|
Name |
Accession |
Description |
Interval |
E-value |
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
1-1317 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 2797.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1 MATTTLGVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLEGGATLNDLNGHAAALGDDAGEVA--TDHAHQCFLE 78
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADtpAEEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 79 FAESILPQSVLRSAITAAYRRPEQEVVPMLLEQARLPAAQAEATNKLAATLADKLRNQKSAGGRAGIVQGLLQEFSLSSQ 158
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGRAGMVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 159 EGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNESGLTSSLTRIIGKSG 238
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 239 EPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFESKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGI 318
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 319 YEGPGISIKLSALHPRYSRAQYERVMSELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGIG 398
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 399 FVIQAYQKRCPYVIDYVIDLAKRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLAVPEAI 478
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 479 YPQFATHNAHTLSAIYTIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVAEGKLNRPCRVYAPVGTHETLLAYLVRRLLEN 558
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 559 GANTSFVNRIADHSISIQELVADPVTSIERMATQEGGIGLPHPRIPMPRELYGSERANSAGIDMANEHRLASLSCALLAT 638
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLAS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 639 AHNDWKAAPLLACATSEQAAAPVLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAE 718
Cdd:PRK11809 641 AHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQ 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 719 IQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRNDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVL 798
Cdd:PRK11809 721 MQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 799 AKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGRPIPL 878
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 879 IAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVI 958
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 959 DAEAKAGIEKHIQGMRDKGRSVYQVAIADGAEVKRGTFVMPTLIELESFDELQREIFGPVLHVVRYNRKNLDQLIEQINA 1038
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQINA 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1039 SGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPADAIARHFA 1118
Cdd:PRK11809 1041 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAVTLA 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1119 RTDADAKVDTALRDQQLKPLTLLKSWAEgNQQAELAALCAQFAEQTQSGITRVLPGPTGERNTYTVLPREHVLCLADNEA 1198
Cdd:PRK11809 1121 RQDAEYPVDAQLRAALLAPLTALREWAA-EREPELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADTEQ 1199
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1199 DLLAQLAAVLAVGSSAVFQDGEPAKSLRGRLPKELQAKVKLVADWSKDEVAFDAVIHHGDSDQLRGICEQVATRAGAIVG 1278
Cdd:PRK11809 1200 DALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPIVS 1279
|
1290 1300 1310
....*....|....*....|....*....|....*....
gi 2063477733 1279 VNGLSSGDYQIALERLVIERAVSVNTAAAGGNASLMTIG 1317
Cdd:PRK11809 1280 VQGFARGETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
76-1317 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 2073.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 76 FLEFAESILPQSVLRSAITAAYRRPEQEVVPMLLEQARLPAAQAEATNKLAATLADKLRNQKSAGGragiVQGLLQEFSL 155
Cdd:PRK11905 2 FQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTG----VEALLQEYSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 156 SSQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNESGLTSSLTRIIG 235
Cdd:PRK11905 78 SSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 236 KSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFESKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHG 315
Cdd:PRK11905 158 RLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 316 RGIYEGPGISIKLSALHPRYSRAQYERVMSELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWN 395
Cdd:PRK11905 238 RGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 396 GIGFVIQAYQKRCPYVIDYVIDLAKRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLAVP 475
Cdd:PRK11905 318 GIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAAR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 476 EAIYPQFATHNAHTLSAIYTIAGQNYypgQYEFQCLHGMGEPLYEQVVGKvaeGKLNRPCRVYAPVGTHETLLAYLVRRL 555
Cdd:PRK11905 398 DVIYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGK---EKLGRPCRIYAPVGTHETLLAYLVRRL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 556 LENGANTSFVNRIADHSISIQELVADPVTSIERMAtqeggiGLPHPRIPMPRELYGSERANSAGIDMANEHRLASLSCAL 635
Cdd:PRK11905 472 LENGANSSFVNRIVDENVPVEELIADPVEKVAAMG------VAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEAL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 636 LATAHNDWKAAPLLACATSEQAAAPVLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLM 715
Cdd:PRK11905 546 NAFAAKTWHAAPLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLM 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 716 EAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRNDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGN 795
Cdd:PRK11905 626 EAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGN 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 796 PVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqGRP 875
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GPP 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 876 IPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIG 955
Cdd:PRK11905 783 VPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVG 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 956 PVIDAEAKAGIEKHIQGMRDKGRSVYQVAIADgaEVKRGTFVMPTLIELESFDELQREIFGPVLHVVRYNRKNLDQLIEQ 1035
Cdd:PRK11905 863 PVIDAEAQANIEAHIEAMRAAGRLVHQLPLPA--ETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDD 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1036 INASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLStRPADAIAR 1115
Cdd:PRK11905 941 INATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVR-EAPTPIPP 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1116 HFARTDADAkvdtalrdqqlkPLTLLKSWAEGNQQAELAALCAQFAEQTQSGITRVLPGPTGERNTYTVLPREHVLCLAD 1195
Cdd:PRK11905 1020 AHESVDTDA------------AARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVAD 1087
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1196 NEADLLAQLAAVLAVGSSAVFQDGEPAKSLRGRLPKELQAKVKLVADWSKDeVAFDAVIHHGDSDQLRGICEQVATRAGA 1275
Cdd:PRK11905 1088 TEEALLRQLAAALATGNVAVVAADSGLAAALADLPGLVAARIDWTQDWEAD-DPFAGALLEGDAERARAVRQALAARPGA 1166
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|..
gi 2063477733 1276 IVGVNGlSSGDYQIALERLVIERAVSVNTAAAGGNASLMTIG 1317
Cdd:PRK11905 1167 IVPLIA-AEPTDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
77-1108 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1613.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 77 LEFAESILPQSVLRSAITAAYRRPEQEVVPMLLEQARLPAAQAEATNKLAATLADKLRNQKsagGRAGIVQGLLQEFSLS 156
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKK---KKLGGIDAFLQEYSLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 157 SQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNESG--LTSSLTRII 234
Cdd:PRK11904 78 TEEGIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADgtPSGVLKRLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 235 GKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFESKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASH 314
Cdd:PRK11904 158 NRLGEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 315 GRGIYEGPGISIKLSALHPRYSRAQYERVMSELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGW 394
Cdd:PRK11904 238 GADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 395 NGIGFVIQAYQKRCPYVIDYVIDLAKRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLAV 474
Cdd:PRK11904 318 GGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 475 PEAIYPQFATHNAHTLSAIYTIAGQnyypGQYEFQCLHGMGEPLYEQVVgkvaeGKLNRPCRVYAPVGTHETLLAYLVRR 554
Cdd:PRK11904 398 RGAIYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 555 LLENGANTSFVNRIADHSISIQELVADPVTSIERMATqeggigLPHPRIPMPRELYGSERANSAGIDMANEHRLASLSCA 634
Cdd:PRK11904 469 LLENGANSSFVHRLVDPDVPIEELVADPVEKLRSFET------LPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 635 LLATAHNDWKAAPLLAcatSEQAAAPVLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADL 714
Cdd:PRK11904 543 IAAFLEKQWQAGPIIN---GEGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 715 MEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRN----------DN---CRPLGPVVCISPWNFPLA 781
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGApeklpgptgeSNelrLHGRGVFVCISPWNFPLA 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 782 IFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLL 861
Cdd:PRK11904 700 IFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARII 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 862 QRNIAGRldnQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAE 941
Cdd:PRK11904 780 NRTLAAR---DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAE 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 942 SRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVYQVAIADGAEvkRGTFVMPTLIELESFDELQREIFGPVLHV 1021
Cdd:PRK11904 857 LKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTE--NGHFVAPTAFEIDSISQLEREVFGPILHV 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1022 VRYNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1101
Cdd:PRK11904 935 IRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYL 1014
|
....*..
gi 2063477733 1102 YRLLSTR 1108
Cdd:PRK11904 1015 LRFATEK 1021
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
80-1314 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1568.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 80 AESILPQSVLRSAITAAYRRPEQEVVPMLLEQARLPAAQAEATNKLAATLADKLRNQKSAGGRAGIVQGLLQEFSLSSQE 159
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 160 GVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNESGLTSS--LTRIIGKS 237
Cdd:COG4230 81 SEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLAsgLLRLLGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 238 GEPMIRKGVDMAMRLMGEQFVTGETIAEALANASKFESKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRG 317
Cdd:COG4230 161 GRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 318 IYEGPGISIKLSALHPRYSRAQYERVMSELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGI 397
Cdd:COG4230 241 GGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 398 GFVIQAYQKRCPYVIDYVIDLAKRSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLAVPEA 477
Cdd:COG4230 321 GGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 478 IYPQFATHNAHTLSAIYTIAGQNYYPGQYEFQCLHGMGEPLYEQVVgkvaEGKLNRPCRVYAPVGTHETLLAYLVRRLLE 557
Cdd:COG4230 401 AQPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVG----RGKLGRPCRIYAPVGSHEDLLAYLVRRLLE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 558 NGANTSFVNRIADHSISIQELVADPVTSIERMAtqeggiGLPHPRIPMPRELYGSERANSAGIDMANEHRLASLSCALLA 637
Cdd:COG4230 477 NGANSSFVNRIADEDVPVEELIADPVEKARALG------GAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 638 TAHNDWKAAPLLACATSEQAAAPVLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEA 717
Cdd:COG4230 551 AAEKQWQAAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEA 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 718 EIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRND-NCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:COG4230 631 HRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPtVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNT 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 797 VLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRldnQGRPI 876
Cdd:COG4230 711 VLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR---DGPIV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 877 PLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGP 956
Cdd:COG4230 788 PLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGP 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 957 VIDAEAKAGIEKHIQGMRDKGRSVYQVAIADGAEvkRGTFVMPTLIELESFDELQREIFGPVLHVVRYNRKNLDQLIEQI 1036
Cdd:COG4230 868 VIDAEARANLEAHIERMRAEGRLVHQLPLPEECA--NGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAI 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1037 NASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPADaiarh 1116
Cdd:COG4230 946 NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVT----- 1020
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1117 fartdadakVDTAlrdqqlkpltllkswAEGNqQAELAALCAQFAEQTQsgiTRVLPGPTGERNTYTVLPREHVLCLADN 1196
Cdd:COG4230 1021 ---------VNTT---------------AAGG-NASLLALGDWLASLLG---ALTLPGPTGERNTLTLRPRGRVLCLADS 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1197 EADLLAQLAAVLAVGSSAVFQDGEPAKslrgRLPKELQAkvklvadwskdevAFDAVIHHGdsdQLRGICEQVATRAGAI 1276
Cdd:COG4230 1073 LEALLAQLAAALATGNRAVVAADLALA----GLPAVLLP-------------PFDAVLFEG---RLRALRQALAARDGAI 1132
|
1210 1220 1230
....*....|....*....|....*....|....*...
gi 2063477733 1277 VGVNGLssgdyQIALERLVIEravsvntaaAGGNASLM 1314
Cdd:COG4230 1133 VPVIDA-----GYDLERLLEE---------AGGNASLM 1156
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
608-1109 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 757.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 608 ELYGSERANSAGIDMANEHRLASLSCALLATAHNDWKAAPLLA-CATSEQAAAPVLNPSDHRDVVGQVQEASVADASNAV 686
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGhSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 687 QCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRNDNCRP 766
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 767 LGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERV 846
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 847 KGVMFTGSTEVARLLQRNIAGRLDNqgrPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQED 926
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 927 SADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVYQVAIADGAEVKRGTFVMPTLIELES 1006
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFELDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1007 FDELQREIFGPVLHVVRYNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGE 1086
Cdd:TIGR01238 398 IAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQ 477
|
490 500
....*....|....*....|...
gi 2063477733 1087 GLSGTGPKAGGPLYLYRLLSTRP 1109
Cdd:TIGR01238 478 GLSGTGPKAGGPHYLYRLTQVQY 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
112-1118 |
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: 700.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 112 ARLPAAQAEATNKLAATLADKLRNQksaggRAGIVQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKIStgn 191
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAA-----PEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 192 wqphlgNSPSLFVNAATWGLLLTgklvsthnesgltssltrIIGKSGEPMIRKGVDMAMRLMGEQFVTGETIAEALANAS 271
Cdd:COG0506 75 ------KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 272 KFESKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKAShgrgiYEGPGISIKLSALHPRYSRAQYERVMSELYPRL 351
Cdd:COG0506 131 KLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 352 LSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGIGFVIQAYQKRCPYVIDYVIDLAKRSRHRLMIRLV 431
Cdd:COG0506 206 RPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 432 KGAYWDSEIKRAQVEGLeGYPVYTRKVYTDVSYIACARKLLAVPEAIYPQFATHNAHTLSAIYTIAGQ-NYYPGQYEFQC 510
Cdd:COG0506 286 KGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 511 LHGMGEPLYEQVVgKVAEGKLNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADHSISIQELVADPVTSIERMA 590
Cdd:COG0506 365 LYGMGEDLQRALA-AVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 591 tqeggiGLPHPRIPMPRELYGSERANSAGIDMANEHRLASLSCAL-LATAHNDWKAAPLLACATSEQAAAPVLNPSDHRD 669
Cdd:COG0506 444 ------PTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAaAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 670 VVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLR 749
Cdd:COG0506 518 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAA 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 750 YYAVQARND-------LRNDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIP 822
Cdd:COG0506 598 AAAAAARAAappppppGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLL 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 823 EGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGRPIPLIAETGGQNAMIVDSSALTEQVVID 902
Cdd:COG0506 678 GGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVA 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 903 VVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVYQ 982
Cdd:COG0506 758 ASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLP 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 983 VAIADGAEVkRGTFVMPTLIELESFDELQREIFGPVLHVVRYNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNV 1062
Cdd:COG0506 838 GGGPLVPGL-LTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGG 916
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*.
gi 2063477733 1063 NAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTRPADAIARHFA 1118
Cdd:COG0506 917 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAA 972
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
625-1108 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 696.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 625 EHRLASLSCALLATAHNDWKAAPLL-ACATSEQAAAPVLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAE 703
Cdd:cd07125 13 EVPLEALADALKAFDEKEWEAIPIInGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 704 RAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRNDN------------CRPLGPVV 771
Cdd:cd07125 93 RAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPElpgptgelngleLHGRGVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 772 CISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMF 851
Cdd:cd07125 173 CISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 852 TGSTEVARLLQRNIAGRldnQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRV 931
Cdd:cd07125 253 TGSTETAKLINRALAER---DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 932 IEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVYQVAIADGaevkRGTFVMPTLIELESFDELQ 1011
Cdd:cd07125 330 IEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDG----NGYFVAPGIIEIVGIFDLT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1012 REIFGPVLHVVRYNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGT 1091
Cdd:cd07125 406 TEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGT 485
|
490
....*....|....*..
gi 2063477733 1092 GPKAGGPLYLYRLLSTR 1108
Cdd:cd07125 486 GPKAGGPNYLLRFGNEK 502
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
266-567 |
1.08e-154 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 466.97 E-value: 1.08e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 266 ALANASKFESKGFRYSYDMLGEAALTEHDAQKYLASYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMS 345
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 346 ELYPRLLSLTLLAKQYDIGLNIDAEEADRLELSLDLLERLCFEPSLAGWNGIGFVIQAYQKRCPYVIDYVIDLAKRSRHR 425
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 426 LMIRLVKGAYWDSEIKRAQvEGLEGYPVYTRKVYTDVSYIACARKLLAVPEAIYPQFATHNAHTLSAIYTIAGQ-NYYPG 504
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2063477733 505 QYEFQCLHGMGEPLYEQVVGKvaegklNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNR 567
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAA------GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
643-1106 |
5.21e-153 |
|
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: 470.52 E-value: 5.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 643 WKAAPLLA----CATSEQAAapVLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAE 718
Cdd:cd07083 16 GRAYPLVIggewVDTKERMV--SVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 719 IQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARN-------------DLRNDNCRPLGPVVCISPWNFPLAIFSG 785
Cdd:cd07083 94 RRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRlrypavevvpypgEDNESFYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 786 QVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNI 865
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 866 AGRLDNQGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLG 945
Cdd:cd07083 254 ARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 946 NPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVYQVAIADGAevkrGTFVMPTLIELESFDE--LQREIFGPVLHVVR 1023
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGE----GYFVAPTVVEEVPPKAriAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1024 YNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1103
Cdd:cd07083 410 YKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRR 489
|
...
gi 2063477733 1104 LLS 1106
Cdd:cd07083 490 FLE 492
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
660-1102 |
2.21e-135 |
|
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: 424.33 E-value: 2.21e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07124 49 ESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQARnDLR---------NDN---CRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:cd07124 129 DVAEAIDFLEYYAREML-RLRgfpvemvpgEDNryvYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 808 IAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVA-RLLQRniAGRLD-NQGRPIPLIAETGGQ 885
Cdd:cd07124 208 IAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlRIYER--AAKVQpGQKWLKRVIAEMGGK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 886 NAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAG 965
Cdd:cd07124 286 NAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 966 IEKHIQGMRDKGRSVYQVAIADGAEvkRGTFVMPTLIE-LESFDEL-QREIFGPVLHVVRYnrKNLDQLIEQINASGYGL 1043
Cdd:cd07124 366 IRRYIEIGKSEGRLLLGGEVLELAA--EGYFVQPTIFAdVPPDHRLaQEEIFGPVLAVIKA--KDFDEALEIANDTEYGL 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2063477733 1044 TLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1102
Cdd:cd07124 442 TGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLL 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
652-1097 |
8.18e-133 |
|
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: 416.45 E-value: 8.18e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 652 ATSEQAAAPVLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAG 731
Cdd:COG1012 16 AAASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 732 KTYANAIAEVREAVDFLRYYAVQARN------DLRNDN------CRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:COG1012 95 KPLAEARGEVDRAADFLRYYAGEARRlygetiPSDAPGtrayvrREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 800 KPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLI 879
Cdd:COG1012 175 KPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVID 959
Cdd:COG1012 249 LELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLIS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 960 AEAKAGIEKHIQGMRDKGRSVyqvaIADG--AEVKRGTFVMPTLIEL--ESFDELQREIFGPVLHVVRYnrKNLDQLIEQ 1035
Cdd:COG1012 329 EAQLERVLAYIEDAVAEGAEL----LTGGrrPDGEGGYFVEPTVLADvtPDMRIAREEIFGPVLSVIPF--DDEEEAIAL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1036 INASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGvQPFGGEGLSGTGPKAGG 1097
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
654-1101 |
2.41e-126 |
|
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: 398.44 E-value: 2.41e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 654 SEQAAAPVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKT 733
Cdd:pfam00171 4 SESETIEVINPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 734 YANAIAEVREAVDFLRYYAVQARND----LRNDNCR-------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRLdgetLPSDPGRlaytrrePLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 803 EQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAET 882
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEA 962
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 963 KAGIEKHIQGMRDKGrsvYQVAIADGAEVKRGTFVMPTLIE-LESFDELQR-EIFGPVLHVVRYnrKNLDQLIEQINASG 1040
Cdd:pfam00171 317 LERVLKYVEDAKEEG---AKLLTGGEAGLDNGYFVEPTVLAnVTPDMRIAQeEIFGPVLSVIRF--KDEEEAIEIANDTE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063477733 1041 YGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVqPFGGEGLSGTGpKAGGPLYL 1101
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGL 450
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
685-1108 |
4.34e-118 |
|
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: 375.01 E-value: 4.34e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 685 AVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQAR-------- 756
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARrlhgevip 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 757 ---NDLRNDNCR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGR 832
Cdd:cd07078 83 spdPGELAIVRRePLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 833 GETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAG 912
Cdd:cd07078 163 GDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 913 QRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVyqvaIADGAEVK 992
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKL----LCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 993 R--GTFVMPTLIELESFDEL--QREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMY 1068
Cdd:cd07078 313 GgkGYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVW 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2063477733 1069 VNRNIVGAVVGvQPFGGEGLSGTGpKAGGPLYLYRLLSTR 1108
Cdd:cd07078 391 INDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEEYTEPK 428
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
661-1102 |
1.75e-113 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 365.80 E-value: 1.75e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:PRK03137 54 SINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRYYAVQA-----------RNDLRND-NCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLI 808
Cdd:PRK03137 134 TAEAIDFLEYYARQMlkladgkpvesRPGEHNRyFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVA-RLLQRniAGRL-DNQGRPIPLIAETGGQN 886
Cdd:PRK03137 214 AAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYER--AAKVqPGQIWLKRVIAEMGGKD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSvDIGPVIDAEAkagi 966
Cdd:PRK03137 292 AIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQAS---- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 967 EKHIQGMRDKGRSVYQVAIADGAEVKRGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYnrKNLDQLIEQINASGYGLT 1044
Cdd:PRK03137 367 FDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQPTIFaDVDPKARImQEEIFGPVVAFIKA--KDFDHALEIANNTEYGLT 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2063477733 1045 LGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1102
Cdd:PRK03137 445 GAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
662-1108 |
2.42e-109 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 354.56 E-value: 2.42e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 662 LNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEV 741
Cdd:TIGR01237 51 INPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 742 REAVDFLRYYAVQA--------RNDLRNDNCR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIA 809
Cdd:TIGR01237 131 AEAIDFMEYYARQMielakgkpVNSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 810 AQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGRPIPLIAETGGQNAMI 889
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 890 VDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKH 969
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 970 IQGMRDKGRsvyqVAIADGAEVKRGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGV 1047
Cdd:TIGR01237 371 IEIGKAEGR----LVSGGCGDDSKGYFIGPTIFaDVDRKARLaQEEIFGPVVAFIRA--SDFDEALEIANNTEYGLTGGV 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063477733 1048 HTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTR 1108
Cdd:TIGR01237 445 ISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAK 505
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
656-1098 |
1.85e-97 |
|
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: 320.74 E-value: 1.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 656 QAAAPVLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYA 735
Cdd:cd07097 13 GDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 736 NAIAEVREAVDFLRYYAVQA-----------RNDLRNDNCR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07097 93 EARGEVTRAGQIFRYYAGEAlrlsgetlpstRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 804 QTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRldnqGRPIPLiaETG 883
Cdd:cd07097 173 LTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR----GARVQL--EMG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAK 963
Cdd:cd07097 247 GKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 964 AGIEKHIQGMRDKGRSVyqvaIADGAEVKRGT---FVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQINA 1038
Cdd:cd07097 327 EKDLRYIEIARSEGAKL----VYGGERLKRPDegyYLAPALFAGVTNDMriAREEIFGPVAAVIRV--RDYDEALAIAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1039 SGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVqPFGGEGLSGTGPKAGGP 1098
Cdd:cd07097 401 TEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
689-1108 |
1.63e-93 |
|
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: 305.69 E-value: 1.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 689 AVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQAR--------NDLR 760
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADklggpelpSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 761 NDNC----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETV 836
Cdd:cd06534 83 GGEAyvrrEPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 837 GAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCS 916
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 917 ALRVLCLQEDSADRVIEMLKGamaesrlgnperLSVDIGPvidaeakagiekhiqgmrdkgrsvyqvaiadgaevkrgtf 996
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVT------------VLVDVDP---------------------------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 997 vmptlieleSFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGA 1076
Cdd:cd06534 265 ---------DMPIAQEEIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV 333
|
410 420 430
....*....|....*....|....*....|..
gi 2063477733 1077 VVGvQPFGGEGLSGTGpKAGGPLYLYRLLSTR 1108
Cdd:cd06534 334 GPE-APFGGVKNSGIG-REGGPYGLEEYTRTK 363
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
661-1092 |
9.00e-92 |
|
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: 303.97 E-value: 9.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:cd07103 1 VINPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRYYAVQARND------LRNDNCR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLI 808
Cdd:cd07103 80 VDYAASFLEWFAEEARRIygrtipSPAPGKRilvikqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAM 888
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 889 IVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLClQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 968 KHIQGMRDKGRsvyQVAIADGAEVKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTL 1045
Cdd:cd07103 313 ALVEDAVAKGA---KVLTGGKRLGLGGYFYEPTVLTdvTDDMLIMNEETFGPVAPIIPF--DTEDEVIARANDTPYGLAA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2063477733 1046 GVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVvgVQPFGGEGLSGTG 1092
Cdd:cd07103 388 YVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
661-1096 |
6.62e-90 |
|
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: 299.86 E-value: 6.62e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRDVVGqVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:cd07086 17 SRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDfLRYYAV-QAR-------------NDLRnDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:cd07086 96 VQEMID-ICDYAVgLSRmlygltipserpgHRLM-EQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 807 LIAAQAVRLLLEA----GIPEGVLQLLPGRGEtVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqGRPiplIAET 882
Cdd:cd07086 174 LTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRV---LLEL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07086 247 GGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 963 KAGIEKHIQGMRDKGRSVyqvaIADGAEVKR---GTFVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQIN 1037
Cdd:cd07086 327 VEKYLNAIEIAKSQGGTV----LTGGKRIDGgepGNYVEPTIVTGVTDDAriVQEETFAPILYVIKF--DSLEEAIAINN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063477733 1038 ASGYGLTLGVHTRIDETIAKVVGN--VNAGNMYVNRNIVGAVVGVqPFGGEGLSGTGPKAG 1096
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
662-1098 |
4.51e-89 |
|
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: 297.34 E-value: 4.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 662 LNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEV 741
Cdd:cd07131 19 RNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 742 REAVDFLRYYAVQAR--------NDLRNDNC----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIA 809
Cdd:cd07131 99 QEAIDMAQYAAGEGRrlfgetvpSELPNKDAmtrrQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 810 AQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRnIAGRLdnqGRPIPLiaETGGQNAMI 889
Cdd:cd07131 179 LKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE-TCARP---NKRVAL--EMGGKNPII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 890 VDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKH 969
Cdd:cd07131 253 VMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 970 IQGMRDKGRSV-YQVAIADGAEVKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLG 1046
Cdd:cd07131 333 NEIGKEEGATLlLGGERLTGGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEV--SSLEEAIEIANDTEYGLSSA 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1047 VHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVqPFGGEGLSGTGPKAGGP 1098
Cdd:cd07131 411 IYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
660-1108 |
1.05e-82 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 279.15 E-value: 1.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07088 16 DVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQAR--------NDLRNDNC----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:cd07088 95 EVEFTADYIDYMAEWARriegeiipSDRPNENIfifkVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 808 IAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNA 887
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVSLELGGKAP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKagie 967
Cdd:cd07088 249 AIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAAL---- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 968 KHIQGMRDKgrsvyqvAIADGAEV---------KRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYNrkNLDQLIEQI 1036
Cdd:cd07088 325 DKVEEMVER-------AVEAGATLltggkrpegEKGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKFS--SLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1037 NASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQpfGGEGLSGTGpKAGGPLYLYRLLSTR 1108
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLG-GADGKHGLEEYLQTK 464
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
661-1108 |
1.19e-80 |
|
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: 275.23 E-value: 1.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQP-LMGLLVREAGKTYANA-I 738
Cdd:cd07123 50 QVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYeLNAATMLGQGKNVWQAeI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 739 AEVREAVDFLR---YYAVQ------------ARNDLRNdncRPL-GPVVCISPWNFPlAIfSGQVAAALA-AGNPVLAKP 801
Cdd:cd07123 130 DAACELIDFLRfnvKYAEElyaqqplsspagVWNRLEY---RPLeGFVYAVSPFNFT-AI-GGNLAGAPAlMGNVVLWKP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 802 AEqTPLIAAQAV-RLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQgRPIP-LI 879
Cdd:cd07123 205 SD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRY-RTYPrIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVID 959
Cdd:cd07123 283 GETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVID 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 960 AEAKAGIEKHIqgmrDKGRSVYQVAIADGAEV--KRGTFVMPTLIELE--SFDELQREIFGPVLHVVRYNRKNLDQLIEQ 1035
Cdd:cd07123 363 EKAFDRIKGYI----DHAKSDPEAEIIAGGKCddSVGYFVEPTVIETTdpKHKLMTEEIFGPVLTVYVYPDSDFEETLEL 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2063477733 1036 IN-ASGYGLTLGVHTRiDETIAKVVGNV---NAGNMYVNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTR 1108
Cdd:cd07123 439 VDtTSPYALTGAIFAQ-DRKAIREATDAlrnAAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPR 514
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
660-1092 |
6.04e-80 |
|
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: 271.01 E-value: 6.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07149 2 EVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQARN--------------------DLRndncRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRlagetipfdaspggegrigfTIR----EPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 800 KPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRnIAGRldnqgRPIPLi 879
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIAR-KAGL-----KKVTL- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 880 aETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVI 958
Cdd:cd07149 230 -ELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 959 DAEAKAGIEKHIQGmrdkgrsvyqvAIADGAEV-----KRGTFVMPTLieLESFDELQR----EIFGPVLHVVRYnrKNL 1029
Cdd:cd07149 308 SEAEAERIEEWVEE-----------AVEGGARLltggkRDGAILEPTV--LTDVPPDMKvvceEVFAPVVSLNPF--DTL 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2063477733 1030 DQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07149 373 DEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
660-1092 |
9.78e-79 |
|
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: 268.29 E-value: 9.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQAT-PPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAI 738
Cdd:cd07082 19 EVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 739 AEVREAVDFLRYyAVQARNDLRNDNCR-----------------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKP 801
Cdd:cd07082 98 KEVDRTIDYIRD-TIEELKRLDGDSLPgdwfpgtkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 802 AEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRnIAGRLdnqgrpiPLIAE 881
Cdd:cd07082 177 ATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK-QHPMK-------RLVLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDaE 961
Cdd:cd07082 249 LGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLID-P 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 962 AKAgieKHIQGMRDKgrsvyqvAIADGAEV------KRGTFVMPTLIELESfDELQ---REIFGPVLHVVRYNrkNLDQL 1032
Cdd:cd07082 328 KSA---DFVEGLIDD-------AVAKGATVlngggrEGGNLIYPTLLDPVT-PDMRlawEEPFGPVLPIIRVN--DIEEA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2063477733 1033 IEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVN----RNIvgavvGVQPFGGEGLSGTG 1092
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIG 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
661-1096 |
2.47e-78 |
|
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: 266.34 E-value: 2.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNA--APIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAI 738
Cdd:cd07114 1 SINPATGE-PWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 739 AEVREAVDFLRYYAVQA-----------RNDLRNDNCR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:cd07114 80 AQVRYLAEWYRYYAGLAdkiegavipvdKGDYLNFTRRePLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 807 LIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQN 886
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGI 966
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 967 EKHIQGMRDKG-RSVYQVAIADGAEVKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQINASGYGL 1043
Cdd:cd07114 314 ERYVARAREEGaRVLTGGERPSGADLGAGYFFEPTILADVTNDMriAQEEVFGPVLSVIPF--DDEEEAIALANDSEYGL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2063477733 1044 TLGVHTRiDETIA-KVVGNVNAGNMYVN--RnivgAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:cd07114 392 AAGIWTR-DLARAhRVARAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
661-1092 |
5.05e-78 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 265.58 E-value: 5.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA- 739
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYA----------VQARNDLRNDNCR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLI 808
Cdd:cd07093 80 DIPRAAANFRFFAdyilqldgesYPQDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAM 888
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEakagiek 968
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 969 HiqgmRDKGRSVYQVAIADGAEV------------KRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYNRKnlDQLIE 1034
Cdd:cd07093 307 H----LEKVLGYVELARAEGATIltgggrpelpdlEGGYFVEPTVITGLDNDSrvAQEEIFGPVVTVIPFDDE--EEAIE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2063477733 1035 QINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVvgVQPFGGEGLSGTG 1092
Cdd:cd07093 381 LANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDL--RTPFGGVKASGIG 436
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
659-1092 |
8.61e-76 |
|
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: 259.20 E-value: 8.61e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 659 APVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAI 738
Cdd:cd07145 1 IEVRNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 739 AEVREAVDFLRYYAVQARnDLRNDNCR-----------------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKP 801
Cdd:cd07145 80 VEVERTIRLFKLAAEEAK-VLRGETIPvdayeynerriaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 802 AEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAE 881
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKK------VALE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAE 961
Cdd:cd07145 233 LGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 962 AKAGIEKHIQGMRDKGRSVYQvaiadGAEVKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQINAS 1039
Cdd:cd07145 313 AVERMENLVNDAVEKGGKILY-----GGKRDEGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKV--KDDEEAVEIANST 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2063477733 1040 GYGLTLGVHTRidetiakvvgNVNAGnMYVNRNI-VGAVV---------GVQPFGGEGLSGTG 1092
Cdd:cd07145 386 EYGLQASVFTN----------DINRA-LKVARELeAGGVVindstrfrwDNLPFGGFKKSGIG 437
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
681-1098 |
8.09e-74 |
|
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: 252.84 E-value: 8.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 681 DASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARN--- 757
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 758 -DLRND-----NC---RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP-----LIAaqavRLLLEAGIPE 823
Cdd:cd07104 81 eILPSDvpgkeSMvrrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 824 GVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRnIAGRLdnqgrpIPLIA-ETGGQNAMIVDSSALTEQVVID 902
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGE-LAGRH------LKKVAlELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 903 VVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGmrdkgrsvy 981
Cdd:cd07104 230 AAFGAFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVED--------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 982 qvAIADGAEVK-----RGTFVMPTLI-----ELESFDElqrEIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRI 1051
Cdd:cd07104 300 --AVAAGARLLtggtyEGLFYQPTVLsdvtpDMPIFRE---EIFGPVAPVIPF--DDDEEAVELANDTEYGLSAAVFTRD 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2063477733 1052 DETIAKVVGNVNAGNMYVNRNIV--GAVVgvqPFGGEGLSGTGpKAGGP 1098
Cdd:cd07104 373 LERAMAFAERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
661-1092 |
2.16e-73 |
|
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: 252.15 E-value: 2.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPI-WQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07109 1 VFDPSTGE-VFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYA-----VQARNDLRNDNC------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLI 808
Cdd:cd07109 80 DVEAAARYFEYYGgaadkLHGETIPLGPGYfvytvrEPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAM 888
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPErLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 969 HIQGMRDKG-RSVYQVAIADGAEVKrGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTL 1045
Cdd:cd07109 313 FVARARARGaRIVAGGRIAEGAPAG-GYFVAPTLLdDVPPDSRLaQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2063477733 1046 GVHTRIDETIAKVVGNVNAGNMYVNRniVGAVVGVQ-PFGGEGLSGTG 1092
Cdd:cd07109 390 GVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
670-1092 |
2.70e-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: 252.14 E-value: 2.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 670 VVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLR 749
Cdd:cd07099 8 VLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 750 YYA-----------VQARNDLRNDNC----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVR 814
Cdd:cd07099 88 WAArnaprvlaprkVPTGLLMPNKKAtveyRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 815 LLLEAGIPEGVLQLLPGRGETvGAGLVgDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:cd07099 168 AWAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGSVATGRKVMAAAAERL------IPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMR 974
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 975 DKGrsvyQVAIADGAEV-KRGTFVMPTLI--ELESFDELQREIFGPVLHVVRYNrkNLDQLIEQINASGYGLTLGVHTRI 1051
Cdd:cd07099 320 AKG----AKALTGGARSnGGGPFYEPTVLtdVPHDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2063477733 1052 DETIAKVVGNVNAGNMYVNRNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
660-1096 |
7.09e-73 |
|
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: 251.36 E-value: 7.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPI--WQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTY-AN 736
Cdd:cd07091 22 PTINPATE-EVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLeES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 737 AIAEVREAVDFLRYYA-----VQARNDLRNDNC------RPLGpvVC--ISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07091 101 AKGDVALSIKCLRYYAgwadkIQGKTIPIDGNFlaytrrEPIG--VCgqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 804 QTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPIPLiaETG 883
Cdd:cd07091 179 QTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAA---KSNLKKVTL--ELG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKgAMAESR-LGNPERLSVDIGPVIDAEA 962
Cdd:cd07091 254 GKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFK-ARAEKRvVGDPFDPDTFQGPQVSKAQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 963 KAGIEKHIQGMRDKGRSVyqvaIADGAEV-KRGTFVMPTLielesF----DEL---QREIFGPVLHVVRYnrKNLDQLIE 1034
Cdd:cd07091 333 FDKILSYIESGKKEGATL----LTGGERHgSKGYFIQPTV-----FtdvkDDMkiaKEEIFGPVVTILKF--KTEDEVIE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2063477733 1035 QINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNR-NIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
684-1090 |
1.07e-72 |
|
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: 249.50 E-value: 1.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 684 NAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGK------TYANA-IAEVREAVDFLRYYAVQAR 756
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKplweaqTEVAAmAGKIDISIKAYHERTGERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 757 NDLRNDNC----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGR 832
Cdd:cd07095 84 TPMAQGRAvlrhRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 833 GETvGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQgrpipLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAG 912
Cdd:cd07095 164 RET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 913 QRCSALRVLCLQEDS-ADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHiqgmrdkgrsvYQVAIADGAE- 990
Cdd:cd07095 238 QRCTCARRLIVPDGAvGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLA-----------QQDLLALGGEp 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 991 -------VKRGTFVMPTLIELESFDELQ-REIFGPVLHVVRYNrkNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNV 1062
Cdd:cd07095 307 llamerlVAGTAFLSPGIIDVTDAADVPdEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDDEALFERFLARI 384
|
410 420
....*....|....*....|....*...
gi 2063477733 1063 NAGNMYVNRNIVGAvVGVQPFGGEGLSG 1090
Cdd:cd07095 385 RAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
661-1092 |
1.38e-72 |
|
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: 249.75 E-value: 1.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSdHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:cd07106 1 VINPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRYYAVQARNDLR---NDNCR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQ 811
Cdd:cd07106 80 VGGAVAWLRYTASLDLPDEViedDDTRRvelrrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 812 AVRLLLEAgIPEGVLQLLPGRGEtVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNAMIVD 891
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 892 SSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQ 971
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 972 GMRDKGrsvYQVAIADGAEVKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHT 1049
Cdd:cd07106 312 DAKAKG---AKVLAGGEPLDGPGYFIPPTIVDdpPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVWS 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2063477733 1050 RiDETIAKVVGN-VNAGNMYVNRNivGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07106 387 S-DLERAEAVARrLEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
661-1092 |
1.64e-72 |
|
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: 249.66 E-value: 1.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:cd07094 3 VHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRYYAVQARN----------DLRNDNCR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07094 82 VDRAIDTLRLAAEEAERirgeeipldaTQGSDNRLawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 805 TPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRldnqgrpiPLIAETGG 884
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGK--------RIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 965 GIEKHIQGmrdkgrsvyqvAIADGAEV-----KRGTFVMPTLIELESFDELQR--EIFGPVLHVVRYNrkNLDQLIEQIN 1037
Cdd:cd07094 314 RVERWVEE-----------AVEAGARLlcggeRDGALFKPTVLEDVPRDTKLSteETFGPVVPIIRYD--DFEEAIRIAN 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2063477733 1038 ASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVgAVVGVQPFGGEGLSGTG 1092
Cdd:cd07094 381 STDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
658-1092 |
2.28e-72 |
|
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: 250.13 E-value: 2.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 658 AAPVLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANA 737
Cdd:cd07085 17 WLDVYNPATGE-VIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 738 IAEVR---EAVDF--------LRYYAVQARNDLRNDNCR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQT 805
Cdd:cd07085 96 RGDVLrglEVVEFacsiphllKGEYLENVARGIDTYSYRqPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 806 PLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAgLVGDERVKGVMFTGSTEVARLLQRNIAgrldNQGRPIplIAETGGQ 885
Cdd:cd07085 176 PGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYERAA----ANGKRV--QALGGAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 886 NAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAG 965
Cdd:cd07085 249 NHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKER 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 966 IEKHIQGMRDKGRSVyqvaIADGAEVK-----RGTFVMPTLI-----ELESFDElqrEIFGPVLHVVRYnrKNLDQLIEQ 1035
Cdd:cd07085 329 IEGLIESGVEEGAKL----VLDGRGVKvpgyeNGNFVGPTILdnvtpDMKIYKE---EIFGPVLSIVRV--DTLDEAIAI 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2063477733 1036 INASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIvgAV-VGVQPFGGEGLSGTG 1092
Cdd:cd07085 400 INANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPI--PVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
661-1096 |
2.58e-72 |
|
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: 249.28 E-value: 2.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANA-IA 739
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYA----------VQARNDLRNDNCR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLI 808
Cdd:cd07115 80 DVPRAADTFRYYAgwadkiegevIPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGGQNAM 888
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKR------VSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 969 HIQGMRDKGRSVYQVAIADGAevkRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLG 1046
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGA---RGFFVEPTIFAAVPPEMriAQEEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1047 VHTRIDETIAKVVGNVNAGNMYVnrNIVGAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:cd07115 389 VWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
660-1098 |
4.71e-72 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 248.40 E-value: 4.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07150 2 DDLNPADG-SVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQARN----DLRNDNC--------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:cd07150 81 ETTFTPELLRAAAGECRRvrgeTLPSDSPgtvsmsvrRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 808 IAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVArllqRNIAGRLDNQGRPIPLiaETGGQNA 887
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRHLKKITL--ELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 968 KHIQGMRDKGrsvyqVAIADGAEVKrGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTL 1045
Cdd:cd07150 315 RQVEDAVAKG-----AKLLTGGKYD-GNFYQPTVLTdvTPDMRIFREETFGPVTSVIPA--KDAEEALELANDTEYGLSA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2063477733 1046 GVHTRiDETIA-KVVGNVNAGNMYVNRNIV--GAVVgvqPFGGEGLSGTGpKAGGP 1098
Cdd:cd07150 387 AILTN-DLQRAfKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGE 437
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
661-1092 |
1.78e-71 |
|
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: 247.16 E-value: 1.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIW-QATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07089 1 VINPATE-EVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 -EVREAVDFLRYYAVQARNDLRNDNC----------------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPA 802
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSFPWEFDLpvpalrggpgrrvvrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 803 EQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaET 882
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 963 KAGIEKHIQGMRDKG-RSVYQVAIADGAEVkrGTFVMPTLielesFDEL-------QREIFGPVLHVVRYnrKNLDQLIE 1034
Cdd:cd07089 314 RDRVEGYIARGRDEGaRLVTGGGRPAGLDK--GFYVEPTL-----FADVdndmriaQEEIFGPVLVVIPY--DDDDEAVR 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1035 QINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNrnivGAVVGV--QPFGGEGLSGTG 1092
Cdd:cd07089 385 IANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
661-1095 |
9.70e-71 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 244.96 E-value: 9.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSdHRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTY-ANAIA 739
Cdd:cd07108 1 VINPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYA----------VQARNDLRNDNCR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLi 808
Cdd:cd07108 80 EAAVLADLFRYFGglagelkgetLPFGPDVLTYTVRePLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAM 888
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 889 IVDSSALTEQVVIDVVSSA-FDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 968 KHIqgmrDKGRSVYQVAIADGAE------VKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINAS 1039
Cdd:cd07108 313 GYI----DLGLSTSGATVLRGGPlpgegpLADGFFVQPTIFSgvDNEWRLAREEIFGPVLCAIPW--KDEDEVIAMANDS 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2063477733 1040 GYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNiVGAVVGvQPFGGEGLSGTGPKA 1095
Cdd:cd07108 387 HYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
661-1096 |
1.11e-69 |
|
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: 241.49 E-value: 1.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPiwqATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:cd07146 3 VRNPYTG-EVVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRYYAVQARND----LRNDN-----------CR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07146 79 VGRAADVLRFAAAEALRDdgesFSCDLtangkarkiftLRePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 805 TPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRldnqgrpiPLIAETGG 884
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 965 GIEKHIQGmrdkgrsvyqvAIADGAEV-----KRGTFVMPTLIELESFD-EL-QREIFGPVLHVVRYnrKNLDQLIEQIN 1037
Cdd:cd07146 311 QIENRVEE-----------AIAQGARVllgnqRQGALYAPTVLDHVPPDaELvTEETFGPVAPVIRV--KDLDEAIAISN 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2063477733 1038 ASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNrNIVGAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:cd07146 378 STAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
660-1092 |
2.69e-69 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 240.97 E-value: 2.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHRdVVGQVQEASVADASNAVQCAVNA--APIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANA 737
Cdd:cd07112 5 ATINPATGR-VLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 738 IA-EVREAVDFLRYY-----------AVQARNDL----RNdncrPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKP 801
Cdd:cd07112 84 LAvDVPSAANTFRWYaeaidkvygevAPTGPDALalitRE----PLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 802 AEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPIPLiaE 881
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSG---QSNLKRVWL--E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 882 TGGQNAMIV-DSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDA 960
Cdd:cd07112 235 CGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 961 EAKAGIEKHIQGMRDKGRSVYQVAIADGAEVKrGTFVMPTLielesFDEL-------QREIFGPVLHVVRYNrkNLDQLI 1033
Cdd:cd07112 315 AHFDKVLGYIESGKAEGARLVAGGKRVLTETG-GFFVEPTV-----FDGVtpdmriaREEIFGPVLSVITFD--SEEEAV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2063477733 1034 EQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVnrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07112 387 ALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
660-1097 |
8.98e-69 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 239.80 E-value: 8.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07130 15 TSISPANGE-PIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQAR------------NDLRNDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:cd07130 94 EVQEMIDICDFAVGLSRqlygltipserpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 808 --IAAQAV--RLLLEAGIPEGVLQLLPGRGEtVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqGRpipLIAETG 883
Cdd:cd07130 174 taIAVTKIvaRVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---GR---SLLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAK 963
Cdd:cd07130 247 GNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 964 AGIEKHIQGMRDKGRSVyqvaIADGAEVKR-GTFVMPTLIELESFDEL-QREIFGPVLHVVRYnrKNLDQLIEQINASGY 1041
Cdd:cd07130 327 DNYLAAIEEAKSQGGTV----LFGGKVIDGpGNYVEPTIVEGLSDAPIvKEETFAPILYVLKF--DTLEEAIAWNNEVPQ 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2063477733 1042 GLTLGVHTRIDETIAKVVGNVNAGNMYVNRNI--VGAVVGvQPFGGEGLSGTGPKAGG 1097
Cdd:cd07130 401 GLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIgtSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
660-1092 |
9.42e-68 |
|
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: 236.63 E-value: 9.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAG--KTYANA 737
Cdd:cd07138 17 DVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGapITLARA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 738 iAEVREAVDFLRYYAVQARN---DLRNDNCR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAA 810
Cdd:cd07138 96 -AQVGLGIGHLRAAADALKDfefEERRGNSLvvrePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 811 QAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGGQNAMIV 890
Cdd:cd07138 175 ILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKR------VALELGGKSANII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 891 DSSALTEQVVIDVVSSAFDSAGQRCSAL-RVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKagieKH 969
Cdd:cd07138 249 LDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQF----DR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 970 IQGMRDKGrsvyqvaIADGAEV-----------KRGTFVMPTLielesFDEL-------QREIFGPVLHVVRYNrkNLDQ 1031
Cdd:cd07138 324 VQGYIQKG-------IEEGARLvaggpgrpeglERGYFVKPTV-----FADVtpdmtiaREEIFGPVLSIIPYD--DEDE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1032 LIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNrnivGAVVGVQ-PFGGEGLSGTG 1092
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
651-1092 |
1.72e-67 |
|
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: 236.05 E-value: 1.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 651 CATSEQAAAPVLNPSDhRDVVGQVQEASVADASNAVQCAVNA--APIWQATPPAERAAILERAADLMEAEIQPLMGLLVR 728
Cdd:cd07119 7 VEAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 729 EAGKTYANAIAEVREAVDFLRYYAVQARNDL-----RNDNC------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07119 86 NTGKTLRESEIDIDDVANCFRYYAGLATKETgevydVPPHVisrtvrEPVGVCGLITPWNYPLLQAAWKLAPALAAGNTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 798 LAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpIP 877
Cdd:cd07119 166 VIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK----VA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 878 LiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPV 957
Cdd:cd07119 242 L--ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 958 IDAEAKAGIEKHIQ-GMRDKGRSVYQVAIADGAEVKRGTFVMPTLielesFDELQR-------EIFGPVLHVVRYnrKNL 1029
Cdd:cd07119 320 VSAEHREKVLSYIQlGKEEGARLVCGGKRPTGDELAKGYFVEPTI-----FDDVDRtmrivqeEIFGPVLTVERF--DTE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2063477733 1030 DQLIEQINASGYGLTLGVHTRiDETIA-KVVGNVNAGNMYVNRniVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTK-DIARAnRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
669-1098 |
3.08e-67 |
|
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: 234.11 E-value: 3.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 669 DVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFL 748
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 749 RYYA---VQARNDL------RNDNCR--PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP-----LIAaqa 812
Cdd:cd07152 82 HEAAglpTQPQGEIlpsapgRLSLARrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggvVIA--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 813 vRLLLEAGIPEGVLQLLPGRGEtVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNAMIVDS 892
Cdd:cd07152 159 -RLFEEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHL----KKVSL--ELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 893 SALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQ 971
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 972 GMRDKGRSVYQVAIADGAevkrgtFVMPTLI-----ELESFDElqrEIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLG 1046
Cdd:cd07152 310 DSVAAGARLEAGGTYDGL------FYRPTVLsgvkpGMPAFDE---EIFGPVAPVTVF--DSDEEAVALANDTEYGLSAG 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1047 VHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVgVQPFGGEGLSGTGPKAGGP 1098
Cdd:cd07152 379 IISRDVGRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
660-1096 |
3.16e-66 |
|
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: 232.38 E-value: 3.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNA---APiWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYAN 736
Cdd:cd07142 22 PTIDPRNG-EVIAHVAEGDAEDVDRAVKAARKAfdeGP-WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 737 A-IAEVREAVDFLRYYAVQARN----DLRNDNC-------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07142 100 ArYAEVPLAARLFRYYAGWADKihgmTLPADGPhhvytlhEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 805 TPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPIPLiaETGG 884
Cdd:cd07142 180 TPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA---KSNLKPVTL--ELGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKA 964
Cdd:cd07142 255 KSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 965 GIEKHIQGMRDKGRSVyqvaIADGAEV-KRGTFVMPTLIELESFDEL--QREIFGPVLHVVRYnrKNLDQLIEQINASGY 1041
Cdd:cd07142 335 KILSYIEHGKEEGATL----ITGGDRIgSKGYYIQPTIFSDVKDDMKiaRDEIFGPVQSILKF--KTVDEVIKRANNSKY 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2063477733 1042 GLTLGVHTRIDETIAKVVGNVNAGNMYVN-RNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07142 409 GLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
669-1096 |
3.26e-66 |
|
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: 231.81 E-value: 3.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 669 DVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFL 748
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 749 RYYAVQARNDLR--------------NDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVR 814
Cdd:cd07101 87 RYYARRAERLLKprrrrgaipvltrtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 815 LLLEAGIPEGVLQLLPGRGETVGAGLVgdERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:cd07101 167 LLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMR 974
Cdd:cd07101 239 DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 975 DKGRSVyqvaIADG-AEVKRGT-FVMPTLI-----ELESFDElqrEIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGV 1047
Cdd:cd07101 319 AKGATV----LAGGrARPDLGPyFYEPTVLtgvteDMELFAE---ETFGPVVSIYRV--ADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1048 HTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQ-PFGGEGLSGTGPKAG 1096
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
660-1092 |
3.14e-65 |
|
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: 228.67 E-value: 3.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07147 2 EVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQARN----------DLRNDNCR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07147 81 EVARAIDTFRIAAEEATRiygevlpldiSARGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 804 QTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETvGAGLVGDERVKGVMFTGSTEVARLLqRNIAGRldnqgRPIPLiaETG 883
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-----KKVVL--ELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEA 962
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 963 KAGIEKHIQGmrdkgrsvyqvAIADGAEV-----KRGTFVMPTLIE-LESFDELQR-EIFGPVLHVVRYNRknLDQLIEQ 1035
Cdd:cd07147 311 AERVEGWVNE-----------AVDAGAKLltggkRDGALLEPTILEdVPPDMEVNCeEVFGPVVTVEPYDD--FDEALAA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2063477733 1036 INASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07147 378 VNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIN-DVPTFRVDHMPYGGVKDSGIG 433
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
650-1092 |
6.64e-65 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 228.64 E-value: 6.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 650 ACATSEQAAAPVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVRE 729
Cdd:PRK13473 10 ELVAGEGEKQPVYNPATG-EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 730 AGKTYANAIA-EVREAVDFLRYYAVQARN---------------DLRNDncrPLGPVVCISPWNFPLAIFSGQVAAALAA 793
Cdd:PRK13473 89 CGKPLHLALNdEIPAIVDVFRFFAGAARClegkaageyleghtsMIRRD---PVGVVASIAPWNYPLMMAAWKLAPALAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 794 GNPVLAKPAEQTPLIAAQAVRLLLEAgIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqg 873
Cdd:PRK13473 166 GNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKR-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 874 rpipLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVD 953
Cdd:PRK13473 243 ----THLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 954 IGPVIDAEAKAgiekHIQGMRDKGRSVYQVAIADGAEV--KRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNL 1029
Cdd:PRK13473 319 LGPLISAAHRD----RVAGFVERAKALGHIRVVTGGEApdGKGYYYEPTLLAgaRQDDEIVQREVFGPVVSVTPF--DDE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2063477733 1030 DQLIEQINASGYGLTLGVHTRiDETIA-KVVGNVNAGNMYVNRNIVgaVVGVQPFGGEGLSGTG 1092
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTR-DVGRAhRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
661-1092 |
1.62e-64 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 226.44 E-value: 1.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA- 739
Cdd:cd07092 1 VVDPATGE-EIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQAR---------------NDLRNDncrPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07092 80 ELPGAVDNFRFFAGAARtlegpaageylpghtSMIRRE---PIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 805 TPLIAAQAVRLLLEaGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGG 884
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR------VHLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAK 963
Cdd:cd07092 230 KAPVIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 964 AGIEKHIQGMRDKGRSVYQVAIADGaevkRGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYnrKNLDQLIEQINASGY 1041
Cdd:cd07092 309 ERVAGFVERAPAHARVLTGGRRAEG----PGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPF--DDEDEAIELANDVEY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2063477733 1042 GLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVgaVVGVQPFGGEGLSGTG 1092
Cdd:cd07092 383 GLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
667-1096 |
3.29e-64 |
|
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: 225.68 E-value: 3.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 667 HRDVVGQVQEASVADASNAVQ---CAVNAAPiWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVRE 743
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAaarKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 744 AVDFLRYYAVQAR-------NDLRNDNC-----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQ 811
Cdd:cd07118 85 AADLWRYAASLARtlhgdsyNNLGDDMLglvlrEPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 812 AVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGrpipliAETGGQNAMIVD 891
Cdd:cd07118 165 LAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 892 SSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQ 971
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 972 GMRDKGRSVyqVAIADGAEVKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHT 1049
Cdd:cd07118 319 AGRAEGATL--LLGGERLASAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWS 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2063477733 1050 RIDETIAKVVGNVNAGNMYVNRNIVGAVvgVQPFGGEGLSGTGPKAG 1096
Cdd:cd07118 395 KDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
660-1092 |
2.56e-63 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 224.57 E-value: 2.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:PLN02278 43 PVYNPATG-EVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQARN---DL---RNDNCR------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKRvygDIipsPFPDRRllvlkqPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 808 IAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGGQNA 887
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKR------VSLELGGNAP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 888 MIVDSSALTEQVVIDVVSSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGI 966
Cdd:PLN02278 276 FIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 967 EKHIQGmrdkgrsvyqvAIADGAEV----KR----GTFVMPTLIELESFDEL--QREIFGPVLHVVRYnrKNLDQLIEQI 1036
Cdd:PLN02278 355 ESHVQD-----------AVSKGAKVllggKRhslgGTFYEPTVLGDVTEDMLifREEVFGPVAPLTRF--KTEEEAIAIA 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2063477733 1037 NASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGvqPFGGEGLSGTG 1092
Cdd:PLN02278 422 NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
660-1096 |
7.06e-63 |
|
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: 222.99 E-value: 7.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNA----APiWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYA 735
Cdd:cd07141 25 PTINPATG-EKICEVQEGDKADVDKAVKAARAAfklgSP-WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 736 NA-IAEVREAVDFLRYYAVQArnDLRNDNCRPLG----------PV-VC--ISPWNFPLAIFSGQVAAALAAGNPVLAKP 801
Cdd:cd07141 103 KSyLVDLPGAIKVLRYYAGWA--DKIHGKTIPMDgdfftytrhePVgVCgqIIPWNFPLLMAAWKLAPALACGNTVVLKP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 802 AEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNiAGRlDNQGRpipLIAE 881
Cdd:cd07141 181 AEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA-AGK-SNLKR---VTLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADrviEMLKGAM--AESR-LGNPERLSVDIGPVI 958
Cdd:cd07141 256 LGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYD---EFVKRSVerAKKRvVGNPFDPKTEQGPQI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 959 DAEAKAGIEKHIQGMRDKGRsvyQVAIADGAEVKRGTFVMPTLielesFDELQ-------REIFGPVLHVVRYnrKNLDQ 1031
Cdd:cd07141 333 DEEQFKKILELIESGKKEGA---KLECGGKRHGDKGYFIQPTV-----FSDVTddmriakEEIFGPVQQIFKF--KTIDE 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2063477733 1032 LIEQINASGYGLTLGVHTR-IDETIaKVVGNVNAGNMYVNrniVGAVVGVQ-PFGGEGLSGTGPKAG 1096
Cdd:cd07141 403 VIERANNTTYGLAAAVFTKdIDKAI-TFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
661-1092 |
1.34e-62 |
|
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: 221.10 E-value: 1.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:cd07107 1 VINPATGQ-VLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRYYAVQArNDLRNDNC------------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLI 808
Cdd:cd07107 80 VMVAAALLDYFAGLV-TELKGETIpvggrnlhytlrEPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEAgIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrpiPLIAETGGQNAM 888
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 889 IVDSSALTEQVVIDVVSSA-FDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIE 967
Cdd:cd07107 232 IVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 968 KHIQGMRDKG-RSVYQVAIADGAEVKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLT 1044
Cdd:cd07107 312 HYIDSAKREGaRLVTGGGRPEGPALEGGFYVEPTVFAdvTPGMRIAREEIFGPVLSVLRW--RDEAEMVAQANGVEYGLT 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2063477733 1045 LGVHTRIDETIAKVVGNVNAGNMYVN---RNIVGAvvgvqPFGGEGLSGTG 1092
Cdd:cd07107 390 AAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
669-1092 |
4.81e-62 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 221.68 E-value: 4.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 669 DVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFL 748
Cdd:PRK09407 43 EPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 749 RYYAVQARNDLRND--------------NCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVR 814
Cdd:PRK09407 123 RYYARRAPKLLAPRrragalpvltktteLRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 815 LLLEAGIPEGVLQLLPGRGETVGAGLVgdERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSA 894
Cdd:PRK09407 203 LLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRL------IGFSLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 895 LTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIqgmR 974
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHV---D 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 975 DkgrsvyqvAIADGAEVKRG---------TFVMPTLI-----ELESFDElqrEIFGPVLHVVRYnrKNLDQLIEQINASG 1040
Cdd:PRK09407 352 D--------AVAKGATVLAGgkarpdlgpLFYEPTVLtgvtpDMELARE---ETFGPVVSVYPV--ADVDEAVERANDTP 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2063477733 1041 YGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQ-PFGGEGLSGTG 1092
Cdd:PRK09407 419 YGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
146-257 |
8.45e-62 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 205.82 E-value: 8.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 146 VQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNESG 225
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 2063477733 226 LTSSLTRIIGKSGEPMIRKGVDMAMRLMGEQF 257
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
661-1098 |
1.11e-61 |
|
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: 218.98 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNA--APIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYA-NA 737
Cdd:cd07139 18 VVSPATEE-VVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISwSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 738 IAEVREAVDFLRYYA--------VQARNDLRNDNCR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQT 805
Cdd:cd07139 97 RAQGPGPAALLRYYAalardfpfEERRPGSGGGHVLvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPET 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 806 PLIA---AQAVRlllEAGIPEGVLQLLPGrGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaET 882
Cdd:cd07139 177 PLDAyllAEAAE---EAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL----ARVTL--EL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 883 GGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSAL-RVLCLQEdSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAE 961
Cdd:cd07139 247 GGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVPRS-RYDEVVEALAAAVAALKVGDPLDPATQIGPLASAR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 962 AKAGIEKHIQGMRDKGrsvYQVAIADG--AEVKRGTFVMPTLI-ELESFDEL-QREIFGPVLHVVRYnrKNLDQLIEQIN 1037
Cdd:cd07139 326 QRERVEGYIAKGRAEG---ARLVTGGGrpAGLDRGWFVEPTLFaDVDNDMRIaQEEIFGPVLSVIPY--DDEDDAVRIAN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1038 ASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNrnivGAVVGVQ-PFGGEGLSGTGpKAGGP 1098
Cdd:cd07139 401 DSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGP 457
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
684-1092 |
1.97e-61 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 216.94 E-value: 1.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 684 NAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRND- 762
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADEp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 763 ----------NCRPLGPVVCISPWNFPLAifsgQV----AAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQL 828
Cdd:cd07100 83 ietdagkayvRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 829 LPGRGETVgAGLVGDERVKGVMFTGST----EVARLLQRNIAgrldnqgrpiPLIAETGGQNAMIVDSSALTEQVVIDVV 904
Cdd:cd07100 159 LLIDSDQV-EAIIADPRVRGVTLTGSEragrAVAAEAGKNLK----------KSVLELGGSDPFIVLDDADLDKAVKTAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 905 SSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIqgmrdkgrsvyQV 983
Cdd:cd07100 228 KGRLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQV-----------EE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 984 AIADGAEV--------KRGTFVMPTLI-----ELESFDElqrEIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTR 1050
Cdd:cd07100 296 AVAAGATLllggkrpdGPGAFYPPTVLtdvtpGMPAYDE---ELFGPVAAVIKV--KDEEEAIALANDSPFGLGGSVFTT 370
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2063477733 1051 IDETIAKVVGNVNAGNMYVNRnIVGAVVGVqPFGGEGLSGTG 1092
Cdd:cd07100 371 DLERAERVARRLEAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
662-1071 |
1.54e-60 |
|
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: 215.19 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 662 LNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEV 741
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 742 REAVDFLRYYAVQARNDLRND------------NCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIA 809
Cdd:cd07102 80 RGMLERARYMISIAEEALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 810 AQAVRLLLEAGIPEGVLQLLPGRGETVGAgLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMI 889
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHETSAA-LIADPRIDHVSFTGSVAGGRAIQRAAAGRF------IKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 890 VDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKH 969
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 970 IQGMRDKGrsvyqvAIA--DGAEVKR----GTFVMPT-LIELE-SFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGY 1041
Cdd:cd07102 313 IADAIAKG------ARAliDGALFPEdkagGAYLAPTvLTNVDhSMRVMREETFGPVVGIMKV--KSDAEAIALMNDSEY 384
|
410 420 430
....*....|....*....|....*....|
gi 2063477733 1042 GLTLGVHTRIDETIAKVVGNVNAGNMYVNR 1071
Cdd:cd07102 385 GLTASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
662-1090 |
3.59e-60 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 215.21 E-value: 3.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 662 LNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEV 741
Cdd:PRK09457 20 RNPVSG-EVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 742 -----REAVDFLRYY---------AVQARNDLRNdncRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:PRK09457 99 taminKIAISIQAYHertgekrseMADGAAVLRH---RPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 808 IAAQAVRLLLEAGIPEGVLQLLPGRGETvGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrpIPLIAETGGQNA 887
Cdd:PRK09457 176 VAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPE-----KILALEMGGNNP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDS-ADRVIEMLKGAMAESRLGNPerlsvD------IGPVIDA 960
Cdd:PRK09457 250 LVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRW-----DaepqpfMGAVISE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 961 EAKAGIEKHIQGMRDKGrsvyQVAIADGAEVKRGT-FVMPTLIELESFDEL-QREIFGPVLHVVRYNrkNLDQLIEQINA 1038
Cdd:PRK09457 325 QAAQGLVAAQAQLLALG----GKSLLEMTQLQAGTgLLTPGIIDVTGVAELpDEEYFGPLLQVVRYD--DFDEAIRLANN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1039 SGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAvVGVQPFGGEGLSG 1090
Cdd:PRK09457 399 TRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
660-1092 |
6.58e-60 |
|
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: 213.71 E-value: 6.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07151 13 DVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYA-----VQAR---NDLRNDNCR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP- 806
Cdd:cd07151 92 EWGAAMAITREAAtfplrMEGRilpSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPi 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 807 ----LIAaqavRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVArllqRNIaGRLdnQGRPIPLIA-E 881
Cdd:cd07151 172 tgglLLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG----RHI-GEL--AGRHLKKVAlE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAE 961
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 962 AKAGIEKHIqgmrdkgrsvyQVAIADGAEV-----KRGTFVMPT-LIELESFDELQR-EIFGPVLHVVRYnrKNLDQLIE 1034
Cdd:cd07151 321 QVDGLLDKI-----------EQAVEEGATLlvggeAEGNVLEPTvLSDVTNDMEIAReEIFGPVAPIIKA--DDEEEALE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2063477733 1035 QINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVqPFGGEGLSGTG 1092
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
661-1092 |
8.96e-60 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 212.93 E-value: 8.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRYYAVQARN------DLRNDNC-----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIA 809
Cdd:cd07090 80 IDSSADCLEYYAGLAPTlsgehvPLPGGSFaytrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 810 AQAVRLLLEAGIPEGVLQLLPGRGETvGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNAMI 889
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 890 VDSSALTEQVVIDVVSSAFDSAGQRCS-ALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEakagiek 968
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEE------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 969 HiqgmRDKGRSVYQVAIADGAEV-------------KRGTFVMPTLIElESFDEL---QREIFGPVLHVVRYnrKNLDQL 1032
Cdd:cd07090 305 H----LEKVLGYIESAKQEGAKVlcggervvpedglENGFYVSPCVLT-DCTDDMtivREEIFGPVMSILPF--DTEEEV 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063477733 1033 IEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNR-NIVGAVVgvqPFGGEGLSGTG 1092
Cdd:cd07090 378 IRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
651-1096 |
1.66e-59 |
|
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: 213.04 E-value: 1.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 651 CATSEQAAAPVLNPSDHrDVVGQVQEASVADASNAVQCAVNA-APIWQATPPAERAAILERAADLMEAEIQPLMGLLVRE 729
Cdd:cd07144 17 VKSSDGETIKTVNPSTG-EVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 730 AGKTY-ANAIAEVREAVDFLRYYAVQA-----------RNDLRNDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07144 96 SGKPYhSNALGDLDEIIAVIRYYAGWAdkiqgktiptsPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 798 LAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpIP 877
Cdd:cd07144 176 VIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA----VT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 878 LiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAE-SRLGNPERLSVDIGP 956
Cdd:cd07144 252 L--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 957 VIDAEAKAGIEKHIQGMRDKGRSVYQVAIADGAEVKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIE 1034
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIFTdvPQDMRIVKEEIFGPVVVISKF--KTYEEAIK 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1035 QINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAvVGVqPFGGEGLSGTGPKAG 1096
Cdd:cd07144 408 KANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
661-1092 |
3.18e-59 |
|
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: 211.44 E-value: 3.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:cd07110 1 VINPATEA-TIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRYYAVQARnDLRND--------------NCR--PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07110 80 VDDVAGCFEYYADLAE-QLDAKaeravplpsedfkaRVRrePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 805 TPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAgrldNQGRPIPLiaETGG 884
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA----QDIKPVSL--ELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 885 QNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDaeaka 964
Cdd:cd07110 233 KSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVS----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 965 giekhiQGMRDKGRSVYQVAIADGAEV----------KRGTFVMPTLI-ELESFDELQR-EIFGPVLHVVRYNRKnlDQL 1032
Cdd:cd07110 308 ------QAQYEKVLSFIARGKEEGARLlcggrrpahlEKGYFIAPTVFaDVPTDSRIWReEIFGPVLCVRSFATE--DEA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1033 IEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVnrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07110 380 IALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
661-1096 |
2.13e-58 |
|
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: 209.69 E-value: 2.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDHRdVVGQVQEASVADASNAVQCAVNA--APIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAI 738
Cdd:cd07143 26 VYNPSTGK-LITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 739 A-EVREAVDFLRYYAVQARND----LRNDNCR-------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:cd07143 105 RvDVQASADTFRYYGGWADKIhgqvIETDIKKltytrhePIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 807 LIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIA-GRLDNqgrpipLIAETGGQ 885
Cdd:cd07143 185 LSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAkSNLKK------VTLELGGK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 886 NAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAG 965
Cdd:cd07143 259 SPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 966 IEKHIQGMRDKGRSVYQVAIADGAEvkrGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGL 1043
Cdd:cd07143 339 IMSYIESGKAEGATVETGGKRHGNE---GYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKF--KTEEEAIKRANDSTYGL 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2063477733 1044 TLGVHTRIDETIAKVVGNVNAGNMYVN-RNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07143 414 AAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
660-1105 |
3.49e-58 |
|
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: 209.17 E-value: 3.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKtyanAIA 739
Cdd:cd07111 40 PTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK----PIR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVRE-----AVDFLRYYAVQAR-NDLRNDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAV 813
Cdd:cd07111 115 ESRDcdiplVARHFYHHAGWAQlLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 814 RLLLEAGIPEGVLQLLPGRGETvGAGLVGDERVKGVMFTGSTEVARLLQRNIAGrldnQGRPIPLiaETGGQNAMIVDSS 893
Cdd:cd07111 195 EICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAG----TGKKLSL--ELGGKSPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 894 ALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGM 973
Cdd:cd07111 268 ADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 974 RDKGRSVYQvaiADGAEVKRGTFVMPTLIE-LESFDEL-QREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRI 1051
Cdd:cd07111 348 RAEGADVFQ---PGADLPSKGPFYPPTLFTnVPPASRIaQEEIFGPVLVVLTF--RTAKEAVALANNTPYGLAASVWSEN 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2063477733 1052 DETIAKVVGNVNAGNMYVN-RNIVGAVVgvqPFGGEGLSGTGpKAGGPLYLYRLL 1105
Cdd:cd07111 423 LSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEYL 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
662-1092 |
1.58e-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: 206.43 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 662 LNPSDHrDVVGQVQEASVADASNAVQCAVNA--APIWqATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07120 2 IDPATG-EVIGTYADGGVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQARN------DLRNDNC-----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLI 808
Cdd:cd07120 80 EISGAISELRYYAGLARTeagrmiEPEPGSFslvlrEPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEA-GIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNQGrpipliAETGGQNA 887
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAkagie 967
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRAN----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 968 khiqgmRDKGRSVYQVAIADGAEV-----------KRGTFVMPTLIELE--SFDELQREIFGPVLHVVRYNrkNLDQLIE 1034
Cdd:cd07120 309 ------VDRVDRMVERAIAAGAEVvlrggpvteglAKGAFLRPTLLEVDdpDADIVQEEIFGPVLTLETFD--DEAEAVA 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063477733 1035 QINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVN---RNIVGAvvgvqPFGGEGLSGTG 1092
Cdd:cd07120 381 LANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINdwnKLFAEA-----EEGGYRQSGLG 436
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
661-1092 |
6.82e-57 |
|
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: 205.37 E-value: 6.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQA-TPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:cd07113 19 ITNPAT-EQVIASVASATEADVDAAVASAWRAFVSAWAkTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 -EVREAVDFLRYYA--------------VQARNDLRNDNC---RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKP 801
Cdd:cd07113 98 fEVGQSANFLRYFAgwatkingetlapsIPSMQGERYTAFtrrEPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 802 AEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGEtVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAE 881
Cdd:cd07113 178 SEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTR------VTLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 882 TGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDae 961
Cdd:cd07113 251 LGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLAN-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 962 akagiEKHIqgmrDKGRSVYQVAIADGAEVKRGT--------FVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQ 1031
Cdd:cd07113 329 -----QPHF----DKVCSYLDDARAEGDEIVRGGealagegyFVQPTLVLARSADSrlMREETFGPVVSFVPY--EDEEE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1032 LIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVN-RNIVGAVVgvqPFGGEGLSGTG 1092
Cdd:cd07113 398 LIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
660-1092 |
3.46e-56 |
|
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: 203.34 E-value: 3.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGK----TYA 735
Cdd:cd07559 19 DNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKpireTLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 736 naiAEVREAVDFLRYYAVQAR------NDLRNDNC-----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQ 804
Cdd:cd07559 98 ---ADIPLAIDHFRYFAGVIRaqegslSEIDEDTLsyhfhEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 805 TPLIAAQAVRLLLEAgIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGG 884
Cdd:cd07559 175 TPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------IPVTLELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 885 QNAMIVDSSALTEQVVID------VVSSAFDSaGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVI 958
Cdd:cd07559 248 KSPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 959 DAEAKAGIEKHIQGMRDKGRSVyqvaIADGAEVKR-----GTFVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQ 1031
Cdd:cd07559 327 SKDQLEKILSYVDIGKEEGAEV----LTGGERLTLggldkGYFYEPTLIKGGNNDMriFQEEIFGPVLAVITF--KDEEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 1032 LIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVN-RNIVGAVVgvqPFGGEGLSGTG 1092
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
660-1096 |
1.68e-55 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 202.73 E-value: 1.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNA---APiWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYAN 736
Cdd:PLN02466 76 PTLDPRTG-EVIAHVAEGDAEDVNRAVAAARKAfdeGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 737 AI-AEVREAVDFLRYYA------------------VQARNDlrndncrPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:PLN02466 154 SAkAELPMFARLFRYYAgwadkihgltvpadgphhVQTLHE-------PIGVAGQIIPWNFPLLMFAWKVGPALACGNTI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 798 LAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQrNIAGRldNQGRPIP 877
Cdd:PLN02466 227 VLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVL-ELAAK--SNLKPVT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 878 LiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPV 957
Cdd:PLN02466 304 L--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 958 IDAEAKAGIEKHIQGMRDKGRSVyqvaIADGAEV-KRGTFVMPTLIELESFDEL--QREIFGPVLHVVRYnrKNLDQLIE 1034
Cdd:PLN02466 382 IDSEQFEKILRYIKSGVESGATL----ECGGDRFgSKGYYIQPTVFSNVQDDMLiaQDEIFGPVQSILKF--KDLDEVIR 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2063477733 1035 QINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVN-RNIVGAVVgvqPFGGEGLSGTGPKAG 1096
Cdd:PLN02466 456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
669-1096 |
1.95e-54 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 198.89 E-value: 1.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 669 DVVGQVQEASVADASNAVQCAVNA---APiWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYA-NAIAEVREA 744
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAAREAfdhGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 745 VDFLRYYAvQARNDLRNDNCR------------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQA 812
Cdd:PLN02766 126 AGLLRYYA-GAADKIHGETLKmsrqlqgytlkePIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 813 VRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPIPLiaETGGQNAMIVDS 892
Cdd:PLN02766 205 AHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAA---TSNLKQVSL--ELGGKSPLLIFD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 893 SALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQG 972
Cdd:PLN02766 280 DADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEH 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 973 MRDKGRSVYQVAIADGaevKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTR 1050
Cdd:PLN02766 360 GKREGATLLTGGKPCG---DKGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAGIVTK 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2063477733 1051 IDETIAKVVGNVNAGNMYVNRNIvgAVVGVQPFGGEGLSGTGPKAG 1096
Cdd:PLN02766 435 DLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
681-1092 |
4.08e-53 |
|
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: 192.79 E-value: 4.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 681 DASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDL- 759
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 760 -----RNDNC------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQL 828
Cdd:cd07105 81 gsipsDKPGTlamvvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 829 L---PGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRnIAGR-LdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVV 904
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAE-TAAKhL------KPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 905 SSAFDSAGQRC-SALRVLcLQEDSADRVIEMLKGAMAESRLGnperlSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVYQV 983
Cdd:cd07105 234 FGAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 984 AIADgaEVKRGTFVMPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRiDETIA-KVVG 1060
Cdd:cd07105 308 GLAD--ESPSGTSMPPTILDnvTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR-DLARAlAVAK 382
|
410 420 430
....*....|....*....|....*....|....*
gi 2063477733 1061 NVNAGNMYVNrnivGAVVGVQ---PFGGEGLSGTG 1092
Cdd:cd07105 383 RIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
660-1101 |
1.17e-51 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 190.12 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:PRK11241 29 DVTNPANG-DKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQARNdLRNDNC-------------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTP 806
Cdd:PRK11241 108 EISYAASFIEWFAEEGKR-IYGDTIpghqadkrlivikQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 807 LIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQN 886
Cdd:PRK11241 187 FSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI----KKVSL--ELGGNA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 887 AMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGI 966
Cdd:PRK11241 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 967 EKHIQGMRDKGRSVyqvaIADG-AEVKRGTFVMPT-LIELESFDELQR-EIFGPVLHVVRYnrKNLDQLIEQINASGYGL 1043
Cdd:PRK11241 341 EEHIADALEKGARV----VCGGkAHELGGNFFQPTiLVDVPANAKVAKeETFGPLAPLFRF--KDEADVIAQANDTEFGL 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2063477733 1044 TLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGvqPFGG---EGLSGTGPKAGGPLYL 1101
Cdd:PRK11241 415 AAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
656-1096 |
3.64e-51 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 189.27 E-value: 3.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 656 QAAAPV---LNPSDHRdVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGK 732
Cdd:PLN02315 30 RANGPLvssVNPANNQ-PIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 733 TYANAIAEVREAVDFLRYYAVQAR------------NDLRNDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAK 800
Cdd:PLN02315 109 ILAEGIGEVQEIIDMCDFAVGLSRqlngsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 801 PAEQTPLIAAQAVRLLLEA----GIPEGVLQLLPGrGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpi 876
Cdd:PLN02315 189 GAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGK----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 877 pLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGP 956
Cdd:PLN02315 263 -CLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 957 VIDAEAKAGIEKHIQGMRDKGRSVyqvaIADGAEVKR-GTFVMPTLIELE-SFDELQREIFGPVLHVVRYnrKNLDQLIE 1034
Cdd:PLN02315 342 LHTPESKKNFEKGIEIIKSQGGKI----LTGGSAIESeGNFVQPTIVEISpDADVVKEELFGPVLYVMKF--KTLEEAIE 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2063477733 1035 QINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIV--GAVVGvQPFGGEGLSGTGPKAG 1096
Cdd:PLN02315 416 INNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPtnGAEIG-GAFGGEKATGGGREAG 478
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
661-1092 |
8.65e-50 |
|
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: 183.77 E-value: 8.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDhRDVVGQVQEASVADASNAVQCA------VNAapiWqaTPPAERAAILERAADLMEAEIQPLMGLLVREAGKTY 734
Cdd:cd07148 3 VVNPFD-LKPIGEVPTVDWAAIDKALDTAhalfldRNN---W--LPAHERIAILERLADLMEERADELALLIAREGGKPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 735 ANAIAEVREAVDFLRYyAVQARNDLRNDNC-----------------RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPV 797
Cdd:cd07148 77 VDAKVEVTRAIDGVEL-AADELGQLGGREIpmgltpasagriafttrEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 798 LAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGEtVGAGLVGDERVKGVMFTGSTEVARLLQRNIAgrldnQGRPIP 877
Cdd:cd07148 156 IVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLA-----PGTRCA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 878 LiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPV 957
Cdd:cd07148 230 L--EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 958 IDAEAKAGIEKHIQGMRDKGRSVyqvaIADGAEVKRGTFvMPTLIELESFDEL--QREIFGPVlhVVRYNRKNLDQLIEQ 1035
Cdd:cd07148 308 IRPREVDRVEEWVNEAVAAGARL----LCGGKRLSDTTY-APTVLLDPPRDAKvsTQEIFGPV--VCVYSYDDLDEAIAQ 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2063477733 1036 INASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNiVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07148 381 ANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
705-1071 |
1.49e-49 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 181.86 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 705 AAILERAADLMEaeiqplmgLLVREAGKTYANAIAEVREAVDFLRYYAVQAR--------NDLRNDNC----RPLGPVVC 772
Cdd:PRK10090 6 AGIRERASEISA--------LIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegeiiqSDRPGENIllfkRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 773 ISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFT 852
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 853 GSTEV-ARLLQ---RNIagrldnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSA 928
Cdd:PRK10090 158 GSVSAgEKIMAaaaKNI----------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 929 DRVIEMLKGAMAESRLGNP-ERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSvyqVAIADGAEVKRGTFVMPTLIE--LE 1005
Cdd:PRK10090 228 DQFVNRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGAR---VALGGKAVEGKGYYYPPTLLLdvRQ 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2063477733 1006 SFDELQREIFGPVLHVVRYNrkNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNR 1071
Cdd:PRK10090 305 EMSIMHEETFGPVLPVVAFD--TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR 368
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
662-1096 |
1.52e-49 |
|
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: 183.85 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 662 LNPSDHRdVVGQVQEASVADASNAVQCAVNA--APIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAI- 738
Cdd:cd07140 26 INPTDGS-VICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 739 AEVREAVDFLRYYA-----VQAR----NDLR-NDNC-----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07140 105 THVGMSIQTFRYFAgwcdkIQGKtipiNQARpNRNLtltkrEPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 804 QTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAgrlDNQGRPIPLiaETG 883
Cdd:cd07140 185 VTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA---VSNLKKVSL--ELG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSAD----RVIEMLKgamaESRLGNPERLSVDIGPvid 959
Cdd:cd07140 260 GKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDefvrRVVEEVK----KMKIGDPLDRSTDHGP--- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 960 AEAKAGIEKHI----QGMRDKGRSVYqvaiaDGAEVKR-GTFVMPTL---IELESFDElQREIFGPVLHVVRYNRKNLDQ 1031
Cdd:cd07140 333 QNHKAHLDKLVeyceRGVKEGATLVY-----GGKQVDRpGFFFEPTVftdVEDHMFIA-KEESFGPIMIISKFDDGDVDG 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2063477733 1032 LIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVN---RNIVGAvvgvqPFGGEGLSGTGPKAG 1096
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynKTDVAA-----PFGGFKQSGFGKDLG 469
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
660-1092 |
1.75e-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: 183.42 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKtyanAIA 739
Cdd:cd07117 19 DSYNPANG-ETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGK----PIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVRE-----AVDFLRYYAVQAR------NDLRNDNC-----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAE 803
Cdd:cd07117 94 ETRAvdiplAADHFRYFAGVIRaeegsaNMIDEDTLsivlrEPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 804 QTPLIAAQAVRLLLEAgIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETG 883
Cdd:cd07117 174 TTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------IPATLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 884 GQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAK 963
Cdd:cd07117 247 GKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 964 AGIEKHIQGMRDKGRSVyqvaIADG-----AEVKRGTFVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQI 1036
Cdd:cd07117 327 DKILSYVDIAKEEGAKI----LTGGhrlteNGLDKGFFIEPTLIVNVTNDMrvAQEEIFGPVATVIKF--KTEDEVIDMA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2063477733 1037 NASGYGLTLGVHTRiDETIA-KVVGNVNAGNMYVNR-NIVGAVVgvqPFGGEGLSGTG 1092
Cdd:cd07117 401 NDSEYGLGGGVFTK-DINRAlRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
648-1085 |
2.61e-49 |
|
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: 183.16 E-value: 2.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 648 LLACATSEQAAA---PVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMG 724
Cdd:TIGR01722 4 WIGGKFAEGASGtyiPVTNPATN-EVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 725 LLVREAGKTYANAIAEVR---EAVDFLRYYAVQARNDLRNDNCR---------PLGPVVCISPWNFPLAIFSGQVAAALA 792
Cdd:TIGR01722 83 LITAEHGKTHSDALGDVArglEVVEHACGVNSLLKGETSTQVATrvdvysirqPLGVCAGITPFNFPAMIPLWMFPIAIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 793 AGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAgLVGDERVKGVMFTGSTEVARLlqrnIAGRLDNQ 872
Cdd:TIGR01722 163 CGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDR-LLEHPDVKAVSFVGSTPIGRY----IHTTGSAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 873 GRPIPliAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQeDSADRVIEMLKGAMAESRLGNPERLSV 952
Cdd:TIGR01722 238 GKRVQ--ALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDPGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 953 DIGPVIDAEAKAGIEKHIQGMRDKGRSVyqvaIADGAEVK-----RGTFVMPTLIELESFDE--LQREIFGPVLHVVRYN 1025
Cdd:TIGR01722 315 EMGPLITPQAKDRVASLIAGGAAEGAEV----LLDGRGYKvdgyeEGNWVGPTLLERVPPTMkaYQEEIFGPVLCVLEAD 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1026 rkNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIvGAVVGVQPFGG 1085
Cdd:TIGR01722 391 --TLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPI-PVPLPYFSFTG 447
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
660-1092 |
6.49e-49 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 182.00 E-value: 6.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAI- 738
Cdd:PRK13252 25 EVINPATG-EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 739 AEVREAVDFLRYYAVQA------RNDLRNDNC-----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPL 807
Cdd:PRK13252 104 VDIVTGADVLEYYAGLApalegeQIPLRGGSFvytrrEPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 808 IAAQAVRLLLEAGIPEGVLQLLPGRGEtVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrpiPLIAETGGQNA 887
Cdd:PRK13252 184 TALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK------EVTMELGGKSP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 888 MIVDSSALTEQVVIDVVSSAFDSAGQRCS-ALRVLcLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGI 966
Cdd:PRK13252 257 LIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 967 EKHI-QGMRDKGRSVYQVAIADGAEVKRGTFVMPTLielesF----DEL---QREIFGPVLHVVRYNRKnlDQLIEQINA 1038
Cdd:PRK13252 336 LGYIeKGKAEGARLLCGGERLTEGGFANGAFVAPTV-----FtdctDDMtivREEIFGPVMSVLTFDDE--DEVIARAND 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2063477733 1039 SGYGLTLGVHTRiDETIA-KVVGNVNAGNMYVNRniVGAVVGVQPFGGEGLSGTG 1092
Cdd:PRK13252 409 TEYGLAAGVFTA-DLSRAhRVIHQLEAGICWINT--WGESPAEMPVGGYKQSGIG 460
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
660-1055 |
7.83e-46 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 173.40 E-value: 7.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA 739
Cdd:PLN00412 34 AITNPST-RKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 740 EVREAVDFLRYYAVQARNDL---------------RNDNCR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAK 800
Cdd:PLN00412 113 EVVRSGDLISYTAEEGVRILgegkflvsdsfpgneRNKYCLtskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 801 PAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFT-GSTEVArllqrniagrLDNQGRPIPLI 879
Cdd:PLN00412 193 PPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA----------ISKKAGMVPLQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 880 AETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERlSVDIGPVID 959
Cdd:PLN00412 263 MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 960 AEAKAGIEKHIQGMRDKGRSVYQvaiadgaEVKR-GTFVMPTLIELESFDE--LQREIFGPVLHVVRYNrkNLDQLIEQI 1036
Cdd:PLN00412 342 ESSANFIEGLVMDAKEKGATFCQ-------EWKReGNLIWPLLLDNVRPDMriAWEEPFGPVLPVIRIN--SVEEGIHHC 412
|
410 420
....*....|....*....|
gi 2063477733 1037 NASGYGLTLGVHTR-IDETI 1055
Cdd:PLN00412 413 NASNFGLQGCVFTRdINKAI 432
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
651-1092 |
1.02e-44 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 170.08 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 651 CATSEQAAAPVLNPSDHRDVvGQVQEASVADASNAVQCA--VNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVR 728
Cdd:PRK09847 29 TAAAENETFETVDPVTQAPL-AKIARGKSVDIDRAVSAArgVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 729 EAGKTYANAIAE-VREAVDFLRYYAVQA-----------RNDLRNDNCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNP 796
Cdd:PRK09847 108 DTGKPIRHSLRDdIPGAARAIRWYAEAIdkvygevattsSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 797 VLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNiAGRlDNQGRpi 876
Cdd:PRK09847 188 VILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKD-AGD-SNMKR-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 877 pLIAETGGQNAMIV--DSSALtEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDI 954
Cdd:PRK09847 264 -VWLEAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 955 GPVIDAEAKAGIEKHIQGMRDKGRsvyqvAIADGAEVKRGTFVMPT-LIELESFDELQR-EIFGPVLHVVRYnrKNLDQL 1032
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKGQ-----LLLDGRNAGLAAAIGPTiFVDVDPNASLSReEIFGPVLVVTRF--TSEEQA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1033 IEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVvgVQPFGGEGLSGTG 1092
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
696-1092 |
9.26e-44 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 166.07 E-value: 9.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 696 WQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRND------------- 762
Cdd:PRK09406 39 YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALLADEpadaaavgasray 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 763 -NCRPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLpgrgeTVGAGLV 841
Cdd:PRK09406 119 vRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTL-----LVGSGAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 842 ----GDERVKGVMFTGSTEVARLLQrNIAGRLDNqgrpiPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSA 917
Cdd:PRK09406 194 eailRDPRVAAATLTGSEPAGRAVA-AIAGDEIK-----KTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 918 LRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVyqvaIADGAEVKR-GTF 996
Cdd:PRK09406 268 AKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATI----LCGGKRPDGpGWF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 997 VMPTLI-----ELESFDElqrEIFGPVLHVvrYNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNr 1071
Cdd:PRK09406 344 YPPTVItditpDMRLYTE---EVFGPVASL--YRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN- 417
|
410 420
....*....|....*....|...
gi 2063477733 1072 nivGAVVGVQ--PFGGEGLSGTG 1092
Cdd:PRK09406 418 ---GMTVSYPelPFGGVKRSGYG 437
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
673-1092 |
2.78e-43 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 165.32 E-value: 2.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 673 QVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAI-AEVREAVDFLRYY 751
Cdd:cd07116 31 EVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 752 AVQAR------NDLRNDNC-----RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLiaaqAVRLLLEA- 819
Cdd:cd07116 111 AGCIRaqegsiSEIDENTVayhfhEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPA----SILVLMELi 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 820 --GIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTE 897
Cdd:cd07116 187 gdLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI------IPVTLELGGKSPNIFFADVMDA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 898 QvvidvvSSAFDSA-----------GQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPerlsVDIGPVIDAEAKAGI 966
Cdd:cd07116 261 D------DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNP----LDTETMIGAQASLEQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 967 EKHIQGMRDKGRSVYQVAIADGAEVKR-----GTFVMPTLI----ELESFdelQREIFGPVLHVVRYnrKNLDQLIEQIN 1037
Cdd:cd07116 331 LEKILSYIDIGKEEGAEVLTGGERNELggllgGGYYVPTTFkggnKMRIF---QEEIFGPVLAVTTF--KDEEEALEIAN 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2063477733 1038 ASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVnrNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07116 406 DTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
766-1092 |
1.01e-42 |
|
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: 162.31 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAgIPEGVLQLLPGrGETVGAGLVgDER 845
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GVEVATALL-AEP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 846 VKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQE 925
Cdd:cd07087 177 FDHIFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 926 DSADRVIEMLKGAMAESRLGNPERlSVDIGPVIDaeakagiEKH---IQGMRDKGRSVYqvaiadGAEVKRGT-FVMPTL 1001
Cdd:cd07087 251 SIKDELIEELKKAIKEFYGEDPKE-SPDYGRIIN-------ERHfdrLASLLDDGKVVI------GGQVDKEErYIAPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1002 IELESFDE--LQREIFGPVLHVVRYNrkNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVG 1079
Cdd:cd07087 317 LDDVSPDSplMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIP 394
|
330
....*....|...
gi 2063477733 1080 VQPFGGEGLSGTG 1092
Cdd:cd07087 395 NLPFGGVGNSGMG 407
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
660-1070 |
3.64e-42 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 162.59 E-value: 3.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 660 PVLNPSDHrDVVGQVQEASVADASNAVQCAVNA-----APIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTY 734
Cdd:PLN02467 26 PVVNPATE-ETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 735 ANAIAEVREAVDFLRYYAVQARN-DLRND----------NCR----PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLA 799
Cdd:PLN02467 105 DEAAWDMDDVAGCFEYYADLAEAlDAKQKapvslpmetfKGYvlkePLGVVGLITPWNYPLLMATWKVAPALAAGCTAVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 800 KPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLi 879
Cdd:PLN02467 185 KPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMV----KPVSL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 880 aETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVID 959
Cdd:PLN02467 260 -ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 960 AEAKAGIEKHIQGMRDKGRSVYqVAIADGAEVKRGTFVMPTLI-ELESFDELQR-EIFGPVLHVVRYNRKnlDQLIEQIN 1037
Cdd:PLN02467 339 EGQYEKVLKFISTAKSEGATIL-CGGKRPEHLKKGFFIEPTIItDVTTSMQIWReEVFGPVLCVKTFSTE--DEAIELAN 415
|
410 420 430
....*....|....*....|....*....|...
gi 2063477733 1038 ASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVN 1070
Cdd:PLN02467 416 DSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
766-1096 |
4.28e-38 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 149.76 E-value: 4.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEA----GIPEGVLQLLPGRGETvGAGLV 841
Cdd:cd07098 120 PLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 842 GDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVL 921
Cdd:cd07098 199 SHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 922 CLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKG-RSVYQVAIADGAEVKRGTFVMPT 1000
Cdd:cd07098 273 IVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGaRLLAGGKRYPHPEYPQGHYFPPT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1001 LIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVV 1078
Cdd:cd07098 353 LLVdvTPDMKIAQEEVFGPVMVVMKA--SDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYV 430
|
330
....*....|....*...
gi 2063477733 1079 GVQPFGGEGLSGTGPKAG 1096
Cdd:cd07098 431 QQLPFGGVKGSGFGRFAG 448
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
685-1054 |
2.19e-37 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 147.30 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 685 AVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARN------- 757
Cdd:cd07129 4 AAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgswldar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 758 --------------DLRNDNcRPLGPVVCISPWNFPLAiFS---GQVAAALAAGNPVLAKP-------AEQTPLIAAQAV 813
Cdd:cd07129 84 idpadpdrqplprpDLRRML-VPLGPVAVFGASNFPLA-FSvagGDTASALAAGCPVVVKAhpahpgtSELVARAIRAAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 814 RlllEAGIPEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLDnqgrPIPLIAETGGQNAMIVDSS 893
Cdd:cd07129 162 R---ATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGSVNPVFILPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 894 ALTE---QVVIDVVSSAFDSAGQRCSALRVLCLQEDSA-DRVIEMLKGAMAESrlgNPERLsvdIGPVIDAEAKAGIEkH 969
Cdd:cd07129 235 ALAErgeAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAA---PAQTM---LTPGIAEAYRQGVE-A 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 970 IQGmRDKGRSVYQVAIADGAEVKRGTFVMPTLIELESFDELQREIFGPVLHVVRYNrkNLDQLIEQINASGYGLTLGVHT 1049
Cdd:cd07129 308 LAA-APGVRVLAGGAAAEGGNQAAPTLFKVDAAAFLADPALQEEVFGPASLVVRYD--DAAELLAVAEALEGQLTATIHG 384
|
....*
gi 2063477733 1050 RIDET 1054
Cdd:cd07129 385 EEDDL 389
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
661-1070 |
4.87e-37 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 149.13 E-value: 4.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 661 VLNPSDhRDVVGQVQEASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAE 740
Cdd:PLN02419 133 VINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 741 VREAVDFLRY-----------YAVQARNDLRNDNCR-PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLI 808
Cdd:PLN02419 212 IFRGLEVVEHacgmatlqmgeYLPNVSNGVDTYSIRePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 809 AAQAVRLLLEAGIPEGVLQLLPGRGETVGAgLVGDERVKGVMFTGSTEVArllqRNIAGRLDNQGRPIPliAETGGQNAM 888
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAG----MHIYARAAAKGKRIQ--SNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 889 IVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQEDSA---DRVIEMLKgAMAESRLGNPErlsVDIGPVIDAEAKAG 965
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVERAK-ALKVTCGSEPD---ADLGPVISKQAKER 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 966 IEKHIQGMRDKGRSVyqvaIADGAEV-----KRGTFVMPTLI-----ELESFDElqrEIFGPVLHVVRYNrkNLDQLIEQ 1035
Cdd:PLN02419 441 ICRLIQSGVDDGAKL----LLDGRDIvvpgyEKGNFIGPTILsgvtpDMECYKE---EIFGPVLVCMQAN--SFDEAISI 511
|
410 420 430
....*....|....*....|....*....|....*
gi 2063477733 1036 INASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVN 1070
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
766-1097 |
5.10e-36 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 142.75 E-value: 5.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVlQLLPGRGETVGAGLvgDER 845
Cdd:cd07134 100 PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEGDAEVAQALL--ELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 846 VKGVMFTGSTEVARLLQRNIAGRLdnqgRPIPLiaETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQE 925
Cdd:cd07134 177 FDHIFFTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 926 DSADRVIEMLKGAMAESRLGNPERL-SVDIGPVIDaeakagiEKHIQGMRDkgrsVYQVAIADGAEVKRG-------TFV 997
Cdd:cd07134 251 SVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVN-------DRHFDRLKG----LLDDAVAKGAKVEFGgqfdaaqRYI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 998 MPTLIE--LESFDELQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVG 1075
Cdd:cd07134 320 APTVLTnvTPDMKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLH 397
|
330 340
....*....|....*....|..
gi 2063477733 1076 AVVGVQPFGGEGLSGTGpKAGG 1097
Cdd:cd07134 398 FLNPNLPFGGVNNSGIG-SYHG 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
766-1092 |
3.61e-35 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 141.32 E-value: 3.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIaAQAVRLLLEAGIPEGVLQLLPGrGETVGAGLVgDER 845
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT-SKLMAKLLTKYLDPSYVRVIEG-GVEVTTELL-KEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 846 VKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCLQE 925
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 926 DSADRVIEMLKGAMAESRLGNPERlSVDIGPVIDAEAkagIEKHIQGMRDKGRSVYQvaiadGAEVKRGT-FVMPTLIEL 1004
Cdd:PTZ00381 260 SIKDKFIEALKEAIKEFFGEDPKK-SEDYSRIVNEFH---TKRLAELIKDHGGKVVY-----GGEVDIENkYVAPTIIVN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1005 ESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQP 1082
Cdd:PTZ00381 331 PDLDSplMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLP 408
|
330
....*....|
gi 2063477733 1083 FGGEGLSGTG 1092
Cdd:PTZ00381 409 FGGVGNSGMG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
692-1108 |
1.62e-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: 132.36 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 692 AAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQARNDLRNDNCR------ 765
Cdd:cd07084 11 STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHEPGNhlgqgl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 ---------PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGI-PEGVLQLLPGRGET 835
Cdd:cd07084 91 kqqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 836 vGAGLVGDERVKGVMFTGSTEVARLLQRNIAgrldnqgrPIPLIAETGGQNAMIVDSSALTEQVVID-VVSSAFDSAGQR 914
Cdd:cd07084 171 -MQALLLHPNPKMVLFTGSSRVAEKLALDAK--------QARIYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTACSGQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 915 CSALRVLCLQEDSADR-VIEMLKGAMAESRLGnperlSVDIGPVIDAEAKAGIEKhiqgMRDKGRSVYQVAIAD------ 987
Cdd:cd07084 242 CTAQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQTFTTLAMIAH----MENLLGSVLLFSGKElknhsi 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 988 ----GAEVKRGTFVM--PTLIELESFDElqrEIFGPVLHVVRYNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGN 1061
Cdd:cd07084 313 psiyGACVASALFVPidEILKTYELVTE---EIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGN 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2063477733 1062 VN-AGNMY-VNRNIVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSTR 1108
Cdd:cd07084 390 LWvAGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCH 438
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
766-1092 |
1.99e-32 |
|
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: 131.84 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAqAVRLLLEAGIPEGVLQLLPGRGEtVGA---GLVG 842
Cdd:cd07133 101 PLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSA-LLAELLAEYFDEDEVAVVTGGAD-VAAafsSLPF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 843 DErvkgVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLC 922
Cdd:cd07133 179 DH----LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 923 LQEDSADRVIEMLKGAMAE---SRLGNPerlsvDIGPVIDAEAKAGIEKHIQGMRDKGRSVYQvaIADGAEVKRGTFVMP 999
Cdd:cd07133 249 VPEDKLEEFVAAAKAAVAKmypTLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIE--LNPAGEDFAATRKLP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1000 TLIELESFDE---LQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGA 1076
Cdd:cd07133 322 PTLVLNVTDDmrvMQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHV 399
|
330
....*....|....*.
gi 2063477733 1077 VVGVQPFGGEGLSGTG 1092
Cdd:cd07133 400 AQDDLPFGGVGASGMG 415
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
765-1092 |
4.70e-32 |
|
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: 130.80 E-value: 4.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 765 RPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLiAAQAVRLLLEAGIPEGVLQLLPGRGETVGAGLvgDE 844
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPH-TAALLAELVPKYLDPDAFQVVQGGVPETTALL--EQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 845 RVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALR-VLCl 923
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAKHL------TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDyVLV- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 924 QEDSADRVIEMLKGAMAESRLGNPERLSvDIGPVIDAEAKAGIEKHIQgmRDKGRSVYqvaiadGAEVKRGT-FVMPTLI 1002
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLD--TTKGKVVI------GGEMDEATrFIPPTIV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1003 ELESFDE--LQREIFGPVLHVVRYNrkNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGV 1080
Cdd:cd07135 328 SDVSWDDslMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDN 405
|
330
....*....|..
gi 2063477733 1081 QPFGGEGLSGTG 1092
Cdd:cd07135 406 APFGGVGDSGYG 417
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
677-1070 |
1.76e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 123.82 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 677 ASVADASNAVQCAVNAAPIWQATPPAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYAVQAR 756
Cdd:PRK13968 26 AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 757 NDLR-------NDNC----RPLGPVVCISPWNFPL-AIFSGQVAAALAaGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEG 824
Cdd:PRK13968 106 AMLKaeptlveNQQAvieyRPLGTILAIMPWNFPLwQVMRGAVPILLA-GNGYLLKHAPNVMGCAQLIAQVFKDAGIPQG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 825 VLQLLPGRGETVGAgLVGDERVKGVMFTGSTEVARLLQRNIAGRLDNqgrpipLIAETGGQNAMIVDSSALTEQVVIDVV 904
Cdd:PRK13968 185 VYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDPFIVLNDADLELAVKAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 905 SSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEakagiekhiqgMRDKGRSVYQVA 984
Cdd:PRK13968 258 AGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFD-----------LRDELHHQVEAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 985 IADGAEV--------KRGTFVMPTLI-----ELESFDElqrEIFGPVLHVVRynRKNLDQLIEQINASGYGLTLGVHTRI 1051
Cdd:PRK13968 327 LAEGARLllggekiaGAGNYYAPTVLanvtpEMTAFRE---ELFGPVAAITV--AKDAEHALELANDSEFGLSATIFTTD 401
|
410
....*....|....*....
gi 2063477733 1052 DETIAKVVGNVNAGNMYVN 1070
Cdd:PRK13968 402 ETQARQMAARLECGGVFIN 420
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
759-1092 |
8.06e-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: 121.56 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 759 LRNDncrPLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLL-----------LEAGIPEgVLQ 827
Cdd:cd07132 96 IYKE---PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyldkecypvVLGGVEE-TTE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 828 LLpgrgetvgaglvgDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSA 907
Cdd:cd07132 172 LL-------------KQRFDYIFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAWGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 908 FDSAGQRCSALR-VLCLQEdSADRVIEMLKGAMAESrLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRdkgrsvyqvaIA 986
Cdd:cd07132 233 FINAGQTCIAPDyVLCTPE-VQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGK----------VA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 987 DGAEVKRGT-FVMPT-LIELESFDEL-QREIFGPVLHVVryNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVN 1063
Cdd:cd07132 301 IGGQTDEKErYIAPTvLTDVKPSDPVmQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTS 378
|
330 340
....*....|....*....|....*....
gi 2063477733 1064 AGNMYVNRNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07132 379 SGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
766-1092 |
4.73e-27 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 116.06 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFP--LAIfsGQVAAALAAGNPVLAKPAEQTPLIAAqAVRLLLEAGIPEGVLQLLPGRGETVGAGLvgD 843
Cdd:cd07136 100 PYGVVLIIAPWNYPfqLAL--APLIGAIAAGNTAVLKPSELTPNTSK-VIAKIIEETFDEEYVAVVEGGVEENQELL--D 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 844 ERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQRCSALRVLCL 923
Cdd:cd07136 175 QKFDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 924 QEDSADRVIEMLKGAmAESRLGNPERLSVDIGPVIDaeakagiEKH---IQGMRDKGRSVYqvaiadGAEVKRGT-FVMP 999
Cdd:cd07136 249 HESVKEKFIKELKEE-IKKFYGEDPLESPDYGRIIN-------EKHfdrLAGLLDNGKIVF------GGNTDRETlYIEP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1000 TLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAV 1077
Cdd:cd07136 315 TILDNVTWDDpvMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLA 392
|
330
....*....|....*
gi 2063477733 1078 VGVQPFGGEGLSGTG 1092
Cdd:cd07136 393 NPYLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
766-1092 |
1.57e-26 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 114.43 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLL-----------LEAGIPEGVlQLLpgrge 834
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIpeyldtkaikvIEGGVPETT-ALL----- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 835 tvgaglvgDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDS-AGQ 913
Cdd:cd07137 175 --------EQKWDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 914 RCSALRVLCLQEDSADRVIEMLKgAMAESRLGNPERLSVDIGPVIDAeakagieKHIQ--GMRDKGRSVYQVAIADGAEV 991
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALK-NTLEKFFGENPKESKDLSRIVNS-------HHFQrlSRLLDDPSVADKIVHGGERD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 992 KRGTFVMPTLIELESFDEL--QREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYV 1069
Cdd:cd07137 313 EKNLYIEPTILLDPPLDSSimTEEIFGPLLPIITV--KKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTF 390
|
330 340
....*....|....*....|...
gi 2063477733 1070 NRNIVGAVVGVQPFGGEGLSGTG 1092
Cdd:cd07137 391 NDTVVQYAIDTLPFGGVGESGFG 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
702-1059 |
1.89e-26 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 115.44 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 702 AERAAILERAADLMEAEIQPLMGLLVReAGKTYANAIAEVREAVDFLRYYAVQARNDLRNDNCRPLGPV----------- 770
Cdd:cd07128 59 HERAAMLKALAKYLMERKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVeplskdgtfvg 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 771 -----------VCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGI-PEGVLQLLpgrgetvgA 838
Cdd:cd07128 138 qhiltprrgvaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLI--------C 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 839 GLVGD--ERVKG---VMFTGSTEVARLLQRNiagrlDN-QGRPIPLIAETGGQNAMIV--DSSALTEQ---VVIDVVSSA 907
Cdd:cd07128 210 GSVGDllDHLGEqdvVAFTGSAATAAKLRAH-----PNiVARSIRFNAEADSLNAAILgpDATPGTPEfdlFVKEVAREM 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 908 FDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVY---QVA 984
Cdd:cd07128 285 TVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFggpDRF 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2063477733 985 IADGAEVKRGTFVMPTLIELESFDELQR----EIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRIDETIAKVV 1059
Cdd:cd07128 365 EVVGADAEKGAFFPPTLLLCDDPDAATAvhdvEAFGPVATLMPY--DSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
766-1092 |
1.64e-24 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 109.05 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAqavrlLLEAGIPE----GVLQLLPGrGETVGAGLV 841
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPKyldsKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 842 gDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVD--SSALTEQVVID-VVSSAFDS-AGQRCSA 917
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDslSSSRDTKVAVNrIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 918 LRVLCLQEDSADRVIEMLKgAMAESRLGNPERLSVDIGPVIDaeakagiEKHIQGMRD--KGRSVyQVAIADGAEVKRGT 995
Cdd:PLN02203 255 IDYVLVEERFAPILIELLK-STIKKFFGENPRESKSMARILN-------KKHFQRLSNllKDPRV-AASIVHGGSIDEKK 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 996 -FVMPTLIELESFDE--LQREIFGPVLHVVRYnrKNLDQLIEQINASGYGLTLGVHTRiDETIAK-VVGNVNAGNMYVNR 1071
Cdd:PLN02203 326 lFIEPTILLNPPLDSdiMTEEIFGPLLPIITV--KKIEDSIAFINSKPKPLAIYAFTN-NEKLKRrILSETSSGSVTFND 402
|
330 340
....*....|....*....|.
gi 2063477733 1072 NIVGAVVGVQPFGGEGLSGTG 1092
Cdd:PLN02203 403 AIIQYACDSLPFGGVGESGFG 423
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
725-1068 |
1.07e-21 |
|
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: 100.26 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 725 LLVREAGKTYANAIAEVREAVDFLRYYAvqarndlrNDNCR----------------------PLGPVVCISPWNFPLAI 782
Cdd:cd07126 87 LIQRVAPKSDAQALGEVVVTRKFLENFA--------GDQVRflarsfnvpgdhqgqqssgyrwPYGPVAIITPFNFPLEI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 783 FSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGVLQLLPGRGETVGAgLVGDERVKGVMFTGSTEVARLLQ 862
Cdd:cd07126 159 PALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK-ILLEANPRMTLFTGSSKVAERLA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 863 RNIAGRLDnqgrpiplIAETGgqnamiVDSSALTEQVV-IDVVS-----SAFDSAGQRCSALRVLCLQEDSADRVIEMLK 936
Cdd:cd07126 238 LELHGKVK--------LEDAG------FDWKILGPDVSdVDYVAwqcdqDAYACSGQKCSAQSILFAHENWVQAGILDKL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 937 GAMAESRlgNPERLSvdIGPVIDAEAKAgIEKH------IQGMRDK--GRSVYQVAIAD--GAEVKRGTFV-MPTLIELE 1005
Cdd:cd07126 304 KALAEQR--KLEDLT--IGPVLTWTTER-ILDHvdkllaIPGAKVLfgGKPLTNHSIPSiyGAYEPTAVFVpLEEIAIEE 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2063477733 1006 SFDELQREIFGPVLHVVRYNRKNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMY 1068
Cdd:cd07126 379 NFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
702-1024 |
2.69e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 99.39 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 702 AERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIAEVREAVDFLRYYA--------VQARND-----LRNDN----- 763
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalgdARLLRDgeavqLGKDPafqgq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 764 --CRPL-GPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGI-PEGVLQLLPGRGetvgAG 839
Cdd:PRK11903 143 hvLVPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSS----AG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 840 L---VGDERVkgVMFTGSTEVARLLqRNIAGRLDNQGRpipLIAETGGQNAMI-----VDSSALTEQVVIDVVSSAFDSA 911
Cdd:PRK11903 219 LldhLQPFDV--VSFTGSAETAAVL-RSHPAVVQRSVR---VNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 912 GQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVY---QVAIADg 988
Cdd:PRK11903 293 GQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFdggGFALVD- 371
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2063477733 989 AEVKRGTFVMPTLIELESFDELQR----EIFGPVLHVVRY 1024
Cdd:PRK11903 372 ADPAVAACVGPTLLGASDPDAATAvhdvEVFGPVATLLPY 411
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
766-1096 |
6.75e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 91.65 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRlLLEAGIPEGVLQLLPGRGETVGAGLvgDER 845
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAK-LLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 846 VKGVMFTGSTEVARLLQRNIAGRLdnqgrpIPLIAETGGQNAMIVDSSALTEQVVIDVVSSAFD-SAGQRCSALRVLCLQ 924
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 925 EDSADRVIEMLKGAMAESRLGNPERlSVDIGPVIDAEAKAGIEKHIQGMRDKGRSVYqvaiadGAEVKRGTF-VMPTLIE 1003
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVY------GGEKDRENLkIAPTILL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 1004 LESFDEL--QREIFGPVLHVVRYNrkNLDQLIEQINASGYGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAVVGVQ 1081
Cdd:PLN02174 336 DVPLDSLimSEEIFGPLLPILTLN--NLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTL 413
|
330
....*....|....*
gi 2063477733 1082 PFGGEGLSGTGPKAG 1096
Cdd:PLN02174 414 PFGGVGESGMGAYHG 428
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
87-134 |
6.32e-18 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 78.27 E-value: 6.32e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2063477733 87 SVLRSAITAAYRRPEQEVVPMLLEQARLPAAQAEATNKLAATLADKLR 134
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-70 |
9.39e-15 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 70.24 E-value: 9.39e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 2 ATTTLGVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLEggatlNDLNGHAAALGD-DAGEVATD 70
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREE-----WREALIQEGLAAaDAGEFVSH 65
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
692-1077 |
1.08e-11 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 69.04 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 692 AAPIWQATPPAERAA----ILERAADLMEAEIQPLMG------LLVREAGKTYA-----NAIAEVREAVDFL----RYYA 752
Cdd:cd07127 96 AMPGWRDAGARARAGvcleILQRLNARSFEMAHAVMHttgqafMMAFQAGGPHAqdrglEAVAYAWREMSRIpptaEWEK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 753 VQARND-LRNDNC-----RPLGPVVCISP---WNFPLAIFsgqvaAALAAGNPVLAKPAEQTPLIAAQAVR----LLLEA 819
Cdd:cd07127 176 PQGKHDpLAMEKTftvvpRGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVQvareVLAEA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 820 GI-PEGVLQLLPGRGETVGAGLVGDERVKGVMFTGSTEVARLLQRNIAGRLdnqgrpipLIAETGGQNAMIVDSsalTEQ 898
Cdd:cd07127 251 GFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--------VYTEKAGVNTVVVDS---TDD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 899 VVIDVVSSAFDSA---GQRCSALRVLCLQED---------SADRVIEMLkGAMAESRLGNPERLSVDIGPVIDAEAKAGI 966
Cdd:cd07127 320 LKAMLRNLAFSLSlysGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADL-AAAIDGLLADPARAAALLGAIQSPDTLARI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 967 EKHIQG---MRDkGRSVYQVAIADgAEVKrgtfvMPTLIELESFDE--LQREIFGPVLHVVRYNRKN--LDQLIEQINAS 1039
Cdd:cd07127 399 AEARQLgevLLA-SEAVAHPEFPD-ARVR-----TPLLLKLDASDEaaYAEERFGPIAFVVATDSTDhsIELARESVREH 471
|
410 420 430
....*....|....*....|....*....|....*...
gi 2063477733 1040 GyGLTLGVHTRIDETIAKVVGNVNAGNMYVNRNIVGAV 1077
Cdd:cd07127 472 G-AMTVGVYSTDPEVVERVQEAALDAGVALSINLTGGV 508
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-45 |
1.55e-09 |
|
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar proteins; This family includes the N-terminal ribbon-helix-helix (RHH) domain of Shewanella oneidensis CopA(SO), a newly identified type II antitoxin, as well as the N-terminal RHH domain of Escherichia coli PutA flavoprotein, among other similar proteins, many of which are as yet uncharacterized. CopA(SO) is a typical RHH antitoxin that includes an ordered N-terminal domain (CopA(SO)-N) and a disordered C-terminal domain (CopA(SO)-C). Biophysical investigation indicates allosteric effects of CopA(SO)-N on CopA(SO)-C; DNA binding of CopA(SO)-N appears to induce CopA(SO)-C to fold and self-associate the C-terminal domain. The multifunctional E. coli proline utilization A (PutA) flavoprotein functions as a membrane-associated proline catabolic enzyme as well as a transcriptional repressor of the proline utilization genes putA and putP. The N-terminal domain of PutA is a transcriptional regulator with an RHH fold; structure studies show that it forms a homodimer to bind one DNA duplex. This family also includes orphan antitoxin ParD2, an antitoxin component of a non-functional type II toxin-antitoxin (TA system); it does not neutralize the effect of any of the RelE or ParE toxins.
Pssm-ID: 409023 Cd Length: 44 Bit Score: 54.30 E-value: 1.55e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2063477733 4 TTLGVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLE 45
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREE 42
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
701-968 |
3.61e-08 |
|
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: 57.23 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 701 PAERAAILERAADLMEAEIQPLMGLLVREAGKTYANAIA-----------EVREAVDFLRY-YAVQAR--NDLRNDN--- 763
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIAnwiammgcsesKLYKNIDTERGiTASVGHiqDVLLPDNget 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 764 ---CRPLGPVVCISPWNFPLA-IFSgqVAAALAAGNPVLAKPAEQTPlIAAQAVRLLLEAGIPEG----VLQLLPGRGET 835
Cdd:cd07077 95 yvrAFPIGVTMHILPSTNPLSgITS--ALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkiLVLYVPHPSDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 836 VGAGLVGDERVKGVMFTGSTEVARLLQRNiagrldnqGRPIPLIAETGGQNAMIVDSSALTEQVVIDVVSSA-FDSAGqr 914
Cdd:cd07077 172 LAEELLSHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA-- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2063477733 915 CSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAEAKAGIEK 968
Cdd:cd07077 242 CASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFDDEALES 295
|
|
| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-45 |
3.51e-07 |
|
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins; This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.
Pssm-ID: 409020 Cd Length: 42 Bit Score: 47.89 E-value: 3.51e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2063477733 4 TTLGVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLE 45
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLERLE 42
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
199-558 |
1.21e-06 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 52.78 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 199 SPSLFVNAATWGLLLTGKLVsTHNESGLTSSLTRIIGKSGEPMIRKGVdmamrlmGEQFVTGETIAEALANASKFESKGF 278
Cdd:PLN02681 38 TSELLRSLLVLQLCAIGPLV-DLGEWLLTSPLMVLGRAIVLALVKATF-------YSHFCAGEDAEEAARTVRRLWELGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 279 R----YSYDMLGEAALTEHDAQKYLASYEQAIHSIGKAS-------------------------HGRGIYEGPGI--SIK 327
Cdd:PLN02681 110 GgildYAAEDAGDNAACDRNLEKFLAAIRAAATLPPSSSsaavkitalcppsllervsdllrwqDRDPNGKLPWKqwSFP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 328 LSALH-PRYS--------RAQYERVMSELYPRLLSLTLLAKQYDIGLNIDAEEAdRLELSLDlleRLCFEPSLAGWNGIG 398
Cdd:PLN02681 190 LFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYT-SLQPAID---YITYDLAREFNKGKD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 399 F-----VIQAYQKRCPyviDYVIDLAKRSRHR---LMIRLVKGAYWDSEIKRAQVEGLEGyPVYTRKVYTDVSYIACARK 470
Cdd:PLN02681 266 RpivygTYQAYLKDAR---ERLRLDLERSEREgvpLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAEF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 471 LLAVP-----EAIypqFATHNAHTLSAIYTIA---GQNYYPGQYEFQCLHGMGEPLyeqvvgkvAEGKLNRPCRV--YAP 540
Cdd:PLN02681 342 LLEKAsngdgEVM---LATHNVESGELAAAKMnelGLHKGDPRVQFAQLLGMSDNL--------SFGLGNAGFRVskYLP 410
|
410
....*....|....*...
gi 2063477733 541 VGTHETLLAYLVRRLLEN 558
Cdd:PLN02681 411 YGPVEEVIPYLLRRAEEN 428
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
766-1058 |
6.28e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 50.34 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 766 PLGPVVCISPWNFPLAIFSGQVAAALAAGNPVLAKPAEQTPLIAAQAVRLLLEAGIPEGvlqllpgrgetvgaglvGDER 845
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAG-----------------APEN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 846 VKGVMFTGSTEVA-RLLQRNIAGRLDNQGRPI----------PLIAETGGQNAMIVDSSALTEQVVIDVVSSAFDSAGQR 914
Cdd:cd07081 158 LIGWIDNPSIELAqRLMKFPGIGLLLATGGPAvvkaayssgkPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063477733 915 CSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIgpvidaeakagIEKHIQGMRD-KGRSVYQVAIADGAEVKR 993
Cdd:cd07081 238 CASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPV-----------ILKNGDVNRDiVGQDAYKIAAAAGLKVPQ 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2063477733 994 GTFVMptLIELESFDE---LQREIFGPVLHVVRYnrKNLDQLIEQ----INASGYGLTLGVHTRIDETIAKV 1058
Cdd:cd07081 307 ETRIL--IGEVTSLAEhepFAHEKLSPVLAMYRA--ANFADADAKalalKLEGGCGHTSAMYSDNIKAIENM 374
|
|
| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
1-45 |
7.55e-04 |
|
Predicted DNA-binding protein with an HTH domain [General function prediction only];
Pssm-ID: 443745 Cd Length: 76 Bit Score: 39.50 E-value: 7.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2063477733 1 MATTTlgVKLDDPTRERLKAAAQSIDRTPHWLIKQAIFNYLEKLE 45
Cdd:COG4710 1 MKMLS--IRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
|
|
| |
