|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
6-1172 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1953.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 6 PFADFAPPIREQDALRQAITAAYRWPEHDCIAALLPQATLSDAARAEASALARRLVEALRARPKGSSVDQLVQEFALSTQ 85
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTGVEALLQEYSLSSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 86 EGVALMCLAEALLRIPDDATRDALIRDKIAGGDWRAHIGGNRSLFVNAATWGLVVTGKLTASVDDRNLGNALTRLIARAG 165
Cdd:PRK11905 81 EGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIARLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 166 EPIIRRGVDLAMRMMGEQFVTGRTIEEALERAHELEAKGFRYSYDMLGEAAMTAEDAARYLADYQNAIRAIGRASAGRGI 245
Cdd:PRK11905 161 EPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 246 VEGPGISIKLSALHPRYARAQADRVMAELLPRVKGLCELAKRFDIGLNIDAEEADRLELSLDLLESLALDPDLAGWNGLG 325
Cdd:PRK11905 241 YDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 326 FVVQGYGKRCPHVIDWIIALARRSGRRIMVRLVKGAYWDAEIKRAQVDGLADFPVYTRKVHTDVAYIACARRLLDAPDAV 405
Cdd:PRK11905 321 FVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 406 FPQFATHNAHTLATIHAMAGPDFaigAYEFQCLHGMGEPLYEEVVGADKLDRPCRIYAPVGTHETLLAYLVRRLLENGAN 485
Cdd:PRK11905 401 YPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGAN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 486 SSFVNRIANETVPVEEIIADPVEQVRAMpiPGAPHPNIALPGALY-PGRRNSKGVDLSSEAVLADLAERFATASREPAHA 564
Cdd:PRK11905 478 SSFVNRIVDENVPVEELIADPVEKVAAM--GVAPHPQIPLPRDLYgPERRNSKGLDLSDEATLAALDEALNAFAAKTWHA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 565 AP--SPRLATLPARPVRNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLAL 642
Cdd:PRK11905 556 APllAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFAL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 643 IVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLAGST--PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEET 720
Cdd:PRK11905 636 AVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGhkPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQT 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 721 PLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatGRPIPLIAETGGQ 799
Cdd:PRK11905 716 PLIAARAVRLLHEAGVPKDALQLLPGDGRtVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GPPVPLIAETGGQ 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 800 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQAR 879
Cdd:PRK11905 793 NAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQAN 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 880 IEAHIEAMRARGRTVERLPLPDETRAGTFVAPTIIELEALSDLEQEVFGPVLHVIRYRRQDIDALIDAINAWGFGLTFGL 959
Cdd:PRK11905 873 IEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 960 HTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPRPALPFPVDA---------- 1029
Cdd:PRK11905 953 HSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPIPPAHEsvdtdaaard 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 1030 ----------------------------EVVLPGPVGEHNLYRIGPAGRVILFAQNSAALAEQIEAATANSNAAVIADPA 1081
Cdd:PRK11905 1033 flawldkegkaalaaaardararsalglEQELPGPTGESNLLSLHPRGRVLCVADTEEALLRQLAAALATGNVAVVAADS 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 1082 LVP----SLPSALADRVLAPADWRQAGPFARALVNGDSAFVTAVQQALAALPGPIVTAEAPCAAGGYARAMLVGEQSVSI 1157
Cdd:PRK11905 1113 GLAaalaDLPGLVAARIDWTQDWEADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEPTDAYDLARLVEERSVSI 1192
|
1210
....*....|....*
gi 1632883983 1158 NTTAAGGNASLMTLA 1172
Cdd:PRK11905 1193 NTTAAGGNASLMALG 1207
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
3-1171 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1785.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 3 TRPPFADFAPPIREQDALRQAITAAYRWPEHDCIAALLPQATLSDAARAEASALARRLVEALRARPKGSS----VDQLVQ 78
Cdd:PRK11809 74 PHQPFLEFAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGragmVQGLLQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 79 EFALSTQEGVALMCLAEALLRIPDDATRDALIRDKIAGGDWRAHIGGNRSLFVNAATWGLVVTGKLTASVDDRNLGNALT 158
Cdd:PRK11809 154 EFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 159 RLIARAGEPIIRRGVDLAMRMMGEQFVTGRTIEEALERAHELEAKGFRYSYDMLGEAAMTAEDAARYLADYQNAIRAIGR 238
Cdd:PRK11809 234 RIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 239 ASAGRGIVEGPGISIKLSALHPRYARAQADRVMAELLPRVKGLCELAKRFDIGLNIDAEEADRLELSLDLLESLALDPDL 318
Cdd:PRK11809 314 ASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 319 AGWNGLGFVVQGYGKRCPHVIDWIIALARRSGRRIMVRLVKGAYWDAEIKRAQVDGLADFPVYTRKVHTDVAYIACARRL 398
Cdd:PRK11809 394 AGWNGIGFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 399 LDAPDAVFPQFATHNAHTLATIHAMAGPDFAIGAYEFQCLHGMGEPLYEEVVGA---DKLDRPCRIYAPVGTHETLLAYL 475
Cdd:PRK11809 474 LAVPNLIYPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKvadGKLNRPCRIYAPVGTHETLLAYL 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 476 VRRLLENGANSSFVNRIANETVPVEEIIADPVEQVRAMPIP----GAPHPNIALPGALY-PGRRNSKGVDLSSEAVLADL 550
Cdd:PRK11809 554 VRRLLENGANTSFVNRIADTSLPLDELVADPVEAVEKLAQQegqlGLPHPKIPLPRDLYgKGRANSAGLDLANEHRLASL 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 551 AERFATASREPAHAAPS--PRLATLPARPVRNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERA 628
Cdd:PRK11809 634 SSALLASAHQKWQAAPMleDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERA 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 629 ADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLAGST--PLGPVVCISPWNFPLAIFTGQVAAAL 706
Cdd:PRK11809 714 ADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDThrPLGPVVCISPWNFPLAIFTGQVAAAL 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 707 VAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDG-AIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSA 785
Cdd:PRK11809 794 AAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGeTVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDP 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 786 TGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLA 865
Cdd:PRK11809 874 QGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLS 953
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 866 ADIGPVITAEAQARIEAHIEAMRARGRTVERLPLPDET--RAGTFVAPTIIELEALSDLEQEVFGPVLHVIRYRRQDIDA 943
Cdd:PRK11809 954 TDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEdwQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDE 1033
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 944 LIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPRPA- 1022
Cdd:PRK11809 1034 LIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEd 1113
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 1023 ----------LPFPVDAEV---------------------------------------VLPGPVGEHNLYRIGPAGRVIL 1053
Cdd:PRK11809 1114 alavtlarqdAEYPVDAQLraallapltalrewaaerepelaalcdqyaelaqagttrLLPGPTGERNTYTLLPRERVLC 1193
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 1054 FAQNSAALAEQIEAATANSNAAVIADP----ALVPSLPSALADRVLAPADWRQAG-PFARALVNGDSAFVTAVQQALAAL 1128
Cdd:PRK11809 1194 LADTEQDALTQLAAVLAVGSQALWPDDalhrALVAALPAAVQARIQLAKDWQLADqPFDAVLFHGDSDQLRALCEQVAQR 1273
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 1632883983 1129 PGPIVTAEAPCAAG-GYARAMLVGEQSVSINTTAAGGNASLMTL 1171
Cdd:PRK11809 1274 DGPIVSVQGFARGEtNILLERLLIERSLSVNTAAAGGNASLMTI 1317
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
13-1020 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1518.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 13 PIREQDALRQAITAAYRWPEHDCIAALLPQATLSDAARAEASALARRLVEALRARPKG-SSVDQLVQEFALSTQEGVALM 91
Cdd:PRK11904 6 ILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKlGGIDAFLQEYSLSTEEGIALM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 92 CLAEALLRIPDDATRDALIRDKIAGGDWRAHIGGNRSLFVNAATWGLVVTGKL--TASVDDRNLGNALTRLIARAGEPII 169
Cdd:PRK11904 86 CLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVvkLDKKADGTPSGVLKRLVNRLGEPVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 170 RRGVDLAMRMMGEQFVTGRTIEEALERAHELEAKGFRYSYDMLGEAAMTAEDAARYLADYQNAIRAIGRASAGRGIVEGP 249
Cdd:PRK11904 166 RKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADLPARP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 250 GISIKLSALHPRYARAQADRVMAELLPRVKGLCELAKRFDIGLNIDAEEADRLELSLDLLESLALDPDLAGWNGLGFVVQ 329
Cdd:PRK11904 246 GISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLAVQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 330 GYGKRCPHVIDWIIALARRSGRRIMVRLVKGAYWDAEIKRAQVDGLADFPVYTRKVHTDVAYIACARRLLDAPDAVFPQF 409
Cdd:PRK11904 326 AYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAIYPQF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 410 ATHNAHTLATIHAMAGPDfaigAYEFQCLHGMGEPLYEEVVGAdkLDRPCRIYAPVGTHETLLAYLVRRLLENGANSSFV 489
Cdd:PRK11904 406 ATHNAHTVAAILEMAGHR----GFEFQRLHGMGEALYDALLDA--PGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSFV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 490 NRIANETVPVEEIIADPVEQVRAMpiPGAPHPNIALPGALY-PGRRNSKGVDLSSEAVLADLAERFATASREPAHAAPSP 568
Cdd:PRK11904 480 HRLVDPDVPIEELVADPVEKLRSF--ETLPNPKIPLPRDIFgPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPII 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 569 RlATLPARPVRNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAG 648
Cdd:PRK11904 558 N-GEGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAG 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 649 KSVPNAVAEVREAVDFLRYYAVRARSDLAGSTPL-GPV--------------VCISPWNFPLAIFTGQVAAALVAGNPVL 713
Cdd:PRK11904 637 KTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLpGPTgesnelrlhgrgvfVCISPWNFPLAIFLGQVAAALAAGNTVI 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 714 AKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRlsaTGRPIPL 792
Cdd:PRK11904 717 AKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGAtVGAALTADPRIAGVAFTGSTETARIINRTLAAR---DGPIVPL 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 793 IAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVI 872
Cdd:PRK11904 794 IAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVI 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 873 TAEAQARIEAHIEAMRARGRTVERLPLPDETRAGTFVAPTIIELEALSDLEQEVFGPVLHVIRYRRQDIDALIDAINAWG 952
Cdd:PRK11904 874 DAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAINATG 953
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1632883983 953 FGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPR 1020
Cdd:PRK11904 954 YGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEK 1021
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
5-1169 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1398.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 5 PPFADFAPPIREQDALRQAITAAYRWPEHDCIAALLPQATLSDAARAEASALARRLVEALRARPKGSSVDQLVQEFALST 84
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 85 QEGVALMCLAEALLRIPDDATRDALIRDKIAGGDWRAHIGGNRSLFVNAATWGLVVTGKLTASVDDRNLGNALTRLIARA 164
Cdd:COG4230 81 SEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 165 GEPIIRRGVDLAMRMMGEQFVTGRTIEEALERAHELEAKGFRYSYDMLGEAAMTAEDAARYLADYQNAIRAIGRASAGRG 244
Cdd:COG4230 161 GRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 245 IVEGPGISIKLSALHPRYARAQADRVMAELLPRVKGLCELAKR----FDIGLNIDAEEADRLELSLDLLESLALDPDLAG 320
Cdd:COG4230 241 GGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALaainINIDEEEDAEELLLLLLLLDLLAALLLDGGLGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 321 WNGLGFVVQGYGKRCPHVIDWIIALARRSGRRIMVRLVKGAYWDAEIKRAQVDGLADFPVYTRKVHTDVAYIACARRLLD 400
Cdd:COG4230 321 GGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 401 APDAVFPQFATHNAHTLATIHAMAGPDFaigaYEFQCLHGMGEPLYEeVVGADKLDRPCRIYAPVGTHETLLAYLVRRLL 480
Cdd:COG4230 401 AQPAFAPQFATHAAATAAAAAAAGGGGE----FEFQCLHGMGEYLYD-QVGRGKLGRPCRIYAPVGSHEDLLAYLVRRLL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 481 ENGANSSFVNRIANETVPVEEIIADPVEQVRAMPipGAPHPNIALPGALY-PGRRNSKGVDLSSEAVLADLAERFATASR 559
Cdd:COG4230 476 ENGANSSFVNRIADEDVPVEELIADPVEKARALG--GAPHPRIPLPRDLYgPERRNSAGLDLSDEAVLAALSAALAAAAE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 560 EPAHAAP--SPRLATLPARPVRNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMP 637
Cdd:COG4230 554 KQWQAAPliAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRA 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 638 DLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLAGST---PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLA 714
Cdd:COG4230 634 ELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvlrGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 715 KPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRlsaTGRPIPLI 793
Cdd:COG4230 714 KPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGEtVGAALVADPRIAGVAFTGSTETARLINRTLAAR---DGPIVPLI 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 794 AETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVIT 873
Cdd:COG4230 791 AETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVID 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 874 AEAQARIEAHIEAMRARGRTVERLPLPDETRAGTFVAPTIIELEALSDLEQEVFGPVLHVIRYRRQDIDALIDAINAWGF 953
Cdd:COG4230 871 AEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATGY 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 954 GLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPRPALPFPV------ 1027
Cdd:COG4230 951 GLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTaaggna 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 1028 ------------DAEVVLPGPVGEHNLYRIGPAGRVILFAQNSAALAEQIEAATANSNAAVIADPALVPSLPSALADrvl 1095
Cdd:COG4230 1031 sllalgdwlaslLGALTLPGPTGERNTLTLRPRGRVLCLADSLEALLAQLAAALATGNRAVVAADLALAGLPAVLLP--- 1107
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1632883983 1096 apadwrqagPFARALVNGDSAfvtAVQQALAALPGPIVtaeaPCAAGGYARAMLVGEqsvsinttaAGGNASLM 1169
Cdd:COG4230 1108 ---------PFDAVLFEGRLR---ALRQALAARDGAIV----PVIDAGYDLERLLEE---------AGGNASLM 1156
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
484-1017 |
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: 652.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 484 ANSSFVNRIANETVPVE----EIIADPVEQVRAMPIpgaphpnialpgalYPGRRNSKGVdlsseavladlaerfatasr 559
Cdd:cd07125 1 ANSSFVNRIFDLEVPLEaladALKAFDEKEWEAIPI--------------INGEETETGE-------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 560 epahaapsprlatlpARPVRNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDL 639
Cdd:cd07125 47 ---------------GAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGEL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 640 LALIVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLAGS--------------TPLGPVVCISPWNFPLAIFTGQVAAA 705
Cdd:cd07125 112 IALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPelpgptgelnglelHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 706 LVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLS 784
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEeIGEALVAHPRIDGVIFTGSTETAKLINRALAERDG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 785 ATgrpIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRL 864
Cdd:cd07125 272 PI---LPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 865 AADIGPVITAEAQARIEAHIEAMRARGRTVERLPLPDETraGTFVAPTIIELEALSDLEQEVFGPVLHVIRYRRQDIDAL 944
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGN--GYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEA 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1632883983 945 IDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLV 1017
Cdd:cd07125 427 IEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFG 499
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
532-1021 |
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: 611.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 532 GRRNSKGVDLSSEAVLADLAERFATASREPAHAAP----SPRlATLPARPVRNPAEHDDTVGTVADVTAEAAREAVRIAA 607
Cdd:TIGR01238 6 GRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPiighSYK-ADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 608 GAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLAGST--PLGPV 685
Cdd:TIGR01238 85 QAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSveSRGVF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 686 VCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVM 764
Cdd:TIGR01238 165 VCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGAdVGAALTSDPRIAGVA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 765 FTGSTDVGRLIQKQLSTRLSAtgrPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADR 844
Cdd:TIGR01238 245 FTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 845 VLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVERLPLPD--ETRAGTFVAPTIIELEALSDL 922
Cdd:TIGR01238 322 VLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDsrACQHGTFVAPTLFELDDIAEL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 923 EQEVFGPVLHVIRYRRQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSG 1002
Cdd:TIGR01238 402 SEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSG 481
|
490
....*....|....*....
gi 1632883983 1003 TGPKAGGPLYLQRLVQPRP 1021
Cdd:TIGR01238 482 TGPKAGGPHYLYRLTQVQY 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
43-1024 |
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: 570.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 43 ATLSDAARAEASALARRLVEALRARPKGSsVDQLVQEFALSTQEGVALMCLAEALLRIPDDATRDALIRDKIAGGDwrah 122
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAAPEGG-VEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSP---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 123 iggnrSLFVNAATWGLVVTgkltasvddrnlgnaltrLIARAGEPIIRRGVDLAMRMMGEQFVTGRTIEEALERAHELEA 202
Cdd:COG0506 78 -----SFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 203 KGFRYSYDMLGEAAMTAEDAARYLADYQNAIRAIGRASagrgiVEGPGISIKLSALHPRYARAQADRVMAELLPRVKGLC 282
Cdd:COG0506 135 KGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 283 ELAKRFDIGLNIDAEEADRLELSLDLLESLALDPDLAGWNGLGFVVQGYGKRCPHVIDWIIALARRSGRRIMVRLVKGAY 362
Cdd:COG0506 210 RAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 363 WDAEIKRAQVDGLaDFPVYTRKVHTDVAYIACARRLLDAPDAVFPQFATHNAHTLATIHAMAGP-DFAIGAYEFQCLHGM 441
Cdd:COG0506 290 WDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQMLYGM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 442 GEPLYEEV--VGADKLDRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNRIANETVPVEEIIADPVEQVRAMPIPGAP 519
Cdd:COG0506 369 GEDLQRALaaVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPP 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 520 HPNIALPGALYPGRRNSKGVDLSSEAVLADLAERFATASREPAHAAPSPRLATLPARPVRNPAEHDDTVGTVADVTAEAA 599
Cdd:COG0506 449 PPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 600 REAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARS----- 674
Cdd:COG0506 529 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAAraaap 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 675 ------DLAGSTPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDG 748
Cdd:COG0506 609 pppppgGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLG 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 749 AIGAALVGAPETAGVM--FTGSTDVGRLIQKQLSTRLSATGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAG 826
Cdd:COG0506 689 AGGGAGGAAALTLAAAaaAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASA 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 827 QRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVERLPLPDETRAG 906
Cdd:COG0506 769 SLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLT 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 907 TFVAPTIIELEALSDLEQEVFGPVLHVIRYRRQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVI 986
Cdd:COG0506 849 APLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGG 928
|
970 980 990
....*....|....*....|....*....|....*...
gi 1632883983 987 GAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPRPALP 1024
Cdd:COG0506 929 GGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATA 966
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
193-491 |
8.03e-143 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 432.30 E-value: 8.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 193 ALERAHELEAKGFRYSYDMLGEAAMTAEDAARYLADYQNAIRAIGRASAGRGIVEGPGISIKLSALHPRYARAQADRVMA 272
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 273 ELLPRVKGLCELAKRFDIGLNIDAEEADRLELSLDLLESLALDPDLAGWNGLGFVVQGYGKRCPHVIDWIIALARRSGRR 352
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 353 IMVRLVKGAYWDAEIKRAQVdGLADFPVYTRKVHTDVAYIACARRLLDAPDAVFPQFATHNAHTLATIHAMAG-PDFAIG 431
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEeLGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 432 AYEFQCLHGMGEPLYEEVVGAdklDRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNR 491
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAA---GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
580-1020 |
4.07e-136 |
|
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: 422.76 E-value: 4.07e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVR 659
Cdd:cd07083 38 SPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 660 EAVDFLRYYAVRARS---------DLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIA 724
Cdd:cd07083 118 EAIDFIRYYARAALRlrypavevvPYPGEDnesfyvGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 725 AEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSATGRPIPLIAETGGQNAMI 803
Cdd:cd07083 198 YKVFEIFHEAGFPPGVVQFLPGVGEeVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAII 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 804 VDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAH 883
Cdd:cd07083 278 VDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSY 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 884 IEAMRARGRTVERLPLPDETraGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYRRQDIDALIDAINAWGFGLTFGLHT 961
Cdd:cd07083 358 IEHGKNEGQLVLGGKRLEGE--GYFVAPTVVEEVPPKAriAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYS 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1632883983 962 RLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPR 1020
Cdd:cd07083 436 RKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEMK 494
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
577-1020 |
8.04e-125 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 393.51 E-value: 8.04e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:cd07124 49 ESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRAR-------SDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLI 723
Cdd:cd07124 129 DVAEAIDFLEYYAREMLrlrgfpvEMVPGEDnryvyrPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 724 AAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSATGRPIPLIAETGGQNAM 802
Cdd:cd07124 209 AAKLVEILEEAGLPPGVVNFLPGPGEeVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 803 IVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEA 882
Cdd:cd07124 289 IVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 883 HIEAMRARGRTVERLPLPDETRAGTFVAPTIIE-LEALSDLEQ-EVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLH 960
Cdd:cd07124 369 YIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFAdVPPDHRLAQeEIFGPVLAVIKAK--DFDEALEIANDTEYGLTGGVF 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 961 TRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPR 1020
Cdd:cd07124 447 SRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPK 506
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
577-1009 |
1.65e-116 |
|
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: 370.23 E-value: 1.65e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:COG1012 24 DVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRAR--------SDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPL 722
Cdd:COG1012 103 EVDRAADFLRYYAGEARrlygetipSDAPGTRayvrrePLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 723 IAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQlstrlsATGRPIPLIAETGGQNA 801
Cdd:COG1012 183 SALLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAVGRRIAAA------AAENLKRVTLELGGKNP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIE 881
Cdd:COG1012 257 AIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 882 AHIEAMRARGRTV----ERLPLPDetraGTFVAPTIIElEALSDLE---QEVFGPVLHVIRYRrqDIDALIDAINAWGFG 954
Cdd:COG1012 337 AYIEDAVAEGAELltggRRPDGEG----GYFVEPTVLA-DVTPDMRiarEEIFGPVLSVIPFD--DEEEAIALANDTEYG 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1632883983 955 LTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGvQPFGGHGLSGTGPKAGG 1009
Cdd:COG1012 410 LAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
577-1013 |
1.50e-109 |
|
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: 350.68 E-value: 1.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:pfam00171 10 EVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRARsDLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPL 722
Cdd:pfam00171 89 EVDRAIDVLRYYAGLAR-RLDGETlpsdpgrlaytrrePLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 723 IAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQlstrlsATGRPIPLIAETGGQNA 801
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVTGSGAeVGEALVEHPDVRKVSFTGSTAVGRHIAEA------AAQNLKRVTLELGGKNP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIE 881
Cdd:pfam00171 242 LIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 882 AHIEAMRARGRTVErLPLPDETRAGTFVAPTIIE-LEALSDLEQ-EVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGL 959
Cdd:pfam00171 322 KYVEDAKEEGAKLL-TGGEAGLDNGYFVEPTVLAnVTPDMRIAQeEIFGPVLSVIRFK--DEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1632883983 960 HTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVqPFGGHGLSGTGpKAGGPLYL 1013
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGL 450
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
580-1020 |
1.20e-104 |
|
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: 339.53 E-value: 1.20e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVR 659
Cdd:TIGR01237 52 NPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 660 EAVDFLRYYAvRARSDLAGS---------------TPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIA 724
Cdd:TIGR01237 132 EAIDFMEYYA-RQMIELAKGkpvnsregetnqyvyTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 725 AEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSATGRPIPLIAETGGQNAMI 803
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSeVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 804 VDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAH 883
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 884 IEAMRARGRTVerLPLPDETRAGTFVAPTII-ELEALSDLEQ-EVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHT 961
Cdd:TIGR01237 371 IEIGKAEGRLV--SGGCGDDSKGYFIGPTIFaDVDRKARLAQeEIFGPVVAFIRAS--DFDEALEIANNTEYGLTGGVIS 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1632883983 962 RLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPR 1020
Cdd:TIGR01237 447 NNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAK 505
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
593-1020 |
8.09e-102 |
|
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: 329.17 E-value: 8.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 593 DVTAEAAREAvriaagaAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRA 672
Cdd:cd07078 1 DAAVAAARAA-------FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 673 R--------SDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPA 738
Cdd:cd07078 74 RrlhgevipSPDPGELaivrrePLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 739 DVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQlstrlsATGRPIPLIAETGGQNAMIVDSSALAEQVVADV 817
Cdd:cd07078 154 GVLNVVTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRA------AAENLKRVTLELGGKSPLIVFDDADLDAAVKGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 818 IASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVERL 897
Cdd:cd07078 228 VFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 898 PLPDETRAGTFVAPTIIE--LEALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIH 975
Cdd:cd07078 308 GKRLEGGKGYFVPPTVLTdvDPDMPIAQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1632883983 976 VGNIYVNRNVIGAVVGvQPFGGHGLSGTGpKAGGPLYLQRLVQPR 1020
Cdd:cd07078 386 AGTVWINDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEEYTEPK 428
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
580-1018 |
1.02e-101 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 331.51 E-value: 1.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVR 659
Cdd:PRK03137 56 NPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 660 EAVDFLRYYAVRARSDLAGS--------------TPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAA 725
Cdd:PRK03137 136 EAIDFLEYYARQMLKLADGKpvesrpgehnryfyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 726 EAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQkQLSTRLSATGRPIP-LIAETGGQNAMI 803
Cdd:PRK03137 216 KFVEVLEEAGLPAGVVNFVPGSGSeVGDYLVDHPKTRFITFTGSREVGLRIY-ERAAKVQPGQIWLKrVIAEMGGKDAIV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 804 VDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRlAADIGPVITAEAQARIEAH 883
Cdd:PRK03137 295 VDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSY 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 884 IEAMRARGRTV---ERLPlpdetRAGTFVAPTII-ELEALSDLEQ-EVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFG 958
Cdd:PRK03137 374 IEIGKEEGRLVlggEGDD-----SKGYFIQPTIFaDVDPKARIMQeEIFGPVVAFIKAK--DFDHALEIANNTEYGLTGA 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 959 LHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQ 1018
Cdd:PRK03137 447 VISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQ 506
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
575-1010 |
5.49e-86 |
|
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: 287.22 E-value: 5.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 575 ARPVRNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNA 654
Cdd:cd07097 15 GEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 655 VAEVREAVDFLRYYA---VRARSDLAGST-----------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEET 720
Cdd:cd07097 95 RGEVTRAGQIFRYYAgeaLRLSGETLPSTrpgvevettrePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 721 PLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGGQ 799
Cdd:cd07097 175 PASAWALVEILEEAGLPAGVFNLVMGSGSeVGQALVEHPDVDAVSFTGSTAVGRRIAA------AAAARGARVQLEMGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 800 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQAR 879
Cdd:cd07097 249 NPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 880 IEAHIEAMRARGRTV----ERLPLPDEtraGTFVAPTIIElEALSDL---EQEVFGPVLHVIRYRrqDIDALIDAINAWG 952
Cdd:cd07097 329 DLRYIEIARSEGAKLvyggERLKRPDE---GYYLAPALFA-GVTNDMriaREEIFGPVAAVIRVR--DYDEALAIANDTE 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1632883983 953 FGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVqPFGGHGLSGTGPKAGGP 1010
Cdd:cd07097 403 FGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
578-1004 |
5.30e-78 |
|
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: 264.29 E-value: 5.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAE 657
Cdd:cd07103 1 VINPAT-GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 658 VREAVDFLRYYAVRAR--------SDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLI 723
Cdd:cd07103 80 VDYAASFLEWFAEEARriygrtipSPAPGKRilvikqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 724 AAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAM 802
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAeIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 803 IVDSSALAEQVVADVIASAFDSAGQRC-SALRVLClQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIE 881
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 882 AHIEAMRARGRTV----ERLPLPdetraGTFVAPTIieleaLSD-------LEQEVFGPVLHVIRYRrqDIDALIDAINA 950
Cdd:cd07103 313 ALVEDAVAKGAKVltggKRLGLG-----GYFYEPTV-----LTDvtddmliMNEETFGPVAPIIPFD--TEDEVIARAND 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1632883983 951 WGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVvgVQPFGGHGLSGTG 1004
Cdd:cd07103 381 TPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
578-1008 |
9.16e-76 |
|
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: 259.03 E-value: 9.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEHDDTV----GTVADVTA--EAAREAVRIAAgaaatwaSTPINARATCLERAADALEAAMPDLLALIVREAGKSV 651
Cdd:cd07086 17 SRNPANGEPIArvfpASPEDVEAavAAAREAFKEWR-------KVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKIL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 652 PNAVAEVREAVDfLRYYAVRARSDLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKP 716
Cdd:cd07086 90 PEGLGEVQEMID-ICDYAVGLSRMLYGLTipserpghrlmeqwnPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 717 AEETPLIAAEAVRLLHAA----GVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatGRPIpl 792
Cdd:cd07086 169 SETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRVL-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 793 iAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVI 872
Cdd:cd07086 244 -LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 873 TAEAQARIEAHIEAMRARGRTV----ERLplpDETRAGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYRrqDIDALID 946
Cdd:cd07086 323 NQAAVEKYLNAIEIAKSQGGTVltggKRI---DGGEPGNYVEPTIVTGVTDDAriVQEETFAPILYVIKFD--SLEEAIA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1632883983 947 AINAWGFGLTFGLHTRLDDTIARVTSR--IHVGNIYVNRNVIGAVVGVqPFGGHGLSGTGPKAG 1008
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
597-1020 |
1.43e-75 |
|
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: 254.46 E-value: 1.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 597 EAAREAvriaagaAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARsDL 676
Cdd:cd06534 1 AAARAA-------FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLAD-KL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 677 AGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVL 741
Cdd:cd06534 73 GGPElpspdpggeayvrrePLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 742 QFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQlstrlsATGRPIPLIAETGGQNAMIVDSSALAEQVVADVIAS 820
Cdd:cd06534 153 NVVPGGGDeVGAALLSHPRVDKISFTGSTAVGKAIMKA------AAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 821 AFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAElrIGHTDRLAadigpvitaeaqarieahieamrargrtverlplp 900
Cdd:cd06534 227 AFFNAGQICTAASRLLVHESIYDEFVEKLVTVLVD--VDPDMPIA----------------------------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 901 detragtfvaptiielealsdlEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIY 980
Cdd:cd06534 270 ----------------------QEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVY 325
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1632883983 981 VNRNVIGAVVGvQPFGGHGLSGTGpKAGGPLYLQRLVQPR 1020
Cdd:cd06534 326 INDSSIGVGPE-APFGGVKNSGIG-REGGPYGLEEYTRTK 363
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
579-1010 |
2.94e-75 |
|
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: 257.66 E-value: 2.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 579 RNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEV 658
Cdd:cd07131 19 RNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 659 REAVDFLRYYAVRARSdLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLI 723
Cdd:cd07131 99 QEAIDMAQYAAGEGRR-LFGETvpselpnkdamtrrqPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPAC 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 724 AAEAVRLLHAAGVPADVLQFVPG-DGAIGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlsATGRPIPLIA-ETGGQNA 801
Cdd:cd07131 178 ALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGE-------TCARPNKRVAlEMGGKNP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIE 881
Cdd:cd07131 251 IIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 882 AHIEAMRARGRTV----ERLPlPDETRAGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYrrQDIDALIDAINAWGFGL 955
Cdd:cd07131 331 NYNEIGKEEGATLllggERLT-GGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEV--SSLEEAIEIANDTEYGL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1632883983 956 TFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVqPFGGHGLSGTGPKAGGP 1010
Cdd:cd07131 408 SSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
575-983 |
6.89e-74 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 253.34 E-value: 6.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 575 ARPVRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNA 654
Cdd:cd07088 14 TIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 655 VAEVREAVDFLRYYAVRAR--------SDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEET 720
Cdd:cd07088 93 RVEVEFTADYIDYMAEWARriegeiipSDRPNENififkvPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEET 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 721 PLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQ 799
Cdd:cd07088 173 PLNALEFAELVDEAGLPAGVLNIVTGRGSvVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVSLELGGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 800 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQAR 879
Cdd:cd07088 247 APAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 880 IEAHIEAMRARGRTVERLPLPDETRAGTFVAPTIieleaLSDLEQ-------EVFGPVLHVIRYRrqDIDALIDAINAWG 952
Cdd:cd07088 327 VEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTV-----LTNVRQdmeivqeEIFGPVLPVVKFS--SLDEAIELANDSE 399
|
410 420 430
....*....|....*....|....*....|.
gi 1632883983 953 FGLTFGLHTRLDDTIARVTSRIHVGNIYVNR 983
Cdd:cd07088 400 YGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
601-1002 |
2.71e-71 |
|
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: 244.87 E-value: 2.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 601 EAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREA---VDF-LRYYAVRA---R 673
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMagkIDIsIKAYHERTgerA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 674 SDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGD 747
Cdd:cd07095 84 TPMAQGRavlrhrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 748 GAIGAALVGAPETAGVMFTGSTDVGRLIQKQLStrlsatGRPIPLIA-ETGGQNAMIVDSSALAEQVVADVIASAFDSAG 826
Cdd:cd07095 164 RETGEALAAHEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 827 QRCSALRVLCLQED-VADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIE-AMRARGRTVERLPLPDETR 904
Cdd:cd07095 238 QRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQdLLALGGEPLLAMERLVAGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 905 AgtFVAPTIIELEALSDL-EQEVFGPVLHVIRYrrQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNR 983
Cdd:cd07095 318 A--FLSPGIIDVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNR 393
|
410
....*....|....*....
gi 1632883983 984 NVIGAvVGVQPFGGHGLSG 1002
Cdd:cd07095 394 PTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
578-1004 |
8.46e-70 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 240.89 E-value: 8.46e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAE 657
Cdd:cd07106 1 VINPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 658 VREAVDFLRYYA-----VRARSDLAGS------TPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAE 726
Cdd:cd07106 80 VGGAVAWLRYTAsldlpDEVIEDDDTRrvelrrKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 727 AVRLLHAAgVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSatgrpiPLIAETGGQNAMIVDS 806
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLK------RVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 807 SALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEA 886
Cdd:cd07106 233 DVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 887 MRARGRTVERLPLPDEtRAGTFVAPTII----ELEALSDLEQevFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTR 962
Cdd:cd07106 313 AKAKGAKVLAGGEPLD-GPGYFIPPTIVddppEGSRIVDEEQ--FGPVLPVLKYS--DEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1632883983 963 LDDTIARVTSRIHVGNIYVNRnvIGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07106 388 DLERAEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
577-1004 |
9.27e-70 |
|
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: 241.35 E-value: 9.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:cd07149 2 EVISPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRARSdLAGST-------------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPA 717
Cdd:cd07149 81 EVDRAIETLRLSAEEAKR-LAGETipfdaspggegrigftirePIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 718 EETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRlsatgrpiPLIAET 796
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--------KVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 797 GGQNAMIVDSSALAEQVVADVIASAFDSAGQRC-SALRVLcLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAE 875
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 876 AQARIEAHIEAMRARGRTVERLPlpdeTRAGTFVAPTIIEL--EALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGF 953
Cdd:cd07149 311 EAERIEEWVEEAVEGGARLLTGG----KRDGAILEPTVLTDvpPDMKVVCEEVFAPVVSLNPFD--TLDEAIAMANDSPY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 954 GLTFGLHTRLDDTIARVTSRIHVGNIYVNrNVIGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07149 385 GLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
579-1020 |
1.03e-69 |
|
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: 240.97 E-value: 1.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 579 RNPAEHDDtVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEV 658
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 659 REAVDFLRYYAVRARSDLAGST-----------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP 721
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKvptgllmpnkkatveyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 722 LIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGApETAGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNA 801
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERL------IPVVLELGGKDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAeAQARI- 880
Cdd:cd07099 233 MIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTA-RQLDIv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 881 EAHIEAMRARGRTVeRLPLPDETRAGTFVAPTII--ELEALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFG 958
Cdd:cd07099 312 RRHVDDAVAKGAKA-LTGGARSNGGGPFYEPTVLtdVPHDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYGLSAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632883983 959 LHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGHGLSGTGpKAGGPLYLQRLVQPR 1020
Cdd:cd07099 389 VFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPK 449
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
589-1008 |
2.11e-67 |
|
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: 234.75 E-value: 2.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 589 GTVADVTA--EAAREAVRiaagaAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLR 666
Cdd:cd07114 16 ASAADVDRavAAARAAFE-----GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 667 YYAVRARSdLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLL 731
Cdd:cd07114 91 YYAGLADK-IEGAVipvdkgdylnftrrePLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 732 HAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALA 810
Cdd:cd07114 170 EEAGFPPGVVNVVTGFGPeTGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKSPNIVFDDADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 811 EQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRAR 890
Cdd:cd07114 244 DAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 891 GRTV----ERLPLPDeTRAGTFVAPTIIE--LEALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRlD 964
Cdd:cd07114 324 GARVltggERPSGAD-LGAGYFFEPTILAdvTNDMRIAQEEVFGPVLSVIPFD--DEEEAIALANDSEYGLAAGIWTR-D 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1632883983 965 DTIA-RVTSRIHVGNIYVN---RNVIGAvvgvqPFGGHGLSGTGPKAG 1008
Cdd:cd07114 400 LARAhRVARAIEAGTVWVNtyrALSPSS-----PFGGFKDSGIGRENG 442
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
578-1007 |
2.24e-65 |
|
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: 228.78 E-value: 2.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSV-PNAVA 656
Cdd:cd07108 1 VINPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRArSDLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPL 722
Cdd:cd07108 80 EAAVLADLFRYFGGLA-GELKGETlpfgpdvltytvrePLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 723 IAAEAVRLLHAAgVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGGQNA 801
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEeCGAALVDHPDVDKVTFTGSTEVGKIIYR------AAADRLIPVSLELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASA-FDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARI 880
Cdd:cd07108 232 MIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 881 EAHIEAMRAR-GRTVER---LPLPDETRAGTFVAPTIIE-LEALSDLEQ-EVFGPVLHVIRYRrqDIDALIDAINAWGFG 954
Cdd:cd07108 312 CGYIDLGLSTsGATVLRggpLPGEGPLADGFFVQPTIFSgVDNEWRLAReEIFGPVLCAIPWK--DEDEVIAMANDSHYG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1632883983 955 LTFGLHTRLDDTIARVTSRIHVGNIYVNRNViGAVVGvQPFGGHGLSGTGPKA 1007
Cdd:cd07108 390 LAAYVWTRDLGRALRAAHALEAGWVQVNQGG-GQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
578-1020 |
1.07e-63 |
|
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: 225.93 E-value: 1.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAM-PDLLALIVREAGKSVPNAVA 656
Cdd:cd07123 50 QVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNVWQAEI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVR-EAVDFLRYYAVRAR--------SDLAGST------PL-GPVVCISPWNFPlAIFTGQVAAALVAGNPVLAKPAEeT 720
Cdd:cd07123 130 DAAcELIDFLRFNVKYAEelyaqqplSSPAGVWnrleyrPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSD-T 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 721 PLIAAEAV-RLLHAAGVPADVLQFVPGDG-AIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsATGRPIP-LIAETG 797
Cdd:cd07123 208 AVLSNYLVyKILEEAGLPPGVINFVPGDGpVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENL-DRYRTYPrIVGETG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 798 GQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQ 877
Cdd:cd07123 287 GKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAF 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 878 ARIEAHIEAMR--------ARGRTverlplpDETRaGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYRRQDIDALIDA 947
Cdd:cd07123 367 DRIKGYIDHAKsdpeaeiiAGGKC-------DDSV-GYFVEPTVIETTDPKHklMTEEIFGPVLTVYVYPDSDFEETLEL 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1632883983 948 INAWG-FGLTFGLHTRLDDTIARVTSRIH--VGNIYVNRNVIGAVVGVQPFGGHGLSGTGPKAGGPLYLQRLVQPR 1020
Cdd:cd07123 439 VDTTSpYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPR 514
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
578-1008 |
1.39e-63 |
|
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: 223.39 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATwasTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAE 657
Cdd:cd07146 3 VRNPYT-GEVVGTVPAGTEEALREALALAASYRST---LTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 658 VREAVDFLRYYAVRARSDlAGST-------------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAE 718
Cdd:cd07146 79 VGRAADVLRFAAAEALRD-DGESfscdltangkarkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 719 ETPLIAAEAVRLLHAAGVPADVLQFVPGD-GAIGAALVGAPETAGVMFTGSTDVGRLIqkqlstrlSATGRPIPLIAETG 797
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAI--------AATAGYKRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 798 GQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQ 877
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 878 ARIEAHIEAMRARGRTVerlpLPDETRAGTFVAPTIIEL--EALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGL 955
Cdd:cd07146 310 IQIENRVEEAIAQGARV----LLGNQRQGALYAPTVLDHvpPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1632883983 956 TFGLHTRLDDTIARVTSRIHVGNIYVNrNVIGAVVGVQPFGGHGLSGTGPKAG 1008
Cdd:cd07146 384 SSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
589-1004 |
2.36e-63 |
|
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: 222.88 E-value: 2.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 589 GTVADVTA--EAAREAVRiaagaaATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLR 666
Cdd:cd07109 16 GGAADVDRavQAARRAFE------SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 667 YYAVRARS----------DLAGST---PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHA 733
Cdd:cd07109 90 YYGGAADKlhgetiplgpGYFVYTvrePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 734 AGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGGQNAMIVDSSALAEQ 812
Cdd:cd07109 170 AGLPAGALNVVTGLGAeAGAALVAHPGVDHISFTGSVETGIAVMR------AAAENVVPVTLELGGKSPQIVFADADLEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 813 VVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGH-TDRLaaDIGPVITAEAQARIEAHIEAMRARG 891
Cdd:cd07109 244 ALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPgLEDP--DLGPLISAKQLDRVEGFVARARARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 892 -RTVER-LPLPDETRAGTFVAPTII-ELEALSDLEQ-EVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTI 967
Cdd:cd07109 322 aRIVAGgRIAEGAPAGGYFVAPTLLdDVPPDSRLAQeEIFGPVLAVMPFD--DEAEAIALANGTDYGLVAGVWTRDGDRA 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 1632883983 968 ARVTSRIHVGNIYVNRnvIGAVVGVQ-PFGGHGLSGTG 1004
Cdd:cd07109 400 LRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
578-1004 |
4.72e-61 |
|
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: 216.34 E-value: 4.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEhDDTVGTVADVTAE-------AAREAVriaagaAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKS 650
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAAdvdaaiaAARRAF------DTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 651 VPNAVA-EVREAVDFLRYYAVRARSD--------------LAGST----PLGPVVCISPWNFPLAIFTGQVAAALVAGNP 711
Cdd:cd07089 74 VMTARAmQVDGPIGHLRYFADLADSFpwefdlpvpalrggPGRRVvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 712 VLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDG-AIGAALVGAPETAGVMFTGSTDVGRLIQKQlstrLSATGRPI 790
Cdd:cd07089 154 VVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDnAVGEALTTDPRVDMVSFTGSTAVGRRIMAQ----AAATLKRV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 791 PLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGP 870
Cdd:cd07089 230 LL--ELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 871 VITAEAQARIEAHIEAMRARGRTV----ERlplPDETRAGTFVAPTIieleaLSDLE-------QEVFGPVLHVIRYRrq 939
Cdd:cd07089 308 LISAAQRDRVEGYIARGRDEGARLvtggGR---PAGLDKGFYVEPTL-----FADVDndmriaqEEIFGPVLVVIPYD-- 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1632883983 940 DIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGvqPFGGHGLSGTG 1004
Cdd:cd07089 378 DDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDA--PFGGYKQSGLG 440
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
73-184 |
5.46e-61 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 203.51 E-value: 5.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 73 VDQLVQEFALSTQEGVALMCLAEALLRIPDDATRDALIRDKIAGGDWRAHIGGNRSLFVNAATWGLVVTGKLTASVDDRN 152
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 1632883983 153 LGNALTRLIARAGEPIIRRGVDLAMRMMGEQF 184
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
577-1004 |
6.63e-61 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 217.25 E-value: 6.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:PLN02278 43 PVYNPAT-GEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYA---VRARSDLAGST-----------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPL 722
Cdd:PLN02278 122 EVAYGASFLEYFAeeaKRVYGDIIPSPfpdrrllvlkqPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 723 IAAEAVRLLHAAGVPADVLQFVPGDG-AIGAALVGAPETAGVMFTGSTDVGRLIQKQlstrLSATGRPIPLiaETGGQNA 801
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDApEIGDALLASPKVRKITFTGSTAVGKKLMAG----AAATVKRVSL--ELGGNAP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASAFDSAGQRC-SALRVLcLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARI 880
Cdd:PLN02278 276 FIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 881 EAHIEAMRARGRTV----ERLplpdeTRAGTFVAPTIIElEALSDL---EQEVFGPVLHVIRYRRQDiDALIDAiNAWGF 953
Cdd:PLN02278 355 ESHVQDAVSKGAKVllggKRH-----SLGGTFYEPTVLG-DVTEDMlifREEVFGPVAPLTRFKTEE-EAIAIA-NDTEA 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 954 GLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGvqPFGGHGLSGTG 1004
Cdd:PLN02278 427 GLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
588-1004 |
7.16e-61 |
|
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: 215.89 E-value: 7.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 588 VGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA-EVREAVDFLR 666
Cdd:cd07093 10 LAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 667 YYAVRARSdLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLH 732
Cdd:cd07093 90 FFADYILQ-LDGESypqdggalnyvlrqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 733 AAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALAE 811
Cdd:cd07093 169 EAGLPPGVVNVVHGFGPeAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPNIVFADADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 812 QVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARG 891
Cdd:cd07093 243 RAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 892 RTV---ERLPLPDETRAGTFVAPTIIelEALSD----LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLD 964
Cdd:cd07093 323 ATIltgGGRPELPDLEGGYFVEPTVI--TGLDNdsrvAQEEIFGPVVTVIPFD--DEEEAIELANDTPYGLAAYVWTRDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1632883983 965 DTIARVTSRIHVGNIYVN----RNVigavvgVQPFGGHGLSGTG 1004
Cdd:cd07093 399 GRAHRVARRLEAGTVWVNcwlvRDL------RTPFGGVKASGIG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
590-1002 |
2.50e-60 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 215.21 E-value: 2.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 590 TVADVTA--EAAREAvriaagaAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVD---- 663
Cdd:PRK09457 35 TAAQVDAavRAARAA-------FPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINkiai 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 664 FLRYYAVR---ARSDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAA 734
Cdd:PRK09457 108 SIQAYHERtgeKRSEMADGAavlrhrPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 735 GVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLStrlsatGRPIPLIA-ETGGQNAMIVDSSALAEQV 813
Cdd:PRK09457 188 GLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFA------GQPEKILAlEMGGNNPLVIDEVADIDAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 814 VADVIASAFDSAGQRCS-ALRVLCLQEDVADRVLAMLKGALAELRIGHTDrlaAD----IGPVITAEAQARI-EAHIEAM 887
Cdd:PRK09457 262 VHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRWD---AEpqpfMGAVISEQAAQGLvAAQAQLL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 888 RARGRTVERLPLPDETRAgtFVAPTIIELEALSDL-EQEVFGPVLHVIRYrrQDIDALIDAINAWGFGLTFGLHTRLDDT 966
Cdd:PRK09457 339 ALGGKSLLEMTQLQAGTG--LLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDFDEAIRLANNTRFGLSAGLLSDDRED 414
|
410 420 430
....*....|....*....|....*....|....*.
gi 1632883983 967 IARVTSRIHVGNIYVNRNVIGAvVGVQPFGGHGLSG 1002
Cdd:PRK09457 415 YDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
588-1008 |
3.99e-60 |
|
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: 213.71 E-value: 3.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 588 VGTVADVTA--EAAREAVRiaagaaaTWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFL 665
Cdd:cd07101 14 QSTPADVEAafARARAAQR-------AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 666 RYYAVRARSDLA-----------GST-----PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVR 729
Cdd:cd07101 87 RYYARRAERLLKprrrrgaipvlTRTtvnrrPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 730 LLHAAGVPADVLQFVPGDGA-IGAALVGapETAGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSA 808
Cdd:cd07101 167 LLIEAGLPRDLWQVVTGPGSeVGGAIVD--NADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 809 LAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMR 888
Cdd:cd07101 239 DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 889 ARGRTVerL----PLPDETRAgtFVAPTIIE--LEALSDLEQEVFGPVLHVirYRRQDIDALIDAINAWGFGLTFGLHTR 962
Cdd:cd07101 319 AKGATV--LaggrARPDLGPY--FYEPTVLTgvTEDMELFAEETFGPVVSI--YRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1632883983 963 LDDTIARVTSRIHVGNIYVNRNVIGAVVGVQ-PFGGHGLSGTGPKAG 1008
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
577-1004 |
4.32e-60 |
|
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: 213.75 E-value: 4.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:cd07145 2 EVRNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRARsDLAGST-------------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPA 717
Cdd:cd07145 81 EVERTIRLFKLAAEEAK-VLRGETipvdayeynerriaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 718 EETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQlstrlsATGRPIPLIAET 796
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSeVGDEIVTNPKVNMISFTGSTAVGLLIASK------AGGTGKKVALEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 797 GGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEA 876
Cdd:cd07145 234 GGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 877 QARIEAHIEAMRARGRTVERLPLPDEtraGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFG 954
Cdd:cd07145 314 VERMENLVNDAVEKGGKILYGGKRDE---GSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVK--DDEEAVEIANSTEYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1632883983 955 LTFGLHTRLDDTIARVTSRIHVGNIYVN---RNVIGAVvgvqPFGGHGLSGTG 1004
Cdd:cd07145 389 LQASVFTNDINRALKVARELEAGGVVINdstRFRWDNL----PFGGFKKSGIG 437
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
577-1004 |
4.48e-60 |
|
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: 213.97 E-value: 4.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEHDdTVGTVADVTAEAAREA-VRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAV 655
Cdd:cd07082 19 EVYSPIDGE-VIGSVPALSALEILEAaETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 656 AEVREAVDFLRYyAVRARSDLAGST-------------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKP 716
Cdd:cd07082 98 KEVDRTIDYIRD-TIEELKRLDGDSlpgdwfpgtkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 717 AEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTrlsatgrpIPLIAE 795
Cdd:cd07082 177 ATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGReIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM--------KRLVLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 796 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAE 875
Cdd:cd07082 249 LGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 876 AQARIEAHIEAMRARGRTVErlpLPDETRAGTFVAPTIIELEAlSDLE---QEVFGPVLHVIRYRrqDIDALIDAINAWG 952
Cdd:cd07082 329 SADFVEGLIDDAVAKGATVL---NGGGREGGNLIYPTLLDPVT-PDMRlawEEPFGPVLPIIRVN--DIEEAIELANKSN 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1632883983 953 FGLTFGLHTRLDDTIARVTSRIHVGNIYVN----RNvigavVGVQPFGGHGLSGTG 1004
Cdd:cd07082 403 YGLQASIFTKDINKARKLADALEVGTVNINskcqRG-----PDHFPFLGRKDSGIG 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
577-1004 |
6.79e-60 |
|
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: 213.53 E-value: 6.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:cd07085 19 DVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVR---EAVDFlryyAVRARSDLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAE 718
Cdd:cd07085 98 DVLrglEVVEF----ACSIPHLLKGEYlenvargidtysyrqPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 719 ETPLIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKqlstRLSATGRPIplIAETGG 798
Cdd:cd07085 174 RVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYE----RAAANGKRV--QALGGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 799 QNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQA 878
Cdd:cd07085 248 KNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 879 RIEAHIE---AMRAR----GRTVERLPLPDetraGTFVAPTIIElEALSDLE---QEVFGPVLHVIRYRrqDIDALIDAI 948
Cdd:cd07085 328 RIEGLIEsgvEEGAKlvldGRGVKVPGYEN----GNFVGPTILD-NVTPDMKiykEEIFGPVLSIVRVD--TLDEAIAII 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1632883983 949 NAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVnrNV-IGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07085 401 NANPYGNGAAIFTRSGAAARKFQREVDAGMVGI--NVpIPVPLAFFSFGGWKGSFFG 455
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
545-1004 |
1.28e-58 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 211.28 E-value: 1.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 545 AVLADLAERFATASRePAHAAPSP----RLATLParpvrnpaehddtVGTVADVTA--EAAREAVRiaagaaaTWASTPI 618
Cdd:PRK09407 17 ERLRRLTARVDGAAG-PTREVTAPftgePLATVP-------------VSTAADVEAafARARAAQR-------AWAATPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 619 NARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLA-----------GST-----PL 682
Cdd:PRK09407 76 RERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAprrragalpvlTKTtelrqPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 683 GPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVgaPETA 761
Cdd:PRK09407 156 GVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPvVGTALV--DNAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 762 GVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDV 841
Cdd:PRK09407 234 YLMFTGSTATGRVLAEQAGRRL------IGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 842 ADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVER--LPLPDETRAgtFVAPTIieleaL 919
Cdd:PRK09407 308 YDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAggKARPDLGPL--FYEPTV-----L 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 920 SDLE-------QEVFGPVLHVirYRRQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGV 992
Cdd:PRK09407 381 TGVTpdmelarEETFGPVVSV--YPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSV 458
|
490
....*....|...
gi 1632883983 993 Q-PFGGHGLSGTG 1004
Cdd:PRK09407 459 DaPMGGMKDSGLG 471
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
599-1010 |
1.43e-58 |
|
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: 208.54 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 599 AREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRAR----- 673
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRrpege 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 674 ---SDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP-----LIAaeavRLLHAAGVPAD 739
Cdd:cd07104 82 ilpSDVPGKEsmvrrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 740 VLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQkqlstrlSATGRPIPLIA-ETGGQNAMIVDSSALAEQVVADV 817
Cdd:cd07104 158 VLNVVPGGGSeIGDALVEHPRVRMISFTGSTAVGRHIG-------ELAGRHLKKVAlELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 818 IASAFDSAGQRC-SALRVLcLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVer 896
Cdd:cd07104 231 AFGAFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 897 lpLPDETRAGTFVAPTIieleaLSDL-------EQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIAR 969
Cdd:cd07104 308 --LTGGTYEGLFYQPTV-----LSDVtpdmpifREEIFGPVAPVIPFD--DDEEAVELANDTEYGLSAAVFTRDLERAMA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1632883983 970 VTSRIHVGNIYVNRNVI--GAVVgvqPFGGHGLSGTGpKAGGP 1010
Cdd:cd07104 379 FAERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
588-1004 |
2.31e-58 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 208.44 E-value: 2.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 588 VGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRY 667
Cdd:cd07094 12 IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 668 YAVRARS---------DLAGST---------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVR 729
Cdd:cd07094 92 AAEEAERirgeeipldATQGSDnrlawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 730 LLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLstrlsatgrPIPLIA-ETGGQNAMIVDSS 807
Cdd:cd07094 172 ILVEAGVPEGVLQVVTGEREvLGDAFAADERVAMLSFTGSAAVGEALRANA---------GGKRIAlELGGNAPVIVDRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 808 ALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHI-EA 886
Cdd:cd07094 243 ADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVeEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 887 MRARGRTverlpLPDETRAGTFVAPTIIELEALSDL--EQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLD 964
Cdd:cd07094 323 VEAGARL-----LCGGERDGALFKPTVLEDVPRDTKlsTEETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1632883983 965 DTIARVTSRIHVGNIYVNRNVIgAVVGVQPFGGHGLSGTG 1004
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
577-1004 |
4.35e-58 |
|
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: 208.13 E-value: 4.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGK------- 649
Cdd:cd07138 17 DVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGApitlara 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 650 -SVPNAVAEVREAVDFLRYYAVRARsdlAGST-----PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLI 723
Cdd:cd07138 96 aQVGLGIGHLRAAADALKDFEFEER---RGNSlvvrePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 724 AAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlsATGRPIPLIA-ETGGQNA 801
Cdd:cd07138 173 AIILAEILDEAGLPAGVFNLVNGDGPvVGEALSAHPDVDMVSFTGSTRAGKRVAE-------AAADTVKRVAlELGGKSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIE 881
Cdd:cd07138 246 NIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 882 AHIEAMRARGRTV-----ERlplPDETRAGTFVAPTIieleaLSDL-------EQEVFGPVLHVIRYRrqDIDALIDAIN 949
Cdd:cd07138 326 GYIQKGIEEGARLvaggpGR---PEGLERGYFVKPTV-----FADVtpdmtiaREEIFGPVLSIIPYD--DEDEAIAIAN 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1632883983 950 AWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRnviGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07138 396 DTPYGLAGYVWSADPERARAVARRLRAGQVHING---AAFNPGAPFGGYKQSGNG 447
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
589-962 |
4.71e-58 |
|
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: 208.21 E-value: 4.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 589 GTVADV--TAEAAREAVRIAAgaaatwaSTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLR 666
Cdd:cd07130 31 ATPEDYesTIKAAQEAFKEWR-------DVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 667 YyAVRARSDLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRL- 730
Cdd:cd07130 104 F-AVGLSRQLYGLTipserpghrmmeqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 731 ---LHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatGRpipLIAETGGQNAMIVDSS 807
Cdd:cd07130 183 arvLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---GR---SLLELGGNNAIIVMED 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 808 ALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGhtDRLAAD--IGPVITAEAQARIEAHIE 885
Cdd:cd07130 257 ADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIG--DPLDDGtlVGPLHTKAAVDNYLAAIE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 886 AMRARGRTV----ERLplpdeTRAGTFVAPTIIELEALSDL-EQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLH 960
Cdd:cd07130 335 EAKSQGGTVlfggKVI-----DGPGNYVEPTIVEGLSDAPIvKEETFAPILYVLKFD--TLEEAIAWNNEVPQGLSSSIF 407
|
..
gi 1632883983 961 TR 962
Cdd:cd07130 408 TT 409
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
586-1010 |
9.30e-57 |
|
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: 203.68 E-value: 9.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 586 DTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFL 665
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 666 RYYA-------------VRARSDLAGSTPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP-----LIAaea 727
Cdd:cd07152 82 HEAAglptqpqgeilpsAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggvVIA--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 728 vRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQkqlstrlSATGRPIPLIA-ETGGQNAMIVDS 806
Cdd:cd07152 159 -RLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVG-------EAAGRHLKKVSlELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 807 SALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEA 886
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 887 MRARGRTVErlplPDETRAGTFVAPTIIE--LEALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLD 964
Cdd:cd07152 311 SVAAGARLE----AGGTYDGLFYRPTVLSgvKPGMPAFDEEIFGPVAPVTVFD--SDEEAVALANDTEYGLSAGIISRDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1632883983 965 DTIARVTSRIHVGNIYVNRNVIGAVVgVQPFGGHGLSGTGPKAGGP 1010
Cdd:cd07152 385 GRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
576-1010 |
9.35e-57 |
|
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: 203.72 E-value: 9.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 576 RPVRNPAehDDTV-GTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNA 654
Cdd:cd07150 1 FDDLNPA--DGSVyARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 655 VAEVREAVDFLRYYAVRAR--------SDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEET 720
Cdd:cd07150 79 WFETTFTPELLRAAAGECRrvrgetlpSDSPGTVsmsvrrPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 721 PLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIqkqlSTRLSATGRPIPLiaETGGQ 799
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFNVVTGGGAeVGDELVDDPRVRMVTFTGSTAVGREI----AEKAGRHLKKITL--ELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 800 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQAR 879
Cdd:cd07150 233 NPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 880 IEAHIEAMRARGRTVerlpLPDETRAGTFVAPTIIE--LEALSDLEQEVFGPVLHVIRYrRQDIDALIDAiNAWGFGLTF 957
Cdd:cd07150 313 IKRQVEDAVAKGAKL----LTGGKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPA-KDAEEALELA-NDTEYGLSA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1632883983 958 GLHTRLDDTIARVTSRIHVGNIYVNRNVI--GAVVgvqPFGGHGLSGTGpKAGGP 1010
Cdd:cd07150 387 AILTNDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGE 437
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
576-1004 |
6.85e-56 |
|
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: 202.16 E-value: 6.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 576 RPVRNPAEhDDTVGTVADVTAEAAREAVRIAAGA--AATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPN 653
Cdd:cd07119 15 RDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 654 AVAEVREAVDFLRYYAVRARSDlAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEE 719
Cdd:cd07119 94 SEIDIDDVANCFRYYAGLATKE-TGEVydvpphvisrtvrePVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 720 TPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGG 798
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVNLVTGSGAtVGAELAESPDVDLVSFTGGTATGRSIMR------AAAGNVKKVALELGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 799 QNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQA 878
Cdd:cd07119 247 KNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHRE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 879 RIEAHIEAMRARGRTVE---RLPLPDETRAGTFVAPTIIElEALSDL---EQEVFGPVLHVIRYRRQDiDALIDAiNAWG 952
Cdd:cd07119 327 KVLSYIQLGKEEGARLVcggKRPTGDELAKGYFVEPTIFD-DVDRTMrivQEEIFGPVLTVERFDTEE-EAIRLA-NDTP 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1632883983 953 FGLTFGLHTRlDDTIA-RVTSRIHVGNIYVNRnvIGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07119 404 YGLAGAVWTK-DIARAnRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
580-1008 |
9.60e-55 |
|
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: 198.05 E-value: 9.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAV-AEV 658
Cdd:cd07115 3 NPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 659 REAVDFLRYYAVRARSdLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIA 724
Cdd:cd07115 82 PRAADTFRYYAGWADK-IEGEVipvrgpflnytvrePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 725 AEAVRLLHAAGVPADVLQFVPGDGAI-GAALVGAPETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGGQNAMI 803
Cdd:cd07115 161 LRIAELMAEAGFPAGVLNVVTGFGEVaGAALVEHPDVDKITFTGSTAVGRKIMQ------GAAGNLKRVSLELGGKSANI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 804 VDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAH 883
Cdd:cd07115 235 VFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 884 IEAMRARGRTVERLPLPDETRaGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYRRQDiDALIDAiNAWGFGLTFGLHT 961
Cdd:cd07115 315 VDVGREEGARLLTGGKRPGAR-GFFVEPTIFAAVPPEMriAQEEIFGPVVSVMRFRDEE-EALRIA-NGTEYGLAAGVWT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1632883983 962 RLDDTIARVTSRIHVGNIYVnrNVIGAVVGVQPFGGHGLSGTGPKAG 1008
Cdd:cd07115 392 RDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
588-1010 |
1.81e-54 |
|
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: 197.80 E-value: 1.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 588 VGTVADVTA--EAAREAVRiaagaAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAV-AEVREAVDF 664
Cdd:cd07139 32 EATPADVDAavAAARRAFD-----NGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRrAQGPGPAAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 665 LRYYA--------VRARSDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIA---AEA 727
Cdd:cd07139 107 LRYYAalardfpfEERRPGSGGGHvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAyllAEA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 728 VrllHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatgRPIPLiaETGGQNAMIVDSS 807
Cdd:cd07139 187 A---EEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL----ARVTL--ELGGKSAAIVLDD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 808 ALAEQVVADVIASAFDSAGQRCSAL-RVLCLQEDvADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEA 886
Cdd:cd07139 258 ADLDAAVPGLVPASLMNNGQVCVALtRILVPRSR-YDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 887 MRARGRTV----ERLPLPDEtraGTFVAPTII-ELEALSDLEQ-EVFGPVLHVIRYrrQDIDALIDAINAWGFGLTFGLH 960
Cdd:cd07139 337 GRAEGARLvtggGRPAGLDR---GWFVEPTLFaDVDNDMRIAQeEIFGPVLSVIPY--DDEDDAVRIANDSDYGLSGSVW 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 961 TRLDDTIARVTSRIHVGNIYVNrnviGAVVGVQ-PFGGHGLSGTGpKAGGP 1010
Cdd:cd07139 412 TADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGP 457
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
578-1004 |
2.32e-53 |
|
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: 194.13 E-value: 2.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAE 657
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 658 VREAVDFLRYYAVRArSDLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLI 723
Cdd:cd07107 80 VMVAAALLDYFAGLV-TELKGETipvggrnlhytlrePYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 724 A---AEAVRLLhaagVPADVLQFVPGDGAI-GAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSatgrpiPLIAETGGQ 799
Cdd:cd07107 159 AlrlAELAREV----LPPGVFNILPGDGATaGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 800 NAMIV----DSSALAEQVVADViasAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAE 875
Cdd:cd07107 229 NALIVfpdaDPEAAADAAVAGM---NFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 876 AQARIEAHIEAMRARGR---TVERLPLPDETRAGTFVAPTII-ELEALSDLEQ-EVFGPVLHVIRYRrqDIDALIDAINA 950
Cdd:cd07107 306 QYDRVMHYIDSAKREGArlvTGGGRPEGPALEGGFYVEPTVFaDVTPGMRIAReEIFGPVLSVLRWR--DEAEMVAQANG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1632883983 951 WGFGLTFGLHTRLDDTIARVTSRIHVGNIYVN---RNVIGAvvgvqPFGGHGLSGTG 1004
Cdd:cd07107 384 VEYGLTAAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
578-1004 |
2.21e-52 |
|
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: 191.03 E-value: 2.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAE 657
Cdd:cd07110 1 VINPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 658 VREAVDFLRYYAVRAR--------------SDLAGST---PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEET 720
Cdd:cd07110 80 VDDVAGCFEYYADLAEqldakaeravplpsEDFKARVrrePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 721 PLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQkqlsTRLSATGRPIPLiaETGGQ 799
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDeAGAPLAAHPGIDKISFTGSTATGSQVM----QAAAQDIKPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 800 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQAR 879
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 880 IEAHIEAMRARGRTV----ERlplPDETRAGTFVAPTII-ELEALSDL-EQEVFGPVLHVIRYRRQDiDAlIDAINAWGF 953
Cdd:cd07110 314 VLSFIARGKEEGARLlcggRR---PAHLEKGYFIAPTVFaDVPTDSRIwREEIFGPVLCVRSFATED-EA-IALANDSEY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1632883983 954 GLTFGLHTRLDDTIARVTSRIHVGNIYVNRNvigAVVGVQ-PFGGHGLSGTG 1004
Cdd:cd07110 389 GLAAAVISRDAERCDRVAEALEAGIVWINCS---QPCFPQaPWGGYKRSGIG 437
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
615-1004 |
3.97e-52 |
|
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: 189.59 E-value: 3.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 615 STPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLAGST-------------P 681
Cdd:cd07100 17 KTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADEPietdagkayvryeP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 682 LGPVVCISPWNFPLAiftgQV----AAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGA 757
Cdd:cd07100 97 LGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQVEAIIAD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 758 PETAGVMFTGSTDVGRLIQKQlstrlsaTGRPI-PLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRC-SALRVL 835
Cdd:cd07100 173 PRVRGVTLTGSERAGRAVAAE-------AGKNLkKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCiAAKRFI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 836 cLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTV----ERLPlpdetRAGTFVAP 911
Cdd:cd07100 246 -VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLllggKRPD-----GPGAFYPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 912 TIieleaLSDLE-------QEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNrn 984
Cdd:cd07100 320 TV-----LTDVTpgmpaydEELFGPVAAVIKVK--DEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN-- 390
|
410 420
....*....|....*....|...
gi 1632883983 985 vigAVVGVQ---PFGGHGLSGTG 1004
Cdd:cd07100 391 ---GMVKSDprlPFGGVKRSGYG 410
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
577-1008 |
6.06e-52 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 190.50 E-value: 6.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVA-------DVTAEAAREAVRIAAGAAatwaSTPINaRATCLERAADALEAAMPDLLALIVREAGK 649
Cdd:cd07091 22 PTINPAT-EEVICQVAeadeedvDAAVKAARAAFETGWWRK----MDPRE-RGRLLNKLADLIERDRDELAALESLDNGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 650 SVP-NAVAEVREAVDFLRYYAVRArSDLAGST--------------PLGpvVC--ISPWNFPLAIFTGQVAAALVAGNPV 712
Cdd:cd07091 96 PLEeSAKGDVALSIKCLRYYAGWA-DKIQGKTipidgnflaytrrePIG--VCgqIIPWNFPLLMLAWKLAPALAAGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 713 LAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAI-GAALVGAPETAGVMFTGSTDVGRLIQKQLStrlSATGRPIP 791
Cdd:cd07091 173 VLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTaGAAISSHMDVDKIAFTGSTAVGRTIMEAAA---KSNLKKVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 792 LiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGhtDRLAADI--G 869
Cdd:cd07091 250 L--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG--DPFDPDTfqG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 870 PVITAEAQARIEAHIEAMRARGRTV----ERLPlpdetRAGTFVAPTIieleaLSDLE-------QEVFGPVLHVIRYRr 938
Cdd:cd07091 326 PQVSKAQFDKILSYIESGKKEGATLltggERHG-----SKGYFIQPTV-----FTDVKddmkiakEEIFGPVVTILKFK- 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 939 qDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNR-NVIGAVVgvqPFGGHGLSGTGPKAG 1008
Cdd:cd07091 395 -TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
580-1004 |
1.82e-51 |
|
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: 188.32 E-value: 1.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWA-STPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEV 658
Cdd:cd07120 3 DPAT-GEVIGTYADGGVAEAEAAIAAARRAFDETDwAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 659 REAVDFLRYYAVRARSdLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIA 724
Cdd:cd07120 82 SGAISELRYYAGLART-EAGRMiepepgsfslvlrePMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 725 AEAVRLLHAA-GVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSATGrpipliAETGGQNAM 802
Cdd:cd07120 161 AAIIRILAEIpSLPAGVVNLFTESGSeGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTPC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 803 IVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEA 882
Cdd:cd07120 235 IVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 883 HIE-AMRARGRTVERL-PLPDETRAGTFVAPTIIELE--ALSDLEQEVFGPVLHVIRYRRQDiDALIDAiNAWGFGLTFG 958
Cdd:cd07120 315 MVErAIAAGAEVVLRGgPVTEGLAKGAFLRPTLLEVDdpDADIVQEEIFGPVLTLETFDDEA-EAVALA-NDTDYGLAAS 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1632883983 959 LHTRLDDTIARVTSRIHVGNIYVNRNviGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07120 393 VWTRDLARAMRVARAIRAGTVWINDW--NKLFAEAEEGGYRQSGLG 436
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
579-1008 |
2.35e-51 |
|
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: 188.32 E-value: 2.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 579 RNPAeHDDTVGTVADVTAEAAREAVRIAAGA--AATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:cd07118 2 RSPA-HGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRARSdLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP 721
Cdd:cd07118 81 EIEGAADLWRYAASLART-LHGDSynnlgddmlglvlrePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 722 LIAAEAVRLLHAAGVPADVLQFVPGDGAI-GAALVGAPETAGVMFTGSTDVGRLIqkqlstrLSATGRPIPLIA-ETGGQ 799
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATvGQAMTEHPDVDMVSFTGSTRVGKAI-------AAAAARNLKKVSlELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 800 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQAR 879
Cdd:cd07118 233 NPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 880 IEAHIEAMRARGRTV----ERLPlpdeTRAGTFVAPTIIE--LEALSDLEQEVFGPVLHVIRYrrQDIDALIDAINAWGF 953
Cdd:cd07118 313 ITDYVDAGRAEGATLllggERLA----SAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVY 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1632883983 954 GLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVvgVQPFGGHGLSGTGPKAG 1008
Cdd:cd07118 387 GLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
578-1004 |
5.24e-51 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 187.13 E-value: 5.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAE 657
Cdd:cd07090 1 VIEPAT-GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 658 VREAVDFLRYYAVRArSDLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLI 723
Cdd:cd07090 80 IDSSADCLEYYAGLA-PTLSGEHvplpggsfaytrrePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 724 AAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatgRPIPLiaETGGQNAMI 803
Cdd:cd07090 159 ALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 804 VDSSALAEQVVADVIASAFDSAGQRCS-ALRVLcLQEDVADRVLAMLKGALAELRIGhtDRLAAD--IGPVITAEAQARI 880
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIG--DPLDEDtqMGALISEEHLEKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 881 EAHIEAMRARGRTV----ERLPLPDETRAGTFVAPTIieLEALSD----LEQEVFGPVLHVIRYrrQDIDALIDAINAWG 952
Cdd:cd07090 310 LGYIESAKQEGAKVlcggERVVPEDGLENGFYVSPCV--LTDCTDdmtiVREEIFGPVMSILPF--DTEEEVIRRANDTT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1632883983 953 FGLTFGLHTRLDDTIARVTSRIHVGNIYVNR-NVIGAVVgvqPFGGHGLSGTG 1004
Cdd:cd07090 386 YGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
620-1004 |
9.08e-51 |
|
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: 186.65 E-value: 9.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 620 ARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA-EVREAVDFLRYY-----------AVRARSDLAGST--PLGPV 685
Cdd:cd07112 49 ERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAvDVPSAANTFRWYaeaidkvygevAPTGPDALALITrePLGVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 686 VCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVM 764
Cdd:cd07112 129 GAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHtAGEALGLHMDVDALA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 765 FTGSTDVGRLIQkqlstRLSATGRPIPLIAETGGQNAMIV-DSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVAD 843
Cdd:cd07112 209 FTGSTEVGRRFL-----EYSGQSNLKRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 844 RVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTV----ERLplpDETRAGTFVAPTIIE-LEA 918
Cdd:cd07112 284 EFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEGARLvaggKRV---LTETGGFFVEPTVFDgVTP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 919 LSDLEQ-EVFGPVLHVIRYRRQDiDALIDAiNAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVnrNVIGAVVGVQPFGG 997
Cdd:cd07112 361 DMRIAReEIFGPVLSVITFDSEE-EAVALA-NDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGG 436
|
....*..
gi 1632883983 998 HGLSGTG 1004
Cdd:cd07112 437 FKQSGNG 443
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
578-1004 |
9.25e-51 |
|
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: 186.88 E-value: 9.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEhDDTVGTVADVTAEAAREAVRIAAGA-AATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVP-NAV 655
Cdd:cd07113 19 ITNPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHlSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 656 AEVREAVDFLRYYAVRArSDLAGST--------------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAK 715
Cdd:cd07113 98 FEVGQSANFLRYFAGWA-TKINGETlapsipsmqgerytaftrrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 716 PAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSAtgrpipLIAE 795
Cdd:cd07113 177 PSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTR------VTLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 796 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAE 875
Cdd:cd07113 251 LGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 876 AQARIEAHIEAMRARGRTV----ERLPlpdetRAGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYrrQDIDALIDAIN 949
Cdd:cd07113 331 HFDKVCSYLDDARAEGDEIvrggEALA-----GEGYFVQPTLVLARSADSrlMREETFGPVVSFVPY--EDEEELIQLIN 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1632883983 950 AWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVN-RNVIGAVVgvqPFGGHGLSGTG 1004
Cdd:cd07113 404 DTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
577-1010 |
9.71e-51 |
|
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: 187.22 E-value: 9.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKsvpnAVA 656
Cdd:cd07111 40 PTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK----PIR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVRE-----AVDFLRYYAVRAR---SDLAGSTPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAV 728
Cdd:cd07111 115 ESRDcdiplVARHFYHHAGWAQlldTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 729 RLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQlstrLSATGRPIPLiaETGGQNAMIVDSSA 808
Cdd:cd07111 195 EICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRA----TAGTGKKLSL--ELGGKSPFIVFDDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 809 LAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMR 888
Cdd:cd07111 269 DLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 889 ARGRTVER--LPLPDEtraGTFVAPTIIE-LEALSDLEQ-EVFGPVLHVIRYRRQDiDALIDAiNAWGFGLTFGLHTRLD 964
Cdd:cd07111 349 AEGADVFQpgADLPSK---GPFYPPTLFTnVPPASRIAQeEIFGPVLVVLTFRTAK-EAVALA-NNTPYGLAASVWSENL 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1632883983 965 DTIARVTSRIHVGNIYVN-RNVIGAVVgvqPFGGHGLSGTGpKAGGP 1010
Cdd:cd07111 424 SLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGK 466
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
621-1008 |
2.12e-50 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 186.16 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 621 RATCLERAADALEAAMPDLLALIVREAGKSVPNA-VAEVREAVDFLRYYAVRArSDLAGST--------------PLGPV 685
Cdd:cd07142 67 RSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWA-DKIHGMTlpadgphhvytlhePIGVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 686 VCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVM 764
Cdd:cd07142 146 GQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPtAGAAIASHMDVDKVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 765 FTGSTDVGRLIqkqlsTRLSATGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADR 844
Cdd:cd07142 226 FTGSTEVGKII-----MQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 845 VLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTV----ERLplpdeTRAGTFVAPTIIE--LEA 918
Cdd:cd07142 301 FVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLitggDRI-----GSKGYYIQPTIFSdvKDD 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 919 LSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVN-RNVIGAVVgvqPFGG 997
Cdd:cd07142 376 MKIARDEIFGPVQSILKFK--TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGG 450
|
410
....*....|.
gi 1632883983 998 HGLSGTGPKAG 1008
Cdd:cd07142 451 YKMSGIGREKG 461
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
581-983 |
7.05e-50 |
|
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: 183.60 E-value: 7.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 581 PAEHDDTVGTVADVTAEAAREAVRiaagaaatwasTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVRE 660
Cdd:cd07102 13 PLASLEAVRAALERARAAQKGWRA-----------VPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 661 AVDFLRYYAVRARSDLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAE 726
Cdd:cd07102 82 MLERARYMISIAEEALADIRvpekdgferyirrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 727 AVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGGQNAMIVDS 806
Cdd:cd07102 162 FAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQR------AAAGRFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 807 SALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEA 886
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 887 MRARGRTVE----RLPLPDETraGTFVAPTIieleaLSD-------LEQEVFGPVLHVIRYrrQDIDALIDAINAWGFGL 955
Cdd:cd07102 316 AIAKGARALidgaLFPEDKAG--GAYLAPTV-----LTNvdhsmrvMREETFGPVVGIMKV--KSDAEAIALMNDSEYGL 386
|
410 420
....*....|....*....|....*...
gi 1632883983 956 TFGLHTRLDDTIARVTSRIHVGNIYVNR 983
Cdd:cd07102 387 TASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
593-1008 |
2.62e-49 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 182.73 E-value: 2.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 593 DVTAEAAREAVRiaagaAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA-EVREAVDFLRYYAVR 671
Cdd:cd07143 47 DIAVEVAHAAFE-----TDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 672 ARSDLaGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVP 737
Cdd:cd07143 122 ADKIH-GQVietdikkltytrhePIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 738 ADVLQFVPGDG-AIGAALVGAPETAGVMFTGSTDVGRLIQKQLStrlSATGRPIPLiaETGGQNAMIVDSSALAEQVVAD 816
Cdd:cd07143 201 PGVINVVSGYGrTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA---KSNLKKVTL--ELGGKSPNIVFDDADLESAVVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 817 VIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTV-- 894
Cdd:cd07143 276 TAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVet 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 895 --ERlplpdETRAGTFVAPTIIElEALSDL---EQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIAR 969
Cdd:cd07143 356 ggKR-----HGNEGYFIEPTIFT-DVTEDMkivKEEIFGPVVAVIKFK--TEEEAIKRANDSTYGLAAAVFTNNINNAIR 427
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1632883983 970 VTSRIHVGNIYVN-RNVIGAVVgvqPFGGHGLSGTGPKAG 1008
Cdd:cd07143 428 VANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
577-1004 |
2.68e-49 |
|
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: 182.06 E-value: 2.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEHDdTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:cd07147 2 EVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRARS------DLAGST------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAE 718
Cdd:cd07147 81 EVARAIDTFRIAAEEATRiygevlPLDISArgegrqglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 719 ETPLIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQlstrlsaTGRPiPLIAETGG 798
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKAR-------AGKK-KVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 799 QNAMIVDSSALAEQVVADVIASAFDSAGQRC-SALRVLcLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQ 877
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 878 ARIEAHIEAMRARGRTVerlpLPDETRAGTFVAPTIIELEALSDL--EQEVFGPVLHVIRYrrQDIDALIDAINAWGFGL 955
Cdd:cd07147 312 ERVEGWVNEAVDAGAKL----LTGGKRDGALLEPTILEDVPPDMEvnCEEVFGPVVTVEPY--DDFDEALAAVNDSKFGL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1632883983 956 TFGLHTRLDDTIARVTSRIHVGNIYVNrNVIGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07147 386 QAGVFTRDLEKALRAWDELEVGGVVIN-DVPTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
615-1004 |
4.50e-49 |
|
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: 180.85 E-value: 4.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 615 STPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLAGS--------------T 680
Cdd:cd07105 18 KTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSipsdkpgtlamvvkE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFV---PGDGA-IGAALVG 756
Cdd:cd07105 98 PVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPeVVEALIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 757 APETAGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRC-SALRVL 835
Cdd:cd07105 178 HPAVRKVNFTGSTRVGRIIAETAAKHL------KPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICmSTERII 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 836 cLQEDVADRVLAMLKGALAELRIGHTdrlaaDIGPVITAEAQARIEAHIEAMRARGRTVERLPLPDETRAGTFVAPTIIE 915
Cdd:cd07105 252 -VHESIADEFVEKLKAAAEKLFAGPV-----VLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPPTILD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 916 -LEALSDLEQ-EVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRlDDTIA-RVTSRIHVGNIYVNrnviGAVVGV 992
Cdd:cd07105 326 nVTPDMDIYSeESFGPVVSIIRVK--DEEEAVRIANDSEYGLSAAVFTR-DLARAlAVAKRIESGAVHIN----GMTVHD 398
|
410
....*....|....*
gi 1632883983 993 Q---PFGGHGLSGTG 1004
Cdd:cd07105 399 EptlPHGGVKSSGYG 413
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
578-1004 |
4.72e-48 |
|
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: 178.29 E-value: 4.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA- 656
Cdd:cd07092 1 VVDPAT-GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRARSD--------LAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPL 722
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLegpaageyLPGHTsmirrePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 723 IAAEAVRLLhAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIqkqlstrLSATGRPIP-LIAETGGQN 800
Cdd:cd07092 160 TTLLLAELA-AEVLPPGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKV-------ARAAADTLKrVHLELGGKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 801 AMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARI 880
Cdd:cd07092 232 PVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 881 EAHIEAMRARGRTV---ERLPLPdetraGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGL 955
Cdd:cd07092 312 AGFVERAPAHARVLtggRRAEGP-----GYFYEPTVVAGVAQDDeiVQEEIFGPVVTVQPFD--DEDEAIELANDVEYGL 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1632883983 956 TFGLHTRLDDTIARVTSRIHVGNIYVNRNviGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07092 385 ASSVWTRDVGRAMRLSARLDFGTVWVNTH--IPLAAEMPHGGFKQSGYG 431
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
577-1004 |
5.04e-46 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 172.87 E-value: 5.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:cd07151 13 DVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EV-------REAVDF-LRYYAVRARSDLAGST------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP- 721
Cdd:cd07151 92 EWgaamaitREAATFpLRMEGRILPSDVPGKEnrvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPi 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 722 ----LIAaeavRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQlstrlsaTGRPIPLIA-E 795
Cdd:cd07151 172 tgglLLA----KIFEEAGLPKGVLNVVVGAGSeIGDAFVEHPVPRLISFTGSTPVGRHIGEL-------AGRHLKKVAlE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 796 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGhtDRLAAD--IGPVIT 873
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYG--DPSDPDtvVGPLIN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 874 AEAQARIEAHIEAMRARGRTVerlpLPDETRAGTFVAPTIIElEALSDLE---QEVFGPVLHVIRYRrqDIDALIDAINA 950
Cdd:cd07151 319 ESQVDGLLDKIEQAVEEGATL----LVGGEAEGNVLEPTVLS-DVTNDMEiarEEIFGPVAPIIKAD--DEEEALELAND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1632883983 951 WGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVqPFGGHGLSGTG 1004
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
577-1014 |
5.06e-46 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 173.17 E-value: 5.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:PRK11241 29 DVTNPA-NGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYAVRARSdLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP 721
Cdd:PRK11241 108 EISYAASFIEWFAEEGKR-IYGDTipghqadkrlivikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 722 LIAAEAVRLLHAAGVPADVLQFVPGD-GAIGAALVGAPETAGVMFTGSTDVGRliqkQLSTRLSATGRPIPLiaETGGQN 800
Cdd:PRK11241 187 FSALALAELAIRAGIPAGVFNVVTGSaGAVGGELTSNPLVRKLSFTGSTEIGR----QLMEQCAKDIKKVSL--ELGGNA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 801 AMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARI 880
Cdd:PRK11241 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 881 EAHIEAMRARGRTVERLPLPDEtRAGTFVAPTI-IELEALSDL-EQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFG 958
Cdd:PRK11241 341 EEHIADALEKGARVVCGGKAHE-LGGNFFQPTIlVDVPANAKVaKEETFGPLAPLFRFK--DEADVIAQANDTEFGLAAY 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1632883983 959 LHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGvqPFGG---HGLSGTGPKAGGPLYLQ 1014
Cdd:PRK11241 418 FYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYLE 474
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
577-1014 |
7.05e-46 |
|
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: 172.98 E-value: 7.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVA-------DVTAEAAREAVRiaagaaATWASTPINARATCLERAADALEAAMpDLLALI-VREAG 648
Cdd:cd07144 26 KTVNPST-GEVIASVYaageedvDKAVKAARKAFE------SWWSKVTGEERGELLDKLADLVEKNR-DLLAAIeALDSG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 649 KS-VPNAVAEVREAVDFLRYYAVRArSDLAGST--------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVL 713
Cdd:cd07144 98 KPyHSNALGDLDEIIAVIRYYAGWA-DKIQGKTiptspnklaytlhePYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 714 AKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAI-GAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSAtgrpIPL 792
Cdd:cd07144 177 IKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVaGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA----VTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 793 iaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAE-LRIGHTDRLAADIGPV 871
Cdd:cd07144 253 --ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 872 ITAEAQARIEAHIEAMRARGRTVER--LPLPDETRAGTFVAPTIIE--LEALSDLEQEVFGPVLHVIRYRrqDIDALIDA 947
Cdd:cd07144 331 VSKTQYDRVLSYIEKGKKEGAKLVYggEKAPEGLGKGYFIPPTIFTdvPQDMRIVKEEIFGPVVVISKFK--TYEEAIKK 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 948 INAWGFGLTFGLHTRlDDTIA-RVTSRIHVGNIYVNRNVIGAvVGVqPFGGHGLSGTGP---KAGGPLYLQ 1014
Cdd:cd07144 409 ANDTTYGLAAAVFTK-DIRRAhRVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRelgEYGLETYTQ 476
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
574-1004 |
2.72e-44 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 167.78 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 574 PARPVRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPN 653
Cdd:PRK13473 17 EKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 654 AVA-EVREAVDFLRYYAVRARsDLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPA 717
Cdd:PRK13473 96 ALNdEIPAIVDVFRFFAGAAR-CLEGKAageyleghtsmirrdPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 718 EETPLIAAEAVRLLhAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIqkqlstrLSATGRPIP-LIAE 795
Cdd:PRK13473 175 EITPLTALKLAELA-ADILPPGVLNVVTGRGAtVGDALVGHPKVRMVSLTGSIATGKHV-------LSAAADSVKrTHLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 796 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAE 875
Cdd:PRK13473 247 LGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 876 AQARIEAHIEAMRARG--RTVERLPLPDetRAGTFVAPTIIElEALSDLE---QEVFGPVLHVIRYRRQDiDALIDAiNA 950
Cdd:PRK13473 327 HRDRVAGFVERAKALGhiRVVTGGEAPD--GKGYYYEPTLLA-GARQDDEivqREVFGPVVSVTPFDDED-QAVRWA-ND 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1632883983 951 WGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIgaVVGVQPFGGHGLSGTG 1004
Cdd:PRK13473 402 SDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
578-1004 |
2.28e-43 |
|
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: 164.90 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEHDdTVGTVADVTAEAAREAVRIAAGAAATWAS-TPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:cd07148 3 VVNPFDLK-PIGEVPTVDWAAIDKALDTAHALFLDRNNwLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYyAVRARSDLAGST-------------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPA 717
Cdd:cd07148 82 EVTRAIDGVEL-AADELGQLGGREipmgltpasagriafttrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 718 EETPLIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLstrlsATGRPIPLiaETG 797
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKL-----APGTRCAL--EHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 798 GQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQ 877
Cdd:cd07148 234 GAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 878 ARIEAHIEAMRARGRTVerlpLPDETRAG-TFVAPTIIeLEALSDL---EQEVFGPVLHVIRYRrqDIDALIDAINAWGF 953
Cdd:cd07148 314 DRVEEWVNEAVAAGARL----LCGGKRLSdTTYAPTVL-LDPPRDAkvsTQEIFGPVVCVYSYD--DLDEAIAQANSLPV 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 954 GLTFGLHTRLDDTIARVTSRIHVGNIYVNRNViGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVNDHT-AFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
590-1004 |
6.34e-43 |
|
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: 164.05 E-value: 6.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 590 TVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMpDLLALI-VREAGKSVPNAV-AEVREAVDFLRY 667
Cdd:cd07559 31 EIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENL-ELLAVAeTLDNGKPIRETLaADIPLAIDHFRY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 668 YA--VRAR----SDLAGST-------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAA 734
Cdd:cd07559 110 FAgvIRAQegslSEIDEDTlsyhfhePLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 735 gVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGGQNAMIVDSSALAEQ- 812
Cdd:cd07559 190 -LPKGVVNVVTGFGSeAGKPLASHPRIAKLAFTGSTTVGRLIMQ------YAAENLIPVTLELGGKSPNIFFDDAMDADd 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 813 -----VVADVIASAFDSaGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAM 887
Cdd:cd07559 263 dfddkAEEGQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 888 RARGRTV----ERLPLPDETrAGTFVAPTIIEL--EALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHT 961
Cdd:cd07559 342 KEEGAEVltggERLTLGGLD-KGYFYEPTLIKGgnNDMRIFQEEIFGPVLAVITFK--DEEEAIAIANDTEYGLGGGVWT 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1632883983 962 RLDDTIARVTSRIHVGNIYVN-RNVIGAVVgvqPFGGHGLSGTG 1004
Cdd:cd07559 419 RDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
639-1017 |
8.05e-43 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 161.83 E-value: 8.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 639 LLALIVREAGKSVPNAVAEVREAVDFLRYYAVRAR--------SDLAGST------PLGPVVCISPWNFPLAIFTGQVAA 704
Cdd:PRK10090 15 ISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegeiiqSDRPGENillfkrALGVTTGILPWNFPFFLIARKMAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 705 ALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIqkqlstrL 783
Cdd:PRK10090 95 ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGEtVGQELAGNPKVAMVSMTGSVSAGEKI-------M 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 784 SATGRPIPLIA-ETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHT- 861
Cdd:PRK10090 168 AAAAKNITKVClELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 862 DRLAADIGPVITAEAQARIEAHIEAMRARGRTVERLPLPDETRaGTFVAPTIieleaLSDLEQ-------EVFGPVLHVI 934
Cdd:PRK10090 248 ERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGK-GYYYPPTL-----LLDVRQemsimheETFGPVLPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 935 RYrrQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQP-FGGHGLSGTGPKAGGPLYL 1013
Cdd:PRK10090 322 AF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAgWRKSGIGGADGKHGLHEYL 399
|
....
gi 1632883983 1014 QRLV 1017
Cdd:PRK10090 400 QTQV 403
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
577-1004 |
6.70e-42 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 161.20 E-value: 6.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTV-----ADVTA--EAAREAVRIAAGAaatwasTPInARATCLERAADALEAAMPDLLALIVREAGK 649
Cdd:PRK13252 25 EVINPAT-GEVLATVqaatpADVEAavASAKQGQKIWAAM------TAM-ERSRILRRAVDILRERNDELAALETLDTGK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 650 SVPNA-VAEVREAVDFLRYYAVRARS------DLAGST-------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAK 715
Cdd:PRK13252 97 PIQETsVVDIVTGADVLEYYAGLAPAlegeqiPLRGGSfvytrrePLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 716 PAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRliqKQLStrlSATGRPIPLIAE 795
Cdd:PRK13252 177 PSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGK---KVMA---AAAASLKEVTME 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 796 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCS-ALRVLcLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITA 874
Cdd:PRK13252 251 LGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 875 EAQARIEAHIEAMRARGRTV----ERLPlPDETRAGTFVAPTIIE--LEALSDLEQEVFGPVLHVIRYrrQDIDALIDAI 948
Cdd:PRK13252 330 AHRDKVLGYIEKGKAEGARLlcggERLT-EGGFANGAFVAPTVFTdcTDDMTIVREEIFGPVMSVLTF--DDEDEVIARA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1632883983 949 NAWGFGLTFGLHTRlDDTIA-RVTSRIHVGNIYVnrNVIGAVVGVQPFGGHGLSGTG 1004
Cdd:PRK13252 407 NDTEYGLAAGVFTA-DLSRAhRVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
580-1008 |
1.87e-41 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 160.38 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVR 659
Cdd:PLN02315 40 NPA-NNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 660 EAVDFLRYyAVRARSDLAGS---------------TPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIA 724
Cdd:PLN02315 119 EIIDMCDF-AVGLSRQLNGSiipserpnhmmmevwNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 725 AEAVRL----LHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSATgrpiplIAETGGQN 800
Cdd:PLN02315 198 IAMTKLvaevLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKC------LLELSGNN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 801 AMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARI 880
Cdd:PLN02315 272 AIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 881 EAHIEAMRAR-------GRTVErlplpdetRAGTFVAPTIIELEALSDL-EQEVFGPVLHVIRYrrQDIDALIDAINAWG 952
Cdd:PLN02315 352 EKGIEIIKSQggkiltgGSAIE--------SEGNFVQPTIVEISPDADVvKEELFGPVLYVMKF--KTLEEAIEINNSVP 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1632883983 953 FGLTFGLHTRLDDTIARVTSRI--HVGNIYVNRNVIGAVVGvQPFGGHGLSGTGPKAG 1008
Cdd:PLN02315 422 QGLSSSIFTRNPETIFKWIGPLgsDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
620-1025 |
1.21e-40 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 157.68 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 620 ARATCLERAADALEAAMPDLLALIVREAGKSVP-NAVAEVREAVDFLRYYA----------VRARSDLAGST---PLGPV 685
Cdd:PLN02766 83 ERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAAAGLLRYYAgaadkihgetLKMSRQLQGYTlkePIGVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 686 VCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAI-GAALVGAPETAGVM 764
Cdd:PLN02766 163 GHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTaGAAIASHMDVDKVS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 765 FTGSTDVGRLIQKQlstrlSATGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADR 844
Cdd:PLN02766 243 FTGSTEVGRKIMQA-----AATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 845 VLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVER--LPLPDEtraGTFVAPTIIE--LEALS 920
Cdd:PLN02766 318 FVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTggKPCGDK---GYYIEPTIFTdvTEDMK 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 921 DLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVnrNVIGAVVGVQPFGGHGL 1000
Cdd:PLN02766 395 IAQDEIFGPVMSLMKFK--TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWV--NCYFAFDPDCPFGGYKM 470
|
410 420 430
....*....|....*....|....*....|
gi 1632883983 1001 SGTGPKAGGPL---YLQ--RLVQPRPALPF 1025
Cdd:PLN02766 471 SGFGRDQGMDAldkYLQvkSVVTPLYNSPW 500
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
616-982 |
8.34e-40 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 155.30 E-value: 8.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 616 TPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYA---VRA-------RSD---------- 675
Cdd:PLN00412 72 TPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAeegVRIlgegkflVSDsfpgnernky 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 676 -LAGSTPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAA 753
Cdd:PLN00412 152 cLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSeIGDF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 754 LVGAPETAGVMFTGStDVGRLIQKQlstrlsatGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALR 833
Cdd:PLN00412 232 LTMHPGVNCISFTGG-DTGIAISKK--------AGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 834 VLCLQEDVADRVLAMLKGALAELRIGHTDRlAADIGPVITAEAQARIEAHIEAMRARGRTVERlplpDETRAGTFVAPTI 913
Cdd:PLN00412 303 VVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQ----EWKREGNLIWPLL 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632883983 914 IElEALSDLE---QEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVN 982
Cdd:PLN00412 378 LD-NVRPDMRiawEEPFGPVLPVIRIN--SVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN 446
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
577-1008 |
9.58e-40 |
|
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: 154.81 E-value: 9.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEHDDTV----GTVADV--TAEAAREAVRIAAGAAATWAStpinARATCLERAADALEAAMPDLLALIVREAGKS 650
Cdd:cd07141 25 PTINPATGEKICevqeGDKADVdkAVKAARAAFKLGSPWRTMDAS----ERGRLLNKLADLIERDRAYLASLETLDNGKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 651 V-PNAVAEVREAVDFLRYYAVRARSDLAGSTPLG----------PV-VC--ISPWNFPLAIFTGQVAAALVAGNPVLAKP 716
Cdd:cd07141 101 FsKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDgdfftytrhePVgVCgqIIPWNFPLLMAAWKLAPALACGNTVVLKP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 717 AEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAI-GAALVGAPETAGVMFTGSTDVGRLIQKqlstrlsATGRP----IP 791
Cdd:cd07141 181 AEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTaGAAISSHPDIDKVAFTGSTEVGKLIQQ-------AAGKSnlkrVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 792 LiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPV 871
Cdd:cd07141 254 L--ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 872 ITAEAQARIEAHIEAMRARGRTVE----RLPLPdetraGTFVAPTIieleaLSDL-------EQEVFGPVLHVIRYRrqD 940
Cdd:cd07141 332 IDEEQFKKILELIESGKKEGAKLEcggkRHGDK-----GYFIQPTV-----FSDVtddmriaKEEIFGPVQQIFKFK--T 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1632883983 941 IDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNrnvIGAVVGVQ-PFGGHGLSGTGPKAG 1008
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
577-1004 |
1.71e-39 |
|
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: 153.76 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAeHDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAmPDLLALI-VREAGKSVPNAV 655
Cdd:cd07117 19 DSYNPA-NGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDEN-KELLAMVeTLDNGKPIRETR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 656 A-EVREAVDFLRYYA--VRARSD-----------LAGSTPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP 721
Cdd:cd07117 97 AvDIPLAADHFRYFAgvIRAEEGsanmidedtlsIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 722 LIAAEAVRLLHAAgVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGGQN 800
Cdd:cd07117 177 LSLLELAKIIQDV-LPKGVVNIVTGKGSkSGEYLLNHPGLDKLAFTGSTEVGRDVAI------AAAKKLIPATLELGGKS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 801 AMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARI 880
Cdd:cd07117 250 ANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 881 EAHIEAMRARGRTV----ERLpLPDETRAGTFVAPTIIEL--EALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFG 954
Cdd:cd07117 330 LSYVDIAKEEGAKIltggHRL-TENGLDKGFFIEPTLIVNvtNDMRVAQEEIFGPVATVIKFK--TEDEVIDMANDSEYG 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 955 LTFGLHTRLDDTIARVTSRIHVGNIYVNR-NVIGAVVgvqPFGGHGLSGTG 1004
Cdd:cd07117 407 LGGGVFTKDINRALRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
577-997 |
1.80e-39 |
|
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: 153.88 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVA 656
Cdd:TIGR01722 19 PVTNPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYyAVRARSDLAGST---------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP 721
Cdd:TIGR01722 98 DVARGLEVVEH-ACGVNSLLKGETstqvatrvdvysirqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 722 LIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQkqlsTRLSATGRPIPliAETGGQNA 801
Cdd:TIGR01722 177 SAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIH----TTGSAHGKRVQ--ALGGAKNH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQeDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIE 881
Cdd:TIGR01722 251 MVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 882 AHIEA---------MRARGRTVERLPlpdetrAGTFVAPTIIE--LEALSDLEQEVFGPVLHVIRYrrQDIDALIDAINA 950
Cdd:TIGR01722 330 SLIAGgaaegaevlLDGRGYKVDGYE------EGNWVGPTLLErvPPTMKAYQEEIFGPVLCVLEA--DTLEEAIALINA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1632883983 951 WGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNvIGAVVGVQPFGG 997
Cdd:TIGR01722 402 SPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP-IPVPLPYFSFTG 447
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
681-1004 |
4.03e-39 |
|
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: 151.52 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLhAAGVPADVLQFVPGDGAIGAALVGAPET 760
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI-PKYFDPEAVAVVEGGVEVATALLAEPFD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 761 AgVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQED 840
Cdd:cd07087 179 H-IFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 841 VADRVLAMLKGALAELrIGHTDRLAADIGPVITAEAQARIEAHIEAMR-ARGRTVERlplpdETRagtFVAPTIIELEAL 919
Cdd:cd07087 252 IKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDDGKvVIGGQVDK-----EER---YIAPTILDDVSP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 920 SD--LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGG 997
Cdd:cd07087 323 DSplMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
....*..
gi 1632883983 998 HGLSGTG 1004
Cdd:cd07087 401 VGNSGMG 407
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
615-1009 |
4.11e-39 |
|
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: 151.61 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 615 STPINARATCLERAADALEAAMPDLLALIVREAGKS--------VPNAVAEVREAVDFLRYYA----VRARSDLAGST-- 680
Cdd:cd07134 16 ASTAAERIAKLKRLKKAILARREEIIAALAADFRKPaaevdlteILPVLSEINHAIKHLKKWMkpkrVRTPLLLFGTKsk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 ----PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVpGDGAIGAALVG 756
Cdd:cd07134 96 iryePKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFE-GDAEVAQALLE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 757 APeTAGVMFTGSTDVGRLIQKQLSTRLSatgrPIPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLC 836
Cdd:cd07134 175 LP-FDHIFFTGSPAVGKIVMAAAAKHLA----SVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 837 LQEDVADRVLAMLKGALAELRIGHTDRLA-ADIGPVITAEAQARIEAHIEAMRARGRTVERLPLPDETRagTFVAPTIIE 915
Cdd:cd07134 248 VHESVKDAFVEHLKAEIEKFYGKDAARKAsPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQ--RYIAPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 916 -LEALSD-LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQ 993
Cdd:cd07134 326 nVTPDMKiMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNL 403
|
410
....*....|....*.
gi 1632883983 994 PFGGHGLSGTGpKAGG 1009
Cdd:cd07134 404 PFGGVNNSGIG-SYHG 418
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
621-1008 |
8.07e-39 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 153.04 E-value: 8.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 621 RATCLERAADALEAAMPDLLALIVREAGKSVPNAV-AEVREAVDFLRYYAVRArSDLAGST--------------PLGPV 685
Cdd:PLN02466 121 RSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMFARLFRYYAGWA-DKIHGLTvpadgphhvqtlhePIGVA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 686 VCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAI-GAALVGAPETAGVM 764
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTaGAALASHMDVDKLA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 765 FTGSTDVGRLIQKqlstrLSATGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADR 844
Cdd:PLN02466 280 FTGSTDTGKIVLE-----LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 845 VLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVE----RLplpdeTRAGTFVAPTIieleaLS 920
Cdd:PLN02466 355 FVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLEcggdRF-----GSKGYYIQPTV-----FS 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 921 DLE-------QEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVN-RNVIGAVVgv 992
Cdd:PLN02466 425 NVQddmliaqDEIFGPVQSILKFK--DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI-- 500
|
410
....*....|....*.
gi 1632883983 993 qPFGGHGLSGTGPKAG 1008
Cdd:PLN02466 501 -PFGGYKMSGIGREKG 515
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
577-982 |
1.39e-38 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 151.81 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 577 PVRNPAEhDDTVGTVADVTAE-------AAREAvrIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGK 649
Cdd:PLN02467 26 PVVNPAT-EETIGDIPAATAEdvdaaveAARKA--FKRNKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 650 SVPNAVAEVREAVDFLRYYAVRARS---------DLAGST--------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPV 712
Cdd:PLN02467 103 PLDEAAWDMDDVAGCFEYYADLAEAldakqkapvSLPMETfkgyvlkePLGVVGLITPWNYPLLMATWKVAPALAAGCTA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 713 LAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQkqlsTRLSATGRPIP 791
Cdd:PLN02467 183 VLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTeAGAPLASHPGVDKIAFTGSTATGRKIM----TAAAQMVKPVS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 792 LiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPV 871
Cdd:PLN02467 259 L--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 872 ITAEAQARIEAHIEAMRARGRTV----ERlplPDETRAGTFVAPTIIELEALSD--LEQEVFGPVLHVIRYRRQdiDALI 945
Cdd:PLN02467 337 VSEGQYEKVLKFISTAKSEGATIlcggKR---PEHLKKGFFIEPTIITDVTTSMqiWREEVFGPVLCVKTFSTE--DEAI 411
|
410 420 430
....*....|....*....|....*....|....*..
gi 1632883983 946 DAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVN 982
Cdd:PLN02467 412 ELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
681-1008 |
4.58e-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: 149.37 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAA----GVPADVLQFVPGDGAIGAALVG 756
Cdd:cd07098 120 PLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 757 APETAGVMFTGSTDVGRLIQKqlstrlSATGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLC 836
Cdd:cd07098 200 HPVIDHITFIGSPPVGKKVMA------AAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 837 LQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTV----ERLPLPdETRAGTFVAPT 912
Cdd:cd07098 274 VHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLlaggKRYPHP-EYPQGHYFPPT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 913 IIeLEALSDL---EQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAV 989
Cdd:cd07098 353 LL-VDVTPDMkiaQEEVFGPVMVVMKAS--DDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYY 429
|
330
....*....|....*....
gi 1632883983 990 VGVQPFGGHGLSGTGPKAG 1008
Cdd:cd07098 430 VQQLPFGGVKGSGFGRFAG 448
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
580-1004 |
4.68e-37 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 146.04 E-value: 4.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVR 659
Cdd:PRK09406 7 NPAT-GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 660 EAVDFLRYYAVRARSDLAGST----------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLI 723
Cdd:PRK09406 86 KCAKGFRYYAEHAEALLADEPadaaavgasrayvryqPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 724 AAEAVRLLHAAGVPADVLQ-FVPGDGAIGAALVGaPETAGVMFTGSTDVGRLIQkqlstrlSATGRPI-PLIAETGGQNA 801
Cdd:PRK09406 166 ALYLADLFRRAGFPDGCFQtLLVGSGAVEAILRD-PRVAAATLTGSEPAGRAVA-------AIAGDEIkKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 802 MIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIE 881
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 882 AHIEAMRARGRTV----ERlplPDetRAGTFVAPTIIE--LEALSDLEQEVFGPVLHVirYRRQDIDALIDAINAWGFGL 955
Cdd:PRK09406 318 KQVDDAVAAGATIlcggKR---PD--GPGWFYPPTVITdiTPDMRLYTEEVFGPVASL--YRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 956 TFGLHTRLDDTIARVTSRIHVGNIYVNrnviGAVVGVQ--PFGGHGLSGTG 1004
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
681-1004 |
1.10e-34 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 138.51 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPliaaeavrllHAAGVPADVLQFVPGDGAIGAALVGAPET 760
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTP----------HTAALLAELVPKYLDPDAFQVVQGGVPET 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 761 AG--------VMFTGSTDVGRLIQKQLSTRLSatgrpiPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSAL 832
Cdd:cd07135 178 TAlleqkfdkIFYTGSGRVGRIIAEAAAKHLT------PVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 833 R-VLClQEDVADRVLAMLKGALAELRIGHTDRlAADIGPVITAEAQARIEAHIEamRARGRTVerlpLPDETRAGT-FVA 910
Cdd:cd07135 252 DyVLV-DPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLD--TTKGKVV----IGGEMDEATrFIP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 911 PTIIELEALSD--LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGA 988
Cdd:cd07135 324 PTIVSDVSWDDslMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHV 401
|
330
....*....|....*.
gi 1632883983 989 VVGVQPFGGHGLSGTG 1004
Cdd:cd07135 402 GVDNAPFGGVGDSGYG 417
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
616-1004 |
1.31e-34 |
|
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: 139.12 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 616 TPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAV-AEVREAVDFLRYYA--VRAR----SDLAGST-------P 681
Cdd:cd07116 57 TSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFAgcIRAQegsiSEIDENTvayhfheP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 682 LGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETP---LIAAEAVRLLhaagVPADVLQFVPGDGA-IGAALVGA 757
Cdd:cd07116 137 LGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPasiLVLMELIGDL----LPPGVVNVVNGFGLeAGKPLASS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 758 PETAGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALAEQ------VVADVIASAFDSaGQRCSA 831
Cdd:cd07116 213 KRIAKVAFTGETTTGRLIMQYASENI------IPVTLELGGKSPNIFFADVMDADdaffdkALEGFVMFALNQ-GEVCTC 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 832 LRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTV----ERLPLPDETRAGT 907
Cdd:cd07116 286 PSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVltggERNELGGLLGGGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 908 FVAPTIIELEALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVnrNVIG 987
Cdd:cd07116 366 YVPTTFKGGNKMRIFQEEIFGPVLAVTTFK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYH 441
|
410
....*....|....*..
gi 1632883983 988 AVVGVQPFGGHGLSGTG 1004
Cdd:cd07116 442 LYPAHAAFGGYKQSGIG 458
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
580-1008 |
4.00e-34 |
|
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: 138.01 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINAR--ATCLERAADALEAAMPDLLALIVREAGKSVPNAV-A 656
Cdd:cd07140 27 NPTD-GSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARdrGRLMYRLADLMEEHQEELATIESLDSGAVYTLALkT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 657 EVREAVDFLRYYA-------------VRARSD----LAGSTPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEE 719
Cdd:cd07140 106 HVGMSIQTFRYFAgwcdkiqgktipiNQARPNrnltLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 720 TPLIAAEAVRLLHAAGVPADVLQFVPGDGA-IGAALVGAPETAGVMFTGSTDVGRLIQKQlstrlSATGRPIPLIAETGG 798
Cdd:cd07140 186 TPLTALKFAELTVKAGFPKGVINILPGSGSlVGQRLSDHPDVRKLGFTGSTPIGKHIMKS-----CAVSNLKKVSLELGG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 799 QNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPvitAEAQA 878
Cdd:cd07140 261 KSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP---QNHKA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 879 RIEAHIEAMR---ARGRTVE----RLPLPdetraGTFVAPTIieleaLSDLE-------QEVFGPVLHVIRYRRQDIDAL 944
Cdd:cd07140 338 HLDKLVEYCErgvKEGATLVyggkQVDRP-----GFFFEPTV-----FTDVEdhmfiakEESFGPIMIISKFDDGDVDGV 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1632883983 945 IDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGvqPFGGHGLSGTGPKAG 1008
Cdd:cd07140 408 LQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLG 469
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
681-1004 |
1.10e-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: 132.61 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGvPADVLQFVPGDGAIGAALVGAPeT 760
Cdd:cd07133 101 PLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF-DEDEVAVVTGGADVAAAFSSLP-F 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 761 AGVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALR-VLCLQE 839
Cdd:cd07133 179 DHLLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDyVLVPED 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 840 DVaDRVLAMLKGALAELRIghTDRLAADIGPVITAEAQARIEAHIEAMRARG-RTVERLPLPDETRAGTFVAPTIIeLEA 918
Cdd:cd07133 253 KL-EEFVAAAKAAVAKMYP--TLADNPDYTSIINERHYARLQGLLEDARAKGaRVIELNPAGEDFAATRKLPPTLV-LNV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 919 LSD---LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPF 995
Cdd:cd07133 329 TDDmrvMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPF 406
|
....*....
gi 1632883983 996 GGHGLSGTG 1004
Cdd:cd07133 407 GGVGASGMG 415
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
589-1004 |
1.41e-31 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 130.40 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 589 GTVADVtaEAAREAVRIAAGAAATWASTPInARATCLERAADALEAAMPDLLALIVREAGK--------SVPNAVAEVR- 659
Cdd:PRK09847 54 GKSVDI--DRAVSAARGVFERGDWSLSSPA-KRKAVLNKLADLMEAHAEELALLETLDTGKpirhslrdDIPGAARAIRw 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 660 --EAVDflRYYAVRARSD-----LAGSTPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLH 732
Cdd:PRK09847 131 yaEAID--KVYGEVATTSshelaMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 733 AAGVPADVLQFVPGDG-AIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTrlSATGRpipLIAETGGQNAMIV--DSSAL 809
Cdd:PRK09847 209 EAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD--SNMKR---VWLEAGGKSANIVfaDCPDL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 810 aEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRA 889
Cdd:PRK09847 284 -QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGES 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 890 RGRTverlpLPDETRAG--TFVAPTII-ELEALSDLEQ-EVFGPVLHVIRYRRQDiDALIDAiNAWGFGLTFGLHTRLDD 965
Cdd:PRK09847 363 KGQL-----LLDGRNAGlaAAIGPTIFvDVDPNASLSReEIFGPVLVVTRFTSEE-QALQLA-NDSQYGLGAAVWTRDLS 435
|
410 420 430
....*....|....*....|....*....|....*....
gi 1632883983 966 TIARVTSRIHVGNIYVNRNVIGAVvgVQPFGGHGLSGTG 1004
Cdd:PRK09847 436 RAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
681-1004 |
2.84e-31 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 129.38 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAgVPADVLQFVPGDGAIGAALVGAPET 760
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELLKEPFD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 761 AgVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQED 840
Cdd:PTZ00381 188 H-IFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 841 VADRVLAMLKGALAELrIGHTDRLAADIGPVITAEAQARIEAHIEamRARGRTVERLPLPDETRagtFVAPTIIELEALS 920
Cdd:PTZ00381 261 IKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIK--DHGGKVVYGGEVDIENK---YVAPTIIVNPDLD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 921 D--LEQEVFGPVLHVIRYrrQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQPFGGH 998
Cdd:PTZ00381 335 SplMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
....*.
gi 1632883983 999 GLSGTG 1004
Cdd:PTZ00381 413 GNSGMG 418
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
580-982 |
2.29e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 123.05 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 580 NPAEhDDTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVR 659
Cdd:PRK13968 13 NPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 660 EAVDFLRYYAVRARSDLAGST-------------PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAE 726
Cdd:PRK13968 92 KSANLCDWYAEHGPAMLKAEPtlvenqqavieyrPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 727 AVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSATgrpiplIAETGGQNAMIVDS 806
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKC------VLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 807 SALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEA 886
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 887 MRARGrtvERLPLPDETRAG--TFVAPTIIE--LEALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTR 962
Cdd:PRK13968 326 TLAEG---ARLLLGGEKIAGagNYYAPTVLAnvTPEMTAFREELFGPVAAITVAK--DAEHALELANDSEFGLSATIFTT 400
|
410 420
....*....|....*....|
gi 1632883983 963 LDDTIARVTSRIHVGNIYVN 982
Cdd:PRK13968 401 DETQARQMAARLECGGVFIN 420
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
621-1020 |
1.55e-28 |
|
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: 120.42 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 621 RATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYAVRARSDLAGST-----------------PLG 683
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHEPgnhlgqglkqqshgyrwPYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 684 PVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAG-VPADVLQFVPGDGAIGAALVGAPETAG 762
Cdd:cd07084 103 PVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTMQALLLHPNPKM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 763 VMFTGSTDVGRliqkqlstRLSATGRPIPLIAETGGQNAMIVDSSALAEQVVAD-VIASAFDSAGQRCSALRVLCLQEDV 841
Cdd:cd07084 183 VLFTGSSRVAE--------KLALDAKQARIYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTACSGQKCTAQSMLFVPENW 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 842 ADRVLAMLKGALAELRIGHTdrlaADIGPVITAEAQARI---EAHIEAMRARGRTVERLPLPDETrAGTFVAP----TII 914
Cdd:cd07084 255 SKTPLVEKLKALLARRKLED----LLLGPVQTFTTLAMIahmENLLGSVLLFSGKELKNHSIPSI-YGACVASalfvPID 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 915 ELEALSDL-EQEVFGPVLHVIRYRRQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHV-GNIY-VNRNVIGAVVG 991
Cdd:cd07084 330 EILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVaGRTYaILRGRTGVAPN 409
|
410 420
....*....|....*....|....*....
gi 1632883983 992 VQPFGGHGLSGTGPKAGGPLYLQRLVQPR 1020
Cdd:cd07084 410 QNHGGGPAADPRGAGIGGPEAIKLVWRCH 438
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
593-982 |
3.92e-28 |
|
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: 119.18 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 593 DVTAEAAREAvriaagaAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYA--- 669
Cdd:cd07129 2 DAAAAAAAAA-------FESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFAdlv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 670 -----VRARSDLAGST--------------PLGPVVCISPWNFPLAIFT--GQVAAALVAGNPVLAK--PAE-ETPLIAA 725
Cdd:cd07129 75 regswLDARIDPADPDrqplprpdlrrmlvPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAHpGTSELVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 726 EAVR-LLHAAGVPADVLQFVPGDG-AIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLsatgRPIPLIAETGGQNAMI 803
Cdd:cd07129 155 RAIRaALRATGLPAGVFSLLQGGGrEVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARP----EPIPFYAELGSVNPVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 804 VDSSALAEQvvADVIASAFD-----SAGQRCSALRVLCLQEDVA-DRVLAMLKGALAelrightdrlAADIGPVITAEAQ 877
Cdd:cd07129 231 ILPGALAER--GEAIAQGFVgsltlGAGQFCTNPGLVLVPAGPAgDAFIAALAEALA----------AAPAQTMLTPGIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 878 ARIEAHIEAMRARGrTVERLPLPDETRAGTFVAPTIIE-----LEALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWG 952
Cdd:cd07129 299 EAYRQGVEALAAAP-GVRVLAGGAAAEGGNQAAPTLFKvdaaaFLADPALQEEVFGPASLVVRYD--DAAELLAVAEALE 375
|
410 420 430
....*....|....*....|....*....|....*
gi 1632883983 953 FGLTFGLHTRLDDT-----IARVTSRIhVGNIYVN 982
Cdd:cd07129 376 GQLTATIHGEEDDLalareLLPVLERK-AGRLLFN 409
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
681-1004 |
4.45e-27 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 115.78 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPliaaeavrllHAAGVPADVL-QFVPGDgAIGAALVGAPE 759
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP----------ATAKLLAELIpKYLDKE-CYPVVLGGVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 760 TAG--------VMFTGSTDVGRLIQKQLSTRLSatgrpiPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSA 831
Cdd:cd07132 169 TTEllkqrfdyIFYTGSTSVGKIVMQAAAKHLT------PVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 832 LR-VLCLQEdVADRVLAMLKGALAELrIGHTDRLAADIGPVITAEAQARIEAHIEAMR-ARGRTVErlplpDETRagtFV 909
Cdd:cd07132 243 PDyVLCTPE-VQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGKvAIGGQTD-----EKER---YI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 910 APTIieleaLSD-------LEQEVFGPVLHVIRYrrQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVN 982
Cdd:cd07132 313 APTV-----LTDvkpsdpvMQEEIFGPILPIVTV--NNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN 385
|
330 340
....*....|....*....|..
gi 1632883983 983 RNVIGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07132 386 DTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
679-1004 |
4.86e-24 |
|
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: 106.73 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 679 STPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLhAAGVPADVLQFVPGDGAIGAALVgAP 758
Cdd:cd07137 99 SEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEGGVPETTALL-EQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 759 ETAGVMFTGSTDVGRLIQKQLSTRLSatgrpiPLIAETGGQNAMIVDSSALAEQVVADVIASAFDS-AGQRCSALRVLCL 837
Cdd:cd07137 177 KWDKIFFTGSPRVGRIIMAAAAKHLT------PVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 838 QEDVADRVLAMLKGALAELrIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTV---ERlplpDETRagTFVAPTII 914
Cdd:cd07137 251 EESFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVhggER----DEKN--LYIEPTIL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 915 eLEALSD---LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVG 991
Cdd:cd07137 324 -LDPPLDssiMTEEIFGPLLPIITVK--KIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
330
....*....|...
gi 1632883983 992 VQPFGGHGLSGTG 1004
Cdd:cd07137 401 TLPFGGVGESGFG 413
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
679-1004 |
9.43e-24 |
|
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: 106.05 E-value: 9.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 679 STPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAgVPADVLQFVPGDGAIGAALVGAP 758
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLDQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 759 ETAgVMFTGSTDVGRLIQKQLSTRLsatgrpIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQ 838
Cdd:cd07136 177 FDY-IFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 839 EDVADRVLAMLKGALAEL------------RI---GHTDRLAA--DIGPVITaeaqarieahieamrarGRTVERlplpd 901
Cdd:cd07136 250 ESVKEKFIKELKEEIKKFygedplespdygRIineKHFDRLAGllDNGKIVF-----------------GGNTDR----- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 902 ETRagtFVAPTIIELEALSD--LEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNI 979
Cdd:cd07136 308 ETL---YIEPTILDNVTWDDpvMQEEIFGPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGG 382
|
330 340
....*....|....*....|....*
gi 1632883983 980 YVNRNVIGAVVGVQPFGGHGLSGTG 1004
Cdd:cd07136 383 CINDTIMHLANPYLPFGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
578-982 |
7.52e-23 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 104.83 E-value: 7.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 578 VRNPAEHDdTVGTVADVTAEAAREAVRIAAGAAATWASTPINARATCLERAADALEAAMPDLLALIVREAGKSVPNAVAE 657
Cdd:PLN02419 133 VINPATQE-VVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 658 VREAVDFLRYYAVRARSDLAG--------------STPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLI 723
Cdd:PLN02419 212 IFRGLEVVEHACGMATLQMGEylpnvsngvdtysiREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 724 AAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGrliqKQLSTRLSATGRPIPliAETGGQNAMI 803
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAG----MHIYARAAAKGKRIQ--SNMGAKNHGL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 804 VDSSALAEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAeLRIGHTDRLAADIGPVITAEAQARIEAH 883
Cdd:PLN02419 366 VLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKA-LKVTCGSEPDADLGPVISKQAKERICRL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 884 IEAMRARGRTV----ERLPLPDETRaGTFVAPTIIElEALSDLE---QEVFGPVLhvIRYRRQDIDALIDAINAWGFGLT 956
Cdd:PLN02419 445 IQSGVDDGAKLlldgRDIVVPGYEK-GNFIGPTILS-GVTPDMEcykEEIFGPVL--VCMQANSFDEAISIINKNKYGNG 520
|
410 420
....*....|....*....|....*.
gi 1632883983 957 FGLHTRLDDTIARVTSRIHVGNIYVN 982
Cdd:PLN02419 521 AAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
642-947 |
4.99e-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: 97.95 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 642 LIVREAGKSVPNAVAEVREAVDFLRYYA---VR--ARS-----DLAGST------PLGPVVCISPWNFPLAIFTGQVAAA 705
Cdd:cd07126 87 LIQRVAPKSDAQALGEVVVTRKFLENFAgdqVRflARSfnvpgDHQGQQssgyrwPYGPVAIITPFNFPLEIPALQLMGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 706 LVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPADVLQFVPGDGAIGAALVGAPETAGVMFTGSTDVGRLIQKQLSTRLSa 785
Cdd:cd07126 167 LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERLALELHGKVK- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 786 tgrpipliAETGGQNAMIVDSSALAEQVVADVI-ASAFDSAGQRCSALRVLCLQEDVADRVLAMLKGALAELRigHTDRL 864
Cdd:cd07126 246 --------LEDAGFDWKILGPDVSDVDYVAWQCdQDAYACSGQKCSAQSILFAHENWVQAGILDKLKALAEQR--KLEDL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 865 AadIGPVITAEAQaRIEAHIEAMRA-RGRTVE--RLPLPDETRAGTFVA--PT--IIELEALSDLE------QEVFGPVL 931
Cdd:cd07126 316 T--IGPVLTWTTE-RILDHVDKLLAiPGAKVLfgGKPLTNHSIPSIYGAyePTavFVPLEEIAIEEnfelvtTEVFGPFQ 392
|
330
....*....|....*.
gi 1632883983 932 HVIRYRRQDIDALIDA 947
Cdd:cd07126 393 VVTEYKDEQLPLVLEA 408
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
680-1023 |
3.39e-19 |
|
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: 92.72 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 680 TPLGPV-VCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGV-PADVLQFVPGDGaiGAALVGA 757
Cdd:cd07128 142 TPRRGVaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSV--GDLLDHL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 758 PETAGVMFTGSTDVGrliqKQLSTRLSATGRPIPLIAETGGQNAMIvdssaLAEQVVADviASAFD------------SA 825
Cdd:cd07128 220 GEQDVVAFTGSAATA----AKLRAHPNIVARSIRFNAEADSLNAAI-----LGPDATPG--TPEFDlfvkevaremtvKA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 826 GQRCSALRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVERLPLPDETR- 904
Cdd:cd07128 289 GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVg 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 905 ----AGTFVAPTII----ELEALSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRI-- 974
Cdd:cd07128 369 adaeKGAFFPPTLLlcddPDAATAVHDVEAFGPVATLMPYD--SLAEAIELAARGRGSLVASVVTNDPAFARELVLGAap 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1632883983 975 HVGNIYV-NRNVIGAVVG---VQP---FGGHGLSGTGPKAGG----PLYLQRL-VQPRPAL 1023
Cdd:cd07128 447 YHGRLLVlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGGlrgvKHYMQRTaVQGSPTM 507
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
681-1004 |
3.50e-19 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 92.48 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAeavrlLHAAGVP----ADVLQFVPGDGAIGAALVG 756
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPkyldSKAVKVIEGGPAVGEQLLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 757 APETAgVMFTGSTDVGRLIQKQLSTRLSatgrpiPLIAETGGQNAMIVDSSALA---EQVVADVIASAFDS-AGQRCSAL 832
Cdd:PLN02203 183 HKWDK-IFFTGSPRVGRIIMTAAAKHLT------PVALELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQACIAI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 833 RVLCLQEDVADRVLAMLKGALAELrIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVERLPLPDETragTFVAPT 912
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKK---LFIEPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 913 II---ELEAlSDLEQEVFGPVLHVIRYRrqDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAV 989
Cdd:PLN02203 332 ILlnpPLDS-DIMTEEIFGPLLPIITVK--KIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYA 408
|
330
....*....|....*
gi 1632883983 990 VGVQPFGGHGLSGTG 1004
Cdd:PLN02203 409 CDSLPFGGVGESGFG 423
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
679-1008 |
9.25e-18 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 87.79 E-value: 9.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 679 STPLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGVPAdVLQFVPGDGAIGAALVgAP 758
Cdd:PLN02174 110 SEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALL-EQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 759 ETAGVMFTGSTDVGRLIQKQLSTRLSatgrpiPLIAETGGQNAMIVDSSALAEQVVADVIASAFD-SAGQRCSALRVLCL 837
Cdd:PLN02174 188 KWDKIFYTGSSKIGRVIMAAAAKHLT------PVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 838 QEDVADRVLAMLKGALaELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTVERlplPDETRAGTFVAPTI---I 914
Cdd:PLN02174 262 TKEYAPKVIDAMKKEL-ETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYG---GEKDRENLKIAPTIlldV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 915 ELEALSdLEQEVFGPVLHVIRYrrQDIDALIDAINAWGFGLTFGLHTRLDDTIARVTSRIHVGNIYVNRNVIGAVVGVQP 994
Cdd:PLN02174 338 PLDSLI-MSEEIFGPLLPILTL--NNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLP 414
|
330
....*....|....
gi 1632883983 995 FGGHGLSGTGPKAG 1008
Cdd:PLN02174 415 FGGVGESGMGAYHG 428
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
621-937 |
2.96e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 83.22 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 621 RATCLERAADALEAAMPDLLALIVREAGKSVPNAVAEVREAVDFLRYYA--------VRARSDLA----GSTPL------ 682
Cdd:PRK11903 65 RAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalgdARLLRDGEavqlGKDPAfqgqhv 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 683 -----GPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLHAAGV-PADVLQFVPGDGAIGAALVG 756
Cdd:PRK11903 145 lvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 757 APETagVMFTGSTDVGRLIQkqlsTRLSATGRPIPLIAETGGQNAMI-----VDSSALAEQVVADVIASAFDSAGQRCSA 831
Cdd:PRK11903 225 PFDV--VSFTGSAETAAVLR----SHPAVVQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQKCTA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 832 LRVLCLQEDVADRVLAMLKGALAELRIGHTDRLAADIGPVITAEAQARIEAHIEAMRARGRTV---ERLPLPDETRA-GT 907
Cdd:PRK11903 299 IRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLfdgGGFALVDADPAvAA 378
|
330 340 350
....*....|....*....|....*....|....
gi 1632883983 908 FVAPTII----ELEALSDLEQEVFGPVLHVIRYR 937
Cdd:PRK11903 379 CVGPTLLgasdPDAATAVHDVEVFGPVATLLPYR 412
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
19-65 |
8.47e-09 |
|
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: 52.47 E-value: 8.47e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1632883983 19 ALRQAITAAYRWPEHDCIAALLPQATLSDAARAEASALARRLVEALR 65
Cdd:pfam18327 2 PLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
682-934 |
3.25e-08 |
|
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: 57.87 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 682 LGPVVCISP---WNFPLAIFtgqvaAALVAGNPVLAKPAEETPLIAAEAVR----LLHAAGVPADVLQFV---PGDGaIG 751
Cdd:cd07127 196 VALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVQvareVLAEAGFDPNLVTLAadtPEEP-IA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 752 AALVGAPETAGVMFTGSTDVGrliqkqlsTRLSATGRPIPLIAETGGQNAMIVDSSalaEQVVADVIASAFDSA---GQR 828
Cdd:cd07127 270 QTLATRPEVRIIDFTGSNAFG--------DWLEANARQAQVYTEKAGVNTVVVDST---DDLKAMLRNLAFSLSlysGQM 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 829 CSALRVLCLQED---------VADRVLAMLKGALAELrIGHTDRLAADIGPVITAEAQARIE---AHIEAMRArGRTVER 896
Cdd:cd07127 339 CTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAearQLGEVLLA-SEAVAH 416
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1632883983 897 LPLPD-ETRagtfvAPTIIELEALSD--LEQEVFGPVLHVI 934
Cdd:cd07127 417 PEFPDaRVR-----TPLLLKLDASDEaaYAEERFGPIAFVV 452
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
681-855 |
1.50e-06 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 51.84 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTgQVAAALVAGNPVLAKPAEETPlIAAEAVRLLH----AAGVPADVLQFVP-GDGAIGAALV 755
Cdd:cd07077 100 PIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAP-FTNRALALLFqaadAAHGPKILVLYVPhPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 756 GAPETAGVMFTGSTDVGRLIQKQlstrlsatGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSaGQRCSALRVL 835
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNL 248
|
170 180
....*....|....*....|
gi 1632883983 836 CLQEDVADRVLAMLKGALAE 855
Cdd:cd07077 249 YVVDDVLDPLYEEFKLKLVV 268
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
681-1006 |
1.74e-03 |
|
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: 42.25 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 681 PLGPVVCISPWNFPLAIFTGQVAAALVAGNPVLAKPAEETPLIAAEAVRLLH----AAGVPADVLQFVPG-DGAIGAALV 755
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLqaavAAGAPENLIGWIDNpSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 756 GAPETAGVMFTGSTDVGRliqkqlstrlSATGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRVL 835
Cdd:cd07081 175 KFPGIGLLLATGGPAVVK----------AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 836 CLQEDVADRVLAMLKGALA-ELRIGHTDRLA------ADIGPVITAEAQARIEAHIEamrargrtverLPLPDETRAgtf 908
Cdd:cd07081 245 IVVDSVYDEVMRLFEGQGAyKLTAEELQQVQpvilknGDVNRDIVGQDAYKIAAAAG-----------LKVPQETRI--- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632883983 909 vapTIIELEALSDLE---QEVFGPVLHVIRYRRQDiDALIDA---INAWGFGLTFGLHTRLDDTIARV--------TSRI 974
Cdd:cd07081 311 ---LIGEVTSLAEHEpfaHEKLSPVLAMYRAANFA-DADAKAlalKLEGGCGHTSAMYSDNIKAIENMnqfanamkTSRF 386
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1632883983 975 HV---------GNIYVNRNVIGAVVGVQPFGGHGLS-GTGPK 1006
Cdd:cd07081 387 VKngpcsqgglGDLYNFRGWPSMTLGCGTWGGNSVSeNVGPK 428
|
|
| |
