|....*...
gi 589266809 1067 GVQPFGGEGLSGTGPKAG 1084
Cdd:PLN02174 411 HTLPFGGVGESGMGAYHG 428
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
86-131 |
2.21e-15 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 70.96 E-value: 2.21e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 589266809 86 SVLRAAITAAYRRPEPECVAMLVDQAESSQPER--VETLARRLVQTLR 131
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERaaIRALARKLVEALR 48
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
664-1013 |
1.09e-14 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 78.59 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 664 IEADEADVRAALGRA-EYAAPIWQATPPAERAQCLRHAAQLMEDEMQSAIGLIVREAGKSFPNAIAEVREAVDFLRYYAv 742
Cdd:PRK11903 35 VSATGLDLAAAFAFArEQGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 743 RIEESFSNDSHRPLGP----------------------VLCISPWNFPLAIFTGQVAAALAAGNVVLAKPAEQTALIAAY 800
Cdd:PRK11903 114 KLGAALGDARLLRDGEavqlgkdpafqgqhvlvptrgvALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 801 GVSVLHRAGI-PADAVQLLPGRGETVGAALVASPAVRgvlFTGSTEVARLIAATLAErldgAGHPVPLIAETGGQNALI- 878
Cdd:PRK11903 194 MVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVVS---FTGSAETAAVLRSHPAV----VQRSVRVNVEADSLNSALl 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 879 ----VDSSALTEQVVYDVLSSAFDSAGQRCSALRVLCVQEDCADRTLAMLRGAMNELRVGRPELLSTDIGPVIDAE---- 950
Cdd:PRK11903 267 gpdaAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAqlaa 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589266809 951 ARAVIERHVQAMQAAgHAVDRYPLDEAQTRHGTFVAPTLIEI--ADIAEL--EREVFGPVLHVLRYR 1013
Cdd:PRK11903 347 VRAGLAALRAQAEVL-FDGGGFALVDADPAVAACVGPTLLGAsdPDAATAvhDVEVFGPVATLLPYR 412
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
664-1064 |
2.18e-10 |
|
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: 64.81 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 664 IEADEADVRAALGRAEYAAPIWQ-ATPPAERAQCLRHAAQLMEDEMQSAIGlIVREAGKSF--------PNA-------I 727
Cdd:cd07127 79 VTYPQCDPDALLAAARAAMPGWRdAGARARAGVCLEILQRLNARSFEMAHA-VMHTTGQAFmmafqaggPHAqdrgleaV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 728 AEVREAVDFLRYYAVRIEESFSNDS----------HRPLGPVLCISP---WNFPLAIFtgqvaAALAAGNVVLAKPAEQT 794
Cdd:cd07127 158 AYAWREMSRIPPTAEWEKPQGKHDPlamektftvvPRGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 795 ALIAAYGV----SVLHRAGIPADAVQLLP-GRGETVGAALVASPAVRGVLFTGSTEVARLIAATLAERLdgaghpvpLIA 869
Cdd:cd07127 233 ILPLAITVqvarEVLAEAGFDPNLVTLAAdTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--------VYT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 870 ETGGQNALIVDSsalTEQVVYDVLSSAFDSA---GQRCSALRVLCVQED---------CADRTLAMLRGAMNELrVGRPE 937
Cdd:cd07127 305 EKAGVNTVVVDS---TDDLKAMLRNLAFSLSlysGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 938 LLSTDIGPVIDAEARAVIErhvQAMQAAGHAVDRYPLDEAQTRHGTFVAPTLIEI--ADIAELEREVFGPVLHVLryRRQ 1015
Cdd:cd07127 381 RAAALLGAIQSPDTLARIA---EARQLGEVLLASEAVAHPEFPDARVRTPLLLKLdaSDEAAYAEERFGPIAFVV--ATD 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 589266809 1016 DLDAVIDAING--RGYG-LTFGVHTRLDETVRHVIERIHAGNVYVNRNIVGA 1064
Cdd:cd07127 456 STDHSIELAREsvREHGaMTVGVYSTDPEVVERVQEAALDAGVALSINLTGG 507
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
318-551 |
9.67e-09 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 59.33 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 318 SIKLSALH-PRYS--------RAQRDRVMEELLPRMVGLAALARRYDIGLNIDAEEA------DRLELSLdlleALCF-- 380
Cdd:PLN02681 187 SFPLFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYTslqpaiDYITYDL----AREFnk 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 381 -DERLRGWNgigfVIQAYQKRAPFVIDFVIDLARRSKHRLMVRLVKGAYWDSEVKRAQVDGLEGyPVYTRKIHTDVSYLA 459
Cdd:PLN02681 263 gKDRPIVYG----TYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNR 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 460 CARKLLSA----PEAVFpqFATHNAQTL-ASIYYMAGENYYPG--QYEFQCLHGMGEPLyeevvgpvSKGRLNRPCRV-- 530
Cdd:PLN02681 338 CAEFLLEKasngDGEVM--LATHNVESGeLAAAKMNELGLHKGdpRVQFAQLLGMSDNL--------SFGLGNAGFRVsk 407
|
250 260
....*....|....*....|.
gi 589266809 531 YAPVGTHETLLAYLVRRLLEN 551
Cdd:PLN02681 408 YLPYGPVEEVIPYLLRRAEEN 428
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-60 |
7.20e-07 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 47.51 E-value: 7.20e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 2 ATVTLGVKVDEALRERLRVLAESLGCTPHWLHKQALLSYIEAIERGQvpAEIDR-RADAD 60
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWRE--ALIQEgLAAAD 58
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
755-952 |
2.80e-06 |
|
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: 51.07 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 755 PLGPVLCISPWNFPLAIFTgQVAAALAAGNVVLAKP---AEQTALIAAYGVSVLHRAGIPADAVQLLPGRGETVGAALVA 831
Cdd:cd07077 100 PIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPhpsAPFTNRALALLFQAADAAHGPKILVLYVPHPSDELAEELLS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 832 SPAVRGVLFTGSTEVARLIAAtlaerldgAGHPVPLIAETGGQNALIVDSSALTEQVVYDVLSSA-FDSAGqrCSALRVL 910
Cdd:cd07077 179 HPKIDLIVATGGRDAVDAAVK--------HSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA--CASEQNL 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 589266809 911 CVQEDCADRTLAMLRGAMNELRVGRPE---LLSTDIGPVIDAEAR 952
Cdd:cd07077 249 YVVDDVLDPLYEEFKLKLVVEGLKVPQetkPLSKETTPSFDDEAL 293
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
777-961 |
3.96e-04 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 44.29 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 777 AAALA--AGNVVL---AKPAEQT--ALIAAYgVSVLHRAGIPADAVQLLPGRG-ETVGAALVASPAV-----RGvlftGs 843
Cdd:PRK00197 133 AAALClkSGNAVIlrgGSEAIHSnrALVAVI-QEALEEAGLPADAVQLVETTDrAAVGELLKLDGYVdviipRG----G- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589266809 844 tevARLIAATLAE-RldgaghpVPLIaETG-GQNALIVDSSALTEQVVyDVlssAFDSAGQR---CSALRVLCVQEDCAD 918
Cdd:PRK00197 207 ---AGLIRRVVENaT-------VPVI-EHGdGICHIYVDESADLDKAL-KI---VLNAKTQRpsvCNALETLLVHEAIAE 271
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 589266809 919 RTLAMLRGAMNELRVgrpELLStdigpviDAEARAVIERHVQA 961
Cdd:PRK00197 272 EFLPKLAEALAEAGV---ELRG-------DEAALALLPDVVPA 304
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
5-46 |
5.19e-04 |
|
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar proteins; This family includes the N-terminal ribbon-helix-helix (RHH) domain of Shewanella oneidensis CopA(SO), a newly identified type II antitoxin, as well as the N-terminal RHH domain of Escherichia coli PutA flavoprotein, among other similar proteins, many of which are as yet uncharacterized. CopA(SO) is a typical RHH antitoxin that includes an ordered N-terminal domain (CopA(SO)-N) and a disordered C-terminal domain (CopA(SO)-C). Biophysical investigation indicates allosteric effects of CopA(SO)-N on CopA(SO)-C; DNA binding of CopA(SO)-N appears to induce CopA(SO)-C to fold and self-associate the C-terminal domain. The multifunctional E. coli proline utilization A (PutA) flavoprotein functions as a membrane-associated proline catabolic enzyme as well as a transcriptional repressor of the proline utilization genes putA and putP. The N-terminal domain of PutA is a transcriptional regulator with an RHH fold; structure studies show that it forms a homodimer to bind one DNA duplex. This family also includes orphan antitoxin ParD2, an antitoxin component of a non-functional type II toxin-antitoxin (TA system); it does not neutralize the effect of any of the RelE or ParE toxins.
Pssm-ID: 409023 Cd Length: 44 Bit Score: 38.89 E-value: 5.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 589266809 5 TLGVKVDEALRERLRVLAESLGCTPHWLHKQALLSYIEAIER 46
Cdd:cd22233 2 TLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREEW 43
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1112-1135 |
3.09e-03 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 42.11 E-value: 3.09e-03
10 20
....*....|....*....|....
gi 589266809 1112 PLTLPGPTGETNQYHLKPRGTVLC 1135
Cdd:PRK11904 667 PEKLPGPTGESNELRLHGRGVFVC 690
|
|
| |
