|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
15-1224 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 2146.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 15 IFQNFAPPVREQTLLRKAITAAYRRTEEECMAPLIEAATVTAEQAKAIRETARKLIEALRAKTKGTGVEGLVQEYSLSSH 94
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTGVEALLQEYSLSSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 95 EGVALMCLAEALLRIPDTATRDALIRDKIARGDWKSHIGGGRSLFVNAATWGLVITGKLTSTVNDSGLSAALTKLIARAG 174
Cdd:PRK11905 81 EGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIARLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 175 EPVIRRGVDMAMRMMGEQFVTGETIGEAIKRSRPLEEQGFQYSYDMLGEAATTAKDAERYYKDYENAIHAIGKASAGRGI 254
Cdd:PRK11905 161 EPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 255 YGGPGISIKLSALHPRYARAQAERVMAELLPRVKSLMLLSKKYDIGLNIDAEEADRLELSLDLLEELALDKDLAGWNGLG 334
Cdd:PRK11905 241 YDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 335 FVVQAYGRRCPFVLDYIIDLARRSNRRIMVRLVKGAYWDAEIKRAQVEGLEDFPVFTRKVHTDVSYIACARKLLAARDVI 414
Cdd:PRK11905 321 FVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 415 FPQFATHNAQSMATIYHLAGPDFklgDYEFQCLHGMGEPLYSEVVGKRKLDRPCRFYAPVGTHETLLAYLVRRLLENGAN 494
Cdd:PRK11905 401 YPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGAN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 495 SSFVNRIADPAVPVDSLLEDPAAVVKAHnvPGARHDRIAAPADLFGPQRKNSAGLDLSSETTLAALDKVLKAGASAEWKA 574
Cdd:PRK11905 478 SSFVNRIVDENVPVEELIADPVEKVAAM--GVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAAKTWHA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 575 ----AAPQAGGATRPVLNPGDHNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGL 648
Cdd:PRK11905 556 apllAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAqaAFPEWSATPAAERAAILERAADLMEAHMPELFAL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VMREAGKSMPNAIAEVREAIDFLRYYAAEARRNFT-AGEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEET 727
Cdd:PRK11905 636 AVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNgPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQT 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 728 PLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlanGQPVPLIAETGGQ 806
Cdd:PRK11905 716 PLIAARAVRLLHEAGVPKDALQLLPGDGRTvGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GPPVPLIAETGGQ 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 807 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGT 886
Cdd:PRK11905 793 NAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQAN 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 887 IEKHIEDMRSLGHRIEQITLAGETGKGTFVPPTIIEMKSLADLKREVFGPVLHVIRFKRDNLDRLIDEINATGYGLTFGL 966
Cdd:PRK11905 873 IEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 967 HTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRMTQKAPKIDRIA---SQQDQAAVD 1043
Cdd:PRK11905 953 HSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPIPPAhesVDTDAAARD 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 1044 LARWLDENGETVAAEAARQAAALSGLGFETELAGPVGERNVYALHPRGKVLLVPATEQGLYRQLAAALAAGNAVVIDNAS 1123
Cdd:PRK11905 1033 FLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVADTEEALLRQLAAALATGNVAVVAADS 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 1124 GLEKSIYGLPATVTSRIVWADDWAKSGPFAGALVEGDAERVVEINRKISALSGPLVLVQAATTealsgeSQPYTLDWLVE 1203
Cdd:PRK11905 1113 GLAAALADLPGLVAARIDWTQDWEADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEP------TDAYDLARLVE 1186
|
1210 1220
....*....|....*....|.
gi 739227363 1204 EVSVSVNTTAAGGNASLMSIG 1224
Cdd:PRK11905 1187 ERSVSINTTAAGGNASLMALG 1207
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
16-1224 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1897.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 16 FQNFAPPVREQTLLRKAITAAYRRTEEECMAPLIEAATVTAEQAKAIRETARKLIEALRAKTKGTG----VEGLVQEYSL 91
Cdd:PRK11809 78 FLEFAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGragmVQGLLQEFSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 92 SSHEGVALMCLAEALLRIPDTATRDALIRDKIARGDWKSHIGGGRSLFVNAATWGLVITGKLTSTVNDSGLSAALTKLIA 171
Cdd:PRK11809 158 SSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 172 RAGEPVIRRGVDMAMRMMGEQFVTGETIGEAIKRSRPLEEQGFQYSYDMLGEAATTAKDAERYYKDYENAIHAIGKASAG 251
Cdd:PRK11809 238 KSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 252 RGIYGGPGISIKLSALHPRYARAQAERVMAELLPRVKSLMLLSKKYDIGLNIDAEEADRLELSLDLLEELALDKDLAGWN 331
Cdd:PRK11809 318 RGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 332 GLGFVVQAYGRRCPFVLDYIIDLARRSNRRIMVRLVKGAYWDAEIKRAQVEGLEDFPVFTRKVHTDVSYIACARKLLAAR 411
Cdd:PRK11809 398 GIGFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVP 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 412 DVIFPQFATHNAQSMATIYHLAGPDFKLGDYEFQCLHGMGEPLYSEVVGKR---KLDRPCRFYAPVGTHETLLAYLVRRL 488
Cdd:PRK11809 478 NLIYPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVadgKLNRPCRIYAPVGTHETLLAYLVRRL 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 489 LENGANSSFVNRIADPAVPVDSLLEDPAAVV----KAHNVPGARHDRIAAPADLFGPQRKNSAGLDLSSETTLAALDKVL 564
Cdd:PRK11809 558 LENGANTSFVNRIADTSLPLDELVADPVEAVeklaQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSAL 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 565 KAGASAEWKAA----APQAGGATRPVLNPGDHNDIVGYVTEPTEADVEAAMQRAASSN--WPSTPVEERAACLERAADAM 638
Cdd:PRK11809 638 LASAHQKWQAApmleDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAApiWFATPPAERAAILERAADLM 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 639 QAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARRNFT-AGEKPLGPVVCISPWNFPLAIFIGQVTAALVAGN 717
Cdd:PRK11809 718 EAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDnDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGN 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 718 PVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVLANGQP 796
Cdd:PRK11809 798 SVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETvGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRP 877
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 797 VPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVG 876
Cdd:PRK11809 878 IPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIG 957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 877 PVITAEAKGTIEKHIEDMRSLGHRIEQITL--AGETGKGTFVPPTIIEMKSLADLKREVFGPVLHVIRFKRDNLDRLIDE 954
Cdd:PRK11809 958 PVIDAEAKANIERHIQAMRAKGRPVFQAARenSEDWQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQ 1037
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 955 INATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRMTQKAPK--IDR 1032
Cdd:PRK11809 1038 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEdaLAV 1117
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 1033 IASQQD--------------QAAVDLARWLDENgETVAAEAARQAAALSGLGFETELAGPVGERNVYALHPRGKVLLVPA 1098
Cdd:PRK11809 1118 TLARQDaeypvdaqlraallAPLTALREWAAER-EPELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLAD 1196
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 1099 TEQGLYRQLAAALAAGNAVVIDNASGLEKSIYGLPATVTSRIVWADDWAKSG-PFAGALVEGDAERVVEINRKISALSGP 1177
Cdd:PRK11809 1197 TEQDALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADqPFDAVLFHGDSDQLRALCEQVAQRDGP 1276
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*..
gi 739227363 1178 LVLVQAATtealSGESQpYTLDWLVEEVSVSVNTTAAGGNASLMSIG 1224
Cdd:PRK11809 1277 IVSVQGFA----RGETN-ILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
19-1022 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1541.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 19 FAPPVREQTL--LRKAITAAYRRTEEECMAPLIEAATVTAEQAKAIRETARKLIEALRAKTKG-TGVEGLVQEYSLSSHE 95
Cdd:PRK11904 1 LLGIYILQSLdeLRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKlGGIDAFLQEYSLSTEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 96 GVALMCLAEALLRIPDTATRDALIRDKIARGDWKSHIGGGRSLFVNAATWGLVITGKL--TSTVNDSGLSAALTKLIARA 173
Cdd:PRK11904 81 GIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVvkLDKKADGTPSGVLKRLVNRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 174 GEPVIRRGVDMAMRMMGEQFVTGETIGEAIKRSRPLEEQGFQYSYDMLGEAATTAKDAERYYKDYENAIHAIGKASAGRG 253
Cdd:PRK11904 161 GEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 254 IYGGPGISIKLSALHPRYARAQAERVMAELLPRVKSLMLLSKKYDIGLNIDAEEADRLELSLDLLEELALDKDLAGWNGL 333
Cdd:PRK11904 241 LPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 334 GFVVQAYGRRCPFVLDYIIDLARRSNRRIMVRLVKGAYWDAEIKRAQVEGLEDFPVFTRKVHTDVSYIACARKLLAARDV 413
Cdd:PRK11904 321 GLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 414 IFPQFATHNAQSMATIYHLAGPDfklgDYEFQCLHGMGEPLYSEVVGkrKLDRPCRFYAPVGTHETLLAYLVRRLLENGA 493
Cdd:PRK11904 401 IYPQFATHNAHTVAAILEMAGHR----GFEFQRLHGMGEALYDALLD--APGIPCRIYAPVGSHKDLLPYLVRRLLENGA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 494 NSSFVNRIADPAVPVDSLLEDPAAVVKAHnvPGARHDRIAAPADLFGPQRKNSAGLDLSSETTLAALDKVLKAGASAEWK 573
Cdd:PRK11904 475 NSSFVHRLVDPDVPIEELVADPVEKLRSF--ETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 574 AA-APQAGGATRPVLNPGDHNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVM 650
Cdd:PRK11904 553 AGpIINGEGEARPVVSPADRRRVVGEVAFADAEQVEQALAaaRAAFPAWSRTPVEERAAILERAADLLEANRAELIALCV 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 651 REAGKSMPNAIAEVREAIDFLRYYAAEARRNFTAGEKPLGPV--------------VCISPWNFPLAIFIGQVTAALVAG 716
Cdd:PRK11904 633 REAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTgesnelrlhgrgvfVCISPWNFPLAIFLGQVAAALAAG 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 717 NPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRvlaNGQ 795
Cdd:PRK11904 713 NTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATvGAALTADPRIAGVAFTGSTETARIINRTLAAR---DGP 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 796 PVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDV 875
Cdd:PRK11904 790 IVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDV 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 876 GPVITAEAKGTIEKHIEDMRSLGHRIEQITLAGETGKGTFVPPTIIEMKSLADLKREVFGPVLHVIRFKRDNLDRLIDEI 955
Cdd:PRK11904 870 GPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAI 949
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227363 956 NATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGR 1022
Cdd:PRK11904 950 NATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLR 1016
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
16-1221 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1477.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 16 FQNFAPPVREQTLLRKAITAAYRRTEEECMAPLIEAATVTAEQAKAIRETARKLIEALRAKTKGTGVEGLVQEYSLSSHE 95
Cdd:COG4230 3 FALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLSSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 96 GVALMCLAEALLRIPDTATRDALIRDKIARGDWKSHIGGGRSLFVNAATWGLVITGKLTSTVNDSGLSAALTKLIARAGE 175
Cdd:COG4230 83 ALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRLGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 176 PVIRRGVDMAMRMMGEQFVTGETIGEAIKRSRPLEEQGFQYSYDMLGEAATTAKDAERYYKDYENAIHAIGKASAGRGIY 255
Cdd:COG4230 163 PGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGSGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 256 GGPGISIKLSALHPRYARAQAERVMAELLPRVKSLMLLSKKYDIGLNIDAEEADRLELSLDLLEELALDKDLAGWNGLGF 335
Cdd:COG4230 243 PGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 336 VVQAYGRRCPFVLDYIIDLARRSNRRIMVRLVKGAYWDAEIKRAQVEGLEDFPVFTRKVHTDVSYIACARKLLAARDVIF 415
Cdd:COG4230 323 GVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAAQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 416 PQFATHNAQSMATIYHLAGPDFKLGDYEFQCLHGMGEPLYsEVVGKRKLDRPCRFYAPVGTHETLLAYLVRRLLENGANS 495
Cdd:COG4230 403 PAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLY-DQVGRGKLGRPCRIYAPVGSHEDLLAYLVRRLLENGANS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 496 SFVNRIADPAVPVDSLLEDPAAVVKAHnvPGARHDRIAAPADLFGPQRKNSAGLDLSSETTLAALDKVLKAGASAEWKAA 575
Cdd:COG4230 482 SFVNRIADEDVPVEELIADPVEKARAL--GGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQAA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 576 ----APQAGGATRPVLNPGDHNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLV 649
Cdd:COG4230 560 pliaGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAqaAFPAWSATPVEERAAILERAADLLEAHRAELMALL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 650 MREAGKSMPNAIAEVREAIDFLRYYAAEARRNFTAGEK--PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEET 727
Cdd:COG4230 640 VREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVlrGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQT 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 728 PLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRvlaNGQPVPLIAETGGQ 806
Cdd:COG4230 720 PLIAARAVRLLHEAGVPADVLQLLPGDGETvGAALVADPRIAGVAFTGSTETARLINRTLAAR---DGPIVPLIAETGGQ 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 807 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGT 886
Cdd:COG4230 797 NAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARAN 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 887 IEKHIEDMRSLGHRIEQITLAGETGKGTFVPPTIIEMKSLADLKREVFGPVLHVIRFKRDNLDRLIDEINATGYGLTFGL 966
Cdd:COG4230 877 LEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGV 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 967 HTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGR-MTQKAPKIDRIASQQDQAAVDLA 1045
Cdd:COG4230 957 HSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRfATERTVTVNTTAAGGNASLLALG 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 1046 RWldengetvaaeaarqaaaLSGLGFETELAGPVGERNVYALHPRGKVLLVPATEQGLYRQLAAALAAGNAVVIDNASGL 1125
Cdd:COG4230 1037 DW------------------LASLLGALTLPGPTGERNTLTLRPRGRVLCLADSLEALLAQLAAALATGNRAVVAADLAL 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 1126 EksiyGLPATVtsrivwaddwakSGPFAGALVEGdaeRVVEINRKISALSGPLVLVQAATtealsgesqpYTLDWLVEEv 1205
Cdd:COG4230 1099 A----GLPAVL------------LPPFDAVLFEG---RLRALRQALAARDGAIVPVIDAG----------YDLERLLEE- 1148
|
1210
....*....|....*.
gi 739227363 1206 svsvnttaAGGNASLM 1221
Cdd:COG4230 1149 --------AGGNASLM 1156
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
493-1023 |
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: 666.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 493 ANSSFVNRIADPAVPvdslledpaavvkahnvpgarhdriaapadlfgpqrknsagldlssettLAALDKVLKAGASAEW 572
Cdd:cd07125 1 ANSSFVNRIFDLEVP-------------------------------------------------LEALADALKAFDEKEW 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 573 KA-----AAPQAGGATRPVLNPGDHNDIVGYVTEPTEADVEAAMQRAAS--SNWPSTPVEERAACLERAADAMQAEMPDL 645
Cdd:cd07125 32 EAipiinGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAafAGWSATPVEERAEILEKAADLLEANRGEL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 646 LGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARRNFTAGE-------------KPLGPVVCISPWNFPLAIFIGQVTAA 712
Cdd:cd07125 112 IALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPElpgptgelnglelHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 713 LVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRvl 791
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEiGEALVAHPRIDGVIFTGSTETAKLINRALAER-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 792 aNGQPVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRL 871
Cdd:cd07125 270 -DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 872 SVDVGPVITAEAKGTIEKHIEDMRSLGHRIEQITLagETGKGTFVPPTIIEMKSLADLKREVFGPVLHVIRFKRDNLDRL 951
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPL--DDGNGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEA 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 952 IDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRM 1023
Cdd:cd07125 427 IEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRF 498
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
537-1028 |
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: 650.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 537 DLFGPQRKNSAGLDLSSETTLAALDKVLKAGASAEWKAA-----APQAGGATRPVLNPGDHNDIVGYVTEPTEADVEAAM 611
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAApiighSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 612 QRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARR---NFTAge 686
Cdd:TIGR01238 81 DSAqqAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDvlgEFSV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 687 KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSP 765
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADvGAALTSDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 766 LTAGVMFTGSTEVARLIQGQLAGRVLAngqPVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQ 845
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 846 EDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEQITLAG--ETGKGTFVPPTIIEM 923
Cdd:TIGR01238 316 EDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDsrACQHGTFVAPTLFEL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 924 KSLADLKREVFGPVLHVIRFKRDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFG 1003
Cdd:TIGR01238 396 DDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFG 475
|
490 500
....*....|....*....|....*
gi 739227363 1004 GRGLSGTGPKAGGPLYLGRMTQKAP 1028
Cdd:TIGR01238 476 GQGLSGTGPKAGGPHYLYRLTQVQY 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
51-1022 |
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: 623.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 51 AATVTAEQAKAIRETARKLIEALRAKtKGTGVEGLVQEYSLSSHEGVALMCLAEALLRIPDTATRDALIRDKIARGDwks 130
Cdd:COG0506 2 TAALDEALRARAVALARRLVEAIRAA-PEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 131 higggrSLFVNAATWGLVITgkltstvndsglsaaltkLIARAGEPVIRRGVDMAMRMMGEQFVTGETIGEAIKRSRPLE 210
Cdd:COG0506 78 ------SFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 211 EQGFQYSYDMLGEAATTAKDAERYYKDYENAIHAIGKASagrgiYGGPGISIKLSALHPRYARAQAERVMAELLPRVKSL 290
Cdd:COG0506 134 AKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 291 MLLSKKYDIGLNIDAEEADRLELSLDLLEELALDKDLAGWNGLGFVVQAYGRRCPFVLDYIIDLARRSNRRIMVRLVKGA 370
Cdd:COG0506 209 ARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 371 YWDAEIKRAQVEGLeDFPVFTRKVHTDVSYIACARKLLAARDVIFPQFATHNAQSMATIYHLAGP-DFKLGDYEFQCLHG 449
Cdd:COG0506 289 YWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQMLYG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 450 MGEPLYSEVVGKRK--LDRPCRFYAPVGTHETLLAYLVRRLLENGANSSFVNRIADPAVPVDSLLEDPAAVVKAHNVPga 527
Cdd:COG0506 368 MGEDLQRALAAVDGgrLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPT-- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 528 RHDRIAAPADLFGPQRKNSAGLDLSSETTLAALDKVLKAGASAEWKAAAPQAGG-----ATRPVLNPGDHNDIVGYVTEP 602
Cdd:COG0506 446 PPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAaaaaaAVAVVPAAAAAVVAAAAAAAA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 603 TEADVEAAMQRAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARR-- 680
Cdd:COG0506 526 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAAra 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 681 --------NFTAGEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLP 752
Cdd:COG0506 606 aappppppGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVL 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 753 GDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVLANGQPVPL--IAETGGQNAMIVDSSALAEQVVADVIASAFD 830
Cdd:COG0506 686 VLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAaaAAAGGAAAAAAAAAAAAAVAAVAASAAASAS 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 831 SAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEQITLAGET 910
Cdd:COG0506 766 ASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPG 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 911 GKGTFVPPTIIEMKSLADLKREVFGPVLHVIRFKRDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNR 990
Cdd:COG0506 846 LLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGG 925
|
970 980 990
....*....|....*....|....*....|..
gi 739227363 991 NIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGR 1022
Cdd:COG0506 926 GGGGGGGGGGGGGGGGGGGGGGGGGGAGTLAL 957
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
202-500 |
4.06e-139 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 423.83 E-value: 4.06e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 202 AIKRSRPLEEQGFQYSYDMLGEAATTAKDAERYYKDYENAIHAIGKASAGRGIYGGPGISIKLSALHPRYARAQAERVMA 281
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 282 ELLPRVKSLMLLSKKYDIGLNIDAEEADRLELSLDLLEELALDKDLAGWNGLGFVVQAYGRRCPFVLDYIIDLARRSNRR 361
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 362 IMVRLVKGAYWDAEIKRAQvEGLEDFPVFTRKVHTDVSYIACARKLLAARDVIFPQFATHNAQSMATIYHLAG-PDFKLG 440
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEeLGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 441 DYEFQCLHGMGEPLYSEVVGKrklDRPCRFYAPVGTHETLLAYLVRRLLENGANSSFVNR 500
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAA---GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
587-1033 |
4.79e-137 |
|
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: 426.61 E-value: 4.79e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 587 LNPGDHNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEV 664
Cdd:cd07083 37 VSPFAPSEVVGTTAKADKAEAEAALEAAwaAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 665 REAIDFLRYYAAEARRNFTAGE--------------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLI 730
Cdd:cd07083 117 AEAIDFIRYYARAALRLRYPAVevvpypgednesfyVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 731 AAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVLANGQPVPLIAETGGQNAM 809
Cdd:cd07083 197 GYKVFEIFHEAGFPPGVVQFLPGVGEEvGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 810 IVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEK 889
Cdd:cd07083 277 IVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 890 HIEDMRSLGHRIEQITLagETGKGTFVPPTIIEMKSLAD--LKREVFGPVLHVIRFKRDNLDRLIDEINATGYGLTFGLH 967
Cdd:cd07083 357 YIEHGKNEGQLVLGGKR--LEGEGYFVAPTVVEEVPPKAriAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVY 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227363 968 TRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRMTQKAPKIDRI 1033
Cdd:cd07083 435 SRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
580-1020 |
2.58e-126 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 398.52 E-value: 2.58e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 580 GGATRPVLNPGDHNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSM 657
Cdd:cd07124 44 TEEKIESRNPADPSEVLGTVQKATKEEAEAAVQaaRAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 658 PNAIAEVREAIDFLRYYAAEARRN------FTAGE------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAE 725
Cdd:cd07124 124 AEADADVAEAIDFLEYYAREMLRLrgfpveMVPGEdnryvyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 726 ETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAgrVLANGQPV--PLIAE 802
Cdd:cd07124 204 DTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEvGDYLVEHPDVRFIAFTGSREVGLRIYERAA--KVQPGQKWlkRVIAE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 803 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAE 882
Cdd:cd07124 282 MGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 883 AKGTIEKHIEDMRSLGHRIEQITLAGETGKGTFVPPTIIE----MKSLAdlKREVFGPVLHVIRFkrDNLDRLIDEINAT 958
Cdd:cd07124 362 ARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFAdvppDHRLA--QEEIFGPVLAVIKA--KDFDEALEIANDT 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 959 GYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYL 1020
Cdd:cd07124 438 EYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYL 499
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
571-1025 |
1.75e-122 |
|
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: 387.17 E-value: 1.75e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGL 648
Cdd:COG1012 13 EWVAAA---SGETFDVINPAT-GEVLARVPAATAEDVDAAVAaaRAAFPAWAATPPAERAAILLRAADLLEERREELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VMREAGKSMPNAIAEVREAIDFLRYYAAEARRNftAGE---------------KPLGPVVCISPWNFPLAIFIGQVTAAL 713
Cdd:COG1012 89 LTLETGKPLAEARGEVDRAADFLRYYAGEARRL--YGEtipsdapgtrayvrrEPLGVVGAITPWNFPLALAAWKLAPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 714 VAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVla 792
Cdd:COG1012 167 AAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 793 ngqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLS 872
Cdd:COG1012 245 ----KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 873 VDVGPVITAEAKGTIEKHIEDMRSLGHRIeqitLAG----ETGKGTFVPPTIIE-----MKsLAdlKREVFGPVLHVIRF 943
Cdd:COG1012 321 TDMGPLISEAQLERVLAYIEDAVAEGAEL----LTGgrrpDGEGGYFVEPTVLAdvtpdMR-IA--REEIFGPVLSVIPF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 944 krDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGvQPFGGRGLSGTGPKaGGPLYLGRM 1023
Cdd:COG1012 394 --DDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGRE-GGREGLEEY 469
|
..
gi 739227363 1024 TQ 1025
Cdd:COG1012 470 TE 471
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
579-1025 |
7.61e-113 |
|
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: 360.69 E-value: 7.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 579 AGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKS 656
Cdd:pfam00171 4 SESETIEVINPAT-GEVIATVPAATAEDVDAAIAaaRAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 657 MPNAIAEVREAIDFLRYYAAEARR------NFTAGE------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPA 724
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRldgetlPSDPGRlaytrrEPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 725 EETPLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIqGQLAGRVLAngqpvPLIAET 803
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAeVGEALVEHPDVRKVSFTGSTAVGRHI-AEAAAQNLK-----RVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 804 GGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEA 883
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 884 KGTIEKHIEDMRSLGHRIEqitLAGETG--KGTFVPPTII-----EMKSladLKREVFGPVLHVIRFKrdNLDRLIDEIN 956
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLL---TGGEAGldNGYFVEPTVLanvtpDMRI---AQEEIFGPVLSVIRFK--DEEEAIEIAN 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227363 957 ATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVqPFGGRGLSGTGpKAGGPLYLGRMTQ 1025
Cdd:pfam00171 389 DTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLEEYTE 455
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
604-1025 |
4.86e-107 |
|
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: 343.81 E-value: 4.86e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 604 EADVEAAmqRAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARRNF- 682
Cdd:cd07078 1 DAAVAAA--RAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 683 ------TAGEK------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQL 750
Cdd:cd07078 79 evipspDPGELaivrrePLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 751 LPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAF 829
Cdd:cd07078 159 VTGDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 830 DSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIeqitLAG- 908
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKL----LCGg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 909 ---ETGKGTFVPPTIIEMKSLADL--KREVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAA 983
Cdd:cd07078 309 krlEGGKGYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEA 386
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 739227363 984 GNLYVNRNIIGAVVGvQPFGGRGLSGTGpKAGGPLYLGRMTQ 1025
Cdd:cd07078 387 GTVWINDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEEYTE 426
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
586-1020 |
2.83e-103 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 336.52 E-value: 2.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDHNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAE 663
Cdd:PRK03137 54 SINPANKSEVVGRVSKATKELAEKAMQAAleAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 664 VREAIDFLRYYAAEARR-------NFTAGE------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLI 730
Cdd:PRK03137 134 TAEAIDFLEYYARQMLKladgkpvESRPGEhnryfyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 731 AAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEV--------ARLIQGQL-AGRVlangqpvplI 800
Cdd:PRK03137 214 AAKFVEVLEEAGLPAGVVNFVPGSGSEvGDYLVDHPKTRFITFTGSREVglriyeraAKVQPGQIwLKRV---------I 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 801 AETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSvDVGPVIT 880
Cdd:PRK03137 285 AEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVIN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 881 AEAKGTIEKHIEdmrsLGHRIEQITLAGET--GKGTFVPPTIIemkslADLKR-------EVFGPVLHVIRFKrdNLDRL 951
Cdd:PRK03137 364 QASFDKIMSYIE----IGKEEGRLVLGGEGddSKGYFIQPTIF-----ADVDPkarimqeEIFGPVVAFIKAK--DFDHA 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227363 952 IDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYL 1020
Cdd:PRK03137 433 LEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYL 501
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
587-1025 |
1.23e-100 |
|
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: 329.52 E-value: 1.23e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 587 LNPGDHNDIVGYVTEPTEADVEAAMQRAASS--NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEV 664
Cdd:TIGR01237 51 INPCDKSEVVGTVSKASQEHAEHALQAAAKAfeAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 665 REAIDFLRYYAAEARR-------NFTAGEK------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIA 731
Cdd:TIGR01237 131 AEAIDFMEYYARQMIElakgkpvNSREGETnqyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 732 AQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQgQLAGRVLANGQPVP-LIAETGGQNAM 809
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSeVGDYLVDHPKTSLITFTGSREVGTRIF-ERAAKVQPGQKHLKrVIAEMGGKDTV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 810 IVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEK 889
Cdd:TIGR01237 290 IVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIME 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 890 HIEDMRSLGhrieQITLAGETG--KGTFVPPTIIemkslADLKR-------EVFGPVLHVIRFKrdNLDRLIDEINATGY 960
Cdd:TIGR01237 370 YIEIGKAEG----RLVSGGCGDdsKGYFIGPTIF-----ADVDRkarlaqeEIFGPVVAFIRAS--DFDEALEIANNTEY 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227363 961 GLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRMTQ 1025
Cdd:TIGR01237 439 GLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQ 503
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
571-1017 |
3.77e-84 |
|
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: 282.60 E-value: 3.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWkaaapQAGGATRPVLNPGDHNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGL 648
Cdd:cd07097 8 EW-----VAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAaaAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VMREAGKSMPNAIAEVREAIDFLRYYAAEARRnfTAGE---------------KPLGPVVCISPWNFPLAIFIGQVTAAL 713
Cdd:cd07097 83 LTREEGKTLPEARGEVTRAGQIFRYYAGEALR--LSGEtlpstrpgvevettrEPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 714 VAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGSTEVARliqgQLAGRVLA 792
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGsEVGQALVEHPDVDAVSFTGSTAVGR----RIAAAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 793 NGQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLS 872
Cdd:cd07097 237 RGARVQL--EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 873 VDVGPVITAEAKGTIEKHIEDMRSLGHRIEQ--ITLAGETgKGTFVPPTII-----EMKSladLKREVFGPVLHVIRFkr 945
Cdd:cd07097 315 VDIGPVVSERQLEKDLRYIEIARSEGAKLVYggERLKRPD-EGYYLAPALFagvtnDMRI---AREEIFGPVAAVIRV-- 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 946 DNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVqPFGGRGLSGTGPKAGGP 1017
Cdd:cd07097 389 RDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
586-1011 |
1.36e-82 |
|
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: 277.78 E-value: 1.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQRAASS--NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAE 663
Cdd:cd07103 1 VINPAT-GEVIGEVPDAGAADADAAIDAAAAAfkTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 664 VREAIDFLRYYAAEARRnfTAGE---------------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETP 728
Cdd:cd07103 80 VDYAASFLEWFAEEARR--IYGRtipspapgkrilvikQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 729 LIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangqpVPLIAETGGQN 807
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEiGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGGNA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 808 AMIVDSSALAEQVVADVIASAFDSAGQRC-SALRILClQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGT 886
Cdd:cd07103 232 PFIVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 887 IEKHIEDMRSLGHRIeqitLAG---ETGKGTFVPPTII-EMKSLADL-KREVFGPVLHVIRFkrDNLDRLIDEINATGYG 961
Cdd:cd07103 311 VEALVEDAVAKGAKV----LTGgkrLGLGGYFYEPTVLtDVTDDMLImNEETFGPVAPIIPF--DTEDEVIARANDTPYG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 739227363 962 LTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVvgVQPFGGRGLSGTG 1011
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
608-1026 |
1.79e-81 |
|
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: 271.41 E-value: 1.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 608 EAAmqRAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARRNFTAGEK 687
Cdd:cd06534 1 AAA--RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 -------------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGD 754
Cdd:cd06534 79 spdpggeayvrrePLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 755 GKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAG 833
Cdd:cd06534 159 GDEvGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 834 QRCSALRILCLQEDVADRTLTMLKGalhelrigrtdrLSVDVGPvitaeakgtiekhieDMRSlghrieqitlagetgkg 913
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLVT------------VLVDVDP---------------DMPI----------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 914 tfvpptiiemksladLKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNII 993
Cdd:cd06534 269 ---------------AQEEIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSI 331
|
410 420 430
....*....|....*....|....*....|...
gi 739227363 994 GAVVGvQPFGGRGLSGTGpKAGGPLYLGRMTQK 1026
Cdd:cd06534 332 GVGPE-APFGGVKNSGIG-REGGPYGLEEYTRT 362
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
571-1017 |
4.10e-81 |
|
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: 274.61 E-value: 4.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWkaaAPQAGGATRPVLNPGDHNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGL 648
Cdd:cd07131 6 EW---VDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEaaREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VMREAGKSMPNAIAEVREAIDFLRYYAAEARRNF---TAGE----------KPLGPVVCISPWNFPLAIFIGQVTAALVA 715
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFgetVPSElpnkdamtrrQPIGVVALITPWNFPVAIPSWKIFPALVC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 716 GNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPG-DGKTGAALVGSPLTAGVMFTGSTEVARLIqGQLAGRvlaNG 794
Cdd:cd07131 163 GNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERI-GETCAR---PN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 795 QPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVD 874
Cdd:cd07131 239 KRVAL--EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 875 VGPVITAEAKGTIEKHIEDMRSLGHRI----EQITlAGETGKGTFVPPTIIEM--KSLADLKREVFGPVLHVIRFkrDNL 948
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLllggERLT-GGGYEKGYFVEPTVFTDvtPDMRIAQEEIFGPVVALIEV--SSL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227363 949 DRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVqPFGGRGLSGTGPKAGGP 1017
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
579-1015 |
5.91e-81 |
|
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: 274.06 E-value: 5.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 579 AGGATRPVLNPGDHNDIVGyVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKS 656
Cdd:cd07086 10 SGGETFTSRNPANGEPIAR-VFPASPEDVEAAVAAAreAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 657 MPNAIAEVREAIDFLRYYAAEARRNF---TAGE----------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKP 723
Cdd:cd07086 89 LPEGLGEVQEMIDICDYAVGLSRMLYgltIPSErpghrlmeqwNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 724 AEETPLIAAQGVRLLHEA----GVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRvlaNGqpvPL 799
Cdd:cd07086 169 SETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARR---FG---RV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 800 IAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVI 879
Cdd:cd07086 243 LLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 880 TAEAKGTIEKHIEDMRSLGHRIEqitLAGE----TGKGTFVPPTIIEMK--SLADLKREVFGPVLHVIRFkrDNLDRLID 953
Cdd:cd07086 323 NQAAVEKYLNAIEIAKSQGGTVL---TGGKridgGEPGNYVEPTIVTGVtdDARIVQEETFAPILYVIKF--DSLEEAIA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227363 954 EINATGYGLTFGLHTRLDDTIQHVLSRVA--AGNLYVNRNIIGAVVGVqPFGGRGLSGTGPKAG 1015
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWLGPKGsdCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
606-1009 |
4.09e-74 |
|
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: 252.96 E-value: 4.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 606 DVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVRE-------AIDFLRYYAA 676
Cdd:cd07095 1 QVDAAVAaaRAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAmagkidiSIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 677 EaRRNFTAG------EKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQL 750
Cdd:cd07095 81 E-RATPMAQgravlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 751 LPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRvlangqPVPLIA-ETGGQNAMIVDSSALAEQVVADVIASAF 829
Cdd:cd07095 160 VQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGR------PGKILAlEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 830 DSAGQRCS-ALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRieqITLAG 908
Cdd:cd07095 234 LTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGE---PLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 909 E--TGKGTFVPPTIIEMKSLADL-KREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGN 985
Cdd:cd07095 311 ErlVAGTAFLSPGIIDVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI 388
|
410 420
....*....|....*....|....
gi 739227363 986 LYVNRNIIGAvVGVQPFGGRGLSG 1009
Cdd:cd07095 389 VNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
581-1024 |
7.19e-72 |
|
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: 249.81 E-value: 7.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 581 GATRPVLNPGDHNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEM-PDLLGLVMREAGKSM 657
Cdd:cd07123 45 GNTGKQVMPHDHAHVLATYHYADAALVEKAIEAAleARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 658 PNA-IAEVREAIDFLRYYAAEARR-------NFTAGE------KPL-GPVVCISPWNFPlAIFIGQVTAALVAGNPVLAK 722
Cdd:cd07123 125 WQAeIDAACELIDFLRFNVKYAEElyaqqplSSPAGVwnrleyRPLeGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 723 PAEeTPLIAAQGV-RLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRvLANGQPVP-L 799
Cdd:cd07123 204 PSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVvGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEN-LDRYRTYPrI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 800 IAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSAL-RI---LCLQEDVADRTLTMLKgalhELRIGRTDRLSVDV 875
Cdd:cd07123 282 VGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAAsRAyvpESLWPEVKERLLEELK----EIKMGDPDDFSNFM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 876 GPVITAEAKGTIEKHIEDMR-SLGHRIeqitLAGETG---KGTFVPPTIIEMKSLAD--LKREVFGPVLHVIRFKRDNLD 949
Cdd:cd07123 358 GAVIDEKAFDRIKGYIDHAKsDPEAEI----IAGGKCddsVGYFVEPTVIETTDPKHklMTEEIFGPVLTVYVYPDSDFE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227363 950 RLIDEINATG-YGLT---FGLHTRLDDTIQHVLsRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRMT 1024
Cdd:cd07123 434 ETLELVDTTSpYALTgaiFAQDRKAIREATDAL-RNAAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWV 511
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
587-1026 |
1.38e-70 |
|
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: 243.67 E-value: 1.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 587 LNPGDHNDiVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEV 664
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARAraAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 665 REAIDFLRYYAAEA----------RRNFTAGEK------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETP 728
Cdd:cd07099 80 LLALEAIDWAARNAprvlaprkvpTGLLMPNKKatveyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 729 LIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAgVMFTGSTEVARLIQGQLAGRvlangqPVPLIAETGGQNA 808
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAGVDK-VAFTGSVATGRKVMAAAAER------LIPVVLELGGKDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 809 MIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIE 888
Cdd:cd07099 233 MIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 889 KHIEDMRSLGHRIeqitLAG---ETGKGTFVPPTII-----EMKSladLKREVFGPVLHVIRFkrDNLDRLIDEINATGY 960
Cdd:cd07099 313 RHVDDAVAKGAKA----LTGgarSNGGGPFYEPTVLtdvphDMDV---MREETFGPVLPVMPV--ADEDEAIALANDSRY 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227363 961 GLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTGpKAGGPLYLGRMTQK 1026
Cdd:cd07099 384 GLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRP 448
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
585-1011 |
8.07e-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: 241.73 E-value: 8.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 585 PVLNPGDhNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIA 662
Cdd:cd07149 2 EVISPYD-GEVIGRVPVASEEDVEKAIAAAkeGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 EVREAIDFLRYYAAEARRNftAGE-------------------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKP 723
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRL--AGEtipfdaspggegrigftirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 724 AEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQgQLAGRvlangqpVPLIAE 802
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETvGDALVTDPRVRMISFTGSPAVGEAIA-RKAGL-------KKVTLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 803 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGrtDRLS--VDVGPVI 879
Cdd:cd07149 231 LGSNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVG--DPLDedTDVGPMI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 880 TAEAKGTIEKHIEDMRSLGHRIeqitLAGETGKGTFVPPTIIE--MKSLADLKREVFGPVLHVIRFkrDNLDRLIDEINA 957
Cdd:cd07149 308 SEAEAERIEEWVEEAVEGGARL----LTGGKRDGAILEPTVLTdvPPDMKVVCEEVFAPVVSLNPF--DTLDEAIAMAND 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 739227363 958 TGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNrNIIGAVVGVQPFGGRGLSGTG 1011
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
577-1011 |
1.00e-68 |
|
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: 239.09 E-value: 1.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 577 PQAGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAG 654
Cdd:cd07088 8 PSSSGETIDVLNPAT-GEVVATVPAATAEDADRAVDaaEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 655 KSMPNAIAEVREAIDFLRYYAAEARR-------NFTAGEK------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLA 721
Cdd:cd07088 87 KTLSLARVEVEFTADYIDYMAEWARRiegeiipSDRPNENififkvPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 722 KPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARliqgqlagRVLANGQP--VP 798
Cdd:cd07088 167 KPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSvVGDALVAHPKVGMISLTGSTEAGQ--------KIMEAAAEniTK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 799 LIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPV 878
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 879 ITAEAKGTIEKHIEDMRSLGHRIEQITLAGETGKGTFVPPTIIE--MKSLADLKREVFGPVLHVIRFkrDNLDRLIDEIN 956
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELAN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 739227363 957 ATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQpfGGRGLSGTG 1011
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLG 449
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
571-1011 |
2.88e-68 |
|
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: 237.85 E-value: 2.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKaaapQAGGATRPVLNPGDHNdIVGYVTEPTEADVEAAMQRAAS---SNWPSTPVEERAACLERAADAMQAEMPDLLG 647
Cdd:cd07082 9 EWK----ESSGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDagrGWWPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 648 LVMREAGKSMPNAIAEVREAIDFLRYYAAEARR----------NFTAGEK-------PLGPVVCISPWNFPLAIFIGQVT 710
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRldgdslpgdwFPGTKGKiaqvrrePLGVVLAIGPFNYPLNLTVSKLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 711 AALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQgQLAGR 789
Cdd:cd07082 164 PALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGReIGDPLVTHGRIDVISFTGSTEVGNRLK-KQHPM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 790 vlangqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTD 869
Cdd:cd07082 243 -------KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 870 RLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIeqitLAGETGK-GTFVPPTIIE-----MKsLAdlKREVFGPVLHVIRF 943
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATV----LNGGGREgGNLIYPTLLDpvtpdMR-LA--WEEPFGPVLPIIRV 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 944 KrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVN----RNIigavvGVQPFGGRGLSGTG 1011
Cdd:cd07082 389 N--DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIG 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
586-1015 |
3.34e-68 |
|
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: 237.06 E-value: 3.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQRAA----SSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAI 661
Cdd:cd07114 1 SINPAT-GEPWARVPEASAADVDRAVAAARaafeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 662 AEVREAIDFLRYYAAEARR--------------NFTAGEkPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEET 727
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKiegavipvdkgdylNFTRRE-PLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 728 PLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIqGQLAGRVLAngqpvPLIAETGGQ 806
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPeTGEALVEHPLVAKIAFTGGTETGRHI-ARAAAENLA-----PVTLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 807 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGT 886
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 887 IEKHIEDMRSLGHRI----EQITLAgETGKGTFVPPTIIE--MKSLADLKREVFGPVLHVIRFkrDNLDRLIDEINATGY 960
Cdd:cd07114 313 VERYVARAREEGARVltggERPSGA-DLGAGYFFEPTILAdvTNDMRIAQEEVFGPVLSVIPF--DDEEEAIALANDSEY 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 739227363 961 GLTFGLHTRlDDTIQH-VLSRVAAGNLYVN--RniigAVVGVQPFGGRGLSGTGPKAG 1015
Cdd:cd07114 390 GLAAGIWTR-DLARAHrVARAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
596-1015 |
1.45e-67 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 235.28 E-value: 1.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 596 VGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRY 673
Cdd:cd07101 9 LGELPQSTPADVEAAFAraRAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 674 YAAEARRnFTAGEK----------------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRL 737
Cdd:cd07101 89 YARRAER-LLKPRRrrgaipvltrttvnrrPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 738 LHEAGVPQDAVQLLPGDGktgaALVGSPLTAG---VMFTGSTEVARLIqGQLAGRVLangqpVPLIAETGGQNAMIVDSS 814
Cdd:cd07101 168 LIEAGLPRDLWQVVTGPG----SEVGGAIVDNadyVMFTGSTATGRVV-AERAGRRL-----IGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 815 ALAEQVVADVIASAFDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIED 893
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCvSIERIY-VHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 894 MRSLGHRIeqitLAGetGKGT------FVPPTIIE--MKSLADLKREVFGPVLHVIRFKRDnlDRLIDEINATGYGLTFG 965
Cdd:cd07101 317 AVAKGATV----LAG--GRARpdlgpyFYEPTVLTgvTEDMELFAEETFGPVVSIYRVADD--DEAIELANDTDYGLNAS 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 739227363 966 LHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQ-PFGGRGLSGTGPKAG 1015
Cdd:cd07101 389 VWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
586-1011 |
2.04e-67 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 234.73 E-value: 2.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGdHNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAE 663
Cdd:cd07106 1 VINPA-TGEVFASAPVASEAQLDQAVAaaKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 664 VREAIDFLRYYA----------------AEARRnftageKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEET 727
Cdd:cd07106 80 VGGAVAWLRYTAsldlpdeviedddtrrVELRR------KPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 728 PLIAAQGVRLLHEAgVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangQPVPLiaETGGQN 807
Cdd:cd07106 154 PLCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGND 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 808 AMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTI 887
Cdd:cd07106 227 AAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 888 EKHIEDMRSLGHRIeqitLAGET---GKGTFVPPTIIemKSLADLKR----EVFGPVLHVIRFkrDNLDRLIDEINATGY 960
Cdd:cd07106 307 KELVEDAKAKGAKV----LAGGEpldGPGYFIPPTIV--DDPPEGSRivdeEQFGPVLPVLKY--SDEDEVIARANDSEY 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 739227363 961 GLTFGLHTRLDDTIQHVLSRVAAGNLYVNRniIGAVVGVQPFGGRGLSGTG 1011
Cdd:cd07106 379 GLGASVWSSDLERAEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
606-1025 |
6.23e-67 |
|
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: 232.81 E-value: 6.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 606 DVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARR--- 680
Cdd:cd07104 1 DVDRAYAAAaaAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 681 ----NFTAGE------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETP-----LIAaqgvRLLHEAGVPQ 745
Cdd:cd07104 81 eilpSDVPGKesmvrrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 746 DAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIqGQLAGRVLAngqPVPLiaETGGQNAMIVDSSALAEQVVADV 824
Cdd:cd07104 157 GVLNVVPGGGSeIGDALVEHPRVRMISFTGSTAVGRHI-GELAGRHLK---KVAL--ELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 825 IASAFDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIeq 903
Cdd:cd07104 231 AFGAFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 904 itLAGETGKGTFVPPTIiemksLADLKR-------EVFGPVLHVIRFKRDnlDRLIDEINATGYGLTFGLHTRLDDTIQH 976
Cdd:cd07104 308 --LTGGTYEGLFYQPTV-----LSDVTPdmpifreEIFGPVAPVIPFDDD--EEAVELANDTEYGLSAAVFTRDLERAMA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 739227363 977 VLSRVAAGNLYVNRNII--GAVVgvqPFGGRGLSGTGpKAGGPLYLGRMTQ 1025
Cdd:cd07104 379 FAERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGPASLEEFTE 425
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
586-1011 |
2.67e-66 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 231.74 E-value: 2.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ---RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIA 662
Cdd:cd07109 1 VFDPST-GEVFARIARGGAADVDRAVQaarRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 EVREAIDFLRYYAAEARR-------------NFTAGEkPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPL 729
Cdd:cd07109 80 DVEAAARYFEYYGGAADKlhgetiplgpgyfVYTVRE-PHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 730 IAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangqpVPLIAETGGQNA 808
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAeAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 809 MIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGrTDRLSVDVGPVITAEAKGTIE 888
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 889 KHIEDMRSLGHRIeqIT----LAGETGKGTFVPPTIIEMKSLADL--KREVFGPVLHVIRFkrDNLDRLIDEINATGYGL 962
Cdd:cd07109 312 GFVARARARGARI--VAggriAEGAPAGGYFVAPTLLDDVPPDSRlaQEEIFGPVLAVMPF--DDEAEAIALANGTDYGL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 739227363 963 TFGLHTRlDDTIQHVLSR-VAAGNLYVNRniIGAVVGVQ-PFGGRGLSGTG 1011
Cdd:cd07109 388 VAGVWTR-DGDRALRVARrLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
603-1025 |
3.92e-66 |
|
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: 230.64 E-value: 3.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 603 TEADVEAAMQRAASSN--WPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAA---- 676
Cdd:cd07152 11 DAADVDRAAARAAAAQraWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGlptq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 677 --------EARRNFTAGEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETP-----LIAaqgvRLLHEAGV 743
Cdd:cd07152 91 pqgeilpsAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggvVIA----RLFEEAGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 744 PQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIqGQLAGRVLangQPVPLiaETGGQNAMIVDSSALAEQVVAD 823
Cdd:cd07152 167 PAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKV-GEAAGRHL---KKVSL--ELGGKNALIVLDDADLDLAASN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 824 VIASAFDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIE 902
Cdd:cd07152 241 GAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 903 qitlAGETGKGTFVPPTII-----EMKSladLKREVFGPVLHVIRFKRDnlDRLIDEINATGYGLTFGLHTRLDDTIQHV 977
Cdd:cd07152 320 ----AGGTYDGLFYRPTVLsgvkpGMPA---FDEEIFGPVAPVTVFDSD--EEAVALANDTEYGLSAGIISRDVGRAMAL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 739227363 978 LSRVAAGNLYVNRNIIGAVVgVQPFGGRGLSGTGPKAGGPLYLGRMTQ 1025
Cdd:cd07152 391 ADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGPANWEEFTQ 437
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
574-1011 |
1.11e-65 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 232.08 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 574 AAAPQAGGATRPVLNP--GDHndiVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLV 649
Cdd:PRK09407 24 ARVDGAAGPTREVTAPftGEP---LATVPVSTAADVEAAFARAraAQRAWAATPVRERAAVLLRFHDLVLENREELLDLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 650 MREAGKSMPNAIAEVREAIDFLRYYAAEARRNF-------------TAGE--KPLGPVVCISPWNFPLAIFIGQVTAALV 714
Cdd:PRK09407 101 QLETGKARRHAFEEVLDVALTARYYARRAPKLLaprrragalpvltKTTElrQPKGVVGVISPWNYPLTLAVSDAIPALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 715 AGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGktgaALVGSPLTAG---VMFTGSTEVARLIqGQLAGRVL 791
Cdd:PRK09407 181 AGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPG----PVVGTALVDNadyLMFTGSTATGRVL-AEQAGRRL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 792 angqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGRTDR 870
Cdd:PRK09407 256 -----IGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCiSIERIY-VHESIYDEFVRAFVAAVRAMRLGAGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 871 LSVDVGPVITAEAKGTIEKHIEDMRSLGHRIeqitLAGetGKGT------FVPPTII-----EMKSLADlkrEVFGPVLH 939
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDDAVAKGATV----LAG--GKARpdlgplFYEPTVLtgvtpDMELARE---ETFGPVVS 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227363 940 VIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQ-PFGGRGLSGTG 1011
Cdd:PRK09407 401 VYPV--ADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
586-1015 |
1.54e-65 |
|
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: 229.17 E-value: 1.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQRAASSNWPSTPvEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVR 665
Cdd:cd07146 3 VRNPYT-GEVVGTVPAGTEEALREALALAASYRSTLTR-YQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 666 EAIDFLRYYAAEARR---------NFTAGE--------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETP 728
Cdd:cd07146 81 RAADVLRFAAAEALRddgesfscdLTANGKarkiftlrEPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 729 LIAAQGVRLLHEAGVPQDAVQLLPGD-GKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRvlangqpvPLIAETGGQN 807
Cdd:cd07146 161 LSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 808 AMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTI 887
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 888 EKHIEDMRSLGHRIeqitLAGETGKGTFVPPTIIEM--KSLADLKREVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFG 965
Cdd:cd07146 313 ENRVEEAIAQGARV----LLGNQRQGALYAPTVLDHvpPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 739227363 966 LHTRLDDTIQHVLSRVAAGNLYVNrNIIGAVVGVQPFGGRGLSGTGPKAG 1015
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
585-1011 |
8.01e-65 |
|
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: 227.62 E-value: 8.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 585 PVLNPGDhNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIA 662
Cdd:cd07145 2 EVRNPAN-GEVIDTVPSLSREEVREAIEVAekAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 EVREAIDFLRYYAAEARR---------NFTAGEK--------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAE 725
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVlrgetipvdAYEYNERriaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 726 ETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIqgqlAGRVLANGQPVplIAETG 804
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEvGDEIVTNPKVNMISFTGSTAVGLLI----ASKAGGTGKKV--ALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 805 GQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAK 884
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 885 GTIEKHIEDMRSLGHRIEqitLAGETGKGTFVPPTIIEMKSL--ADLKREVFGPVLHVIRFKRDnlDRLIDEINATGYGL 962
Cdd:cd07145 315 ERMENLVNDAVEKGGKIL---YGGKRDEGSFFPPTVLENDTPdmIVMKEEVFGPVLPIAKVKDD--EEAVEIANSTEYGL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 739227363 963 TFGLHTRLDDTIQHVLSRVAAGNLYVNR-------NIigavvgvqPFGGRGLSGTG 1011
Cdd:cd07145 390 QASVFTNDINRALKVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG 437
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
586-1025 |
1.79e-63 |
|
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: 223.46 E-value: 1.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAE 663
Cdd:cd07094 3 VHNPYD-GEVIGKVPADDRADAEEALAtaRAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 664 VREAIDFLRYYAAEARRNF--------TAGEK---------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEE 726
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRgeeipldaTQGSDnrlawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 727 TPLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVLAngqpvpliAETGG 805
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREvLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIA--------LELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 806 QNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKG 885
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 886 TIEKHIEDMRSLGHRIeqitLAGETGKGTFVPPTIIEMKSLADL--KREVFGPVLHVIRFkrDNLDRLIDEINATGYGLT 963
Cdd:cd07094 314 RVERWVEEAVEAGARL----LCGGERDGALFKPTVLEDVPRDTKlsTEETFGPVVPIIRY--DDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 964 FGLHTRLDDTIQHVLSRVAAGNLYVNRNIIgAVVGVQPFGGRGLSGTGpKAGGPLYLGRMTQ 1025
Cdd:cd07094 388 AGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG-REGVPYAMEEMTE 447
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
82-193 |
5.91e-63 |
|
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: 209.28 E-value: 5.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 82 VEGLVQEYSLSSHEGVALMCLAEALLRIPDTATRDALIRDKIARGDWKSHIGGGRSLFVNAATWGLVITGKLTSTVNDSG 161
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 739227363 162 LSAALTKLIARAGEPVIRRGVDMAMRMMGEQF 193
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
552-1011 |
6.59e-63 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 223.03 E-value: 6.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 552 SSETTLAALDKVLKAG-------ASAEWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQRA--ASSNWPST 622
Cdd:PLN02278 6 SSMDAQSALVKLRNAGllrtqglIGGKWTDAY---DGKTFPVYNPAT-GEVIANVPCMGRAETNDAIASAhdAFPSWSKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 623 PVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARRnfTAGE---------------K 687
Cdd:PLN02278 82 TASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKR--VYGDiipspfpdrrllvlkQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPL 766
Cdd:PLN02278 160 PVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEiGDALLASPK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 767 TAGVMFTGSTEVARLIQGQLAGRVlangQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRC-SALRILcLQ 845
Cdd:PLN02278 240 VRKITFTGSTAVGKKLMAGAAATV----KRVSL--ELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 846 EDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGhriEQITLAGE--TGKGTFVPPTIIEM 923
Cdd:PLN02278 313 EGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKG---AKVLLGGKrhSLGGTFYEPTVLGD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 924 KSLADL--KREVFGPVLHVIRFKRDnlDRLIDEINATGYGLTFGLHTRlddTIQHVLsRVAA----GNLYVNRNIIGAVV 997
Cdd:PLN02278 390 VTEDMLifREEVFGPVAPLTRFKTE--EEAIAIANDTEAGLAAYIFTR---DLQRAW-RVSEaleyGIVGVNEGLISTEV 463
|
490
....*....|....
gi 739227363 998 GvqPFGGRGLSGTG 1011
Cdd:PLN02278 464 A--PFGGVKQSGLG 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
584-1025 |
4.33e-62 |
|
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: 219.51 E-value: 4.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 584 RPVLNPGDhNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAI 661
Cdd:cd07150 1 FDDLNPAD-GSVYARVAVGSRQDAERAIAAAydAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 662 AEVREAIDFLRYYAAEARRNF-------TAGE------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETP 728
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRgetlpsdSPGTvsmsvrRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 729 LIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIqgqlAGRVLANGQPVPLiaETGGQN 807
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEvGDELVDDPRVRMVTFTGSTAVGREI----AEKAGRHLKKITL--ELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 808 AMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTI 887
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 888 EKHIEDMRSLGHRIeqitLAGETGKGTFVPPTIiemksLADLKR-------EVFGPVLHVIRFkrDNLDRLIDEINATGY 960
Cdd:cd07150 314 KRQVEDAVAKGAKL----LTGGKYDGNFYQPTV-----LTDVTPdmrifreETFGPVTSVIPA--KDAEEALELANDTEY 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227363 961 GLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNII--GAVVgvqPFGGRGLSGTGpKAGGPLYLGRMTQ 1025
Cdd:cd07150 383 GLSAAILTNDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSMEEFTE 445
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
586-1011 |
5.63e-62 |
|
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: 219.36 E-value: 5.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKS------- 656
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAaaKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPitlartr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 657 -MPNAIAEVREAIDFLRYYAAEA------RRNFTAgEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPL 729
Cdd:cd07093 80 dIPRAAANFRFFADYILQLDGESypqdggALNYVL-RQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 730 IAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangqpVPLIAETGGQNA 808
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPeAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 809 MIVDSSALAEQVVADVIASAFDSAGQRCSA-LRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTI 887
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAgSRIL-VQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 888 EKHIEDMRSLGHRIeqitLAGET-------GKGTFVPPTIIEMKSLAD--LKREVFGPVLHVIRFKRDnlDRLIDEINAT 958
Cdd:cd07093 312 LGYVELARAEGATI----LTGGGrpelpdlEGGYFVEPTVITGLDNDSrvAQEEIFGPVVTVIPFDDE--EEAIELANDT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 739227363 959 GYGLTFGLHTRLDDTIQHVLSRVAAGNLYVN----RNIigavvgVQPFGGRGLSGTG 1011
Cdd:cd07093 386 PYGLAAYVWTRDLGRAHRVARRLEAGTVWVNcwlvRDL------RTPFGGVKASGIG 436
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
569-1024 |
2.98e-61 |
|
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: 217.84 E-value: 2.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 569 SAEWkaaapQAGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLL 646
Cdd:cd07130 4 DGEW-----GGGGGVVTSISPAN-GEPIARVRQATPEDYESTIKAAqeAFKEWRDVPAPKRGEIVRQIGDALRKKKEALG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 647 GLVMREAGKSMPNAIAEVREAIDFLRY------------YAAEaRRNFTAGEK--PLGPVVCISPWNFPLAIFIGQVTAA 712
Cdd:cd07130 78 KLVSLEMGKILPEGLGEVQEMIDICDFavglsrqlygltIPSE-RPGHRMMEQwnPLGVVGVITAFNFPVAVWGWNAAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 713 LVAGNPVLAKPAEETPL--IAAQGV--RLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAG 788
Cdd:cd07130 157 LVCGNVVVWKPSPTTPLtaIAVTKIvaRVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 789 RVlanGQpvpLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRT 868
Cdd:cd07130 237 RF---GR---SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 869 DRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEqitLAGE--TGKGTFVPPTIIEMKSLADL-KREVFGPVLHVIRFkr 945
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVL---FGGKviDGPGNYVEPTIVEGLSDAPIvKEETFAPILYVLKF-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 946 DNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNI--IGAVVGvQPFGGRGLSGTGPKAGG---PLYL 1020
Cdd:cd07130 386 DTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIgtSGAEIG-GAFGGEKETGGGRESGSdawKQYM 464
|
....
gi 739227363 1021 GRMT 1024
Cdd:cd07130 465 RRST 468
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
569-1009 |
6.47e-61 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 217.13 E-value: 6.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 569 SAEWKAAAPQAG-GATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDL 645
Cdd:PRK09457 1 MTLWINGDWIAGqGEAFESRNPVS-GEVLWQGNDATAAQVDAAVRaaRAAFPAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 646 LGLVMREAGKSMPNAIAEV-----REAIDfLRYYAAEA--RRNFTAG------EKPLGPVVCISPWNFPLAIFIGQVTAA 712
Cdd:PRK09457 80 AEVIARETGKPLWEAATEVtaminKIAIS-IQAYHERTgeKRSEMADgaavlrHRPHGVVAVFGPYNFPGHLPNGHIVPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 713 LVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGR--- 789
Cdd:PRK09457 159 LLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQpek 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 790 VLAngqpvpliAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCS-ALRILCLQEDVADRTLTMLKGALHELRIGRT 868
Cdd:PRK09457 239 ILA--------LEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 869 DrlsVD----VGPVITAEAKGTIEKHIEDMRSLGHR--IEQITLAGETGkgtFVPPTIIEMKSLADL-KREVFGPVLHVI 941
Cdd:PRK09457 311 D---AEpqpfMGAVISEQAAQGLVAAQAQLLALGGKslLEMTQLQAGTG---LLTPGIIDVTGVAELpDEEYFGPLLQVV 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227363 942 RFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAvVGVQPFGGRGLSG 1009
Cdd:PRK09457 385 RY--DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
579-1011 |
7.90e-61 |
|
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: 216.21 E-value: 7.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 579 AGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGks 656
Cdd:cd07138 11 AGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAaaRRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMG-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 657 MPN----------AIAEVREAIDFLRYYAAEARRNFTAGEK-PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAE 725
Cdd:cd07138 88 APItlaraaqvglGIGHLRAAADALKDFEFEERRGNSLVVRePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 726 ETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIqGQLAGRVLANgqpVPLiaETG 804
Cdd:cd07138 168 VAPLSAIILAEILDEAGLPAGVFNLVNGDGPVvGEALSAHPDVDMVSFTGSTRAGKRV-AEAAADTVKR---VAL--ELG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 805 GQNAMIVDSSALAEQVVADVIASAFDSAGQRCSAL-RILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEA 883
Cdd:cd07138 242 GKSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 884 ----KGTIEKHIEDmrslGHRIeqitLAGETG------KGTFVPPTIiemksLADLKR-------EVFGPVLHVIRFkrD 946
Cdd:cd07138 321 fdrvQGYIQKGIEE----GARL----VAGGPGrpegleRGYFVKPTV-----FADVTPdmtiareEIFGPVLSIIPY--D 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227363 947 NLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNrniiGAVVGVQ-PFGGRGLSGTG 1011
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
571-1015 |
2.27e-60 |
|
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: 215.15 E-value: 2.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPS--TPVEERAACLERAADAMQAEMPDLL 646
Cdd:cd07091 11 EFVDSV---SGKTFPTINPAT-EEVICQVAEADEEDVDAAVKaaRAAFETGWWrkMDPRERGRLLNKLADLIERDRDELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 647 GLVMREAGKSMP-NAIAEVREAIDFLRYYAAEARR-------------NFTAGEkPLGpvVC--ISPWNFPLAIFIGQVT 710
Cdd:cd07091 87 ALESLDNGKPLEeSAKGDVALSIKCLRYYAGWADKiqgktipidgnflAYTRRE-PIG--VCgqIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 711 AALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAgr 789
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTaGAAISSHMDVDKIAFTGSTAVGRTIMEAAA-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 790 vLANGQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTD 869
Cdd:cd07091 242 -KSNLKKVTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 870 RLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEqitLAGE--TGKGTFVPPTII-----EMKsLAdlKREVFGPVLHVIR 942
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIESGKKEGATLL---TGGErhGSKGYFIQPTVFtdvkdDMK-IA--KEEIFGPVVTILK 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227363 943 FKrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNR-NIIGAVVgvqPFGGRGLSGTGPKAG 1015
Cdd:cd07091 393 FK--TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
580-1011 |
8.37e-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: 8.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 580 GGATRPVLNPgDHNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSM 657
Cdd:cd07085 14 TTEWLDVYNP-ATGEVIARVPLATAEEVDAAVAaaKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 658 PNAIAEVR---EAIDF--------LRYYAAEARRNFTAGE--KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPA 724
Cdd:cd07085 93 ADARGDVLrglEVVEFacsiphllKGEYLENVARGIDTYSyrQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 725 EETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQgQLAG----RVLANGqpvpli 800
Cdd:cd07085 173 ERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIY-ERAAangkRVQALG------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 801 aetGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVIT 880
Cdd:cd07085 246 ---GAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVIS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 881 AEAKGTIEKHIEDMRSLGHRIE----QITLAGETgKGTFVPPTII-----EMKSladLKREVFGPVLHVIRFkrDNLDRL 951
Cdd:cd07085 323 PAAKERIEGLIESGVEEGAKLVldgrGVKVPGYE-NGNFVGPTILdnvtpDMKI---YKEEIFGPVLSIVRV--DTLDEA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227363 952 IDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIigAV-VGVQPFGGRGLSGTG 1011
Cdd:cd07085 397 IAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPI--PVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
586-1011 |
1.25e-59 |
|
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: 212.49 E-value: 1.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWP-STPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIA 662
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAaaRRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 -EVREAIDFLRYYAAEARR-----NFTAGEK------------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPA 724
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSfpwefDLPVPALrggpgrrvvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 725 EETPLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangQPVPLiaET 803
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNaVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 804 GGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSAL-RILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAE 882
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTtRLL-VPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 883 AKGTIEKHIEDMRSLGHRieqITLAGET----GKGTFVPPTIiemksLADLK-------REVFGPVLHVIRFkrDNLDRL 951
Cdd:cd07089 313 QRDRVEGYIARGRDEGAR---LVTGGGRpaglDKGFYVEPTL-----FADVDndmriaqEEIFGPVLVVIPY--DDDDEA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 952 IDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNrniiGAVVGV--QPFGGRGLSGTG 1011
Cdd:cd07089 383 VRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
571-1011 |
4.19e-59 |
|
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: 211.79 E-value: 4.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAA--SSNWPSTPVEERAACLERAADAMQAEMPDLL 646
Cdd:cd07119 5 EWVEAA---SGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAaaRRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 647 GLVMREAGKSMPNAIAEVREAIDFLRYYA----AEARRNFTAGE--------KPLGPVVCISPWNFPLAIFIGQVTAALV 714
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAglatKETGEVYDVPPhvisrtvrEPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 715 AGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGrvlaN 793
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATvGAELAESPDVDLVSFTGGTATGRSIMRAAAG----N 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 794 GQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSV 873
Cdd:cd07119 237 VKKVAL--ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 874 DVGPVITAEAKGTIEKHIEDMRSLGHRIE---QITLAGETGKGTFVPPTIIE--MKSLADLKREVFGPVLHVIRFkrDNL 948
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVcggKRPTGDELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERF--DTE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227363 949 DRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRniIGAVVGVQPFGGRGLSGTG 1011
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
581-1011 |
1.53e-58 |
|
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: 209.38 E-value: 1.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 581 GATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAA--SSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKS 656
Cdd:cd07112 1 GETFATINPAT-GRVLAEVAACDAADVDRAVAaaRRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 657 MPNAIA-EVREAIDFLRYYA----------AEARRNFTA--GEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKP 723
Cdd:cd07112 80 ISDALAvDVPSAANTFRWYAeaidkvygevAPTGPDALAliTREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 724 AEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQgQLAGRvlANGQPVPLiaE 802
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTaGEALGLHMDVDALAFTGSTEVGRRFL-EYSGQ--SNLKRVWL--E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 803 TGGQNAMIV-DSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITA 881
Cdd:cd07112 235 CGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 882 EAKGTIEKHIEDMRSLGHRIeqitLAG-----ETGKGTFVPPTII-----EMkSLAdlKREVFGPVLHVIRFkrDNLDRL 951
Cdd:cd07112 315 AHFDKVLGYIESGKAEGARL----VAGgkrvlTETGGFFVEPTVFdgvtpDM-RIA--REEIFGPVLSVITF--DSEEEA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 952 IDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVnrNIIGAVVGVQPFGGRGLSGTG 1011
Cdd:cd07112 386 VALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
586-1014 |
1.57e-58 |
|
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: 209.14 E-value: 1.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPgDHNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSM-PNAIA 662
Cdd:cd07108 1 VINP-ATGQVIGEVPRSRAADVDRAVAaaKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 EVREAIDFLRYY---AAEAR-RNFTAGE--------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLI 730
Cdd:cd07108 80 EAAVLADLFRYFgglAGELKgETLPFGPdvltytvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 731 AAQGVRLLHEAgVPQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVLangqPVPLiaETGGQNAM 809
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGeECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLI----PVSL--ELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 810 IVDSSALAEQVVADVIASA-FDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIE 888
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 889 KHIEDMRSL-GHRI---EQITLAGETGKGTFVPPTII-EMKSLADLKR-EVFGPVLHVIRFKrdNLDRLIDEINATGYGL 962
Cdd:cd07108 313 GYIDLGLSTsGATVlrgGPLPGEGPLADGFFVQPTIFsGVDNEWRLAReEIFGPVLCAIPWK--DEDEVIAMANDSHYGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 739227363 963 TFGLHTRLDDTIQHVLSRVAAGNLYVNRNiIGAVVGvQPFGGRGLSGTGPKA 1014
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
586-1015 |
3.57e-58 |
|
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: 208.06 E-value: 3.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNA-IA 662
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAaaRAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 EVREAIDFLRYYAAEARR-------------NFTAGEkPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPL 729
Cdd:cd07115 80 DVPRAADTFRYYAGWADKiegevipvrgpflNYTVRE-PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 730 IAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAGrvlaNGQPVPLiaETGGQNA 808
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEvAGAALVEHPDVDKITFTGSTAVGRKIMQGAAG----NLKRVSL--ELGGKSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 809 MIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIE 888
Cdd:cd07115 233 NIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 889 KHIEDMRSLGHRIeqitLAG---ETGKGTFVPPTIIEMKSLAD--LKREVFGPVLHVIRFKRDNLDRLIdeINATGYGLT 963
Cdd:cd07115 313 DYVDVGREEGARL----LTGgkrPGARGFFVEPTIFAAVPPEMriAQEEIFGPVVSVMRFRDEEEALRI--ANGTEYGLA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 739227363 964 FGLHTRLDDTIQHVLSRVAAGNLYVnrNIIGAVVGVQPFGGRGLSGTGPKAG 1015
Cdd:cd07115 387 AGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
571-1017 |
4.14e-58 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 208.58 E-value: 4.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSN--WPSTPVEERAACLERAADAMQAEMPDLL 646
Cdd:cd07139 6 RWVAPS---GSETIDVVSPAT-EEVVGRVPEATPADVDAAVAaaRRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 647 GLVMREAGksMPNAIAEVRE---AIDFLRYYAA--------EARRNFTAGE-----KPLGPVVCISPWNFPLAIFIGQVT 710
Cdd:cd07139 82 RLWTAENG--MPISWSRRAQgpgPAALLRYYAAlardfpfeERRPGSGGGHvlvrrEPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 711 AALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIqGQLAGRV 790
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRI-AAVCGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 791 LAngqPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSAL-RILCLQEDvADRTLTMLKGALHELRIGRTD 869
Cdd:cd07139 239 LA---RVTL--ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVPRSR-YDEVVEALAAAVAALKVGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 870 RLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIeqitLAG-----ETGKGTFVPPTIiemksLADL-------KREVFGPV 937
Cdd:cd07139 313 DPATQIGPLASARQRERVEGYIAKGRAEGARL----VTGggrpaGLDRGWFVEPTL-----FADVdndmriaQEEIFGPV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 938 LHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNrniiGAVVGVQ-PFGGRGLSGTGpKAGG 1016
Cdd:cd07139 384 LSVIPY--DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGG 456
|
.
gi 739227363 1017 P 1017
Cdd:cd07139 457 P 457
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
607-1011 |
4.91e-57 |
|
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: 203.85 E-value: 4.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 607 VEAAMQRAAS--SNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEA------ 678
Cdd:cd07100 1 IEAALDRAHAafLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAeaflad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 679 -RRNFTAGE-----KPLGPVVCISPWNFPLAifigQV----TAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAV 748
Cdd:cd07100 81 ePIETDAGKayvryEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 749 QLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIqGQLAGRVLangQPVPLiaETGGQNAMIVDSSALAEQVVADVIASA 828
Cdd:cd07100 157 QNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAV-AAEAGKNL---KKSVL--ELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 829 FDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEqitLA 907
Cdd:cd07100 231 LQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLL---LG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 908 GET--GKGTFVPPTIiemksLADLKR-------EVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVL 978
Cdd:cd07100 307 GKRpdGPGAFYPPTV-----LTDVTPgmpaydeELFGPVAAVIKVK--DEEEAIALANDSPFGLGGSVFTTDLERAERVA 379
|
410 420 430
....*....|....*....|....*....|....*.
gi 739227363 979 SRVAAGNLYVNrniigAVVGVQ---PFGGRGLSGTG 1011
Cdd:cd07100 380 RRLEAGMVFIN-----GMVKSDprlPFGGVKRSGYG 410
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
571-1017 |
1.00e-56 |
|
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: 204.55 E-value: 1.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGL 648
Cdd:cd07111 29 KWVKPE---NRKSFPTINPAT-GEVLASVLQAEEEDVDAAVAaaRTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VMREAGKsmpnAIAEVRE-----AIDFLRYYA--AEARRNFTAGEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLA 721
Cdd:cd07111 105 ESLDNGK----PIRESRDcdiplVARHFYHHAgwAQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 722 KPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGrvlaNGQPVPLia 801
Cdd:cd07111 181 KPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAG----TGKKLSL-- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 802 ETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSA-LRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVIT 880
Cdd:cd07111 255 ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAgSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 881 AEAKGTIEKHIEDMRSLGHRIEQITLAGETgKGTFVPPTIIEMKSLAD--LKREVFGPVLHVIRFKrdNLDRLIDEINAT 958
Cdd:cd07111 334 PAQLKRIRELVEEGRAEGADVFQPGADLPS-KGPFYPPTLFTNVPPASriAQEEIFGPVLVVLTFR--TAKEAVALANNT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 959 GYGLTFGLHTRLDDTIQHVLSRVAAGNLYVN-RNIIGAVVgvqPFGGRGLSGTGpKAGGP 1017
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGK 466
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
574-1011 |
2.41e-56 |
|
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: 203.44 E-value: 2.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 574 AAAPQAGGATR--PVLNPGDhNDIVGYVTEPTEADVEAAMQ---RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGL 648
Cdd:cd07113 5 DGRPVAGQSEKrlDITNPAT-EQVIASVASATEADVDAAVAsawRAFVSAWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VMREAGKS-MPNAIAEVREAIDFLRYYAAEARRnfTAGE--------------------KPLGPVVCISPWNFPLAIFIG 707
Cdd:cd07113 84 ETLCSGKSiHLSRAFEVGQSANFLRYFAGWATK--INGEtlapsipsmqgerytaftrrEPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 708 QVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLA 787
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 788 GrvlaNGQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGR 867
Cdd:cd07113 242 S----DLTRVTL--ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 868 TDRLSVDVGPVITAEAKGTIEKHIEDMRSLGhriEQITLAGET--GKGTFVPPTIIEMKSLAD--LKREVFGPVLHVIRF 943
Cdd:cd07113 316 PMDESVMFGPLANQPHFDKVCSYLDDARAEG---DEIVRGGEAlaGEGYFVQPTLVLARSADSrlMREETFGPVVSFVPY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227363 944 krDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVN-RNIIGAVVgvqPFGGRGLSGTG 1011
Cdd:cd07113 393 --EDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
571-1015 |
3.60e-55 |
|
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: 200.33 E-value: 3.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ---RAASSNWPSTPVEERAACLERAADAMQAEMPDLLG 647
Cdd:cd07144 15 EFVKSS---DGETIKTVNPST-GEVIASVYAAGEEDVDKAVKaarKAFESWWSKVTGEERGELLDKLADLVEKNRDLLAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 648 LVMREAGKSM-PNAIAEVREAIDFLRYYAAEARRNF-----TAGEK-------PLGPVVCISPWNFPLAIFIGQVTAALV 714
Cdd:cd07144 91 IEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQgktipTSPNKlaytlhePYGVCGQIIPWNYPLAMAAWKLAPALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 715 AGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGSTEVARLIQgQLAGRVLAN 793
Cdd:cd07144 171 AGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGaVAGSALAEHPDVDKIAFTGSTATGRLVM-KAAAQNLKA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 794 gqpVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSAL-RILcLQEDVADRTLTMLKGALHE-LRIGRTDRL 871
Cdd:cd07144 250 ---VTL--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATsRIY-VQESIYDKFVEKFVEHVKQnYKVGSPFDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 872 SVDVGPVITAEAKGTIEKHIEDMRSLGHRI--EQITLAGETGKGTFVPPTII-----EMKSladLKREVFGPVLHVIRFK 944
Cdd:cd07144 324 DTVVGPQVSKTQYDRVLSYIEKGKKEGAKLvyGGEKAPEGLGKGYFIPPTIFtdvpqDMRI---VKEEIFGPVVVISKFK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 945 RDnlDRLIDEINATGYGLTFGLHTRlDDTIQHVLSR-VAAGNLYVNRNIIGAvVGVqPFGGRGLSGTGPKAG 1015
Cdd:cd07144 401 TY--EEAIKKANDTTYGLAAAVFTK-DIRRAHRVAReLEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
592-1015 |
1.70e-54 |
|
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: 197.56 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 592 HNDIVGYVTEPTEADVEAAMQRAASS----NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREA 667
Cdd:cd07118 6 HGVVVARYAEGTVEDVDAAVAAARKAfdkgPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 668 IDFLRYYAAEARRnfTAGE---------------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAA 732
Cdd:cd07118 86 ADLWRYAASLART--LHGDsynnlgddmlglvlrEPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 733 QGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangQPVPLiaETGGQNAMIV 811
Cdd:cd07118 164 MLAELLIEAGLPAGVVNIVTGYGATvGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNL----KKVSL--ELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 812 DSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHI 891
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 892 EDMRSLGhriEQITLAGE---TGKGTFVPPTIIE--MKSLADLKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGL 966
Cdd:cd07118 318 DAGRAEG---ATLLLGGErlaSAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 739227363 967 HTRLDDTIQHVLSRVAAGNLYVNRNIIGAVvgVQPFGGRGLSGTGPKAG 1015
Cdd:cd07118 393 WSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
586-1011 |
3.27e-54 |
|
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: 196.80 E-value: 3.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAE 663
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRaaRRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 664 VREAIDFLRYYA--AEARRNFTAG--------------EKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEET 727
Cdd:cd07110 80 VDDVAGCFEYYAdlAEQLDAKAERavplpsedfkarvrREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 728 PLIAAQGVRLLHEAGVPQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGSTEVARLIQGQLAgrvlANGQPVPLiaETGGQ 806
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGdEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA----QDIKPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 807 NAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGT 886
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 887 IEKHIEDMRSLGHRIeqitLAG-----ETGKGTFVPPTII-EMKSLADLKR-EVFGPVLHVIRFKRDnlDRLIDEINATG 959
Cdd:cd07110 314 VLSFIARGKEEGARL----LCGgrrpaHLEKGYFIAPTVFaDVPTDSRIWReEIFGPVLCVRSFATE--DEAIALANDSE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 739227363 960 YGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNiigAVVGVQ-PFGGRGLSGTG 1011
Cdd:cd07110 388 YGLAAAVISRDAERCDRVAEALEAGIVWINCS---QPCFPQaPWGGYKRSGIG 437
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
581-1015 |
7.74e-54 |
|
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: 196.21 E-value: 7.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 581 GATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSN-WP-STPVEERAACLERAADAMQAEMPDLLGLVMREAGKS 656
Cdd:cd07143 21 GGTVKVYNPST-GKLITKIAEATEADVDIAVEvaHAAFETdWGlKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 657 MPNAIA-EVREAIDFLRYYAAEARRNF-----TAGEK-------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKP 723
Cdd:cd07143 100 FGTAKRvDVQASADTFRYYGGWADKIHgqvieTDIKKltytrhePIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 724 AEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGrvlANGQPVPLiaE 802
Cdd:cd07143 180 SELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTcGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK---SNLKKVTL--E 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 803 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAE 882
Cdd:cd07143 255 LGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 883 AKGTIEKHIEDMRSLGHRIEqitLAGET--GKGTFVPPTIIE--MKSLADLKREVFGPVLHVIRFKrdNLDRLIDEINAT 958
Cdd:cd07143 335 QYERIMSYIESGKAEGATVE---TGGKRhgNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKFK--TEEEAIKRANDS 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 739227363 959 GYGLTFGLHTRLDDTIQHVLSRVAAGNLYVN-RNIIGAVVgvqPFGGRGLSGTGPKAG 1015
Cdd:cd07143 410 TYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
598-990 |
8.06e-54 |
|
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: 195.54 E-value: 8.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 598 YVTEP--TEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRY 673
Cdd:cd07102 9 IAERPlaSLEAVRAALERAraAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 674 Y---AAEARRNFTAGEK----------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHE 740
Cdd:cd07102 89 MisiAEEALADIRVPEKdgferyirrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 741 AGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangqpVPLIAETGGQNAMIVDSSALAEQV 820
Cdd:cd07102 169 AGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRF------IKVGLELGGKDPAYVRPDADLDAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 821 VADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHR 900
Cdd:cd07102 243 AESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGAR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 901 --IEQITLAGETGKGTFVPPTII-EMK-SLADLKREVFGPVLHVIRFKRDnlDRLIDEINATGYGLTFGLHTRLDDTIQH 976
Cdd:cd07102 323 alIDGALFPEDKAGGAYLAPTVLtNVDhSMRVMREETFGPVVGIMKVKSD--AEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410
....*....|....
gi 739227363 977 VLSRVAAGNLYVNR 990
Cdd:cd07102 401 LGEQLETGTVFMNR 414
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
606-1011 |
2.37e-53 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 193.56 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 606 DVEAAMQRAASS--NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARRNFT 683
Cdd:cd07105 1 DADQAVEAAAAAfpAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 684 -------------AGEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQL 750
Cdd:cd07105 81 gsipsdkpgtlamVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 751 LPGDGKTGA----ALVGSPLTAGVMFTGSTEVARLIqGQLAGRVLangqpVPLIAETGGQNAMIVDSSALAEQVVADVIA 826
Cdd:cd07105 161 VTHSPEDAPevveALIAHPAVRKVNFTGSTRVGRII-AETAAKHL-----KPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 827 SAFDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGrtdrlSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEQIT 905
Cdd:cd07105 235 GAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 906 LAGETGKGTFVPPTIIE-MKSLADLKR-EVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRldDTIQ--HVLSRV 981
Cdd:cd07105 309 LADESPSGTSMPPTILDnVTPDMDIYSeESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR--DLARalAVAKRI 384
|
410 420 430
....*....|....*....|....*....|...
gi 739227363 982 AAGNLYVNrniiGAVVGVQ---PFGGRGLSGTG 1011
Cdd:cd07105 385 ESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
579-1015 |
3.11e-53 |
|
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: 194.25 E-value: 3.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 579 AGGATRPVLNPgDHNDIVGYVTEPTEADVEAAMQRAASS----NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAG 654
Cdd:cd07142 16 ASGKTFPTIDP-RNGEVIAHVAEGDAEDVDRAVKAARKAfdegPWPRMTGYERSRILLRFADLLEKHADELAALETWDNG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 655 KSMPNA-IAEVREAIDFLRYYAAEARRNF-------------TAGEkPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVL 720
Cdd:cd07142 95 KPYEQArYAEVPLAARLFRYYAGWADKIHgmtlpadgphhvyTLHE-PIGVVGQIIPWNFPLLMFAWKVGPALACGNTIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 721 AKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQgQLAGRvlANGQPVPL 799
Cdd:cd07142 174 LKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTaGAAIASHMDVDKVAFTGSTEVGKIIM-QLAAK--SNLKPVTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 800 iaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVI 879
Cdd:cd07142 251 --ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 880 TAEAKGTIEKHIEDMRSLGHRIeqITLAGETG-KGTFVPPTII-----EMKSLADlkrEVFGPVLHVIRFKrdNLDRLID 953
Cdd:cd07142 329 DKEQFEKILSYIEHGKEEGATL--ITGGDRIGsKGYYIQPTIFsdvkdDMKIARD---EIFGPVQSILKFK--TVDEVIK 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227363 954 EINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVN-RNIIGAVVgvqPFGGRGLSGTGPKAG 1015
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
585-1011 |
4.16e-53 |
|
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: 193.23 E-value: 4.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 585 PVLNPGDHnDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIA 662
Cdd:cd07147 2 EVTNPYTG-EVVARVALAGPDDIEEAIAAAvkAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 EVREAIDFLRYYAAEARRN---------FTAGEK--------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAE 725
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIygevlpldiSARGEGrqglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 726 ETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQlAGRvlangQPVPLiaETGG 805
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKAR-AGK-----KKVVL--ELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 806 QNAMIVDSSALAEQVVADVIASAFDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAK 884
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 885 GTIEKHIEDMRSLGHRIeqitLAGETGKGTFVPPTIIEMKSLADL--KREVFGPVLHVIRFkrDNLDRLIDEINATGYGL 962
Cdd:cd07147 312 ERVEGWVNEAVDAGAKL----LTGGKRDGALLEPTILEDVPPDMEvnCEEVFGPVVTVEPY--DDFDEALAAVNDSKFGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 739227363 963 TFGLHTRlddTIQHVLSrvAAGNLYVNRNIIGAV----VGVQPFGGRGLSGTG 1011
Cdd:cd07147 386 QAGVFTR---DLEKALR--AWDELEVGGVVINDVptfrVDHMPYGGVKDSGIG 433
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
580-1011 |
9.89e-52 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 189.74 E-value: 9.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 580 GGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSM 657
Cdd:PRK13473 15 EGEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAaaDAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 658 PNAIA-EVREAIDFLRYYAAEARR--NFTAGE-----------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKP 723
Cdd:PRK13473 94 HLALNdEIPAIVDVFRFFAGAARCleGKAAGEyleghtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 724 AEETPLIAAQGVRLLHEAgVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGrvlaNGQPVPLiaE 802
Cdd:PRK13473 174 SEITPLTALKLAELAADI-LPPGVLNVVTGRGATvGDALVGHPKVRMVSLTGSIATGKHVLSAAAD----SVKRTHL--E 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 803 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCS-ALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITA 881
Cdd:PRK13473 247 LGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTaACRIY-AQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 882 EAKGTIEKHIEDMRSLGHrIEQITlAGET--GKGTFVPPTIIemkslADLK-------REVFGPVLHVIRFkrDNLDRLI 952
Cdd:PRK13473 326 AHRDRVAGFVERAKALGH-IRVVT-GGEApdGKGYYYEPTLL-----AGARqddeivqREVFGPVVSVTPF--DDEDQAV 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 739227363 953 DEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIgaVVGVQPFGGRGLSGTG 1011
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
586-1011 |
4.71e-51 |
|
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: 187.58 E-value: 4.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAE 663
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAaaRAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 664 VREAIDFLRYYAAEARR-------------NFTAGEkPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLI 730
Cdd:cd07107 80 VMVAAALLDYFAGLVTElkgetipvggrnlHYTLRE-PYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 731 AAQGVRLLHEAgVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangQPVPLiaETGGQNAM 809
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATaGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGI----KHVTL--ELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 810 IV----DSSALAEQVVADViasAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKG 885
Cdd:cd07107 232 IVfpdaDPEAAADAAVAGM---NFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 886 TIEKHIEDMRSLGHRIeqitLAG-------ETGKGTFVPPTII-EMKSLADLKR-EVFGPVLHVIRFkrDNLDRLIDEIN 956
Cdd:cd07107 309 RVMHYIDSAKREGARL----VTGggrpegpALEGGFYVEPTVFaDVTPGMRIAReEIFGPVLSVLRW--RDEAEMVAQAN 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 739227363 957 ATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVN---RNIIGAvvgvqPFGGRGLSGTG 1011
Cdd:cd07107 383 GVEYGLTAAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
587-1011 |
4.85e-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: 187.17 E-value: 4.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 587 LNPGDhNDIVGYVTEPTEADVEAAMQRAA----SSNWPSTPvEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIA 662
Cdd:cd07120 2 IDPAT-GEVIGTYADGGVAEAEAAIAAARrafdETDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 EVREAIDFLRYYAAEARRNF-TAGE-----------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLI 730
Cdd:cd07120 80 EISGAISELRYYAGLARTEAgRMIEpepgsfslvlrEPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 731 AAQGVRLLHEA-GVPQDAVQLLPGDGKTGAA-LVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangQPVPLiaETGGQNA 808
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAhLVASPDVDVISFTGSTATGRAIMAAAAPTL----KRLGL--ELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 809 MIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIE 888
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 889 KHIEDMRSLGhriEQITLAGETG-----KGTFVPPTIIEMK--SLADLKREVFGPVLHVIRFkrDNLDRLIDEINATGYG 961
Cdd:cd07120 314 RMVERAIAAG---AEVVLRGGPVteglaKGAFLRPTLLEVDdpDADIVQEEIFGPVLTLETF--DDEAEAVALANDTDYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 739227363 962 LTFGLHTRLDDTIQHVLSRVAAGNLYVN---RNIIGAvvgvqPFGGRGLSGTG 1011
Cdd:cd07120 389 LAASVWTRDLARAMRVARAIRAGTVWINdwnKLFAEA-----EEGGYRQSGLG 436
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
586-1025 |
6.00e-51 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 187.24 E-value: 6.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDHNDIvGYVTEPTEADVEAAMQRAAS-----SNWpsTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNA 660
Cdd:cd07148 3 VVNPFDLKPI-GEVPTVDWAAIDKALDTAHAlfldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 661 IAEVREAIDFLRY------------------YAAEARRNFTAGEkPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAK 722
Cdd:cd07148 80 KVEVTRAIDGVELaadelgqlggreipmgltPASAGRIAFTTRE-PIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 723 PAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGrvlanGQPVPLiaE 802
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAP-----GTRCAL--E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 803 TGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAE 882
Cdd:cd07148 232 HGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 883 AKGTIEKHIEDMRSLGHRIeqITLAGETGKGTFVPPTIIEMKSLADLKR-EVFGPVLHVirFKRDNLDRLIDEINATGYG 961
Cdd:cd07148 312 EVDRVEEWVNEAVAAGARL--LCGGKRLSDTTYAPTVLLDPPRDAKVSTqEIFGPVVCV--YSYDDLDEAIAQANSLPVA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227363 962 LTFGLHTRLDDTIQHVLSRVAAGNLYVNRNiIGAVVGVQPFGGRGLSGTGpkAGG-PLYLGRMTQ 1025
Cdd:cd07148 388 FQAAVFTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG--TGGiPYTMHDMTQ 449
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
586-1011 |
4.90e-50 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 184.43 E-value: 4.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAE 663
Cdd:cd07090 1 VIEPAT-GEVLATVHCAGAEDVDLAVKsaKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 664 VREAIDFLRYYAAEARRnfTAGE--------------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPL 729
Cdd:cd07090 80 IDSSADCLEYYAGLAPT--LSGEhvplpggsfaytrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 730 IAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlangQPVPLiaETGGQNAM 809
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 810 IVDSSALAEQVVADVIASAFDSAGQRCS-ALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIE 888
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 889 KHIEDMRSLGHRI----EQITLAGETGKGTFVPPTII-----EMKSladLKREVFGPVLHVIRFkrDNLDRLIDEINATG 959
Cdd:cd07090 311 GYIESAKQEGAKVlcggERVVPEDGLENGFYVSPCVLtdctdDMTI---VREEIFGPVMSILPF--DTEEEVIRRANDTT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 739227363 960 YGLTFGLHTRlDDTIQH-VLSRVAAGNLYVNR-NIIGAVVgvqPFGGRGLSGTG 1011
Cdd:cd07090 386 YGLAAGVFTR-DLQRAHrVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
571-1015 |
5.02e-50 |
|
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: 185.24 E-value: 5.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAA---SSNWPSTPVEERAACLERAADAMQAEMPDL 645
Cdd:cd07141 14 EWHDSV---SGKTFPTINPAT-GEKICEVQEGDKADVDKAVKaaRAAfklGSPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 646 LGLVMREAGKS-MPNAIAEVREAIDFLRYYAAEARRN-------------FTAGEkPLGPVVCISPWNFPLAIFIGQVTA 711
Cdd:cd07141 90 ASLETLDNGKPfSKSYLVDLPGAIKVLRYYAGWADKIhgktipmdgdfftYTRHE-PVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 712 ALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQgQLAGRV 790
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTaGAAISSHPDIDKVAFTGSTEVGKLIQ-QAAGKS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 791 laNGQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDR 870
Cdd:cd07141 248 --NLKRVTL--ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 871 LSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEqiTLAGETG-KGTFVPPTII-----EMKsLAdlKREVFGPVLHVIRFK 944
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLE--CGGKRHGdKGYFIQPTVFsdvtdDMR-IA--KEEIFGPVQQIFKFK 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 945 rdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNrniIGAVVGVQ-PFGGRGLSGTGPKAG 1015
Cdd:cd07141 399 --TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
571-1011 |
4.79e-49 |
|
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: 181.73 E-value: 4.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGL 648
Cdd:cd07151 2 EWRDGT---SERTIDVLNPYT-GETLAEIPAASKEDVDEAYRAAaaAQKEWAATLPQERAEILEKAAQILEERRDEIVEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VMREAGKSMPNAIAEVREAIDFLRYYAAEARR-------NFTAGE------KPLGPVVCISPWNFPLAIFIGQVTAALVA 715
Cdd:cd07151 78 LIRESGSTRIKANIEWGAAMAITREAATFPLRmegrilpSDVPGKenrvyrEPLGVVGVISPWNFPLHLSMRSVAPALAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 716 GNPVLAKPAEETP-----LIAaqgvRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIqGQLAGR 789
Cdd:cd07151 158 GNAVVLKPASDTPitgglLLA----KIFEEAGLPKGVLNVVVGAGSeIGDAFVEHPVPRLISFTGSTPVGRHI-GELAGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 790 VLANgqpVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSAL-RILcLQEDVADRTLTMLKGALHELRIGRT 868
Cdd:cd07151 233 HLKK---VAL--ELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAInRII-VHEDVYDEFVEKFVERVKALPYGDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 869 DRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRieqiTLAGETGKGTFVPPTII-----EMkSLAdlKREVFGPVLHVIRF 943
Cdd:cd07151 307 SDPDTVVGPLINESQVDGLLDKIEQAVEEGAT----LLVGGEAEGNVLEPTVLsdvtnDM-EIA--REEIFGPVAPIIKA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227363 944 KRDnlDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVqPFGGRGLSGTG 1011
Cdd:cd07151 380 DDE--EEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
565-1011 |
6.20e-49 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 182.03 E-value: 6.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 565 KAGASAEWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEM 642
Cdd:PRK11241 12 QALINGEWLDAN---NGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAAnrALPAWRALTAKERANILRRWFNLMMEHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 643 PDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARR-------------NFTAGEKPLGPVVCISPWNFPLAIFIGQV 709
Cdd:PRK11241 88 DDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRiygdtipghqadkRLIVIKQPIGVTAAITPWNFPAAMITRKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 710 TAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGD-GKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAG 788
Cdd:PRK11241 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSaGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 789 RVlangQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRT 868
Cdd:PRK11241 248 DI----KKVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 869 DRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEQITLAGETGkGTFVPPTIIE--MKSLADLKREVFGPVLHVIRFKRD 946
Cdd:PRK11241 322 LEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG-GNFFQPTILVdvPANAKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227363 947 nlDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGvqPFGGRGLSGTG 1011
Cdd:PRK11241 401 --ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGLG 461
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
586-1011 |
1.72e-47 |
|
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: 176.75 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIA- 662
Cdd:cd07092 1 VVDPAT-GEEIATVPDASAADVDAAVAaaHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 663 EVREAIDFLRYYAAEAR--RNFTAGE-----------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPL 729
Cdd:cd07092 80 ELPGAVDNFRFFAGAARtlEGPAAGEylpghtsmirrEPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 730 IAAQGVRLLHEaGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIqGQLAGRVLANgqpvpLIAETGGQNA 808
Cdd:cd07092 160 TTLLLAELAAE-VLPPGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKV-ARAAADTLKR-----VHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 809 MIVDSSALAEQVVADVIASAFDSAGQRC-SALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTI 887
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 888 EKHIEdmRSLGH-RIEQITLAGEtGKGTFVPPTIIEMKSLAD--LKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTF 964
Cdd:cd07092 312 AGFVE--RAPAHaRVLTGGRRAE-GPGYFYEPTVVAGVAQDDeiVQEEIFGPVVTVQPF--DDEDEAIELANDVEYGLAS 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 739227363 965 GLHTRLDDTIQHVLSRVAAGNLYVNRNIIgaVVGVQPFGGRGLSGTG 1011
Cdd:cd07092 387 SVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
588-1015 |
1.75e-47 |
|
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: 177.11 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 588 NPGDHNDIvGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNA-IAEV 664
Cdd:cd07098 2 DPATGQHL-GSVPADTPEDVDEAIAAAraAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 665 REAIDFLRYYAA--------EARR-NFTAGEK-------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETP 728
Cdd:cd07098 81 LVTCEKIRWTLKhgekalrpESRPgGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 729 LIAAQGVRLLHEA----GVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQgQLAGRVLangqpVPLIAETG 804
Cdd:cd07098 161 WSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVM-AAAAESL-----TPVVLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 805 GQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAK 884
Cdd:cd07098 235 GKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 885 GTIEKHIEDMRSLGHRIeqitLAG-------ETGKGTFVPPTII-----EMKsLAdlKREVFGPVLHVIRFKRDnlDRLI 952
Cdd:cd07098 315 DRLEELVADAVEKGARL----LAGgkryphpEYPQGHYFPPTLLvdvtpDMK-IA--QEEVFGPVMVVMKASDD--EEAV 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227363 953 DEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRniIGAVVGVQ--PFGGRGLSGTGPKAG 1015
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIND--FGVNYYVQqlPFGGVKGSGFGRFAG 448
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
578-1015 |
1.94e-45 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 172.33 E-value: 1.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 578 QAGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGK 655
Cdd:PLN02315 30 RANGPLVSSVNPAN-NQPIAEVVEASLEDYEEGLRacEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 656 SMPNAIAEVREAIDFLRYYAAEARR-----------NFTAGE--KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAK 722
Cdd:PLN02315 109 ILAEGIGEVQEIIDMCDFAVGLSRQlngsiipserpNHMMMEvwNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 723 PAEETPLIAAQGVRL----LHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVlanGQpvp 798
Cdd:PLN02315 189 GAPTTPLITIAMTKLvaevLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GK--- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 799 LIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPV 878
Cdd:PLN02315 263 CLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 879 ITAEAKGTIEKHIEDMRSLGHRIeqitLAGET---GKGTFVPPTIIEMKSLADL-KREVFGPVLHVIRFKrdNLDRLIDE 954
Cdd:PLN02315 343 HTPESKKNFEKGIEIIKSQGGKI----LTGGSaieSEGNFVQPTIVEISPDADVvKEELFGPVLYVMKFK--TLEEAIEI 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227363 955 INATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNII--GAVVGvQPFGGRGLSGTGPKAG 1015
Cdd:PLN02315 417 NNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPtnGAEIG-GAFGGEKATGGGREAG 478
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
688-1011 |
5.95e-44 |
|
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: 165.78 E-value: 5.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAgVPQDAVQLLPGDGKTGAALvgspLT 767
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVATAL----LA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 768 AG---VMFTGSTEVARLIQgQLAGRVLangqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCL 844
Cdd:cd07087 175 EPfdhIFFTGSPAVGKIVM-EAAAKHL-----TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 845 QEDVADRTLTMLKGALHELrIGRTDRLSVDVGPVITaeakgtiEKHIEDMRSLghrIEQITLA--GETGKGT-FVPPTII 921
Cdd:cd07087 249 HESIKDELIEELKKAIKEF-YGEDPKESPDYGRIIN-------ERHFDRLASL---LDDGKVVigGQVDKEErYIAPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 922 EMKSLAD--LKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGV 999
Cdd:cd07087 318 DDVSPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPN 395
|
330
....*....|..
gi 739227363 1000 QPFGGRGLSGTG 1011
Cdd:cd07087 396 LPFGGVGNSGMG 407
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
594-1015 |
8.96e-44 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 167.31 E-value: 8.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 594 DIVGYVTEPTEADVEAAMQRAASS----NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMP-NAIAEVREAI 668
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAAREAfdhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 669 DFLRYYAAEARR-------------NFTAGEkPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGV 735
Cdd:PLN02766 127 GLLRYYAGAADKihgetlkmsrqlqGYTLKE-PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 736 RLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQgQLAGRvlANGQPVPLiaETGGQNAMIVDSS 814
Cdd:PLN02766 206 HLAKLAGVPDGVINVVTGFGPTaGAAIASHMDVDKVSFTGSTEVGRKIM-QAAAT--SNLKQVSL--ELGGKSPLLIFDD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 815 ALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDM 894
Cdd:PLN02766 281 ADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 895 RSLGHRIeqITLAGETG-KGTFVPPTII-----EMKSLADlkrEVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHT 968
Cdd:PLN02766 361 KREGATL--LTGGKPCGdKGYYIEPTIFtdvteDMKIAQD---EIFGPVMSLMKFK--TVEEAIKKANNTKYGLAAGIVT 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 739227363 969 RLDDTIQHVLSRVAAGNLYVNRNIigAVVGVQPFGGRGLSGTGPKAG 1015
Cdd:PLN02766 434 KDLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
579-1015 |
1.06e-43 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 167.68 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 579 AGGATRPVLNPgDHNDIVGYVTEPTEADVEAAMQRAASS----NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAG 654
Cdd:PLN02466 70 ASGKTFPTLDP-RTGEVIAHVAEGDAEDVNRAVAAARKAfdegPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 655 KSMPNAI-AEVREAIDFLRYYA------------AEARRNFTAGEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLA 721
Cdd:PLN02466 149 KPYEQSAkAELPMFARLFRYYAgwadkihgltvpADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 722 KPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQgQLAGRvlANGQPVPLi 800
Cdd:PLN02466 229 KTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTaGAALASHMDVDKLAFTGSTDTGKIVL-ELAAK--SNLKPVTL- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 801 aETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVIT 880
Cdd:PLN02466 305 -ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQID 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 881 AEAKGTIEKHIEdmrslgHRIEQ-ITLagETG------KGTFVPPTII-----EMKSLADlkrEVFGPVLHVIRFKrdNL 948
Cdd:PLN02466 384 SEQFEKILRYIK------SGVESgATL--ECGgdrfgsKGYYIQPTVFsnvqdDMLIAQD---EIFGPVQSILKFK--DL 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227363 949 DRLIDEINATGYGLTFGLHTRLDDTIqHVLSR-VAAGNLYVN-RNIIGAVVgvqPFGGRGLSGTGPKAG 1015
Cdd:PLN02466 451 DEVIRRANNTRYGLAAGVFTQNLDTA-NTLSRaLRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
571-1011 |
8.46e-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: 163.67 E-value: 8.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMpDLLGL 648
Cdd:cd07559 8 EWVAPS---KGEYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDaaHEAFKTWGKTSVAERANILNKIADRIEENL-ELLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VmreagKSMPNAIAeVRE--------AIDFLRYYAAEARrnftAGE----------------KPLGPVVCISPWNFPLAI 704
Cdd:cd07559 83 A-----ETLDNGKP-IREtlaadiplAIDHFRYFAGVIR----AQEgslseidedtlsyhfhEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 705 FIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAgVPQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGSTEVARLIq 783
Cdd:cd07559 153 AAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGsEAGKPLASHPRIAKLAFTGSTTVGRLI- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 784 GQLAGRVLangqpVPLIAETGGQNAMIVDSSALAEQ------VVADVIASAFDSaGQRCSA-LRILcLQEDVADRTLTML 856
Cdd:cd07559 231 MQYAAENL-----IPVTLELGGKSPNIFFDDAMDADddfddkAEEGQLGFAFNQ-GEVCTCpSRAL-VQESIYDEFIERA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 857 KGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRI----EQITLAGETgKGTFVPPTIIE-----MKSla 927
Cdd:cd07559 304 VERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVltggERLTLGGLD-KGYFYEPTLIKggnndMRI-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 928 dLKREVFGPVLHVIRFKRDnlDRLIDEINATGYGLTFGLHTRlDDTIQHVLSR-VAAGNLYVN-RNIIGAVVgvqPFGGR 1005
Cdd:cd07559 381 -FQEEIFGPVLAVITFKDE--EEAIAIANDTEYGLGGGVWTR-DINRALRVARgIQTGRVWVNcYHQYPAHA---PFGGY 453
|
....*.
gi 739227363 1006 GLSGTG 1011
Cdd:cd07559 454 KKSGIG 459
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
603-1011 |
1.71e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 159.52 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 603 TEADVEAAMQRAASS--NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARR 680
Cdd:PRK09406 21 TDDEVDAAIARAHARfrDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 681 nFTAGE----------------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVP 744
Cdd:PRK09406 101 -LLADEpadaaavgasrayvryQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 745 QDAVQ-LLPGDGKTGAALvGSPLTAGVMFTGSTEVARLIqGQLAGRVLAngqpvPLIAETGGQNAMIVDSSALAEQVVAD 823
Cdd:PRK09406 180 DGCFQtLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAV-AAIAGDEIK-----KTVLELGGSDPFIVMPSADLDRAAET 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 824 VIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGhriEQ 903
Cdd:PRK09406 253 AVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAG---AT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 904 ITLAGE--TGKGTFVPPTII-----EMKSLADlkrEVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQH 976
Cdd:PRK09406 330 ILCGGKrpDGPGWFYPPTVItditpDMRLYTE---EVFGPVASLYRV--ADIDEAIEIANATTFGLGSNAWTRDEAEQER 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 739227363 977 VLSRVAAGNLYVNrniiGAVVGVQ--PFGGRGLSGTG 1011
Cdd:PRK09406 405 FIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
579-1004 |
3.84e-41 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 158.89 E-value: 3.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 579 AGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKS 656
Cdd:TIGR01722 13 ASGTYIPVTNPAT-NEVTTKVAFASVDEVDAAVAsaRETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 657 MPNAIAEVREAIDFLRYYAA-------------EARRNFTAGEKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKP 723
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGvnsllkgetstqvATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 724 AEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQgqlaGRVLANGQPVPliAET 803
Cdd:TIGR01722 172 SEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIH----TTGSAHGKRVQ--ALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 804 GGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQeDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEA 883
Cdd:TIGR01722 246 GAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 884 KGTIEKHIEDMRSLGhriEQITLAGETGK------GTFVPPTIIE--MKSLADLKREVFGPVLHVIRfkRDNLDRLIDEI 955
Cdd:TIGR01722 325 KDRVASLIAGGAAEG---AEVLLDGRGYKvdgyeeGNWVGPTLLErvPPTMKAYQEEIFGPVLCVLE--ADTLEEAIALI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 739227363 956 NATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNiIGAVVGVQPFGG 1004
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVP-IPVPLPYFSFTG 447
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
610-1016 |
8.06e-41 |
|
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: 156.62 E-value: 8.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 610 AMQRAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKS--------MPNAIAEVREAIDFLRYYAAEARRN 681
Cdd:cd07134 5 AAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPaaevdlteILPVLSEINHAIKHLKKWMKPKRVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 682 ---FTAGEK------PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAgVPQDAVQLLP 752
Cdd:cd07134 85 tplLLFGTKskiryePKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 753 GDGKTGAALVGSPLTAgVMFTGSTEVARLIQgQLAGRVLAngqPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSA 832
Cdd:cd07134 164 GDAEVAQALLELPFDH-IFFTGSPAVGKIVM-AAAAKHLA---SVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 833 GQRCSALRILCLQEDVADRTLTMLKGALHElRIGRTD--RLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEQitlAGET 910
Cdd:cd07134 237 GQTCIAPDYVFVHESVKDAFVEHLKAEIEK-FYGKDAarKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEF---GGQF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 911 GKGT-FVPPTII-----EMKSLADlkrEVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAG 984
Cdd:cd07134 313 DAAQrYIAPTVLtnvtpDMKIMQE---EIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSG 387
|
410 420 430
....*....|....*....|....*....|..
gi 739227363 985 NLYVNRNIIGAVVGVQPFGGRGLSGTGpKAGG 1016
Cdd:cd07134 388 GVVVNDVVLHFLNPNLPFGGVNNSGIG-SYHG 418
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
645-990 |
1.38e-40 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 155.28 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 645 LLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARR-------------NFTAGEKPLGPVVCISPWNFPLAIFIGQVTA 711
Cdd:PRK10090 15 ISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRyegeiiqsdrpgeNILLFKRALGVTTGILPWNFPFFLIARKMAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 712 ALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKT-GAALVGSPLTAGVMFTGSTEVARLIQGQLAgrv 790
Cdd:PRK10090 95 ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETvGQELAGNPKVAMVSMTGSVSAGEKIMAAAA--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 791 lANGQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRT-D 869
Cdd:PRK10090 172 -KNITKVCL--ELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPaE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 870 RLSVDVGPVITAEAKGTIEKHIEDMRSLGHRieqITLAG--ETGKGTFVPPTIIE--MKSLADLKREVFGPVLHVIRFkr 945
Cdd:PRK10090 249 RNDIAMGPLINAAALERVEQKVARAVEEGAR---VALGGkaVEGKGYYYPPTLLLdvRQEMSIMHEETFGPVLPVVAF-- 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 739227363 946 DNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNR 990
Cdd:PRK10090 324 DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR 368
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
579-1011 |
3.43e-40 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 156.19 E-value: 3.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 579 AGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKS 656
Cdd:PRK13252 19 TSGETFEVINPAT-GEVLATVQAATPADVEAAVAsaKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 657 MPNAI-AEVREAIDFLRYYAAEA------------------RRnftageKPLGPVVCISPWNFPLAIFIGQVTAALVAGN 717
Cdd:PRK13252 98 IQETSvVDIVTGADVLEYYAGLApalegeqiplrggsfvytRR------EPLGVCAGIGAWNYPIQIACWKSAPALAAGN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 718 PVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARliqgqlagRVLAN--GQ 795
Cdd:PRK13252 172 AMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGK--------KVMAAaaAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 796 PVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCS-ALRILcLQEDVADRTLTMLKGALHELRIGRTDRLSVD 874
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 875 VGPVITAEAK----GTIEKHIEDMRSL---GHRIEQitlaGETGKGTFVPPTII-----EMKSladLKREVFGPVLHVIR 942
Cdd:PRK13252 323 FGPLVSFAHRdkvlGYIEKGKAEGARLlcgGERLTE----GGFANGAFVAPTVFtdctdDMTI---VREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 943 FkrDNLDRLIDEINATGYGLTFGLHTRlDDTIQH-VLSRVAAGNLYVNRniIGAVVGVQPFGGRGLSGTG 1011
Cdd:PRK13252 396 F--DDEDEVIARANDTEYGLAAGVFTA-DLSRAHrVIHQLEAGICWINT--WGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
571-1011 |
3.48e-40 |
|
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: 156.08 E-value: 3.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAApqaGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQaEMPDLLGL 648
Cdd:cd07117 8 EWVKGS---SGETIDSYNPAN-GETLSEITDATDADVDRAVKAAqeAFKTWRKTTVAERANILNKIADIID-ENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 649 VmreagKSMPNA--IAEVRE-----AIDFLRYYAAEARrnftAGE----------------KPLGPVVCISPWNFPLAIF 705
Cdd:cd07117 83 V-----ETLDNGkpIRETRAvdiplAADHFRYFAGVIR----AEEgsanmidedtlsivlrEPIGVVGQIIPWNFPFLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 706 IGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAgVPQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGSTEVARLIQG 784
Cdd:cd07117 154 AWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGsKSGEYLLNHPGLDKLAFTGSTEVGRDVAI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 785 QLAGRVlangqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELR 864
Cdd:cd07117 233 AAAKKL------IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 865 IGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRI----EQITLAGeTGKGTFVPPTIIEMKS----LAdlKREVFGP 936
Cdd:cd07117 307 VGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKIltggHRLTENG-LDKGFFIEPTLIVNVTndmrVA--QEEIFGP 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227363 937 VLHVIRFKRDnlDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNR-NIIGAVVgvqPFGGRGLSGTG 1011
Cdd:cd07117 384 VATVIKFKTE--DEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
579-1015 |
1.24e-38 |
|
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: 151.49 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 579 AGGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQRAAS----SNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAG 654
Cdd:cd07140 18 EGGKTYNTINPTD-GSVICKVSLATVEDVDRAVAAAKEafenGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 655 KSMPNAI-AEVREAIDFLRYYA---------------AEARRNFTAGEK-PLGPVVCISPWNFPLAIFIGQVTAALVAGN 717
Cdd:cd07140 97 AVYTLALkTHVGMSIQTFRYFAgwcdkiqgktipinqARPNRNLTLTKRePIGVCGIVIPWNYPLMMLAWKMAACLAAGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 718 PVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAgrvLANGQP 796
Cdd:cd07140 177 TVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSlVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA---VSNLKK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 797 VPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVG 876
Cdd:cd07140 254 VSL--ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 877 PvitaeakgtiEKHIEDMRSLGHRIEQITLAGET----GK-----GTFVPPTIIemKSLAD----LKREVFGPVLHVIRF 943
Cdd:cd07140 332 P----------QNHKAHLDKLVEYCERGVKEGATlvygGKqvdrpGFFFEPTVF--TDVEDhmfiAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227363 944 KRDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGvqPFGGRGLSGTGPKAG 1015
Cdd:cd07140 400 DDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLG 469
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
571-1015 |
3.58e-38 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 150.65 E-value: 3.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAAPqagGATRPVLNPGDhNDIVGYVTEPTEADVEAAMQ-------RAASSNWPSTPVEERAACLERAADAMQAEMP 643
Cdd:PLN02467 15 EWREPVL---GKRIPVVNPAT-EETIGDIPAATAEDVDAAVEaarkafkRNKGKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 644 DLLGLVMREAGKSMPNAIAEVREAIDFLRYYA--AEA--RRNFTAGE------------KPLGPVVCISPWNFPLAIFIG 707
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYAdlAEAldAKQKAPVSlpmetfkgyvlkEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 708 QVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQL 786
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTeAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 787 AGRVlangQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIG 866
Cdd:PLN02467 251 AQMV----KPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKIS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 867 RTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRIeqitLAGET-----GKGTFVPPTIIE--MKSLADLKREVFGPVLH 939
Cdd:PLN02467 325 DPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATI----LCGGKrpehlKKGFFIEPTIITdvTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 940 VIRFKRDnlDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNiigavvgvQ------PFGGRGLSGTGPK 1013
Cdd:PLN02467 401 VKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCS--------QpcfcqaPWGGIKRSGFGRE 470
|
..
gi 739227363 1014 AG 1015
Cdd:PLN02467 471 LG 472
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
563-969 |
2.86e-37 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 147.60 E-value: 2.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 563 VLKAGASAEWKAAApqaGGATRPVLNPGDHNDIVGyVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQA 640
Cdd:PLN00412 15 VYKYYADGEWRTSS---SGKSVAITNPSTRKTQYK-VQACTQEEVNKAMESAkaAQKAWAKTPLWKRAELLHKAAAILKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 641 EMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARR-----------NFTAGEK---------PLGPVVCISPWNF 700
Cdd:PLN00412 91 HKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRilgegkflvsdSFPGNERnkycltskiPLGVVLAIPPFNY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 701 PLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGsteva 779
Cdd:PLN00412 171 PVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGsEIGDFLTMHPGVNCISFTG----- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 780 rliqGQLAGRVLANGQPVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGA 859
Cdd:PLN00412 246 ----GDTGIAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 860 LHELRIGRTDRlSVDVGPVITAEAKGTIEKHIEDMRSLGHRIEQitlaGETGKGTFVPPTIIEmKSLADLK---REVFGP 936
Cdd:PLN00412 322 VAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQ----EWKREGNLIWPLLLD-NVRPDMRiawEEPFGP 395
|
410 420 430
....*....|....*....|....*....|...
gi 739227363 937 VLHVIRFKRDnlDRLIDEINATGYGLTFGLHTR 969
Cdd:PLN00412 396 VLPVIRINSV--EEGIHHCNASNFGLQGCVFTR 426
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
571-1011 |
2.95e-35 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 141.57 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 571 EWKAAAPqagGATRPVLNPGDHNDIVGyVTEPTEADVEAAMQRA----ASSNWPSTPVEERAACLERAADAMQAEMPDLL 646
Cdd:PRK09847 27 EYTAAAE---NETFETVDPVTQAPLAK-IARGKSVDIDRAVSAArgvfERGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 647 GLVMREAGKSMPNAIAE-VREAIDFLRYYAAEARRNFtaGE--------------KPLGPVVCISPWNFPLAIFIGQVTA 711
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDdIPGAARAIRWYAEAIDKVY--GEvattsshelamivrEPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 712 ALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGSTEVARliqgQL---A 787
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGK----QLlkdA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 788 GRvlANGQPVPLiaETGGQNAMIV--DSSALaEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRI 865
Cdd:PRK09847 257 GD--SNMKRVWL--EAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 866 GRTDRLSVDVGPVITAEAKGTIEKHIEDmrslGHRIEQITLAG-ETGKGTFVPPTII-EMKSLADLKR-EVFGPVLHVIR 942
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIRE----GESKGQLLLDGrNAGLAAAIGPTIFvDVDPNASLSReEIFGPVLVVTR 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 943 FKRDnlDRLIDEINATGYGLTFGLHTRlDDTIQHVLSR-VAAGNLYVNRNIIGAVvgVQPFGGRGLSGTG 1011
Cdd:PRK09847 408 FTSE--EQALQLANDSQYGLGAAVWTR-DLSRAHRMSRrLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
688-1011 |
7.92e-35 |
|
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: 138.89 E-value: 7.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAgVPQDAVQLLPGdgktGAALVGSPLT 767
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQG----GVPETTALLE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 768 AG---VMFTGSTEVARLIqGQLAGRVLangqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCL 844
Cdd:cd07135 183 QKfdkIFYTGSGRVGRII-AEAAAKHL-----TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 845 QEDVADRTLTMLKGALHELRIGRTDRLSvDVGPVITAEAKGTIEKHIEDMRSlghrieQITLAGETGKGT-FVPPTIIEM 923
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDTTKG------KVVIGGEMDEATrFIPPTIVSD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 924 KSLAD--LKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQP 1001
Cdd:cd07135 330 VSWDDslMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAP 407
|
330
....*....|
gi 739227363 1002 FGGRGLSGTG 1011
Cdd:cd07135 408 FGGVGDSGYG 417
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
688-1011 |
2.98e-34 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 138.62 E-value: 2.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAgVPQDAVQLLPGDGKTGAALVGSPLT 767
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTELLKEPFD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 768 AgVMFTGSTEVARLIQgQLAGRVLangqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQED 847
Cdd:PTZ00381 188 H-IFFTGSPRVGKLVM-QAAAENL-----TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 848 VADRTLTMLKGALHELrIGRTDRLSVDVGPVITaeakgtiEKHIEDMRSLghrIE----QITLAGETGKGT-FVPPTIIE 922
Cdd:PTZ00381 261 IKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVN-------EFHTKRLAEL---IKdhggKVVYGGEVDIENkYVAPTIIV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 923 MKSLAD--LKREVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQ 1000
Cdd:PTZ00381 330 NPDLDSplMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNL 407
|
330
....*....|.
gi 739227363 1001 PFGGRGLSGTG 1011
Cdd:PTZ00381 408 PFGGVGNSGMG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
610-1011 |
1.84e-33 |
|
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: 134.92 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 610 AMQRAASSNWPSTPVEERAACLERA-----------ADAMQAE----------MPDLLGLvmreagksmpnaIAEVREAI 668
Cdd:cd07133 5 ERQKAAFLANPPPSLEERRDRLDRLkallldnqdalAEAISADfghrsrhetlLAEILPS------------IAGIKHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 669 DFLRYYAAEARRN----FTAGE-----KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLH 739
Cdd:cd07133 73 KHLKKWMKPSRRHvgllFLPAKaeveyQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 740 EAGvPQDAVQLLPGDGKTGAALVGSPLtAGVMFTGSTEVARLIQgQLAGRVLangqpVPLIAETGGQNAMIVDSSALAEQ 819
Cdd:cd07133 153 EYF-DEDEVAVVTGGADVAAAFSSLPF-DHLLFTGSTAVGRHVM-RAAAENL-----TPVTLELGGKSPAIIAPDADLAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 820 VVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRigRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGH 899
Cdd:cd07133 225 AAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMY--PTLADNPDYTSIINERHYARLQGLLEDARAKGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 900 RIEQITLAGETGKGT-FVPPTII-----EMKSladLKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDT 973
Cdd:cd07133 303 RVIELNPAGEDFAATrKLPPTLVlnvtdDMRV---MQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAE 377
|
410 420 430
....*....|....*....|....*....|....*...
gi 739227363 974 IQHVLSRVAAGNLYVNRNIIGAVVGVQPFGGRGLSGTG 1011
Cdd:cd07133 378 QDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
599-1011 |
1.96e-32 |
|
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: 132.96 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 599 VTEPTEADVEAAMQ--RAASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAI-AEVREAIDFLRYYA 675
Cdd:cd07116 32 VPRSTAEDIELALDaaHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 676 AEAR-RNFTAGE-----------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAgV 743
Cdd:cd07116 112 GCIRaQEGSISEidentvayhfhEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-L 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 744 PQDAVQLLPGDG-KTGAALVGSPLTAGVMFTGSTEVARLIQgQLAGRVLangqpVPLIAETGGQNAMIVDSSALAEQ--- 819
Cdd:cd07116 191 PPGVVNVVNGFGlEAGKPLASSKRIAKVAFTGETTTGRLIM-QYASENI-----IPVTLELGGKSPNIFFADVMDADdaf 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 820 ---VVADVIASAFDSaGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRS 896
Cdd:cd07116 265 fdkALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 897 LGHRI----EQITLAGETGKGTFVPPTIIEMKSLADLKREVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHTRLDD 972
Cdd:cd07116 344 EGAEVltggERNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFK--DEEEALEIANDTLYGLGAGVWTRDGN 421
|
410 420 430
....*....|....*....|....*....|....*....
gi 739227363 973 TIQHVLSRVAAGNLYVnrNIIGAVVGVQPFGGRGLSGTG 1011
Cdd:cd07116 422 TAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
603-989 |
2.01e-30 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 126.51 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 603 TEADVEAAMQRAASS--NWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYA----A 676
Cdd:PRK13968 27 GADDIENALQLAAAGfrDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAehgpA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 677 EARRNFTAGE--------KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAV 748
Cdd:PRK13968 107 MLKAEPTLVEnqqavieyRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 749 QLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQlAGRVLANgqpvpLIAETGGQNAMIVDSSALAEQVVADVIASA 828
Cdd:PRK13968 187 GWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQ-AGAALKK-----CVLELGGSDPFIVLNDADLELAVKAAVAGR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 829 FDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLGHRieqITLAG 908
Cdd:PRK13968 261 YQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGAR---LLLGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 909 E--TGKGTFVPPTII-----EMKSladLKREVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRV 981
Cdd:PRK13968 338 EkiAGAGNYYAPTVLanvtpEMTA---FREELFGPVAAITVAK--DAEHALELANDSEFGLSATIFTTDETQARQMAARL 412
|
....*...
gi 739227363 982 AAGNLYVN 989
Cdd:PRK13968 413 ECGGVFIN 420
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
688-1017 |
8.44e-30 |
|
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: 124.27 E-value: 8.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAG-VPQDAVQLLPGDGKTGAALVGSPL 766
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKTMQALLLHPN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 767 TAGVMFTGSTEVARliqgqlagRVLANGQPVPLIAETGGQNAMIVDSSALAEQVVAD-VIASAFDSAGQRCSALRILCLQ 845
Cdd:cd07084 180 PKMVLFTGSSRVAE--------KLALDAKQARIYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTACSGQKCTAQSMLFVP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 846 EDVAdrtLTMLKGALHELRIGRTDRLSVdVGPVITAeakgTIEKHIEDMRSLGHRI------EQITLAGETGKGTFVPPT 919
Cdd:cd07084 252 ENWS---KTPLVEKLKALLARRKLEDLL-LGPVQTF----TTLAMIAHMENLLGSVllfsgkELKNHSIPSIYGACVASA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 920 IIEMKSLADLK-----REVFGPVLHVIRFKRDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVA-AGNLY-VNRNI 992
Cdd:cd07084 324 LFVPIDEILKTyelvtEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGRTYaILRGR 403
|
330 340
....*....|....*....|....*
gi 739227363 993 IGAVVGVQPFGGRGLSGTGPKAGGP 1017
Cdd:cd07084 404 TGVAPNQNHGGGPAADPRGAGIGGP 428
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
688-1011 |
1.22e-26 |
|
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: 114.63 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEetplIAAQGVRLLHEAgVPQ----DAVQLLPGdgktgaalvG 763
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE----VSPATAKLLAEL-IPKyldkECYPVVLG---------G 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 764 SPLTAG--------VMFTGSTEVARLIQgQLAGRVLAngqPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQR 835
Cdd:cd07132 166 VEETTEllkqrfdyIFYTGSTSVGKIVM-QAAAKHLT---PVTL--ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 836 CSALR-ILCLQEdVADRTLTMLKGALHELrIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRslghrieqITLAGETGKGT 914
Cdd:cd07132 240 CIAPDyVLCTPE-VQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGK--------VAIGGQTDEKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 915 -FVPPTIiemksLADLK-------REVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNL 986
Cdd:cd07132 310 rYIAPTV-----LTDVKpsdpvmqEEIFGPILPIVTVN--NLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGV 382
|
330 340
....*....|....*....|....*
gi 739227363 987 YVNRNIIGAVVGVQPFGGRGLSGTG 1011
Cdd:cd07132 383 CVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
623-1011 |
1.69e-26 |
|
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: 114.52 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 623 PVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNA--------IAEVREAIDFLRYYAAEARR-----NFTAGEK-- 687
Cdd:cd07136 18 DVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAymteigfvLSEINYAIKHLKKWMKPKRVktpllNFPSKSYiy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 --PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAgVPQDAVQLLPGDGKTGAALVGSP 765
Cdd:cd07136 98 yePYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELLDQK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 766 LTAgVMFTGSTEVARLIQgQLAGRVLAngqPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQ 845
Cdd:cd07136 177 FDY-IFFTGSVRVGKIVM-EAAAKHLT---PVTL--ELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 846 EDVADRTLTMLKGALHELrIGRTDRLSVDVGPVITaeakgtiEKHIEDMRSLghrIEQ--ITLAGETGKGT-FVPPTIIE 922
Cdd:cd07136 250 ESVKEKFIKELKEEIKKF-YGEDPLESPDYGRIIN-------EKHFDRLAGL---LDNgkIVFGGNTDRETlYIEPTILD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 923 MKSLAD--LKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQ 1000
Cdd:cd07136 319 NVTWDDpvMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYL 396
|
410
....*....|.
gi 739227363 1001 PFGGRGLSGTG 1011
Cdd:cd07136 397 PFGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
586-989 |
3.48e-25 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 112.15 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 586 VLNPGDHnDIVGYVTEPTEADVEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAE 663
Cdd:PLN02419 133 VINPATQ-EVVSKVPLTTNEEFKAAVSAAkqAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 664 VREAIDFLRYYAA-------EARRNFTAG------EKPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLI 730
Cdd:PLN02419 212 IFRGLEVVEHACGmatlqmgEYLPNVSNGvdtysiREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 731 AAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARliqgQLAGRVLANGQPVPliAETGGQNAMI 810
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGM----HIYARAAAKGKRIQ--SNMGAKNHGL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 811 VDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGAlHELRIGRTDRLSVDVGPVITAEAKGTIEKH 890
Cdd:PLN02419 366 VLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERA-KALKVTCGSEPDADLGPVISKQAKERICRL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 891 IEDMRSLGHRI----EQITLAGETgKGTFVPPTIIE--MKSLADLKREVFGPVLhvIRFKRDNLDRLIDEINATGYGLTF 964
Cdd:PLN02419 445 IQSGVDDGAKLlldgRDIVVPGYE-KGNFIGPTILSgvTPDMECYKEEIFGPVL--VCMQANSFDEAISIINKNKYGNGA 521
|
410 420
....*....|....*....|....*
gi 739227363 965 GLHTRLDDTIQHVLSRVAAGNLYVN 989
Cdd:PLN02419 522 AIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
648-987 |
3.83e-24 |
|
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: 107.97 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 648 LVMREAGKSMPNAIAEVREAIDFLRYYAAEA----RRNFT-----AGEK------PLGPVVCISPWNFPLAIFIGQVTAA 712
Cdd:cd07126 87 LIQRVAPKSDAQALGEVVVTRKFLENFAGDQvrflARSFNvpgdhQGQQssgyrwPYGPVAIITPFNFPLEIPALQLMGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 713 LVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPGDGKTGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRVLa 792
Cdd:cd07126 167 LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERLALELHGKVK- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 793 ngqpvpliAETGGQNAMIVDSSALAEQVVADVI-ASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALHELRigrtdRL 871
Cdd:cd07126 246 --------LEDAGFDWKILGPDVSDVDYVAWQCdQDAYACSGQKCSAQSILFAHENWVQAGILDKLKALAEQR-----KL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 872 S-VDVGPVITAEAKgTIEKHIEDMRSL-------------GHRIEQITLAGETgKGTFVP-PTIIEMKSLADLKREVFGP 936
Cdd:cd07126 313 EdLTIGPVLTWTTE-RILDHVDKLLAIpgakvlfggkpltNHSIPSIYGAYEP-TAVFVPlEEIAIEENFELVTTEVFGP 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 739227363 937 VLHVIRFKRDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLY 987
Cdd:cd07126 391 FQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
688-1011 |
1.07e-23 |
|
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: 105.57 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLhEAGVPQDAVQLLPGDGKTGAALVGSPLT 767
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEGGVPETTALLEQKWD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 768 AgVMFTGSTEVARLIQGQLAGRVlangQPVPLiaETGGQNAMIVDSSALAEQVVADVIASAFDS-AGQRCSALRILCLQE 846
Cdd:cd07137 180 K-IFFTGSPRVGRIIMAAAAKHL----TPVTL--ELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 847 DVADRTLTMLKGALHELrIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSLghriEQITLAGE-TGKGTFVPPTII---E 922
Cdd:cd07137 253 SFAPTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVA----DKIVHGGErDEKNLYIEPTILldpP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 923 MKSLAdLKREVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQPF 1002
Cdd:cd07137 328 LDSSI-MTEEIFGPLLPIITVK--KIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPF 404
|
....*....
gi 739227363 1003 GGRGLSGTG 1011
Cdd:cd07137 405 GGVGESGFG 413
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
607-973 |
1.70e-21 |
|
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: 99.15 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 607 VEAAMQRA--ASSNWPSTPVEERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYAAEARR---- 680
Cdd:cd07129 1 VDAAAAAAaaAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgswl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 681 -----------------NFTAGEKPLGPVVCISPWNFPLAIFI--GQVTAALVAGNPVLAK--PAE-ETPLIAAQGVR-L 737
Cdd:cd07129 81 daridpadpdrqplprpDLRRMLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAHpGTSELVARAIRaA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 738 LHEAGVPQDAVQLLPGDGK-TGAALVGSPLTAGVMFTGSTEVARLIQGQLAGRvlanGQPVPLIAETGGQNAMIVDSSAL 816
Cdd:cd07129 161 LRATGLPAGVFSLLQGGGReVGVALVKHPAIKAVGFTGSRRGGRALFDAAAAR----PEPIPFYAELGSVNPVFILPGAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 817 AEQvvADVIASAFD-----SAGQRCSALRILCLQEDVA-DRTLTMLKGALHElrigrtdrlsVDVGPVITAEAKGTIEKH 890
Cdd:cd07129 237 AER--GEAIAQGFVgsltlGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAA----------APAQTMLTPGIAEAYRQG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 891 IEDMRSLGHrIEQITLAGETGKGTFVPPTIIEMKS---LAD--LKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFG 965
Cdd:cd07129 305 VEALAAAPG-VRVLAGGAAAEGGNQAAPTLFKVDAaafLADpaLQEEVFGPASLVVRY--DDAAELLAVAEALEGQLTAT 381
|
....*...
gi 739227363 966 LHTRLDDT 973
Cdd:cd07129 382 IHGEEDDL 389
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
687-1011 |
1.75e-19 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 93.25 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 687 KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAqgvrlLHEAGVPQ----DAVQLLPGDGKTGAALV 762
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPKyldsKAVKVIEGGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 763 GSPLTAgVMFTGSTEVARLIQGQLAGRVlangQPVPLiaETGGQNAMIVDSSALA---EQVVADVIASAFDS-AGQRCSA 838
Cdd:PLN02203 182 QHKWDK-IFFTGSPRVGRIIMTAAAKHL----TPVAL--ELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 839 LRILCLQEDVADRTLTMLKGALHELrIGRTDRLSVDVGPVITaeakgtiEKHIEDMRSL--GHRIEQITLAGET--GKGT 914
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILN-------KKHFQRLSNLlkDPRVAASIVHGGSidEKKL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 915 FVPPTIIEMKSL--ADLKREVFGPVLHVIRFKrdNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNI 992
Cdd:PLN02203 327 FIEPTILLNPPLdsDIMTEEIFGPLLPIITVK--KIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
330
....*....|....*....
gi 739227363 993 IGAVVGVQPFGGRGLSGTG 1011
Cdd:PLN02203 405 IQYACDSLPFGGVGESGFG 423
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
687-1015 |
6.40e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 91.65 E-value: 6.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 687 KPLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLhEAGVPQDAVQLLPGDGKTGAALVGSPL 766
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 767 TAgVMFTGSTEVARLIQGQLAGRVlangqpVPLIAETGGQNAMIVDSSALAEQVVADVIASAFD-SAGQRCSALRILCLQ 845
Cdd:PLN02174 190 DK-IFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 846 EDVADRTLTMLKGALhELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRSlghrIEQITLAGETGKGTF-VPPTI---I 921
Cdd:PLN02174 263 KEYAPKVIDAMKKEL-ETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEV----SDKIVYGGEKDRENLkIAPTIlldV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 922 EMKSLAdLKREVFGPVLHVIRFkrDNLDRLIDEINATGYGLTFGLHTRLDDTIQHVLSRVAAGNLYVNRNIIGAVVGVQP 1001
Cdd:PLN02174 338 PLDSLI-MSEEIFGPLLPILTL--NNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLP 414
|
330
....*....|....
gi 739227363 1002 FGGRGLSGTGPKAG 1015
Cdd:PLN02174 415 FGGVGESGMGAYHG 428
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
29-74 |
2.96e-17 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 76.35 E-value: 2.96e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 739227363 29 LRKAITAAYRRTEEECMAPLIEAATVTAEQAKAIRETARKLIEALR 74
Cdd:pfam18327 3 LRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
688-953 |
2.48e-16 |
|
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: 83.47 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPV-VCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGV-PQDAVQLLPGDgkTGAALvgSP 765
Cdd:cd07128 143 PRRGVaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS--VGDLL--DH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 766 LTAG--VMFTGSTEVARLIQGQLAgrVLANGqpVPLIAETGGQNAMIvdssaLAEQVVADviASAFD------------S 831
Cdd:cd07128 219 LGEQdvVAFTGSAATAAKLRAHPN--IVARS--IRFNAEADSLNAAI-----LGPDATPG--TPEFDlfvkevaremtvK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 832 AGQRCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRS-----LGHRIEQITL 906
Cdd:cd07128 288 AGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAeaevvFGGPDRFEVV 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 739227363 907 AGETGKGTFVPPTII----EMKSLADLKREVFGPVLHVIRFkrDNLDRLID 953
Cdd:cd07128 368 GADAEKGAFFPPTLLlcddPDAATAVHDVEAFGPVATLMPY--DSLAEAIE 416
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
625-937 |
2.29e-13 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 74.36 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 625 EERAACLERAADAMQAEMPDLLGLVMREAGKSMPNAIAEVREAIDFLRYYA--------AEARRNFTA---GEKPL---- 689
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalgdARLLRDGEAvqlGKDPAfqgq 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 690 -------GPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGV-PQDAVQLLPGdgktGAAL 761
Cdd:PRK11903 143 hvlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCG----SSAG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 762 VGSPLTAG--VMFTGSTEVARLIQGQlaGRVLANGqpVPLIAETGGQNAMI-----VDSSALAEQVVADVIASAFDSAGQ 834
Cdd:PRK11903 219 LLDHLQPFdvVSFTGSAETAAVLRSH--PAVVQRS--VRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 835 RCSALRILCLQEDVADRTLTMLKGALHELRIGRTDRLSVDVGPVITAEAKGTIEKHIEDMRS---LGHRIEQITLAG-ET 910
Cdd:PRK11903 295 KCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAqaeVLFDGGGFALVDaDP 374
|
330 340 350
....*....|....*....|....*....|.
gi 739227363 911 GKGTFVPPTIIEMKSL--ADL--KREVFGPV 937
Cdd:PRK11903 375 AVAACVGPTLLGASDPdaATAvhDVEVFGPV 405
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
599-838 |
5.05e-06 |
|
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: 50.55 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 599 VTEP-TEADVEAAMQRAASSNWPSTPVEERAA-CLERAAdAMQAEMPDLLGLVMREAGKSM--------PNAIAEVREAI 668
Cdd:cd07127 79 VTYPqCDPDALLAAARAAMPGWRDAGARARAGvCLEILQ-RLNARSFEMAHAVMHTTGQAFmmafqaggPHAQDRGLEAV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 669 DflryYAAEA----------------------RRNFTAGEKPLGPVVCISP---WNFPLAIFigqvtAALVAGNPVLAKP 723
Cdd:cd07127 158 A----YAWREmsripptaewekpqgkhdplamEKTFTVVPRGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 724 AEETPLIAAQGVR----LLHEAGVPQDAVQLL---PGDGKTGaALVGSPLTAGVMFTGSTEVARLIQgqlagrvlANGQP 796
Cdd:cd07127 229 HPAAILPLAITVQvareVLAEAGFDPNLVTLAadtPEEPIAQ-TLATRPEVRIIDFTGSNAFGDWLE--------ANARQ 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 739227363 797 VPLIAETGGQNAMIVDSSalaEQVVADVIASAFDSA---GQRCSA 838
Cdd:cd07127 300 AQVYTEKAGVNTVVVDST---DDLKAMLRNLAFSLSlysGQMCTT 341
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
261-491 |
1.16e-05 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 49.31 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 261 SIKLSALH-PRYA--------RAQAERVMAELLPRVKSLMLLSKKYDIGLNIDAEEADRLELSLDLLEELALDKDLAGWN 331
Cdd:PLN02681 187 SFPLFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYTSLQPAIDYITYDLAREFNKGKDR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 332 GLGFV-VQAYGRRCPFVLDYIIDLARRSNRRIMVRLVKGAYWDAEIKRAQVEGLeDFPVFTRKVHTDVSYIACARKLLAA 410
Cdd:PLN02681 267 PIVYGtYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGV-PSPVHDTIQDTHACYNRCAEFLLEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 411 R-----DVIfpqFATHNAQSMATIYHLAGpdfKLGDY------EFQCLHGMGEPLYSEVV--GKRKLDrpcrfYAPVGTH 477
Cdd:PLN02681 346 AsngdgEVM---LATHNVESGELAAAKMN---ELGLHkgdprvQFAQLLGMSDNLSFGLGnaGFRVSK-----YLPYGPV 414
|
250
....*....|....
gi 739227363 478 ETLLAYLVRRLLEN 491
Cdd:PLN02681 415 EEVIPYLLRRAEEN 428
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
688-862 |
7.02e-04 |
|
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: 43.37 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIfIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEA---GVPQDAVQLLP-GDGKTGAALVG 763
Cdd:cd07077 100 PIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPhPSDELAEELLS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 764 SPLTAGVMFTGSTEVARLIQgqlagrvlANGQPVPLIAETGGQNAMIVDSSALAEQVVADVIASA-FDSAGqrCSALRIL 842
Cdd:cd07077 179 HPKIDLIVATGGRDAVDAAV--------KHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA--CASEQNL 248
|
170 180
....*....|....*....|
gi 739227363 843 CLQEDVADRTLTMLKGALHE 862
Cdd:cd07077 249 YVVDDVLDPLYEEFKLKLVV 268
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
688-1013 |
2.35e-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: 41.87 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 688 PLGPVVCISPWNFPLAIFIGQVTAALVAGNPVLAKPAEETPLIAAQGVRLLHEAGVPQDAVQLLPG-----DGKTGAALV 762
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGwidnpSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 763 GSPLTAGVMFTGSTEVARliqgqlAGRVLANgqpvPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRIL 842
Cdd:cd07081 175 KFPGIGLLLATGGPAVVK------AAYSSGK----PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 843 CLQEDVADRTLTMLKG-ALHELRIGRTDRL------SVDVGPVITAEAKGTIEKHIedmrslGHRIEQIT--LAGETGKG 913
Cdd:cd07081 245 IVVDSVYDEVMRLFEGqGAYKLTAEELQQVqpvilkNGDVNRDIVGQDAYKIAAAA------GLKVPQETriLIGEVTSL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227363 914 TFVPPTIIEMKSladlkrevfgPVLHVIRFKR--DNLDRLIDEINATGYGLTFGLHTRLDDTIQHV-------------- 977
Cdd:cd07081 319 AEHEPFAHEKLS----------PVLAMYRAANfaDADAKALALKLEGGCGHTSAMYSDNIKAIENMnqfanamktsrfvk 388
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 739227363 978 ---LSRVAAGNLYVNRNIIGAVVGVQPFGGRGLS-GTGPK 1013
Cdd:cd07081 389 ngpCSQGGLGDLYNFRGWPSMTLGCGTWGGNSVSeNVGPK 428
|
|
| |
