|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
1-1206 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1780.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1 MRFDADVPeAPGALRAAITAATRRDEADCVHALVAElqqrrARLGLDDAAVEARAAALVVDVRRRRRGAGGVDQLMHEFS 80
Cdd:PRK11905 3 QMFAPPFR-PQSALRQAITAAYRRDEAEAVQALLEA-----ATLSDEARAAIRERARKLVEALRAKRKGTGVEALLQEYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 81 LSTQEGVALMCLAEALLRIPDHATADRLIRDKIGQGDWRTHLGHSESLFVNAATWGLLISGRLVATRSERALGSALSRLL 160
Cdd:PRK11905 77 LSSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 161 ARGGEPVVRRGVDFAMRLLGQQFVLGETIGAALRRSRDSESRGYSHSFDMLGEAALTAADAERYTRAYEEAIHAIGAAAA 240
Cdd:PRK11905 157 ARLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 241 GHGPRAGPGISIKLSALHPRYCRAQRSRVRAELLPRLAALMRLARGYDIGVNIDAEEADRLELSLDLFEALVADPLLAGW 320
Cdd:PRK11905 237 GRGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 321 DGLGFVVQAYQKRAPFVIDYLVDLAHRSGRRLMIRLVKGAYWDSEIKRAQVEGQAGYPVYTRKAHTDLAYLVCAARLLAE 400
Cdd:PRK11905 317 NGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 401 AGAVYPQFATHNARTVAEVHEMAQCVGaggtlpAYEFQCLHGMGESLYDSVVGGARLGVPCRIYAPVGSHRTLLPYLVRR 480
Cdd:PRK11905 397 RDVIYPQFATHNAQTLAAIYELAGGKG------DFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 481 LLENGANSSFVNRIVDDSMPVAALAADPLQAVLAGDVTPHPSIPLPAGLYGPERRNSAGLDLASDAVLAALEAALVARAG 560
Cdd:PRK11905 471 LLENGANSSFVNRIVDENVPVEELIADPVEKVAAMGVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 561 EPRRAQPLLGSGKLDEAaarqrARPVCNPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRF 640
Cdd:PRK11905 551 KTWHAAPLLAGGDVDGG-----TRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLM 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAPL---VCISPWNFPLAIFVGQLSAALAAGR 717
Cdd:PRK11905 626 EAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLgpvVCISPWNFPLAIFTGQIAAALVAGN 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 718 CVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGaGPEPC 797
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS-GPPVP 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 798 LIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPV 877
Cdd:PRK11905 785 LIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPV 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 878 IDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIEIDGIGDVGREVFGPILHVLRFDAEGLDRLIASINAT 957
Cdd:PRK11905 865 IDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINAT 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 958 GYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLHRLLGTAQLDPAALGlvA 1037
Cdd:PRK11905 945 GYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPIPPAH--E 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1038 PAEPAAALGVLAAWARQRGDSALAARCAEDGARSLAGCHCALPGPTGEANTLRFVGRGVVLCVADSAPALLAQLAAALAT 1117
Cdd:PRK11905 1023 SVDTDAAARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVADTEEALLRQLAAALAT 1102
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1118 GNSALFEAGAAAYRVAAELPSALGGWLGVRGHGP-DPVFAVALFDGDTEAEWLLRRRLAERPGPLVAVLRADGAGRYPLH 1196
Cdd:PRK11905 1103 GNVAVVAADSGLAAALADLPGLVAARIDWTQDWEaDDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEPTDAYDLA 1182
|
1210
....*....|
gi 500091462 1197 RLVAERVVSI 1206
Cdd:PRK11905 1183 RLVEERSVSI 1192
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
14-1221 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1511.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 14 LRAAITAATRRDEADCVHALvaeLQQrrARLGLDDAAVEARAAALVVDVRRRRRGAGGVDQ----LMHEFSLSTQEGVAL 89
Cdd:PRK11809 91 LRAAITAAYRRPETEAVPML---LEQ--ARLPAPLAEAAHKLAYQLAEKLRNQKSAGGRAGmvqgLLQEFSLSSQEGVAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 90 MCLAEALLRIPDHATADRLIRDKIGQGDWRTHLGHSESLFVNAATWGLLISGRLVATRSERALGSALSRLLARGGEPVVR 169
Cdd:PRK11809 166 MCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSGEPLIR 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 170 RGVDFAMRLLGQQFVLGETIGAALRRSRDSESRGYSHSFDMLGEAALTAADAERYTRAYEEAIHAIGAAAAGHGPRAGPG 249
Cdd:PRK11809 246 KGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGIYEGPG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 250 ISIKLSALHPRYCRAQRSRVRAELLPRLAALMRLARGYDIGVNIDAEEADRLELSLDLFEALVADPLLAGWDGLGFVVQA 329
Cdd:PRK11809 326 ISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQA 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 330 YQKRAPFVIDYLVDLAHRSGRRLMIRLVKGAYWDSEIKRAQVEGQAGYPVYTRKAHTDLAYLVCAARLLAEAGAVYPQFA 409
Cdd:PRK11809 406 YQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLIYPQFA 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 410 THNARTVAEVHEMA-QCVGAGgtlpAYEFQCLHGMGESLYDSVVGGA---RLGVPCRIYAPVGSHRTLLPYLVRRLLENG 485
Cdd:PRK11809 486 THNAHTLAAIYHLAgQNYYPG----QYEFQCLHGMGEPLYEQVVGKVadgKLNRPCRIYAPVGTHETLLAYLVRRLLENG 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 486 ANSSFVNRIVDDSMPVAALAADPLQAVLA-----GDV-TPHPSIPLPAGLYGPERRNSAGLDLASDAVLAALEAALVARA 559
Cdd:PRK11809 562 ANTSFVNRIADTSLPLDELVADPVEAVEKlaqqeGQLgLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLASA 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 560 GEPRRAQPLLGsgkldEAAARQRARPVCNPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADR 639
Cdd:PRK11809 642 HQKWQAAPMLE-----DPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADL 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQV-VTLPAPTQA--APLVCISPWNFPLAIFVGQLSAALAAG 716
Cdd:PRK11809 717 MEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVrDDFDNDTHRplGPVVCISPWNFPLAIFTGQVAAALAAG 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 717 RCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAER--GAG- 793
Cdd:PRK11809 797 NSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRldPQGr 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 794 PEPcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATD 873
Cdd:PRK11809 877 PIP-LIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTD 955
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 874 IGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACE--NGSFVAPTLIEIDGIGDVGREVFGPILHVLRFDAEGLDRLI 951
Cdd:PRK11809 956 IGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDwqSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELI 1035
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 952 ASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLHRLLGTAQLDPA 1031
Cdd:PRK11809 1036 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDAL 1115
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1032 ALGLVAPAE-----------PAAALGVLAAWARQRgDSALAARCAEDGARSLAGCHCALPGPTGEANTLRFVGRGVVLCV 1100
Cdd:PRK11809 1116 AVTLARQDAeypvdaqlraaLLAPLTALREWAAER-EPELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCL 1194
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1101 ADSAPALLAQLAAALATGNSALFEAGAAAYRVAAELPSALGGWLGVRG--HGPDPVFAVALFDGDTEAEWLLRRRLAERP 1178
Cdd:PRK11809 1195 ADTEQDALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKdwQLADQPFDAVLFHGDSDQLRALCEQVAQRD 1274
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 500091462 1179 GPLVAVL-RADGAGRYPLHRLVAERVVSINTAAAGGNAALMTLG 1221
Cdd:PRK11809 1275 GPIVSVQgFARGETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
10-1034 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1443.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 10 APGALRAAITAATRRDEADCVHALVAElqqrrARLGLDDAAVEARAAALV-VDVRRRRRGAGGVDQLMHEFSLSTQEGVA 88
Cdd:PRK11904 9 SLDELRAAISALYRVDEAAYLRELLEL-----APLSPEEKARVTARATQLvEAVRAKKKKLGGIDAFLQEYSLSTEEGIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 89 LMCLAEALLRIPDHATADRLIRDKIGQGDWRTHLGHSESLFVNAATWGLLISGRLV--ATRSERALGSALSRLLARGGEP 166
Cdd:PRK11904 84 LMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVklDKKADGTPSGVLKRLVNRLGEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 167 VVRRGVDFAMRLLGQQFVLGETIGAALRRSRDSESRGYSHSFDMLGEAALTAADAERYTRAYEEAIHAIGAAAAGHGPRA 246
Cdd:PRK11904 164 VIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADLPA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 247 GPGISIKLSALHPRYCRAQRSRVRAELLPRLAALMRLARGYDIGVNIDAEEADRLELSLDLFEALVADPLLAGWDGLGFV 326
Cdd:PRK11904 244 RPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 327 VQAYQKRAPFVIDYLVDLAHRSGRRLMIRLVKGAYWDSEIKRAQVEGQAGYPVYTRKAHTDLAYLVCAARLLAEAGAVYP 406
Cdd:PRK11904 324 VQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAIYP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 407 QFATHNARTVAEVHEMAQCVGaggtlpaYEFQCLHGMGESLYDSVVggARLGVPCRIYAPVGSHRTLLPYLVRRLLENGA 486
Cdd:PRK11904 404 QFATHNAHTVAAILEMAGHRG-------FEFQRLHGMGEALYDALL--DAPGIPCRIYAPVGSHKDLLPYLVRRLLENGA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 487 NSSFVNRIVDDSMPVAALAADPLQAVLAGDVTPHPSIPLPAGLYGPERRNSAGLDLASDAVLAALEAALVARAGEPRRAQ 566
Cdd:PRK11904 475 NSSFVHRLVDPDVPIEELVADPVEKLRSFETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 567 PLLGSGKldeaaarqRARPVCNPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAA 646
Cdd:PRK11904 555 PIINGEG--------EARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAE 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 647 LVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQV-------VTLPAPTQAA---------PLVCISPWNFPLAIFVGQLS 710
Cdd:PRK11904 627 LIALCVREAGKTLQDAIAEVREAVDFCRYYAAQArrlfgapEKLPGPTGESnelrlhgrgVFVCISPWNFPLAIFLGQVA 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 711 AALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAER 790
Cdd:PRK11904 707 AALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAAR 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 791 GAGPEPcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAAL 870
Cdd:PRK11904 787 DGPIVP-LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLL 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 871 ATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIEIDGIGDVGREVFGPILHVLRFDAEGLDRL 950
Cdd:PRK11904 866 STDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKV 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 951 IASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLHRLLG--TAQL 1028
Cdd:PRK11904 946 IDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATekTVTV 1025
|
....*.
gi 500091462 1029 DPAALG 1034
Cdd:PRK11904 1026 NTTAAG 1031
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
1-1201 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1242.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1 MRFDADVPEAPGALRAAITAATRRDEADCVHALVAELQQRRARLglddaAVEARAAALVVDVRRRRRGAGGVDQLMHEFS 80
Cdd:COG4230 3 FALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAA-----AAAAAAALAARERVRARRGGGGGLLLLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 81 LSTQEGVALMCLAEALLRIPDHATADRLIRDKIGQGDWRTHLGHSESLFVNAATWGLLISGRLVATRSERALGSALSRLL 160
Cdd:COG4230 78 SLSSEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 161 ARGGEPVVRRGVDFAMRLLGQQFVLGETIGAALRRSRDSESRGYSHSFDMLGEAALTAADAERYTRAYEEAIHAIGAAAA 240
Cdd:COG4230 158 GRLGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 241 GHGPRAGPGISIKLSALHPRYCRAQRSRVRA----ELLPRLAALMRLARGYDIGVNIDAEEADRLELSLDLFEALVADPL 316
Cdd:COG4230 238 GGSGGPGPSISSSLSVLLSARHPRYRRRREErlllLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 317 LAGWDGLGFVVQAYQKRAPFVIDYLVDLAHRSGRRLMIRLVKGAYWDSEIKRAQVEGQAGYPVYTRKAHTDLAYLVCAAR 396
Cdd:COG4230 318 LGGGGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 397 LLAEAGAVYPQFATHNARTVAEVHEMAQcvgaggtLPAYEFQCLHGMGESLYDsVVGGARLGVPCRIYAPVGSHRTLLPY 476
Cdd:COG4230 398 LLAAQPAFAPQFATHAAATAAAAAAAGG-------GGEFEFQCLHGMGEYLYD-QVGRGKLGRPCRIYAPVGSHEDLLAY 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 477 LVRRLLENGANSSFVNRIVDDSMPVAALAADPLQAVLAGDVTPHPSIPLPAGLYGPERRNSAGLDLASDAVLAALEAALV 556
Cdd:COG4230 470 LVRRLLENGANSSFVNRIADEDVPVEELIADPVEKARALGGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 557 ARAGEPRRAQPLLGsgkldEAAARQRARPVCNPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAA 636
Cdd:COG4230 550 AAAEKQWQAAPLIA-----GEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERA 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 637 ADRFEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTL-PAPTQAAPL---VCISPWNFPLAIFVGQLSAA 712
Cdd:COG4230 625 ADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLfAAPTVLRGRgvfVCISPWNFPLAIFTGQVAAA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 713 LAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGA 792
Cdd:COG4230 705 LAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDG 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 793 GPEPcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALAT 872
Cdd:COG4230 785 PIVP-LIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLST 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 873 DIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIEIDGIGDVGREVFGPILHVLRFDAEGLDRLIA 952
Cdd:COG4230 864 DVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVID 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 953 SINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLHRLL--GTAQLDP 1030
Cdd:COG4230 944 AINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFAteRTVTVNT 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1031 AALGlvapaePAAALGVLAAWARQRGDsalaarcaedgarslagcHCALPGPTGEANTLRFVGRGVVLCVADSAPALLAQ 1110
Cdd:COG4230 1024 TAAG------GNASLLALGDWLASLLG------------------ALTLPGPTGERNTLTLRPRGRVLCLADSLEALLAQ 1079
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1111 LAAALATGNSALFEagaaAYRVAAELPSALggwlgvrghgpDPVFAVALFDGDTEAewlLRRRLAERPGPLVAVLRADga 1190
Cdd:COG4230 1080 LAAALATGNRAVVA----ADLALAGLPAVL-----------LPPFDAVLFEGRLRA---LRQALAARDGAIVPVIDAG-- 1139
|
1210
....*....|.
gi 500091462 1191 grYPLHRLVAE 1201
Cdd:COG4230 1140 --YDLERLLEE 1148
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
486-1022 |
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: 627.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 486 ANSSFVNRIVDDSMPVAALAADplqavlagdVTPHPSiplpaglygperrnsagldlasdavlaaleaalvaragEPRRA 565
Cdd:cd07125 1 ANSSFVNRIFDLEVPLEALADA---------LKAFDE--------------------------------------KEWEA 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 566 QPLLGSGKLDEAAARqrarPVCNPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQA 645
Cdd:cd07125 34 IPIINGEETETGEGA----PVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 646 ALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQV------VTLPAPT------QAAPL---VCISPWNFPLAIFVGQLS 710
Cdd:cd07125 110 ELIALAAAEAGKTLADADAEVREAIDFCRYYAAQArelfsdPELPGPTgelnglELHGRgvfVCISPWNFPLAIFTGQIA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 711 AALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAER 790
Cdd:cd07125 190 AALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAER 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 791 GaGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAAL 870
Cdd:cd07125 270 D-GPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 871 ATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPacENGSFVAPTLIEIDGIGDVGREVFGPILHVLRFDAEGLDRL 950
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDD--GNGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEA 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500091462 951 IASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLHRL 1022
Cdd:cd07125 427 IEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRF 498
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
529-1023 |
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: 556.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 529 LYGPERRNSAGLDLASDAVLAALEAALVARAGEPRRAQPLLGsgklDEAAARQRARPVCNPADHADIVGSVVEALPDEVE 608
Cdd:TIGR01238 2 LYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIG----HSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 609 AALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVV-TLPAPT 687
Cdd:TIGR01238 78 AAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRdVLGEFS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 688 QAA--PLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARD 765
Cdd:TIGR01238 158 VESrgVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 766 PRIGGVLFTGSTDVARGLARWLAERGAGPEPcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQR 845
Cdd:TIGR01238 238 PRIAGVAFTGSTEVAQLINQTLAQREDAPVP-LIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 846 DIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPL--PPACENGSFVAPTLIEID 923
Cdd:TIGR01238 317 DVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLddSRACQHGTFVAPTLFELD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 924 GIGDVGREVFGPILHVLRFDAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGG 1003
Cdd:TIGR01238 397 DIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGG 476
|
490 500
....*....|....*....|
gi 500091462 1004 EGLSGTGPKAGGPLYLHRLL 1023
Cdd:TIGR01238 477 QGLSGTGPKAGGPHYLYRLT 496
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
74-1039 |
4.16e-178 |
|
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: 550.80 E-value: 4.16e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 74 QLMHEFSLSTQEGVALMCLAEALLRIPDHATADRLIRDKIGqgdwrthlgHSESLFVNAATWGLLISgrlvatrseralg 153
Cdd:COG0506 34 ALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA---------KSPSFLVNASTWGLMLT------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 154 salsrLLARGGEPVVRRGVDFAMRLLGQQFVLGETIGAALRRSRDSESRGYSHSFDMLGEAALTAADAERYTRAYEEAIH 233
Cdd:COG0506 92 -----LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 234 AIGAAAAghgprAGPGISIKLSALHPRYCRAQRSRVRAELLPRLAALMRLARGYDIGVNIDAEEADRLELSLDLFEALVA 313
Cdd:COG0506 167 AIGAAGV-----DRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 314 DPLLAGWDGLGFVVQAYQKRAPFVIDYLVDLAHRSGRRLMIRLVKGAYWDSEIKRAQVEGQaGYPVYTRKAHTDLAYLVC 393
Cdd:COG0506 242 DPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 394 AARLLAEAGAVYPQFATHNARTVAEVHEMAQCVGAGGTlpAYEFQCLHGMGESLYDSV--VGGARLGVPCRIYAPVGSHR 471
Cdd:COG0506 321 ARKLLEAGDAIYPQFATHNARTIAAALALAGERGRPPD--RFEFQMLYGMGEDLQRALaaVDGGRLLLYCPVVAPVGGDA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 472 TLLPYLVRRLLENGANSSFVNRIVDDSMPVAALAADPLQAVLAGDVTPHPSIPLPAGLYGPERRNSAGLDLASDAVLAAL 551
Cdd:COG0506 399 ALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 552 EAALVaragEPRRAQPLLGSGKLDEAAARQRARPVCNPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARAD 631
Cdd:COG0506 479 ALAAA----AAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 632 ALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAPLVCISPWNFPLAIFVGQLSA 711
Cdd:COG0506 555 AAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAA 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 712 ALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARW----- 786
Cdd:COG0506 635 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATaataa 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 787 --------LAERGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDA 858
Cdd:COG0506 715 aaaaaaalAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDADLVILLLALAAAA 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 859 MGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIEIDGIGDVGREVFGPILH 938
Cdd:COG0506 795 AALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALV 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 939 VLRFDAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLY 1018
Cdd:COG0506 875 LALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGT 954
|
970 980
....*....|....*....|.
gi 500091462 1019 LHRLLGTAQLDPAALGLVAPA 1039
Cdd:COG0506 955 LALAAAAAAATALAAAAAAAA 975
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
192-493 |
4.98e-142 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 431.53 E-value: 4.98e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 192 ALRRSRDSESRGYSHSFDMLGEAALTAADAERYTRAYEEAIHAIGAAAAGHGPRAGPGISIKLSALHPRYCRAQRSRVRA 271
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 272 ELLPRLAALMRLARGYDIGVNIDAEEADRLELSLDLFEALVADPLLAGWDGLGFVVQAYQKRAPFVIDYLVDLAHRSGRR 351
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 352 LMIRLVKGAYWDSEIKRAQvEGQAGYPVYTRKAHTDLAYLVCAARLLAEAGAVYPQFATHNARTVAEVHEMAQcvGAGGT 431
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAE--ELGIP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500091462 432 LPAYEFQCLHGMGESLYDSVVGgarLGVPCRIYAPVGSHRTLLPYLVRRLLENGANSSFVNR 493
Cdd:pfam01619 238 PRRFEFQQLYGMGDNLSFALVA---AGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
560-1023 |
7.85e-118 |
|
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: 375.38 E-value: 7.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 560 GEPRRAQPLLGSGKLDEAAARQRarpVCNPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADR 639
Cdd:cd07083 13 EEFGRAYPLVIGGEWVDTKERMV---SVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAP----------------LVCISPWNFPLA 703
Cdd:cd07083 90 LRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVpypgednesfyvglgaGVVISPWNFPVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 704 IFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGL 783
Cdd:cd07083 170 IFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 784 ARWLAER--GAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGE 861
Cdd:cd07083 250 YEAAARLapGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAER 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 862 LRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPAceNGSFVAPTLIEID--GIGDVGREVFGPILHV 939
Cdd:cd07083 330 LSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEG--EGYFVAPTVVEEVppKARIAQEEIFGPVLSV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 940 LRFDAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1019
Cdd:cd07083 408 IRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYL 487
|
....
gi 500091462 1020 HRLL 1023
Cdd:cd07083 488 RRFL 491
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
647-1019 |
6.17e-105 |
|
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: 341.12 E-value: 6.17e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 647 LVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTL-PAPTQAAPL-------------VCISPWNFPLAIFVGQLSAA 712
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLrGFPVEMVPGednryvyrplgvgAVISPWNFPLAILAGMTTAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 713 LAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVarGLARW-----L 787
Cdd:cd07124 191 LVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREV--GLRIYeraakV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 788 AERGAGPEPClIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDP 867
Cdd:cd07124 269 QPGQKWLKRV-IAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 868 AALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIE-IDGIGDVGR-EVFGPILHVLRFDae 945
Cdd:cd07124 348 EDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFAdVPPDHRLAQeEIFGPVLAVIKAK-- 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500091462 946 GLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1019
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYL 499
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
641-1015 |
1.61e-96 |
|
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: 317.07 E-value: 1.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAPL---------------VCISPWNFPLAIF 705
Cdd:COG1012 79 EERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDApgtrayvrreplgvvGAITPWNFPLALA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 WLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIG 865
Cdd:COG1012 239 AAAENLKR----VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 DPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIEidgigDVGR-------EVFGPILH 938
Cdd:COG1012 315 DPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLA-----DVTPdmriareEIFGPVLS 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500091462 939 VLRFDaeGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1015
Cdd:COG1012 390 VIPFD--DEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
640-1020 |
7.57e-92 |
|
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: 303.30 E-value: 7.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQV-----VTLPAP------TQAAPL---VCISPWNFPLAIF 705
Cdd:pfam00171 64 LEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLArrldgETLPSDpgrlayTRREPLgvvGAITPWNFPLLLP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:pfam00171 144 AWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 WLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIG 865
Cdd:pfam00171 224 AAAQNLKR----VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 DPAALATDIGPVIDNAARDALEAHVARMQAAGRgvfRVPL--PPACENGSFVAPTLIEidgigDVGR-------EVFGPI 936
Cdd:pfam00171 300 DPLDPDTDMGPLISKAQLERVLKYVEDAKEEGA---KLLTggEAGLDNGYFVEPTVLA-----NVTPdmriaqeEIFGPV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 937 LHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVqPFGGEGLSGTGpKAGGP 1016
Cdd:pfam00171 372 LSVIRFKDE--EEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGP 447
|
....
gi 500091462 1017 LYLH 1020
Cdd:pfam00171 448 YGLE 451
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
641-1021 |
3.78e-91 |
|
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: 300.66 E-value: 3.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAPL---------------VCISPWNFPLAIF 705
Cdd:cd07078 34 EERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDpgelaivrreplgvvGAITPWNFPLLLA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:cd07078 114 AWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 WLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIG 865
Cdd:cd07078 194 AAAENLKR----VTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 DPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIEIDGIGD--VGREVFGPILHVLRFD 943
Cdd:cd07078 270 NPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTVLTDVDPDMpiAQEEIFGPVLPVIPFK 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500091462 944 AEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGvQPFGGEGLSGTGpKAGGPLYLHR 1021
Cdd:cd07078 350 DE--EEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEE 423
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
649-1019 |
4.24e-87 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 292.22 E-value: 4.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 649 SVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAPL---------------VCISPWNFPLAIFVGQLSAAL 713
Cdd:PRK03137 117 AWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVESRpgehnryfyiplgvgVVISPWNFPFAIMAGMTLAAI 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 714 AAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVarGLArwLAERGAG 793
Cdd:PRK03137 197 VAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREV--GLR--IYERAAK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 794 PEPC------LIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDP 867
Cdd:PRK03137 273 VQPGqiwlkrVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 868 AAlATDIGPVIDNAARDALEAHVARMQAAGRGVfrvpLPPACEN--GSFVAPTLieidgIGDVGR-------EVFGPILH 938
Cdd:PRK03137 353 ED-NAYMGPVINQASFDKIMSYIEIGKEEGRLV----LGGEGDDskGYFIQPTI-----FADVDPkarimqeEIFGPVVA 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 939 VLR---FDaEGLDrlIAsiNATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGG 1015
Cdd:PRK03137 423 FIKakdFD-HALE--IA--NNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGG 497
|
....
gi 500091462 1016 PLYL 1019
Cdd:PRK03137 498 PDYL 501
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
588-1019 |
4.90e-84 |
|
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: 283.68 E-value: 4.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 588 NPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVR 667
Cdd:TIGR01237 52 NPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 668 EAVDFCRYYAQQVVTLPA-----------------PTQAAplVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLT 730
Cdd:TIGR01237 132 EAIDFMEYYARQMIELAKgkpvnsregetnqyvytPTGVT--VVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 731 AALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVarGLArwLAERGAGPEPC------LIAETGG 804
Cdd:TIGR01237 210 AAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREV--GTR--IFERAAKVQPGqkhlkrVIAEMGG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 805 QNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARD 884
Cdd:TIGR01237 286 KDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFN 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 885 ALEAHVARMQAAGRGVFrvplpPACENGS---FVAPTLieidgIGDVGR-------EVFGPILHVLRfdAEGLDRLIASI 954
Cdd:TIGR01237 366 KIMEYIEIGKAEGRLVS-----GGCGDDSkgyFIGPTI-----FADVDRkarlaqeEIFGPVVAFIR--ASDFDEALEIA 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500091462 955 NATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1019
Cdd:TIGR01237 434 NNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYL 498
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
641-1023 |
2.57e-70 |
|
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: 240.21 E-value: 2.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAPL-------------VC--ISPWNFPLAIF 705
Cdd:cd06534 30 EERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDpggeayvrreplgVVgvITPWNFPLLLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:cd06534 110 AWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 WLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKdamgelrig 865
Cdd:cd06534 190 AAAENLKP----VTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIYDEFVEKLV--------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 dpaalatdigPVIDNAARDALEAHVarmqaagrgvfrvplppacengsfvaptlieidgigdvgrEVFGPILHVLRFDAE 945
Cdd:cd06534 257 ----------TVLVDVDPDMPIAQE----------------------------------------EIFGPVLPVIRFKDE 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500091462 946 glDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGvQPFGGEGLSGTGpKAGGPLYLHRLL 1023
Cdd:cd06534 287 --EEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGGVKNSGIG-REGGPYGLEEYT 360
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
645-1014 |
6.04e-68 |
|
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: 237.08 E-value: 6.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 645 AALVSvlvREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPT------------QAAPL---VCISPWNFPLAIFVGQL 709
Cdd:cd07086 78 GRLVS---LEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTipserpghrlmeQWNPLgvvGVITAFNFPVAVPGWNA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 710 SAALAAGRCVLAKPALATPLTAALAVELMHAA----GIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:cd07086 155 AIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 WLAERGAGPepclIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIG 865
Cdd:cd07086 234 TVARRFGRV----LLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 DPAALATDIGPVIDNAARDALEAHVARMQAAGRGV-FRVPLPPACENGSFVAPTLIEIDGIGD--VGREVFGPILHVLRF 942
Cdd:cd07086 310 DPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVlTGGKRIDGGEPGNYVEPTIVTGVTDDAriVQEETFAPILYVIKF 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500091462 943 DaeGLDRLIASINATGYGLTGGLHSRIDETVERVV--AGLRVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAG 1014
Cdd:cd07086 390 D--SLEEAIAINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
644-1010 |
4.24e-63 |
|
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: 222.31 E-value: 4.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 644 QAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVV-----TLPAPTQAA----------PLVCISPWNFPLAIFVGQ 708
Cdd:cd07103 58 AEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARriygrTIPSPAPGKrilvikqpvgVVAAITPWNFPAAMITRK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 709 LSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLA 788
Cdd:cd07103 138 IAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 789 E---RgagpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRC-SALRVLcVQRDIAEPLLTMLKDAMGELRI 864
Cdd:cd07103 218 DtvkR-------VSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCvCANRIY-VHESIYDEFVEKLVERVKKLKV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 865 GDPAALATDIGPVIDNAARDALEAHVARMQAAG----RGVFRVPLPpacenGSFVAPTLieidgIGDVGR-------EVF 933
Cdd:cd07103 290 GNGLDEGTDMGPLINERAVEKVEALVEDAVAKGakvlTGGKRLGLG-----GYFYEPTV-----LTDVTDdmlimneETF 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500091462 934 GPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1010
Cdd:cd07103 360 GPVAPIIPFDTE--DEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
583-1016 |
3.13e-62 |
|
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: 220.58 E-value: 3.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 583 ARPVCNPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNA 662
Cdd:cd07097 15 GEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 663 VAEVREAVDFCRYYAQQVVTLPAPTQAA------------PL---VCISPWNFPLAIFVGQLSAALAAGRCVLAKPALAT 727
Cdd:cd07097 95 RGEVTRAGQIFRYYAGEALRLSGETLPStrpgvevettrePLgvvGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 728 PLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGAGpepcLIAETGGQNA 807
Cdd:cd07097 175 PASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR----VQLEMGGKNP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 808 MIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALE 887
Cdd:cd07097 251 LVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 888 AHVARMQAAGRGVF----RVPLPpacENGSFVAPTLieIDGIGDVGR----EVFGPILHVLRfdAEGLDRLIASINATGY 959
Cdd:cd07097 331 RYIEIARSEGAKLVyggeRLKRP---DEGYYLAPAL--FAGVTNDMRiareEIFGPVAAVIR--VRDYDEALAIANDTEF 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500091462 960 GLTGGLHSR----IDETVERVVAGLrvgnLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1016
Cdd:cd07097 404 GLSAGIVTTslkhATHFKRRVEAGV----VMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
588-1029 |
6.91e-62 |
|
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: 219.53 E-value: 6.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 588 NPADHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVR 667
Cdd:cd07131 20 NPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 668 EAVDFCRYYAQQVVTLPAPTQAAPLV---------------CISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAA 732
Cdd:cd07131 100 EAIDMAQYAAGEGRRLFGETVPSELPnkdamtrrqpigvvaLITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 733 LAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGAgpEPCLiaETGGQNAMIVDS 812
Cdd:cd07131 180 KLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK--RVAL--EMGGKNPIIVMD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 813 SALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVAR 892
Cdd:cd07131 256 DADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 893 MQAAGRGVFRVPLPP---ACENGSFVAPTLIEIDGIGD-VGR-EVFGPILHVLRFDaeGLDRLIASINATGYGLTGGLHS 967
Cdd:cd07131 336 GKEEGATLLLGGERLtggGYEKGYFVEPTVFTDVTPDMrIAQeEIFGPVVALIEVS--SLEEAIEIANDTEYGLSSAIYT 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500091462 968 RIDETVERVVAGLRVGNLYVNRNMVGAVVGVqPFGGEGLSGTGpkaggplylHRLLGTAQLD 1029
Cdd:cd07131 414 EDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNG---------HREAGTTALD 465
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
74-183 |
3.54e-61 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 203.89 E-value: 3.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 74 QLMHEFSLSTQEGVALMCLAEALLRIPDHATADRLIRDKIGQGDWRTHLGHSESLFVNAATWGLLISGRLVATRSERALG 153
Cdd:pfam14850 3 ALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGTLA 82
|
90 100 110
....*....|....*....|....*....|
gi 500091462 154 SALSRLLARGGEPVVRRGVDFAMRLLGQQF 183
Cdd:pfam14850 83 GALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
691-1008 |
5.17e-59 |
|
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: 209.82 E-value: 5.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 691 PLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGG 770
Cdd:cd07095 100 VMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETGEALAAHEGIDG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 771 VLFTGSTDVARGLARWLAERgagPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCS-ALRVLCVQRDIAE 849
Cdd:cd07095 179 LLFTGSAATGLLLHRQFAGR---PGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTcARRLIVPDGAVGD 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 850 PLLTMLKDAMGELRIGDP-AALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPAceNGSFVAPTLIEIDGIGDV 928
Cdd:cd07095 256 AFLERLVEAAKRLRIGAPdAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVA--GTAFLSPGIIDVTDAADV 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 929 -GREVFGPILHVLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAvVGVQPFGGEGLS 1007
Cdd:cd07095 334 pDEEIFGPLLQVYRYDD--FDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA-SSTAPFGGVGLS 410
|
.
gi 500091462 1008 G 1008
Cdd:cd07095 411 G 411
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
694-1010 |
5.74e-59 |
|
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: 210.50 E-value: 5.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 694 CISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLF 773
Cdd:cd07093 123 LITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISF 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 774 TGSTDVARGLARWLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLT 853
Cdd:cd07093 203 TGETATGRTIMRAAAPNLKP----VSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 854 MLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAG----RGVFRVPLPPaCENGSFVAPTLIEidGIGD-- 927
Cdd:cd07093 279 RFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGatilTGGGRPELPD-LEGGYFVEPTVIT--GLDNds 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 928 --VGREVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVvgVQPFGGEG 1005
Cdd:cd07093 356 rvAQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDL--RTPFGGVK 431
|
....*
gi 500091462 1006 LSGTG 1010
Cdd:cd07093 432 ASGIG 436
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
641-989 |
6.15e-57 |
|
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: 204.81 E-value: 6.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQ-------VVTLPAPTQAAPL--------VCISPWNFPLAIF 705
Cdd:cd07088 71 RENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWarriegeIIPSDRPNENIFIfkvpigvvAGILPWNFPFFLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:cd07088 151 ARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIME 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 WLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIG 865
Cdd:cd07088 231 AAAENITK----VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 DPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIE-IDGIGD-VGREVFGPILHVLRFD 943
Cdd:cd07088 307 DPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTnVRQDMEiVQEEIFGPVLPVVKFS 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 500091462 944 AegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNR 989
Cdd:cd07088 387 S--LDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
640-1014 |
1.32e-56 |
|
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: 203.55 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYA-----QQVVTLP-------APTQAAPL-VC--ISPWNFPLAI 704
Cdd:cd07114 56 IEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAgladkIEGAVIPvdkgdylNFTRREPLgVVaaITPWNSPLLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLA 784
Cdd:cd07114 136 LAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 RWLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRI 864
Cdd:cd07114 216 RAAAENLAP----VTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 865 GDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVF---RVPLPPACENGSFVAPTLIEIDGIGD--VGREVFGPILHV 939
Cdd:cd07114 292 GDPLDPETQMGPLATERQLEKVERYVARAREEGARVLtggERPSGADLGAGYFFEPTILADVTNDMriAQEEVFGPVLSV 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500091462 940 LRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1014
Cdd:cd07114 372 IPFDDE--EEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWV--NTYRALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
668-1021 |
4.17e-56 |
|
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: 203.97 E-value: 4.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 668 EAVDFCR---YYAQQVVTLPAPTQAA---------PL----VCISPWNFPlAIfVGQLSAALA-AGRCVLAKPALATPLT 730
Cdd:cd07123 134 ELIDFLRfnvKYAEELYAQQPLSSPAgvwnrleyrPLegfvYAVSPFNFT-AI-GGNLAGAPAlMGNVVLWKPSDTAVLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 731 AALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGAGPE--PCLIAETGGQNAM 808
Cdd:cd07123 212 NYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRtyPRIVGETGGKNFH 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 809 IVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEA 888
Cdd:cd07123 292 LVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 889 HVARMQAAgrGVFRVPLPPACEN--GSFVAPTLIEIDGIGDV--GREVFGPILHVLRFDAEGLDRLIASINATG-YGLTG 963
Cdd:cd07123 372 YIDHAKSD--PEAEIIAGGKCDDsvGYFVEPTVIETTDPKHKlmTEEIFGPVLTVYVYPDSDFEETLELVDTTSpYALTG 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 964 GLHSRIDETVERVVAGLR--VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLHR 1021
Cdd:cd07123 450 AIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLR 509
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
640-1010 |
6.18e-55 |
|
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: 198.59 E-value: 6.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPA---PTQAAP----------------LVCISPWNF 700
Cdd:cd07149 56 LEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKRLAGetiPFDASPggegrigftirepigvVAAITPFNF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 701 PLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVA 780
Cdd:cd07149 136 PLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 781 RGLArwlaeRGAGPEPcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRC-SALRVLcVQRDIAEPLLTMLKDAM 859
Cdd:cd07149 216 EAIA-----RKAGLKK-VTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAAT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 860 GELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRgvfRVPLPPACEnGSFVAPTLIEidgigDVGR-------EV 932
Cdd:cd07149 289 KKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEAVEGGA---RLLTGGKRD-GAILEPTVLT-----DVPPdmkvvceEV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 933 FGPILHVLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN-----RnmvgavVGVQPFGGEGLS 1007
Cdd:cd07149 360 FAPVVSLNPFDT--LDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdsstfR------VDHMPYGGVKES 431
|
...
gi 500091462 1008 GTG 1010
Cdd:cd07149 432 GTG 434
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
641-1014 |
1.20e-54 |
|
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: 197.58 E-value: 1.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQ---------------------VVTLPAPTQAapLVCISPWN 699
Cdd:cd07146 54 EARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEalrddgesfscdltangkarkIFTLREPLGV--VLAITPFN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 700 FPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDV 779
Cdd:cd07146 132 HPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 780 ARGLARWLAERGagpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAM 859
Cdd:cd07146 212 GKAIAATAGYKR------QLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 860 GELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVfrvpLPPACENGSFVAPTLIE-IDGIGD-VGREVFGPIL 937
Cdd:cd07146 286 AALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARV----LLGNQRQGALYAPTVLDhVPPDAElVTEETFGPVA 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500091462 938 HVLRFdaEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNrNMVGAVVGVQPFGGEGLSGTGPKAG 1014
Cdd:cd07146 362 PVIRV--KDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
641-1010 |
2.81e-54 |
|
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: 196.80 E-value: 2.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQV-----VTLP-----------APTQAAPL---VCISPWNFP 701
Cdd:cd07145 57 ERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAkvlrgETIPvdayeynerriAFTVREPIgvvGAITPFNFP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 702 LAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVAR 781
Cdd:cd07145 137 ANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 782 GLARwlaeRGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGE 861
Cdd:cd07145 217 LIAS----KAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 862 LRIGDPAALATDIGPVIDNAARDALEAHVARMQAAG----RGVFRVPlppacenGSFVAPTLIEIDGIGDV--GREVFGP 935
Cdd:cd07145 293 LKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKGgkilYGGKRDE-------GSFFPPTVLENDTPDMIvmKEEVFGP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 936 ILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNR-------NMvgavvgvqPFGGEGLSG 1008
Cdd:cd07145 366 VLPIAKVKDD--EEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDstrfrwdNL--------PFGGFKKSG 435
|
..
gi 500091462 1009 TG 1010
Cdd:cd07145 436 IG 437
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
647-1010 |
2.75e-53 |
|
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: 193.99 E-value: 2.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 647 LVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQV-----VTLP------APTQAAPL---VCISPWNFPLAIFVGQLSAA 712
Cdd:cd07109 62 LARLESLDTGKPLTQARADVEAAARYFEYYGGAAdklhgETIPlgpgyfVYTVREPHgvtGHIIPWNYPLQITGRSVAPA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 713 LAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGA 792
Cdd:cd07109 142 LAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 793 gpePCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGdPAALAT 872
Cdd:cd07109 222 ---PVTL-ELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 873 DIGPVIDNAARDALEAHVARmqAAGRGVFRV----PLPPACENGSFVAPTLieidgIGDVGR-------EVFGPILHVLR 941
Cdd:cd07109 297 DLGPLISAKQLDRVEGFVAR--ARARGARIVaggrIAEGAPAGGYFVAPTL-----LDDVPPdsrlaqeEIFGPVLAVMP 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 942 FDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRnmVGAVVGVQ-PFGGEGLSGTG 1010
Cdd:cd07109 370 FDDE--AEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
645-1015 |
1.30e-52 |
|
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: 192.42 E-value: 1.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 645 AALVSVlvrEAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPT------------QAAPL---VCISPWNFPLAIFVGQL 709
Cdd:cd07130 77 GKLVSL---EMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTipserpghrmmeQWNPLgvvGVITAFNFPVAVWGWNA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 710 SAALAAGRCVLAKPALATPLTA----ALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:cd07130 154 AIALVCGNVVVWKPSPTTPLTAiavtKIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 WLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIG 865
Cdd:cd07130 233 AVAARFGR----SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIG 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 DPAALATDIGPVIDNAARDALEAHVARMQAAGRGVF----RVPLPpacenGSFVAPTLIEIDG-IGDVGREVFGPILHVL 940
Cdd:cd07130 309 DPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLfggkVIDGP-----GNYVEPTIVEGLSdAPIVKEETFAPILYVL 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500091462 941 RFDaeGLDRLIASINATGYGLTGGLHSRIDETVERVV--AGLRVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1015
Cdd:cd07130 384 KFD--TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLgpKGSDCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
654-1010 |
5.89e-52 |
|
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: 190.12 E-value: 5.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 654 EAGKTWGNAVA-EVREAVDFCRYYAQQVVTL-----PAPTQAAPLV---------CISPWNFPLAIFVGQLSAALAAGRC 718
Cdd:cd07112 75 DMGKPISDALAvDVPSAANTFRWYAEAIDKVygevaPTGPDALALItreplgvvgAVVPWNFPLLMAAWKIAPALAAGNS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 719 VLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGAGPepcL 798
Cdd:cd07112 155 VVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKR---V 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 799 IAETGGQNAMIV-DSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPV 877
Cdd:cd07112 232 WLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 878 IDNAARDALEAHVARMQAAGRGVF----RVplpPACENGSFVAPTLieIDGIGDVGR----EVFGPILHVLRFDAEglDR 949
Cdd:cd07112 312 VSEAHFDKVLGYIESGKAEGARLVaggkRV---LTETGGFFVEPTV--FDGVTPDMRiareEIFGPVLSVITFDSE--EE 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500091462 950 LIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1010
Cdd:cd07112 385 AVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
640-1010 |
1.73e-51 |
|
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: 188.61 E-value: 1.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKT--------WGNAVAEVREAVDFCRYYAQQVvTLPAPTQAAPL-------------VCISPW 698
Cdd:cd07089 55 LEARKEELRALLVAEVGAPvmtaramqVDGPIGHLRYFADLADSFPWEF-DLPVPALRGGPgrrvvrrepvgvvAAITPW 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 699 NFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTD 778
Cdd:cd07089 134 NFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 779 VARglaRWLAERGAGPEPCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDA 858
Cdd:cd07089 214 VGR---RIMAQAAATLKRVLL-ELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 859 MGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAG-RGVFRVPLPPACENGSFVAPTLieidgIGDVG-------R 930
Cdd:cd07089 290 FEALPVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEGaRLVTGGGRPAGLDKGFYVEPTL-----FADVDndmriaqE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 931 EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1010
Cdd:cd07089 365 EIFGPVLVVIPYDDD--DEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDA--PFGGYKQSGLG 440
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
627-1016 |
7.17e-51 |
|
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: 186.20 E-value: 7.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 627 AARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQ-----QVVTLPAPTQA-------APL-- 692
Cdd:cd07104 22 QERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGlprrpEGEILPSDVPGkesmvrrVPLgv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 693 --VcISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAV-ELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIG 769
Cdd:cd07104 102 vgV-ISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 770 GVLFTGSTDVARGLARwLAERGAGPePCLiaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRC-SALRVLcVQRDIA 848
Cdd:cd07104 181 MISFTGSTAVGRHIGE-LAGRHLKK-VAL--ELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICmAAGRIL-VHESVY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 849 EPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVfrvpLPPACENGSFVAPTLieidgIGDV 928
Cdd:cd07104 256 DEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL----LTGGTYEGLFYQPTV-----LSDV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 929 GR-------EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMV--GAVVgvq 999
Cdd:cd07104 327 TPdmpifreEIFGPVAPVIPFDDD--EEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVndEPHV--- 401
|
410
....*....|....*..
gi 500091462 1000 PFGGEGLSGTGpKAGGP 1016
Cdd:cd07104 402 PFGGVKASGGG-RFGGP 417
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
640-1010 |
1.77e-50 |
|
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: 186.24 E-value: 1.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPT----------------QAAPL---VCISPWNF 700
Cdd:cd07082 74 LKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSlpgdwfpgtkgkiaqvRREPLgvvLAIGPFNY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 701 PLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVA 780
Cdd:cd07082 154 PLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 781 RGLARwlaergAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMG 860
Cdd:cd07082 234 NRLKK------QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 861 ELRIGDPAALATDIGPVIDNAARDALE-------AHVARMQAAGRGvfrvplppacENGSFVAPTLIEidgigDVG---- 929
Cdd:cd07082 308 KLKVGMPWDNGVDITPLIDPKSADFVEgliddavAKGATVLNGGGR----------EGGNLIYPTLLD-----PVTpdmr 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 930 ---REVFGPILHVLRFdaEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRnMVGAVVGVQPFGGEGL 1006
Cdd:cd07082 373 lawEEPFGPVLPIIRV--NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-KCQRGPDHFPFLGRKD 449
|
....
gi 500091462 1007 SGTG 1010
Cdd:cd07082 450 SGIG 453
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
697-1008 |
1.83e-50 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 186.70 E-value: 1.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 697 PWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGS 776
Cdd:PRK09457 143 PYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 777 TDVARGLARWLAERgagPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDI-AEPLLTML 855
Cdd:PRK09457 222 ANTGYLLHRQFAGQ---PEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 856 KDAMGELRIGDP-AALATDIGPVIDNAARDALEAHVARMQAAGrGVFRVPLPPACENGSFVAPTLIEIDGIGDV-GREVF 933
Cdd:PRK09457 299 VAVAKRLTVGRWdAEPQPFMGAVISEQAAQGLVAAQAQLLALG-GKSLLEMTQLQAGTGLLTPGIIDVTGVAELpDEEYF 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500091462 934 GPILHVLRFDaeGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAvVGVQPFGGEGLSG 1008
Cdd:PRK09457 378 GPLLQVVRYD--DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
588-1010 |
2.61e-50 |
|
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: 185.12 E-value: 2.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 588 NPADHADiVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVR 667
Cdd:cd07099 2 NPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 668 EAVDFCRYYAQQVVTL----------PAPTQAA-------PLV-CISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPL 729
Cdd:cd07099 81 LALEAIDWAARNAPRVlaprkvptglLMPNKKAtveyrpyGVVgVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 730 TAALAVELMHAAGIPRAALQLLPGrGGSVGQTLArDPRIGGVLFTGSTDVARGLARWLAERgagPEPCLIaETGGQNAMI 809
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTG-DGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAER---LIPVVL-ELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 810 VDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAH 889
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 890 VARMQAAGrGVFRVPLPPACENGSFVAPT-LIEIDGIGDVGR-EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHS 967
Cdd:cd07099 315 VDDAVAKG-AKALTGGARSNGGGPFYEPTvLTDVPHDMDVMReETFGPVLPVMPVADE--DEAIALANDSRYGLSASVFS 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 500091462 968 RIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1010
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
640-1014 |
3.56e-50 |
|
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: 185.49 E-value: 3.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKT-WGNAVAEVREAVDFCRYYAQ-----QVVTLP------APTQAAPL-VC--ISPWNFPLAI 704
Cdd:cd07091 78 IERDRDELAALESLDNGKPlEESAKGDVALSIKCLRYYAGwadkiQGKTIPidgnflAYTRREPIgVCgqIIPWNFPLLM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLA 784
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 RWLAERGAGPepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRI 864
Cdd:cd07091 238 EAAAKSNLKK---VTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 865 GDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVF----RVPlppacENGSFVAPTLieidgIGDVG-------REVF 933
Cdd:cd07091 315 GDPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLtggeRHG-----SKGYFIQPTV-----FTDVKddmkiakEEIF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 934 GPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNR-NMVGAVVgvqPFGGEGLSGTGPK 1012
Cdd:cd07091 385 GPVVTILKFKTE--DEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRE 459
|
..
gi 500091462 1013 AG 1014
Cdd:cd07091 460 LG 461
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
652-1010 |
4.88e-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: 4.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 652 VREAGKTWGNAVAEVREAVDFCRYYAQ-------QVVTLP----APTQAAPL---VCISPWNFPLAIFVGQLSAALAAGR 717
Cdd:cd07090 66 TIDNGKPIEEARVDIDSSADCLEYYAGlaptlsgEHVPLPggsfAYTRREPLgvcAGIGAWNYPIQIASWKSAPALACGN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 718 CVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGStdVARGLaRWLAERGAGPEPC 797
Cdd:cd07090 146 AMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGS--VPTGK-KVMSAAAKGIKHV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 798 LIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCS-ALRVLcVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGP 876
Cdd:cd07090 222 TL-ELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 877 VIDNAARDALEAHVARMQAAG----RGVFRVPLPPACENGSFVAPTLieIDGIGD----VGREVFGPILHVLRFDAEglD 948
Cdd:cd07090 300 LISEEHLEKVLGYIESAKQEGakvlCGGERVVPEDGLENGFYVSPCV--LTDCTDdmtiVREEIFGPVMSILPFDTE--E 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500091462 949 RLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1010
Cdd:cd07090 376 EVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
641-1029 |
6.15e-50 |
|
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: 184.82 E-value: 6.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQ-------QVVTLPAPTQAAPL-----VC--ISPWNFPLAIFV 706
Cdd:cd07119 73 REDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGlatketgEVYDVPPHVISRTVrepvgVCglITPWNYPLLQAA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 707 GQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARw 786
Cdd:cd07119 153 WKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMR- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 787 laeRGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGD 866
Cdd:cd07119 232 ---AAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGN 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 867 PAALATDIGPVIDNAARDALEAHVARMQAAGRGVF---RVPLPPACENGSFVAPTLIEidgigDVGR-------EVFGPI 936
Cdd:cd07119 309 GLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVcggKRPTGDELAKGYFVEPTIFD-----DVDRtmrivqeEIFGPV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 937 LHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGvqPFGGEGLSGTGpkaggp 1016
Cdd:cd07119 384 LTVERFDTE--EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEA--PWGGYKQSGIG------ 453
|
410
....*....|...
gi 500091462 1017 lylhRLLGTAQLD 1029
Cdd:cd07119 454 ----RELGPTGLE 462
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
694-1010 |
8.02e-50 |
|
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: 184.24 E-value: 8.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 694 CISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLF 773
Cdd:cd07138 136 LITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSF 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 774 TGSTDVARGLARWLAERGAgpEPCLiaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLT 853
Cdd:cd07138 216 TGSTRAGKRVAEAAADTVK--RVAL--ELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 854 MLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHV-------ARMQAAGRGvfrvpLPPACENGSFVAPTLieidgIG 926
Cdd:cd07138 292 IAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIqkgieegARLVAGGPG-----RPEGLERGYFVKPTV-----FA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 927 DVGR-------EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRnmvGAVVGVQ 999
Cdd:cd07138 362 DVTPdmtiareEIFGPVLSIIPYDDE--DEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING---AAFNPGA 436
|
330
....*....|.
gi 500091462 1000 PFGGEGLSGTG 1010
Cdd:cd07138 437 PFGGYKQSGNG 447
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
641-1010 |
1.16e-49 |
|
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: 183.32 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQ----------VVTLPAPTQAAPLV--------CISPWNFPL 702
Cdd:cd07110 55 RERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLaeqldakaerAVPLPSEDFKARVRrepvgvvgLITPWNFPL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 703 AIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARG 782
Cdd:cd07110 135 LMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 783 LARWLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGEL 862
Cdd:cd07110 215 VMQAAAQDIKP----VSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 863 RIGDPAALATDIGPVIDNAARDALEAHVARMQAAG-RGVFRVPLPPACENGSFVAPTLieidgIGDVG-------REVFG 934
Cdd:cd07110 291 RVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGaRLLCGGRRPAHLEKGYFIAPTV-----FADVPtdsriwrEEIFG 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500091462 935 PILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1010
Cdd:cd07110 366 PVLCVRSFATE--DEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
640-1020 |
6.59e-49 |
|
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: 180.99 E-value: 6.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDF-------CRYYAQQVVTLPAPTQAA-----PL---VCISPWNFPLAI 704
Cdd:cd07150 56 MERRADDLIDLLIDEGGSTYGKAWFETTFTPELlraaageCRRVRGETLPSDSPGTVSmsvrrPLgvvAGITPFNYPLIL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGla 784
Cdd:cd07150 136 ATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGRE-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 rwLAERGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRI 864
Cdd:cd07150 214 --IAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 865 GDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVfrvpLPPACENGSFVAPTLieidgIGDVGR-------EVFGPIL 937
Cdd:cd07150 292 GDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKL----LTGGKYDGNFYQPTV-----LTDVTPdmrifreETFGPVT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 938 HVLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMV--GAVVgvqPFGGEGLSGTGpKAGG 1015
Cdd:cd07150 363 SVIPAKD--AEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGG 436
|
....*
gi 500091462 1016 PLYLH 1020
Cdd:cd07150 437 EWSME 441
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
641-1030 |
9.58e-49 |
|
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: 180.71 E-value: 9.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAV-AEVREAVDFCRYYAQ-------QVVTLPAP----TQAAPL---VCISPWNFPLAIF 705
Cdd:cd07115 55 LANADELARLESLDTGKPIRAARrLDVPRAADTFRYYAGwadkiegEVIPVRGPflnyTVREPVgvvGAIVPWNFPLMFA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:cd07115 135 AWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 wlaeRGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIG 865
Cdd:cd07115 215 ----GAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 DPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPAcENGSFVAPTLIEIDGIGD-VGR-EVFGPILHVLRFD 943
Cdd:cd07115 291 DPLDPKTQMGPLVSQAQFDRVLDYVDVGREEGARLLTGGKRPG-ARGFFVEPTIFAAVPPEMrIAQeEIFGPVVSVMRFR 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 944 AEGLDRLIAsiNATGYGLTGGLHSRIDETVERVVAGLRVGNLYVnrNMVGAVVGVQPFGGEGLSGTGpkaggplylhRLL 1023
Cdd:cd07115 370 DEEEALRIA--NGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFG----------REM 435
|
....*..
gi 500091462 1024 GTAQLDP 1030
Cdd:cd07115 436 GREALDE 442
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
695-1023 |
2.09e-48 |
|
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: 180.28 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFT 774
Cdd:cd07111 154 IVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFT 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVARGLARWLAerGAGPEPCLiaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTM 854
Cdd:cd07111 233 GSTEVGRALRRATA--GTGKKLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRK 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 855 LKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACEnGSFVAPTLIEidGIGDVGR---- 930
Cdd:cd07111 309 LKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSK-GPFYPPTLFT--NVPPASRiaqe 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 931 EVFGPILHVLRFdaEGLDRLIASINATGYGLTGGLHS-RIDETVErVVAGLRVGNLYVN-RNMVGAVVgvqPFGGEGLSG 1008
Cdd:cd07111 386 EIFGPVLVVLTF--RTAKEAVALANNTPYGLAASVWSeNLSLALE-VALSLKAGVVWINgHNLFDAAA---GFGGYRESG 459
|
330
....*....|....*
gi 500091462 1009 TGpKAGGPLYLHRLL 1023
Cdd:cd07111 460 FG-REGGKEGLYEYL 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
640-1029 |
5.12e-47 |
|
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: 175.61 E-value: 5.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTL------PAPTQAAPLV--------CISPWNFPLAIF 705
Cdd:cd07120 55 FEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEagrmiePEPGSFSLVLrepmgvagIIVPWNSPVVLL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAA-GIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLA 784
Cdd:cd07120 135 VRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIM 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 RWLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRI 864
Cdd:cd07120 215 AAAAPTLKR----LGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 865 GDPAALATDIGPVIDNAARDALEAHVAR-MQAAGRGVFR-VPLPPACENGSFVAPTLIEIDGIGD--VGREVFGPILHVL 940
Cdd:cd07120 291 GPGLDPASDMGPLIDRANVDRVDRMVERaIAAGAEVVLRgGPVTEGLAKGAFLRPTLLEVDDPDAdiVQEEIFGPVLTLE 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 941 RFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMvgAVVGVQPFGGEGLSGTGpkaggplylh 1020
Cdd:cd07120 371 TFDDE--AEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWN--KLFAEAEEGGYRQSGLG---------- 436
|
....*....
gi 500091462 1021 RLLGTAQLD 1029
Cdd:cd07120 437 RLHGVAALE 445
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
640-1010 |
6.24e-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: 175.21 E-value: 6.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVA-EVREAVDFCRYYAQQVVTLPAPTQAA------------PL-VC--ISPWNFPLA 703
Cdd:cd07092 54 IEENAEELAALESRNTGKPLHLVRDdELPGAVDNFRFFAGAARTLEGPAAGEylpghtsmirrePIgVVaqIAPWNYPLM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 704 IFVGQLSAALAAGRCVLAKPALATPLTAALAVELMhAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTD----V 779
Cdd:cd07092 134 MAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRtgkkV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 780 ARGLARWLAErgagpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRC-SALRVLcVQRDIAEPLLTMLKDA 858
Cdd:cd07092 213 ARAAADTLKR--------VHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 859 MGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPAceNGSFVAPTLieIDGIGD----VGREVFG 934
Cdd:cd07092 284 VSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHARVLTGGRRAEG--PGYFYEPTV--VAGVAQddeiVQEEIFG 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500091462 935 PILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1010
Cdd:cd07092 360 PVVTVQPFDDE--DEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
641-1023 |
1.37e-46 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 175.26 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVV-----TLPAPTQAAPL--------VC--ISPWNFPLAIF 705
Cdd:PLN02278 98 IANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKrvygdIIPSPFPDRRLlvlkqpvgVVgaITPWNFPLAMI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLAr 785
Cdd:PLN02278 178 TRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLM- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 wlaeRGAGPEPCLIA-ETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRC-SALRVLcVQRDIAEPLLTMLKDAMGELR 863
Cdd:PLN02278 257 ----AGAAATVKRVSlELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 864 IGDPAALATDIGPVIDNAARDALEAHVARMQAAGrGVFRVPLPPACENGSFVAPTLieidgIGDVGR-------EVFGPI 936
Cdd:PLN02278 332 VGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKG-AKVLLGGKRHSLGGTFYEPTV-----LGDVTEdmlifreEVFGPV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 937 LHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGvqPFGGEGLSGTGpKAGGP 1016
Cdd:PLN02278 406 APLTRFKTE--EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG-REGSK 480
|
....*..
gi 500091462 1017 LYLHRLL 1023
Cdd:PLN02278 481 YGIDEYL 487
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
642-1014 |
1.91e-46 |
|
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: 173.65 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 642 AQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAPLV-----------------CISPWNFPLAI 704
Cdd:cd07101 55 ERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERLLKPRRRRGAIpvltrttvnrrpkgvvgVISPWNYPLTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARdpRIGGVLFTGSTDVARGLA 784
Cdd:cd07101 135 AVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 RWLAERgagpepcLI---AETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGE 861
Cdd:cd07101 213 ERAGRR-------LIgcsLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 862 LRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVF-----RVPLPPAcengsFVAPTLIEidgigDV-------G 929
Cdd:cd07101 286 LRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLaggraRPDLGPY-----FYEPTVLT-----GVtedmelfA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 930 REVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQ-PFGGEGLSG 1008
Cdd:cd07101 356 EETFGPVVSIYRVADD--DEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSG 433
|
....*.
gi 500091462 1009 TGPKAG 1014
Cdd:cd07101 434 LGRRHG 439
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
641-1014 |
2.28e-46 |
|
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: 173.68 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPT------QAAPLVC---------ISPWNFPLAIF 705
Cdd:cd07118 57 RARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSynnlgdDMLGLVLrepigvvgiITPWNFPFLIL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLAR 785
Cdd:cd07118 137 SQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 wlaeRGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIG 865
Cdd:cd07118 217 ----AAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 866 DPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLieidgIGDVGR-------EVFGPILH 938
Cdd:cd07118 293 DPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTI-----FTDVTPdmaiareEIFGPVLS 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500091462 939 VLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVvgVQPFGGEGLSGTGPKAG 1014
Cdd:cd07118 368 VLTFDT--VDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
585-1010 |
6.13e-45 |
|
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: 169.35 E-value: 6.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 585 PVCNPADHaDIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVA 664
Cdd:cd07147 2 EVTNPYTG-EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 665 EVREAVDFCRYYAQQVV-----TLPAPTQAA--------------PLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPAL 725
Cdd:cd07147 81 EVARAIDTFRIAAEEATriygeVLPLDISARgegrqglvrrfpigPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 726 ATPLTAALAVELMHAAGIPRAALQLLPGRGgSVGQTLARDPRIGGVLFTGSTDVArglarWLAERGAGPEPCLIaETGGQ 805
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSR-DDADLLVTDERIKLLSFTGSPAVG-----WDLKARAGKKKVVL-ELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 806 NAMIVDSSALLEQVVQDVLVSAFDSAGQRC-SALRVLcVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARD 884
Cdd:cd07147 234 AAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 885 ALEAHVARMQAAGRGVfrvpLPPACENGSFVAPTLIEIDGIGD--VGREVFGPILHVLRFDaeGLDRLIASINATGYGLT 962
Cdd:cd07147 313 RVEGWVNEAVDAGAKL----LTGGKRDGALLEPTILEDVPPDMevNCEEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQ 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 500091462 963 GGLHSRIDETVERVVAGLRVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1010
Cdd:cd07147 387 AGVFTRDLEKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSGIG 433
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
586-1010 |
1.78e-44 |
|
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: 167.71 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 586 VCNPAdHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAE 665
Cdd:cd07106 1 VINPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 666 VREAVDFCRYYAQ-----QVVTLPAP----TQAAPL-VC--ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAAL 733
Cdd:cd07106 80 VGGAVAWLRYTASldlpdEVIEDDDTrrveLRRKPLgVVaaIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 734 AVELMHAAgIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAE---RgagpepcLIAETGGQNAMIV 810
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKtlkR-------VTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 811 DSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHV 890
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 891 ARMQAAGrgvFRVPL--PPACENGSFVAPTLieIDGIGD----VGREVFGPILHVLRFDaeGLDRLIASINATGYGLTGG 964
Cdd:cd07106 311 EDAKAKG---AKVLAggEPLDGPGYFIPPTI--VDDPPEgsriVDEEQFGPVLPVLKYS--DEDEVIARANDSEYGLGAS 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 500091462 965 LHSRIDETVERVVAGLRVGNLYVNRNmvGAVVGVQPFGGEGLSGTG 1010
Cdd:cd07106 384 VWSSDLERAEAVARRLEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
586-1010 |
6.78e-44 |
|
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: 166.45 E-value: 6.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 586 VCNPADhADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAE 665
Cdd:cd07094 3 VHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 666 VREAVDFCRYYAQQV-----VTLPAPTQAA--------------PLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALA 726
Cdd:cd07094 82 VDRAIDTLRLAAEEAerirgEEIPLDATQGsdnrlawtirepvgVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 727 TPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVArglarWLAERGAGPEPCLIaETGGQN 806
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVG-----EALRANAGGKRIAL-ELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 807 AMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDAL 886
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 887 EAHVARmqAAGRGVFRVplppaCEN---GSFVAPTLIEIDGIGDVGR--EVFGPILHVLRFDAEglDRLIASINATGYGL 961
Cdd:cd07094 316 ERWVEE--AVEAGARLL-----CGGerdGALFKPTVLEDVPRDTKLSteETFGPVVPIIRYDDF--EEAIRIANSTDYGL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 500091462 962 TGGLHSRIDETVERVVAGLRVGNLYVNRNMVgAVVGVQPFGGEGLSGTG 1010
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
594-1016 |
3.13e-43 |
|
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: 164.00 E-value: 3.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 594 DIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVREAVDFC 673
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 674 RyYAQQVVTLPA----PTQAAPLVC-----------ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAV-EL 737
Cdd:cd07152 82 H-EAAGLPTQPQgeilPSAPGRLSLarrvplgvvgvISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 738 MHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGSTDVARGLArwlaeRGAGPEPCLIA-ETGGQNAMIVDSSALL 816
Cdd:cd07152 161 FEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVG-----EAAGRHLKKVSlELGGKNALIVLDDADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 817 EQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAA 896
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 897 GRGVfrvpLPPACENGSFVAPTLieidgIGDV-------GREVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRI 969
Cdd:cd07152 315 GARL----EAGGTYDGLFYRPTV-----LSGVkpgmpafDEEIFGPVAPVTVFDSD--EEAVALANDTEYGLSAGIISRD 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 500091462 970 DETVERVVAGLRVGNLYVNRNMVGAVVgVQPFGGEGLSGTGPKAGGP 1016
Cdd:cd07152 384 VGRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
642-1010 |
4.90e-43 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 165.44 E-value: 4.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 642 AQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAPLV-----------------CISPWNFPLAI 704
Cdd:PRK09407 91 ENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAPRRRAGALpvltkttelrqpkgvvgVISPWNYPLTL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLArdPRIGGVLFTGSTDVARGLA 784
Cdd:PRK09407 171 AVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 RWLAERgagpepcLI---AETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGE 861
Cdd:PRK09407 249 EQAGRR-------LIgfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 862 LRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGR-----GVFRVPLPPAcengsFVAPT-LIEIDGIGDVGR-EVFG 934
Cdd:PRK09407 322 MRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGAtvlagGKARPDLGPL-----FYEPTvLTGVTPDMELAReETFG 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500091462 935 PILHVLRFDaeGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTG 1010
Cdd:PRK09407 397 PVVSVYPVA--DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
640-1010 |
6.41e-43 |
|
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: 163.84 E-value: 6.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVR---EAVDFC--------RYYAQQVVT-LPAPTQAAPL-VC--ISPWNFPLAI 704
Cdd:cd07085 73 LEENLDELARLITLEHGKTLADARGDVLrglEVVEFAcsiphllkGEYLENVARgIDTYSYRQPLgVVagITPFNFPAMI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGSTDVARgla 784
Cdd:cd07085 153 PLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGE--- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 rWLAERGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRI 864
Cdd:cd07085 229 -YIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 865 GDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVF---RVPLPPACENGSFVAPTLieIDGIG---DVGR-EVFGPIL 937
Cdd:cd07085 308 GAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVldgRGVKVPGYENGNFVGPTI--LDNVTpdmKIYKeEIFGPVL 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500091462 938 HVLRfdAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNrnmVGAVVGVQ--PFGGEGLSGTG 1010
Cdd:cd07085 386 SIVR--VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLAffSFGGWKGSFFG 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
640-1010 |
9.21e-43 |
|
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: 163.24 E-value: 9.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKT-------WGNAVAEVREAVDFCryYAQQVVTLPAPTQA-------APL-VC--ISPWNFPL 702
Cdd:cd07151 67 LEERRDEIVEWLIRESGSTrikanieWGAAMAITREAATFP--LRMEGRILPSDVPGkenrvyrEPLgVVgvISPWNFPL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 703 AIFVGQLSAALAAGRCVLAKPALATPLTAALAV-ELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVAR 781
Cdd:cd07151 145 HLSMRSVAPALALGNAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 782 GLARwLAERgAGPEPCLiaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGE 861
Cdd:cd07151 225 HIGE-LAGR-HLKKVAL--ELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 862 LRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGrgvfRVPLPPACENGSFVAPT-LIEIDGIGDVGR-EVFGPILHV 939
Cdd:cd07151 301 LPYGDPSDPDTVVGPLINESQVDGLLDKIEQAVEEG----ATLLVGGEAEGNVLEPTvLSDVTNDMEIAReEIFGPVAPI 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500091462 940 LRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVqPFGGEGLSGTG 1010
Cdd:cd07151 377 IKADDE--EEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
647-1014 |
2.43e-42 |
|
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: 162.31 E-value: 2.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 647 LVSVLVREAGKTWGNAVA-EVREAVDFCRYYA--------QQVVTLP---APTQAAPL-VC--ISPWNFPLAIFVGQLSA 711
Cdd:cd07143 88 LASIEALDNGKTFGTAKRvDVQASADTFRYYGgwadkihgQVIETDIkklTYTRHEPIgVCgqIIPWNFPLLMCAWKIAP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 712 ALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERG 791
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSN 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 792 AGPepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALA 871
Cdd:cd07143 248 LKK---VTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 872 TDIGPVIDNAARDALEAHVARMQAAGRGVF----RvplppaCEN-GSFVAPTLIEiDGIGD---VGREVFGPILHVLRFD 943
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVEtggkR------HGNeGYFIEPTIFT-DVTEDmkiVKEEIFGPVVAVIKFK 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500091462 944 AEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1014
Cdd:cd07143 398 TE--EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
695-1016 |
4.04e-42 |
|
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: 161.59 E-value: 4.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFT 774
Cdd:cd07139 144 IVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVARGLARWLAERGAgpePCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSAL-RVLcVQRDIAEPLLT 853
Cdd:cd07139 223 GSTAAGRRIAAVCGERLA---RVTL-ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 854 MLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGrgvFRV----PLPPACENGSFVAPTLieidgIGDVG 929
Cdd:cd07139 298 ALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAEG---ARLvtggGRPAGLDRGWFVEPTL-----FADVD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 930 -------REVFGPILHVLRFDaeGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVgvqPFG 1002
Cdd:cd07139 370 ndmriaqEEIFGPVLSVIPYD--DEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA---PFG 444
|
330
....*....|....
gi 500091462 1003 GEGLSGTGpKAGGP 1016
Cdd:cd07139 445 GFKQSGIG-REGGP 457
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
586-1013 |
5.55e-42 |
|
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: 160.60 E-value: 5.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 586 VCNPAdHADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTW-GNAVA 664
Cdd:cd07108 1 VINPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 665 EVREAVDFCRYYAQ-----QVVTLP-APTQAA-----PL---VCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLT 730
Cdd:cd07108 80 EAAVLADLFRYFGGlagelKGETLPfGPDVLTytvrePLgvvGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 731 AALAVELMHAAgIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERgagpepcLIA---ETGGQNA 807
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR-------LIPvslELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 808 MIVDSSALLEQVVQDVLVSA-FDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDAL 886
Cdd:cd07108 232 MIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 887 EAHV--ARMQAAGRGVFRVPLPPAC--ENGSFVAPTLI-EIDGIGDVGR-EVFGPILHVLRFDAEglDRLIASINATGYG 960
Cdd:cd07108 312 CGYIdlGLSTSGATVLRGGPLPGEGplADGFFVQPTIFsGVDNEWRLAReEIFGPVLCAIPWKDE--DEVIAMANDSHYG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 500091462 961 LTGGLHSRIDETVERVVAGLRVGNLYVNRNmVGAVVGvQPFGGEGLSGTGPKA 1013
Cdd:cd07108 390 LAAYVWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
658-1014 |
6.13e-42 |
|
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: 161.12 E-value: 6.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 658 TWGN-------AVAEVREAVDFCRYYAQ-----QVVTLPA--PTQAAPLV-------CISPWNFPLAIFVGQLSAALAAG 716
Cdd:cd07142 90 TWDNgkpyeqaRYAEVPLAARLFRYYAGwadkiHGMTLPAdgPHHVYTLHepigvvgQIIPWNFPLLMFAWKVGPALACG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 717 RCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGAGPep 796
Cdd:cd07142 170 NTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKP-- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 797 cLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGP 876
Cdd:cd07142 248 -VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 877 VIDNAARDALEAHV-------ARMQAAGRGVfrvplppaCENGSFVAPTLIE--IDGIGDVGREVFGPILHVLRFDAegL 947
Cdd:cd07142 327 QVDKEQFEKILSYIehgkeegATLITGGDRI--------GSKGYYIQPTIFSdvKDDMKIARDEIFGPVQSILKFKT--V 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500091462 948 DRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1014
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
644-1019 |
1.30e-40 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 157.38 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 644 QAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQ-------------------VVTLPAPTQAAplvcISPWNFPLAI 704
Cdd:PRK11241 87 QDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEgkriygdtipghqadkrliVIKQPIGVTAA----ITPWNFPAAM 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGla 784
Cdd:PRK11241 163 ITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ-- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 rwLAERGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRI 864
Cdd:PRK11241 241 --LMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 865 GDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACEnGSFVAPT-LIEIDGIGDVGR-EVFGPILHVLRF 942
Cdd:PRK11241 319 GDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELG-GNFFQPTiLVDVPANAKVAKeETFGPLAPLFRF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 943 DAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGvqPFGG---EGLSGTGPKAGGPLYL 1019
Cdd:PRK11241 398 KDE--ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
640-1029 |
1.96e-40 |
|
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: 156.80 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTW-GNAVAEVREAVDFCRYYA--------QQVVTLP---APTQAAPL-VC--ISPWNFPLAI 704
Cdd:cd07144 81 VEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAgwadkiqgKTIPTSPnklAYTLHEPYgVCgqIIPWNYPLAM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVarglA 784
Cdd:cd07144 161 AAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT----G 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 RWLAERGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGE-LR 863
Cdd:cd07144 237 RLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYK 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 864 IGDPAALATDIGPVIDNAARDALEA--HVARMQAAGRGVFRVPLPPACENGSFVAPTlIEIDGIGD---VGREVFGPILH 938
Cdd:cd07144 317 VGSPFDDDTVVGPQVSKTQYDRVLSyiEKGKKEGAKLVYGGEKAPEGLGKGYFIPPT-IFTDVPQDmriVKEEIFGPVVV 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 939 VLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNR-NMvgAVVGVqPFGGEGLSGTGpkaggpl 1017
Cdd:cd07144 396 ISKFKTY--EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSsND--SDVGV-PFGGFKMSGIG------- 463
|
410
....*....|..
gi 500091462 1018 ylhRLLGTAQLD 1029
Cdd:cd07144 464 ---RELGEYGLE 472
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
695-1010 |
2.05e-40 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 156.61 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMhAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFT 774
Cdd:PRK13473 145 IAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELA-ADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLT 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVARGLARWLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTM 854
Cdd:PRK13473 224 GSIATGKHVLSAAADSVKR----THLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 855 LKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLI-------EIdgigd 927
Cdd:PRK13473 300 LAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTLLagarqddEI----- 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 928 VGREVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVgaVVGVQPFGGEGLS 1007
Cdd:PRK13473 375 VQREVFGPVVSVTPFDDE--DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQS 450
|
...
gi 500091462 1008 GTG 1010
Cdd:PRK13473 451 GYG 453
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
647-997 |
2.56e-40 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 154.51 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 647 LVSVLVREAGKTWGNAVAEVREAVDFCRYYAQ-------QVVTLPAPTQ-----AAPLVCIS---PWNFPLAIFVGQLSA 711
Cdd:PRK10090 15 ISALIVEEGGKIQQLAEVEVAFTADYIDYMAEwarryegEIIQSDRPGEnillfKRALGVTTgilPWNFPFFLIARKMAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 712 ALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGStdVARGLARWLAERG 791
Cdd:PRK10090 95 ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS--VSAGEKIMAAAAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 792 AGPEPCLiaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPA-AL 870
Cdd:PRK10090 173 NITKVCL--ELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPAeRN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 871 ATDIGPVIDNAARDALEAHVARMQAAGRgvfRVPL--PPACENGSFVAPTLI-----EIDGIGDvgrEVFGPILHVLRFD 943
Cdd:PRK10090 251 DIAMGPLINAAALERVEQKVARAVEEGA---RVALggKAVEGKGYYYPPTLLldvrqEMSIMHE---ETFGPVLPVVAFD 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 500091462 944 AegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVG 997
Cdd:PRK10090 325 T--LEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQG 376
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
607-1010 |
2.64e-39 |
|
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: 152.23 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 607 VEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAP 686
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 687 TQAA--------------PLVCISPWNFPL---AIFVGqlsAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQ 749
Cdd:cd07100 81 EPIEtdagkayvryeplgVVLGIMPWNFPFwqvFRFAA---PNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 750 LLPGRGGSVGQTLArDPRIGGVLFTGSTDVARGLArwlAERGAGPEPCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFD 829
Cdd:cd07100 158 NLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVA---AEAGKNLKKSVL-ELGGSDPFIVLDDADLDKAVKTAVKGRLQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 830 SAGQRC-SALRVLcVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPA 908
Cdd:cd07100 233 NAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 909 cENGSFVAPTLIEidgigDVGR-------EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLR 981
Cdd:cd07100 312 -GPGAFYPPTVLT-----DVTPgmpaydeELFGPVAAVIKVKDE--EEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
410 420
....*....|....*....|....*....
gi 500091462 982 VGNLYVNRnMVGAVVGVqPFGGEGLSGTG 1010
Cdd:cd07100 384 AGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
640-989 |
4.70e-39 |
|
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: 152.01 E-value: 4.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 640 FEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAPTQAAP---------------LVCISPWNFPLAI 704
Cdd:cd07102 53 LAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEkdgferyirreplgvVLIIAPWNYPYLT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 705 FVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGSTDVARGLA 784
Cdd:cd07102 133 AVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 785 RWLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRI 864
Cdd:cd07102 212 RAAAGRFIK----VGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 865 GDPAALATDIGPVIDNAARDALEAHVArmQAAGRGVfRVPLPPA-----CENGSFVAPT-LIEIDGIGDVGR-EVFGPIL 937
Cdd:cd07102 288 GDPLDPSTTLGPVVSARAADFVRAQIA--DAIAKGA-RALIDGAlfpedKAGGAYLAPTvLTNVDHSMRVMReETFGPVV 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 500091462 938 HVLRF--DAEGldrlIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNR 989
Cdd:cd07102 365 GIMKVksDAEA----IALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
665-1010 |
2.02e-38 |
|
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: 150.67 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 665 EVREAVDFCRYYA---------QQVVTLPAP--------TQAAPL---VCISPWNFPLAIFVGQLSAALAAGRCVLAKPA 724
Cdd:cd07113 99 EVGQSANFLRYFAgwatkingeTLAPSIPSMqgerytafTRREPVgvvAGIVPWNFSVMIAVWKIGAALATGCTIVIKPS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 725 LATPLTAALAVELMHAAGIPRAALQLLPGRGGsVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGAGpepcLIAETGG 804
Cdd:cd07113 179 EFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTR----VTLELGG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 805 QNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARD 884
Cdd:cd07113 254 KNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 885 ALEAHVARMQAAGRGVFRVPLPPACEnGSFVAPTLIEIDGIGD--VGREVFGPILHVLRFDAEglDRLIASINATGYGLT 962
Cdd:cd07113 334 KVCSYLDDARAEGDEIVRGGEALAGE-GYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDE--EELIQLINDTPFGLT 410
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 500091462 963 GGLHSRIDETVERVVAGLRVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1010
Cdd:cd07113 411 ASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
687-1014 |
2.16e-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: 150.72 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 687 TQAAPL-VC--ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLA 763
Cdd:cd07140 143 TKREPIgVCgiVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 764 RDPRIGGVLFTGSTDVARGLARWLAErgAGPEPCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCV 843
Cdd:cd07140 223 DHPDVRKLGFTGSTPIGKHIMKSCAV--SNLKKVSL-ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 844 QRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGR----GVFRVPLPpacenGSFVAPTL 919
Cdd:cd07140 300 EESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGAtlvyGGKQVDRP-----GFFFEPTV 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 920 IE--IDGIGDVGREVFGPILHVLRFDAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN---RNMVGA 994
Cdd:cd07140 375 FTdvEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynKTDVAA 454
|
330 340
....*....|....*....|
gi 500091462 995 vvgvqPFGGEGLSGTGPKAG 1014
Cdd:cd07140 455 -----PFGGFKQSGFGKDLG 469
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
586-1010 |
4.40e-38 |
|
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: 149.06 E-value: 4.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 586 VCNPADhADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAE 665
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 666 VREAVDFCRYYAQQVV-----TLPAPTQAAPLVC---------ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTA 731
Cdd:cd07107 80 VMVAAALLDYFAGLVTelkgeTIPVGGRNLHYTLrepygvvarIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 732 ALAVELMHAAgIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAErgaGPEPCLIaETGGQNAMIVD 811
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAE---GIKHVTL-ELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 812 SSALLEQVVQDVLVSA-FDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHV 890
Cdd:cd07107 235 PDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 891 ARMQAAGRGVF---RVPLPPACENGSFVAPT-LIEIDGIGDVGR-EVFGPILHVLRFDAEglDRLIASINATGYGLTGGL 965
Cdd:cd07107 315 DSAKREGARLVtggGRPEGPALEGGFYVEPTvFADVTPGMRIAReEIFGPVLSVLRWRDE--AEMVAQANGVEYGLTAAI 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 500091462 966 HSRIDETVERVVAGLRVGNLYVN---RNMVGAvvgvqPFGGEGLSGTG 1010
Cdd:cd07107 393 WTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
647-1021 |
9.86e-37 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 146.13 E-value: 9.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 647 LVSVlvrEAGKTWGNAVAEVREAVDFCRY---YAQQVVTLPAPTQAA---------PLV---CISPWNFPLAIFVGQLSA 711
Cdd:PLN02315 101 LVSL---EMGKILAEGIGEVQEIIDMCDFavgLSRQLNGSIIPSERPnhmmmevwnPLGivgVITAFNFPCAVLGWNACI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 712 ALAAGRCVLAKPALATPL----TAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGSTDVARGLARWL 787
Cdd:PLN02315 178 ALVCGNCVVWKGAPTTPLitiaMTKLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 788 AERGAgpePCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDP 867
Cdd:PLN02315 257 NARFG---KCLL-ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 868 AALATDIGPVIDNAARDALEAHVARMQAAGrGVFRVPLPPACENGSFVAPTLIEIDGIGDVGR-EVFGPILHVLRFdaEG 946
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQG-GKILTGGSAIESEGNFVQPTIVEISPDADVVKeELFGPVLYVMKF--KT 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 947 LDRLIASINATGYGLTGGLHSRIDETVERVVA--GLRVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG---PLYLHR 1021
Cdd:PLN02315 410 LEEAIEINNSVPQGLSSSIFTRNPETIFKWIGplGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSdswKQYMRR 488
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
641-1014 |
1.42e-35 |
|
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: 142.10 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNA-VAEVREAVDFCRYYAQ-----QVVTLPAP------TQAAPL-VC--ISPWNFPLAIF 705
Cdd:cd07141 83 ERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGwadkiHGKTIPMDgdfftyTRHEPVgVCgqIIPWNFPLLMA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 706 VGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARglar 785
Cdd:cd07141 163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGK---- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 786 wLAERGAGPEPC--LIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELR 863
Cdd:cd07141 239 -LIQQAAGKSNLkrVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 864 IGDPAALATDIGPVIDNAARDALEAHV-------ARMQAAGRgvfrvplpPACENGSFVAPTLieidgIGDVG------- 929
Cdd:cd07141 318 VGNPFDPKTEQGPQIDEEQFKKILELIesgkkegAKLECGGK--------RHGDKGYFIQPTV-----FSDVTddmriak 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 930 REVFGPILHVLRFdaEGLDRLIASINATGYGLTGGLHSR-IDETVErVVAGLRVGNLYVNrnmVGAVVGVQ-PFGGEGLS 1007
Cdd:cd07141 385 EEIFGPVQQIFKF--KTIDEVIERANNTTYGLAAAVFTKdIDKAIT-FSNALRAGTVWVN---CYNVVSPQaPFGGYKMS 458
|
....*..
gi 500091462 1008 GTGPKAG 1014
Cdd:cd07141 459 GNGRELG 465
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
695-1010 |
6.66e-35 |
|
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: 140.17 E-value: 6.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTaalAVELMHAAG--IPRAALQLLPGRGGSVGQTLARDPRIGGVL 772
Cdd:cd07559 143 IIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLS---ILVLMELIGdlLPKGVVNVVTGFGSEAGKPLASHPRIAKLA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 773 FTGSTDVARGLARWLAERgagpepcLIA---ETGGQNAMIVDSSALLEQ------VVQDVLVSAFDSaGQRCSALRVLCV 843
Cdd:cd07559 220 FTGSTTVGRLIMQYAAEN-------LIPvtlELGGKSPNIFFDDAMDADddfddkAEEGQLGFAFNQ-GEVCTCPSRALV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 844 QRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHV-------ARMQAAGRgvfRVPLpPACENGSFVA 916
Cdd:cd07559 292 QESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVdigkeegAEVLTGGE---RLTL-GGLDKGYFYE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 917 PTLIEidGIGDVGR----EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN-RNM 991
Cdd:cd07559 368 PTLIK--GGNNDMRifqeEIFGPVLAVITFKDE--EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQ 443
|
330
....*....|....*....
gi 500091462 992 VGAVVgvqPFGGEGLSGTG 1010
Cdd:cd07559 444 YPAHA---PFGGYKKSGIG 459
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
695-988 |
1.53e-34 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 139.48 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLT----AALAVElmhaAGIPRAALQLLPGRGGSVGQTLARDPRIGG 770
Cdd:PLN02467 158 ITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTclelADICRE----VGLPPGVLNVVTGLGTEAGAPLASHPGVDK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 771 VLFTGSTDVARGLARWLAERgagPEPCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEP 850
Cdd:PLN02467 234 IAFTGSTATGRKIMTAAAQM---VKPVSL-ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 851 LLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVF----RvplPPACENGSFVAPTLIEidgig 926
Cdd:PLN02467 310 FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILcggkR---PEHLKKGFFIEPTIIT----- 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500091462 927 DVGR-------EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN 988
Cdd:PLN02467 382 DVTTsmqiwreEVFGPVLCVKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
695-1010 |
2.20e-34 |
|
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: 137.66 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMhAAGIPRAALQLLPGrGGSVGQTLArDPRIGGVLFT 774
Cdd:cd07087 107 IGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI-PKYFDPEAVAVVEG-GVEVATALL-AEPFDHIFFT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVARGLARWLAERgagPEPClIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTM 854
Cdd:cd07087 184 GSPAVGKIVMEAAAKH---LTPV-TLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 855 LKDAMGELrIGDPAALATDIGPVIDnaardalEAHVARMQA---AGRGVFrvplppaceNGS------FVAPTLIEIDGI 925
Cdd:cd07087 260 LKKAIKEF-YGEDPKESPDYGRIIN-------ERHFDRLASlldDGKVVI---------GGQvdkeerYIAPTILDDVSP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 926 GDV--GREVFGPILHVLRFDaeGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGG 1003
Cdd:cd07087 323 DSPlmQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
....*..
gi 500091462 1004 EGLSGTG 1010
Cdd:cd07087 401 VGNSGMG 407
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
695-1010 |
3.95e-34 |
|
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: 137.97 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTaalAVELMH--AAGIPRAALQLLPGRGGSVGQTLARDPRIGGVL 772
Cdd:cd07117 143 IIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLS---LLELAKiiQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 773 FTGSTDVARGLARWLAERgagpepcLIAET---GGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAE 849
Cdd:cd07117 220 FTGSTEVGRDVAIAAAKK-------LIPATlelGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 850 PLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHV-------ARMQAAGRGVfrvpLPPACENGSFVAPTLIE- 921
Cdd:cd07117 293 EFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVdiakeegAKILTGGHRL----TENGLDKGFFIEPTLIVn 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 922 IDGIGDVGR-EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNR-NMVGAVVgvq 999
Cdd:cd07117 369 VTNDMRVAQeEIFGPVATVIKFKTE--DEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTyNQIPAGA--- 443
|
330
....*....|.
gi 500091462 1000 PFGGEGLSGTG 1010
Cdd:cd07117 444 PFGGYKKSGIG 454
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
695-1014 |
1.92e-33 |
|
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: 135.51 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAA----GIPRAALQLLPGRGGsVGQTLARDPRIGG 770
Cdd:cd07098 127 IVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPE-TAEALTSHPVIDH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 771 VLFTGSTDVARGLARWLAERgAGPepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEP 850
Cdd:cd07098 206 ITFIGSPPVGKKVMAAAAES-LTP---VVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 851 LLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHV-------ARMQAAGRGVFRVPLPpaceNGSFVAPTLieid 923
Cdd:cd07098 282 LLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVadavekgARLLAGGKRYPHPEYP----QGHYFPPTL---- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 924 gIGDVG-------REVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVV 996
Cdd:cd07098 354 -LVDVTpdmkiaqEEVFGPVMVVMKASDD--EEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYV 430
|
330
....*....|....*...
gi 500091462 997 GVQPFGGEGLSGTGPKAG 1014
Cdd:cd07098 431 QQLPFGGVKGSGFGRFAG 448
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
645-1014 |
3.46e-33 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 135.33 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 645 AALVSVlvrEAGKTW-GNAVAEVREAVDFCRYYAQ----------------QVVTLPAPTQAAPLvcISPWNFPLAIFVG 707
Cdd:PLN02766 103 AALDTI---DAGKLFaLGKAVDIPAAAGLLRYYAGaadkihgetlkmsrqlQGYTLKEPIGVVGH--IIPWNFPSTMFFM 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 708 QLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWL 787
Cdd:PLN02766 178 KVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 788 AERGAGPepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDP 867
Cdd:PLN02766 258 ATSNLKQ---VSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 868 AALATDIGPVIDNAARDALEAHV-------ARMQAAGRgvfrvplpPACENGSFVAPTlIEIDGIGD---VGREVFGPIL 937
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIehgkregATLLTGGK--------PCGDKGYYIEPT-IFTDVTEDmkiAQDEIFGPVM 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500091462 938 HVLRFdaEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMvgAVVGVQPFGGEGLSGTGPKAG 1014
Cdd:PLN02766 406 SLMKF--KTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
691-1010 |
4.54e-33 |
|
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: 133.86 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 691 PLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLL---PGRGGSVGQTLARDPR 767
Cdd:cd07105 101 VVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEVVEALIAHPA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 768 IGGVLFTGSTDVARGLARWLAERgagPEPCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRC-SALRVLcVQRD 846
Cdd:cd07105 181 VRKVNFTGSTRVGRIIAETAAKH---LKPVLL-ELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICmSTERII-VHES 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 847 IAEPLLTMLKDAMGELRIGDpaalaTDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENGSFVAPTLIEidgig 926
Cdd:cd07105 256 IADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPPTILD----- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 927 DVGR-------EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNrnmvGAVVGVQ 999
Cdd:cd07105 326 NVTPdmdiyseESFGPVVSIIRVKDE--EEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN----GMTVHDE 399
|
330
....*....|....
gi 500091462 1000 ---PFGGEGLSGTG 1010
Cdd:cd07105 400 ptlPHGGVKSSGYG 413
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
604-1010 |
6.65e-33 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 133.71 E-value: 6.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 604 PDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTL 683
Cdd:PRK09406 22 DDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 684 PAPTQA-----------------APLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRA 746
Cdd:PRK09406 102 LADEPAdaaavgasrayvryqplGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 747 ALQLLPGRGGSVGQTLaRDPRIGGVLFTGSTDVARGLARWlaergAGPE-PCLIAETGGQNAMIVDSSALLEQVVQDVLV 825
Cdd:PRK09406 182 CFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVAAI-----AGDEiKKTVLELGGSDPFIVMPSADLDRAAETAVT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 826 SAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPL 905
Cdd:PRK09406 256 ARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 906 PPAcENGSFVAPTLieidgIGDV-------GREVFGPILHVLRfdAEGLDRLIASINATGYGLTGGLHSRIDETVERVVA 978
Cdd:PRK09406 336 RPD-GPGWFYPPTV-----ITDItpdmrlyTEEVFGPVASLYR--VADIDEAIEIANATTFGLGSNAWTRDEAEQERFID 407
|
410 420 430
....*....|....*....|....*....|..
gi 500091462 979 GLRVGNLYVNrNMVGAVVGVqPFGGEGLSGTG 1010
Cdd:PRK09406 408 DLEAGQVFIN-GMTVSYPEL-PFGGVKRSGYG 437
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
674-1010 |
1.16e-32 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 133.87 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 674 RYYAQQVVTL---PAPTQAAPLVCIS-----------PWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMH 739
Cdd:PRK09847 129 RWYAEAIDKVygeVATTSSHELAMIVrepvgviaaivPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 740 AAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLarwLAERGAGPEPCLIAETGGQNAMIVDSSAL-LEQ 818
Cdd:PRK09847 209 EAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL---LKDAGDSNMKRVWLEAGGKSANIVFADCPdLQQ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 819 VVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGR 898
Cdd:PRK09847 286 AASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQ 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 899 GVF--RVPLPPACengsfVAPT-LIEIDGIGDVGR-EVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVE 974
Cdd:PRK09847 366 LLLdgRNAGLAAA-----IGPTiFVDVDPNASLSReEIFGPVLVVTRFTSE--EQALQLANDSQYGLGAAVWTRDLSRAH 438
|
330 340 350
....*....|....*....|....*....|....*.
gi 500091462 975 RVVAGLRVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1010
Cdd:PRK09847 439 RMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
641-1010 |
7.91e-32 |
|
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: 130.62 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 641 EAQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAP------TQAA-------------PLVCISPWNFP 701
Cdd:cd07148 58 EERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGReipmglTPASagriafttrepigVVVAISAFNHP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 702 LAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGrGGSVGQTLARDPRIGGVLFTGSTDVAr 781
Cdd:cd07148 138 LNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVG- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 782 glarWLAERGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGE 861
Cdd:cd07148 216 ----WMLRSKLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 862 LRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRgvfRVPLPPACENGSFVAPTLIeIDGIGDVG---REVFGPILH 938
Cdd:cd07148 292 LVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGA---RLLCGGKRLSDTTYAPTVL-LDPPRDAKvstQEIFGPVVC 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500091462 939 VLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNrNMVGAVVGVQPFGGEGLSGTG 1010
Cdd:cd07148 368 VYSYDD--LDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVN-DHTAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
655-1014 |
1.03e-31 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 131.47 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 655 AGKTWGN-------AVAEVREAVDFCRYYA----------------QQVVTLPAPTQAAPLvcISPWNFPLAIFVGQLSA 711
Cdd:PLN02466 141 ALETWDNgkpyeqsAKAELPMFARLFRYYAgwadkihgltvpadgpHHVQTLHEPIGVAGQ--IIPWNFPLLMFAWKVGP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 712 ALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERG 791
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 792 AGPepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALA 871
Cdd:PLN02466 299 LKP---VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKG 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 872 TDIGPVIDNAA--------RDALEAHvARMQAAGRgvfrvplpPACENGSFVAPTLIE--IDGIGDVGREVFGPILHVLR 941
Cdd:PLN02466 376 VEQGPQIDSEQfekilryiKSGVESG-ATLECGGD--------RFGSKGYYIQPTVFSnvQDDMLIAQDEIFGPVQSILK 446
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500091462 942 FdaEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1014
Cdd:PLN02466 447 F--KDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
585-1010 |
1.63e-31 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 130.00 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 585 PVCNPADhADIVGSVVEALPDEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWGNA-V 663
Cdd:PRK13252 25 EVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETsV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 664 AEVREAVDFCRYYAQQVVTLP-----------APTQAAPL-VC--ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPL 729
Cdd:PRK13252 104 VDIVTGADVLEYYAGLAPALEgeqiplrggsfVYTRREPLgVCagIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 730 TAALAVELMHAAGIPRAALQLLPGRgGSVGQTLARDPRIGGVLFTGSTDVARglaRWLAERGAGPEPCLIaETGGQNAMI 809
Cdd:PRK13252 184 TALKLAEIYTEAGLPDGVFNVVQGD-GRVGAWLTEHPDIAKVSFTGGVPTGK---KVMAAAAASLKEVTM-ELGGKSPLI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 810 VDSSALLEQVVQDVLVSAFDSAGQRCS-ALRVLcVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEA 888
Cdd:PRK13252 259 VFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 889 HVARMQAAGR----GVFRVPlPPACENGSFVAPTLIE--IDGIGDVGREVFGPILHVLRFDAEglDRLIASINATGYGLT 962
Cdd:PRK13252 338 YIEKGKAEGArllcGGERLT-EGGFANGAFVAPTVFTdcTDDMTIVREEIFGPVMSVLTFDDE--DEVIARANDTEYGLA 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 500091462 963 GGLHSRIDETVERVVAGLRVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1010
Cdd:PRK13252 415 AGVFTADLSRAHRVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
693-1015 |
9.10e-31 |
|
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: 126.96 E-value: 9.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 693 VC--ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAgIPRAALQLLPGrGGSVGQTLARDPrIGG 770
Cdd:cd07134 103 VCliISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEG-DAEVAQALLELP-FDH 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 771 VLFTGSTDVAR----GLARWLAErgagpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRD 846
Cdd:cd07134 180 IFFTGSPAVGKivmaAAAKHLAS--------VTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 847 IAEPLLTMLKDAMGELRIGDPAALAT-DIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPACENgsFVAPTLIEidgi 925
Cdd:cd07134 252 VKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR--YIAPTVLT---- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 926 gDVGR-------EVFGPILHVLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGV 998
Cdd:cd07134 326 -NVTPdmkimqeEIFGPVLPIITYED--LDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPN 402
|
330
....*....|....*..
gi 500091462 999 QPFGGEGLSGTGpKAGG 1015
Cdd:cd07134 403 LPFGGVNNSGIG-SYHG 418
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
642-968 |
1.10e-27 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 118.71 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 642 AQQAALVSVLVREAGKTWGNAVAEVREAVDFCRYYAQQVVTLPAP-------------------TQAAPL---VCISPWN 699
Cdd:PLN00412 90 EHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkflvsdsfpgnernkyclTSKIPLgvvLAIPPFN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 700 FPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDv 779
Cdd:PLN00412 170 YPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDT- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 780 arGLArwlAERGAGPEPcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAM 859
Cdd:PLN00412 249 --GIA---ISKKAGMVP-LQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 860 GELRIGDPAALAtDIGPVIDNAARDALEAHVARMQAAGrGVFRVPLPpacENGSFVAPTLieIDGIGDVGR----EVFGP 935
Cdd:PLN00412 323 AKLTVGPPEDDC-DITPVVSESSANFIEGLVMDAKEKG-ATFCQEWK---REGNLIWPLL--LDNVRPDMRiaweEPFGP 395
|
330 340 350
....*....|....*....|....*....|....*
gi 500091462 936 ILHVLRF--DAEGldrlIASINATGYGLTGGLHSR 968
Cdd:PLN00412 396 VLPVIRInsVEEG----IHHCNASNFGLQGCVFTR 426
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
695-1010 |
7.61e-27 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 116.28 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAgIPRAALQLLPGrGGSVGQTLARDPrIGGVLFT 774
Cdd:PTZ00381 116 IGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVARGLARWLAERGAgpePClIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTM 854
Cdd:PTZ00381 193 GSPRVGKLVMQAAAENLT---PC-TLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 855 LKDAMGELrIGDPAALATDIGPVIDnaardalEAHVARMQA-----AGRGVFRvplPPACENGSFVAPTLIEIDGIGDV- 928
Cdd:PTZ00381 269 LKEAIKEF-FGEDPKKSEDYSRIVN-------EFHTKRLAElikdhGGKVVYG---GEVDIENKYVAPTIIVNPDLDSPl 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 929 -GREVFGPILHVLRFdaEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLS 1007
Cdd:PTZ00381 338 mQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNS 415
|
...
gi 500091462 1008 GTG 1010
Cdd:PTZ00381 416 GMG 418
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
695-1010 |
3.62e-25 |
|
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: 110.00 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAgIPRAALQLLPGRGGSVGQTLarDPRIGGVLFT 774
Cdd:cd07135 115 IGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL--EQKFDKIFYT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVAR----GLARWLAergagpePCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEP 850
Cdd:cd07135 192 GSGRVGRiiaeAAAKHLT-------PVTL-ELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 851 LLTMLKDAMGELRIGDPAAlATDIGPVIDNAARDALEAHVARmqAAGRGVFrvplppaceNGS------FVAPTLIEIDG 924
Cdd:cd07135 264 FVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDT--TKGKVVI---------GGEmdeatrFIPPTIVSDVS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 925 IGD--VGREVFGPILHVLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGVQPFG 1002
Cdd:cd07135 332 WDDslMSEELFGPVLPIIKVDD--LDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFG 409
|
....*...
gi 500091462 1003 GEGLSGTG 1010
Cdd:cd07135 410 GVGDSGYG 417
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
695-1010 |
5.93e-24 |
|
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: 107.15 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAgIPRAALQLLPGRGGSVGQTLARDPRIGGVLFT 774
Cdd:cd07116 143 IIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVARGLARWLAERgagpepcLIA---ETGGQNAMIVDSS------ALLEQVVQDVLVSAFDSaGQRCSALRVLCVQR 845
Cdd:cd07116 222 GETTTGRLIMQYASEN-------IIPvtlELGGKSPNIFFADvmdaddAFFDKALEGFVMFALNQ-GEVCTCPSRALIQE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 846 DIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVF----RVPLPPACENGSFVAPTLIE 921
Cdd:cd07116 294 SIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLtggeRNELGGLLGGGYYVPTTFKG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 922 IDGIGDVGREVFGPILHVLRFDAEglDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVnrNMVGAVVGVQPF 1001
Cdd:cd07116 374 GNKMRIFQEEIFGPVLAVTTFKDE--EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAF 449
|
....*....
gi 500091462 1002 GGEGLSGTG 1010
Cdd:cd07116 450 GGYKQSGIG 458
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
589-988 |
5.14e-23 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 104.17 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 589 PADHADIV----GSVVEALP----DEVEAALAAAAAAAAGWAAVPPAARADALRAAADRFEAQQAALVSVLVREAGKTWG 660
Cdd:PRK13968 5 PATHAISVnpatGEQLSVLPwagaDDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 661 NAVAEVREAVDFCRYYAQQ--VVTLPAPT-----QA-------APLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALA 726
Cdd:PRK13968 85 QARAEVAKSANLCDWYAEHgpAMLKAEPTlvenqQAvieyrplGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 727 TPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLaRDPRIGGVLFTGSTdvaRGLARWLAERGAGPEPCLIaETGGQN 806
Cdd:PRK13968 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSV---RAGAAIGAQAGAALKKCVL-ELGGSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 807 AMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDAL 886
Cdd:PRK13968 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 887 EAHVARMQAAGRGVFRVPLPPACEnGSFVAPTLieidgIGDVGR-------EVFGPILHVLRfdAEGLDRLIASINATGY 959
Cdd:PRK13968 320 HHQVEATLAEGARLLLGGEKIAGA-GNYYAPTV-----LANVTPemtafreELFGPVAAITV--AKDAEHALELANDSEF 391
|
410 420
....*....|....*....|....*....
gi 500091462 960 GLTGGLHSRIDETVERVVAGLRVGNLYVN 988
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
691-1021 |
6.11e-23 |
|
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: 103.47 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 691 PLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGI-PRAALQLLPGrGGSVGQTLARDPRIG 769
Cdd:cd07084 103 PVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLING-DGKTMQALLLHPNPK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 770 GVLFTGSTDVARGLARWLAErgaGPepcLIAETGGQNAMIVDSSA-----LLEQVVQDVLVsafdSAGQRCSALRVLCVQ 844
Cdd:cd07084 182 MVLFTGSSRVAEKLALDAKQ---AR---IYLELAGFNWKVLGPDAqavdyVAWQCVQDMTA----CSGQKCTAQSMLFVP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 845 RDIA-EPLLTMLKDAMGELRIGDpaalaTDIGPVIdnaaRDALEAHVARMQAAGRGVFR-----VPLPPACEN-GSFVAP 917
Cdd:cd07084 252 ENWSkTPLVEKLKALLARRKLED-----LLLGPVQ----TFTTLAMIAHMENLLGSVLLfsgkeLKNHSIPSIyGACVAS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 918 TL-IEIDGIGD----VGREVFGPILHVLRFDAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRV-GNLY-VNRN 990
Cdd:cd07084 323 ALfVPIDEILKtyelVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVaGRTYaILRG 402
|
330 340 350
....*....|....*....|....*....|.
gi 500091462 991 MVGAVVGVQPFGGEGLSGTGPKAGGPLYLHR 1021
Cdd:cd07084 403 RTGVAPNQNHGGGPAADPRGAGIGGPEAIKL 433
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
693-1034 |
2.70e-21 |
|
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: 99.27 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 693 VCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGI-PRAALQLLpgrGGSVGQTLARdprIGG- 770
Cdd:cd07128 149 VHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLI---CGSVGDLLDH---LGEq 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 771 --VLFTGSTDVARGLARW--LAERGAGpepcLIAETGGQNAMI-----VDSSALLEQVVQDVLVSAFDSAGQRCSALRVL 841
Cdd:cd07128 223 dvVAFTGSAATAAKLRAHpnIVARSIR----FNAEADSLNAAIlgpdaTPGTPEFDLFVKEVAREMTVKAGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 842 CVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGVFRVPLPPAC-----ENGSFVA 916
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVvgadaEKGAFFP 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 917 PTLIEIDGIGDVGR----EVFGPILHVLRFDaeGLDRLIASINATGYGLTGGLHSRIDETVERVVAGL--RVGNLYV-NR 989
Cdd:cd07128 379 PTLLLCDDPDAATAvhdvEAFGPVATLMPYD--SLAEAIELAARGRGSLVASVVTNDPAFARELVLGAapYHGRLLVlNR 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 500091462 990 NMVGAVVG---VQP---FGGEGLSGTGPKAGG----PLYLHRllgTA-QLDPAALG 1034
Cdd:cd07128 457 DSAKESTGhgsPLPqlvHGGPGRAGGGEELGGlrgvKHYMQR---TAvQGSPTMLT 509
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
695-1010 |
3.89e-21 |
|
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: 97.94 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAgIPRAALQLLPGrGGSVGQTLARDPrIGGVLFT 774
Cdd:cd07133 108 IVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTG-GADVAAAFSSLP-FDHLLFT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVARGLARWLAERgagpepcLIA---ETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPL 851
Cdd:cd07133 185 GSTAVGRHVMRAAAEN-------LTPvtlELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEF 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 852 LTMLKDAMGEL---RIGDPaalatDIGPVIDNAARDALEAHVArmQAAGRGVFRVPLPPACENGS---FVAPTLIEidgi 925
Cdd:cd07133 258 VAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLE--DARAKGARVIELNPAGEDFAatrKLPPTLVL---- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 926 gDVG-------REVFGPILHVLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGV 998
Cdd:cd07133 327 -NVTddmrvmqEEIFGPILPILTYDS--LDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDD 403
|
330
....*....|..
gi 500091462 999 QPFGGEGLSGTG 1010
Cdd:cd07133 404 LPFGGVGASGMG 415
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
695-1010 |
5.87e-18 |
|
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: 88.05 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELmhaagIPR-------AALQllpgrGGSVGQTLARDPR 767
Cdd:cd07132 107 IGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKyldkecyPVVL-----GGVEETTELLKQR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 768 IGGVLFTGSTDVAR----GLARWLAergagpePCLIaETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALR-VLC 842
Cdd:cd07132 177 FDYIFYTGSTSVGKivmqAAAKHLT-------PVTL-ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDyVLC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 843 vQRDIAEPLLTMLKDAMGELrIGDPAALATDIGPVIDNAARDALEAHVARMQAA--GRGVfrvplppacENGSFVAPT-L 919
Cdd:cd07132 249 -TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAigGQTD---------EKERYIAPTvL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 920 IEIDGIGDV-GREVFGPILHVLrfDAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAVVGV 998
Cdd:cd07132 318 TDVKPSDPVmQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDS 395
|
330
....*....|..
gi 500091462 999 QPFGGEGLSGTG 1010
Cdd:cd07132 396 LPFGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
691-988 |
1.12e-17 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 88.26 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 691 PL-VC--ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVgQTLARDPR 767
Cdd:PLN02419 249 PLgVCagICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDED 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 768 IGGVLFTGSTDVARGLARWLAERGAGPEpcliAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDi 847
Cdd:PLN02419 328 IRAVSFVGSNTAGMHIYARAAAKGKRIQ----SNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 848 AEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDA----LEAHV---ARMQAAGRGVfrvpLPPACENGSFVAPTLI 920
Cdd:PLN02419 403 AKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERicrlIQSGVddgAKLLLDGRDI----VVPGYEKGNFIGPTIL 478
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 921 E--IDGIGDVGREVFGPILHVLRfdAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN 988
Cdd:PLN02419 479 SgvTPDMECYKEEIFGPVLVCMQ--ANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
680-1010 |
1.31e-17 |
|
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: 87.08 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 680 VVTLPAPTQ--AAPL---VCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMhAAGIPRAALQLLPGr 754
Cdd:cd07137 88 LTTFPAKAEivSEPLgvvLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEG- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 755 GGSVGQTLArDPRIGGVLFTGSTDVARgLARWLAERGAGPepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDS-AGQ 833
Cdd:cd07137 166 GVPETTALL-EQKWDKIFFTGSPRVGR-IIMAAAAKHLTP---VTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 834 RCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAAlatdigpvIDNAARDALEAHVARMQaagrGVFRVPLPPAC---- 909
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKE--------SKDLSRIVNSHHFQRLS----RLLDDPSVADKivhg 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 910 ----ENGSFVAPTLIeIDGIGD---VGREVFGPILHVLRfdAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRV 982
Cdd:cd07137 309 gerdEKNLYIEPTIL-LDPPLDssiMTEEIFGPLLPIIT--VKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSS 385
|
330 340
....*....|....*....|....*...
gi 500091462 983 GNLYVNRNMVGAVVGVQPFGGEGLSGTG 1010
Cdd:cd07137 386 GGVTFNDTVVQYAIDTLPFGGVGESGFG 413
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
699-988 |
2.82e-17 |
|
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: 86.06 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 699 NFPLAIFV--GQLSAALAAGRCVLAKPALATPLTAALAVELMHAA----GIPRAALQLLPGRGGSVGQTLARDPRIGGVL 772
Cdd:cd07129 116 NFPLAFSVagGDTASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 773 FTGSTDVARGLARWLAERgagPEPCLI-AETGGQNAMIVDSSALLEQVVQ--DVLVSAFD-SAGQRCSALRVLCVQRDIA 848
Cdd:cd07129 196 FTGSRRGGRALFDAAAAR---PEPIPFyAELGSVNPVFILPGALAERGEAiaQGFVGSLTlGAGQFCTNPGLVLVPAGPA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 849 -EPLLTMLKDAMGElrigdpAALATDIGPVIdnaaRDALEAHVARMQAAGrGVFRVPLPPACENGSFVAPTLIEIDGIGD 927
Cdd:cd07129 273 gDAFIAALAEALAA------APAQTMLTPGI----AEAYRQGVEALAAAP-GVRVLAGGAAAEGGNQAAPTLFKVDAAAF 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 928 VGR-----EVFGPILHVLRfdAEGLDRLIASINATGYGLTGGLHSRIDET--VERVVAGL--RVGNLYVN 988
Cdd:cd07129 342 LADpalqeEVFGPASLVVR--YDDAAELLAVAEALEGQLTATIHGEEDDLalARELLPVLerKAGRLLFN 409
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
695-1010 |
1.82e-14 |
|
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: 77.16 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 695 ISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAgIPRAALQLLPGrGGSVGQTLArDPRIGGVLFT 774
Cdd:cd07136 107 IAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQELL-DQKFDYIFFT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 775 GSTDVARGLARWLAERgagpepcLIA---ETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRDIAEPL 851
Cdd:cd07136 184 GSVRVGKIVMEAAAKH-------LTPvtlELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKF 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 852 LTMLKDAMGELrIGDPAALATDIGPVIDnaardalEAHVARMQA---------AGRgvfrvplppACENGSFVAPTLIEi 922
Cdd:cd07136 257 IKELKEEIKKF-YGEDPLESPDYGRIIN-------EKHFDRLAGlldngkivfGGN---------TDRETLYIEPTILD- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 923 dgigDV-------GREVFGPILHVLRFDAegLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVNRNMVGAV 995
Cdd:cd07136 319 ----NVtwddpvmQEEIFGPILPVLTYDT--LDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLA 392
|
330
....*....|....*
gi 500091462 996 VGVQPFGGEGLSGTG 1010
Cdd:cd07136 393 NPYLPFGGVGNSGMG 407
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
680-1010 |
2.60e-14 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 77.07 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 680 VVTLPAPTQAAP-----LVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAvelmhAAGIPR----AALQL 750
Cdd:PLN02203 95 LVAFPATAEVVPeplgvVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFL-----AANIPKyldsKAVKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 751 LPGrGGSVGQTLARDpRIGGVLFTGSTDVARgLARWLAERGAGPepcLIAETGGQNAMIVD---SSALLEQVVQDVLVSA 827
Cdd:PLN02203 170 IEG-GPAVGEQLLQH-KWDKIFFTGSPRVGR-IIMTAAAKHLTP---VALELGGKCPCIVDslsSSRDTKVAVNRIVGGK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 828 FDS-AGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALatdigpviDNAARDALEAHVARMQaagrGVFRVPLP 906
Cdd:PLN02203 244 WGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRES--------KSMARILNKKHFQRLS----NLLKDPRV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 907 PAC--------ENGSFVAPTLIeIDGIGD---VGREVFGPILHVLRFDAegLDRLIASINATG-----YGLTGglhsriD 970
Cdd:PLN02203 312 AASivhggsidEKKLFIEPTIL-LNPPLDsdiMTEEIFGPLLPIITVKK--IEDSIAFINSKPkplaiYAFTN------N 382
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 500091462 971 ETVE-RVVAGLRVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1010
Cdd:PLN02203 383 EKLKrRILSETSSGSVTFNDAIIQYACDSLPFGGVGESGFG 423
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
659-943 |
3.30e-12 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 70.50 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 659 WGNAVAEVR-----EAVDFCRYYAQQVVTLPAPTQAAPLVcISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAAL 733
Cdd:PRK11903 115 LGAALGDARllrdgEAVQLGKDPAFQGQHVLVPTRGVALF-INAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 734 AVELMHAAGI-PRAALQLLpgrGGSVGQTLARDPRIGGVLFTGSTDVA---RGLARwLAERGAGpepcLIAETGGQNAMI 809
Cdd:PRK11903 194 MVKDVVAAGIlPAGALSVV---CGSSAGLLDHLQPFDVVSFTGSAETAavlRSHPA-VVQRSVR----VNVEADSLNSAL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 810 V------DSSA---LLEQVVQDVLVSAfdsaGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDN 880
Cdd:PRK11903 266 LgpdaapGSEAfdlFVKEVVREMTVKS----GQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSR 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500091462 881 AARDALEAHVARMQA------AGRGVFRVPLPPACenGSFVAPTLIEIDGIGDVGR----EVFGPILHVLRFD 943
Cdd:PRK11903 342 AQLAAVRAGLAALRAqaevlfDGGGFALVDADPAV--AACVGPTLLGASDPDAATAvhdvEVFGPVATLLPYR 412
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
251-484 |
6.69e-12 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 69.34 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 251 SIKLSALH-PRYC--------RAQRSRVRAELLPRLAALMRLARGYDIGVNIDAEEA------DRLELSLDL-FEALVAD 314
Cdd:PLN02681 187 SFPLFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYTslqpaiDYITYDLAReFNKGKDR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 315 PLLAGwdglgfVVQAYQKRAPFVIDYLVDLAHRSGRRLMIRLVKGAYWDSEIKRAQvegQAGY--PVYTRKAHTDLAYLV 392
Cdd:PLN02681 267 PIVYG------TYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAA---SLGVpsPVHDTIQDTHACYNR 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 393 CAARLL--AEAGAVYPQFATHNARTVAEVHEMAQCVGAGGTLPAYEFQCLHGMGESLYDSVvggARLGVPCRIYAPVGSH 470
Cdd:PLN02681 338 CAEFLLekASNGDGEVMLATHNVESGELAAAKMNELGLHKGDPRVQFAQLLGMSDNLSFGL---GNAGFRVSKYLPYGPV 414
|
250
....*....|....
gi 500091462 471 RTLLPYLVRRLLEN 484
Cdd:PLN02681 415 EEVIPYLLRRAEEN 428
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
680-1014 |
4.88e-11 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 66.61 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 680 VVTLPAPTQ--AAPL---VCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLlpgr 754
Cdd:PLN02174 99 LTTFPASAEivSEPLgvvLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVV---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 755 GGSVGQTLA-RDPRIGGVLFTGSTDVARGLARWLAERGAGpepcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFD-SAG 832
Cdd:PLN02174 175 EGAVTETTAlLEQKWDKIFYTGSSKIGRVIMAAAAKHLTP----VVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 833 QRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAAlATDIGPVIDNAARDALEAHVARMQAAGRGVF-----RVPLPp 907
Cdd:PLN02174 251 QACISPDYILTTKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYggekdRENLK- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 908 acengsfVAPTL---IEIDGIgDVGREVFGPILHVLRFDaeGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGN 984
Cdd:PLN02174 329 -------IAPTIlldVPLDSL-IMSEEIFGPLLPILTLN--NLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGG 398
|
330 340 350
....*....|....*....|....*....|
gi 500091462 985 LYVNRNMVGAVVGVQPFGGEGLSGTGPKAG 1014
Cdd:PLN02174 399 IVVNDIAVHLALHTLPFGGVGESGMGAYHG 428
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
691-986 |
6.61e-11 |
|
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: 66.37 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 691 PLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHAAGIPRAALQLLPGRGGSVGQTLAR-DPRIg 769
Cdd:cd07126 145 PVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEaNPRM- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 770 gVLFTGSTDVARGLARWLAERgagpepCLIAETG------GQNAMIVDSSALleQVVQDvlvsAFDSAGQRCSALRVLCV 843
Cdd:cd07126 224 -TLFTGSSKVAERLALELHGK------VKLEDAGfdwkilGPDVSDVDYVAW--QCDQD----AYACSGQKCSAQSILFA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 844 QRDIAE-PLLTMLKDAMGELRIGDpaalaTDIGPVIdNAARDALEAHVARMQA--AGRGVF-RVPLP----PACEnGSfV 915
Cdd:cd07126 291 HENWVQaGILDKLKALAEQRKLED-----LTIGPVL-TWTTERILDHVDKLLAipGAKVLFgGKPLTnhsiPSIY-GA-Y 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500091462 916 APTLIEI--------DGIGDVGREVFGPILHVLRFDAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLY 986
Cdd:cd07126 363 EPTAVFVpleeiaieENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
709-988 |
7.82e-11 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 66.35 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 709 LSAALAAGRCVLAKPALATPLTAALAV----ELMHAAGI-PRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTdvarGL 783
Cdd:cd07127 214 LFASLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSN----AF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 784 ARWLAERGAGPEpcLIAETGGQNAMIVDSSALLEQVVQDVLVSAFDSAGQRCSALRVLCVQRD---------IAEPLLTM 854
Cdd:cd07127 290 GDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAAD 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 855 LKDAMGELrIGDPAALATDIGPVI--DNAARDALEAHVARMQAAGRGVFRvplpPACENGSFVAPTLIEIDGIGD--VGR 930
Cdd:cd07127 368 LAAAIDGL-LADPARAAALLGAIQspDTLARIAEARQLGEVLLASEAVAH----PEFPDARVRTPLLLKLDASDEaaYAE 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500091462 931 EVFGPILHVLRFD--AEGLDRLIASINATGyGLTGGLHSRIDETVERVV-AGLRVG-NLYVN 988
Cdd:cd07127 443 ERFGPIAFVVATDstDHSIELARESVREHG-AMTVGVYSTDPEVVERVQeAALDAGvALSIN 503
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
687-868 |
1.38e-08 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 58.39 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 687 TQAAP---LVCISPWNFPLAIFVGQLSAaLAAGRCVLAKPALATPLTA---ALAVELMHAAGIPRAALQLLPGRGGSVGQ 760
Cdd:cd07077 96 VRAFPigvTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNralALLFQAADAAHGPKILVLYVPHPSDELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 761 TLARDPRIGGVLFTGSTDVARglarwlAERGAGPEPCLIAETGGQNAMIVDSSALLEQVVQDVLVSA-FDSAGqrCSALR 839
Cdd:cd07077 175 ELLSHPKIDLIVATGGRDAVD------AAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA--CASEQ 246
|
170 180
....*....|....*....|....*....
gi 500091462 840 VLCVQRDIAEPLLTMLKDAMGELRIGDPA 868
Cdd:cd07077 247 NLYVVDDVLDPLYEEFKLKLVVEGLKVPQ 275
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
734-988 |
8.26e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, 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: 143440 [Multi-domain] Cd Length: 436 Bit Score: 49.80 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 734 AVELMH----AAGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARglarwLAER------GAGPepcliaetg 803
Cdd:cd07122 141 AAKIMReaavAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGPGMVK-----AAYSsgkpaiGVGP--------- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 804 GQNAMIVDSSALLEQVVQDVLVS-AFDSaGQRCSALRVLCVQRDIAEPLLTML------------KDAMGELRIGDPAAL 870
Cdd:cd07122 207 GNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDDEIYDEVRAELkrrgayflneeeKEKLEKALFDDGGTL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 871 ATDIgpvidnAARDAleAHVARMqaAGrgvFRVPlppacENGSFVaptLIEIDGIGD---VGREVFGPILHVLRFD--AE 945
Cdd:cd07122 286 NPDI------VGKSA--QKIAEL--AG---IEVP-----EDTKVL---VAEETGVGPeepLSREKLSPVLAFYRAEdfEE 344
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 500091462 946 GLDRLIASINATGYGLTGGLHSRIDETVERVVAGLRVGNLYVN 988
Cdd:cd07122 345 ALEKARELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVN 387
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
13-36 |
1.27e-04 |
|
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: 40.52 E-value: 1.27e-04
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1069-1100 |
3.26e-04 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 45.19 E-value: 3.26e-04
10 20 30
....*....|....*....|....*....|..
gi 500091462 1069 ARSLAGCHCALPGPTGEANTLRFVGRGVVLCV 1100
Cdd:PRK11904 660 ARRLFGAPEKLPGPTGESNELRLHGRGVFVCI 691
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
592-1204 |
6.45e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 41.01 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 592 HADIVGSVVEALPDEVEAALAAAAAAaagwaavppaaradalraaadrfEAQQAALVSVLVREAG--KTWGNAVAEVREA 669
Cdd:COG3321 787 LADGVRVFLEVGPGPVLTGLVRQCLA-----------------------AAGDAVVLPSLRRGEDelAQLLTALAQLWVA 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 670 ---VDFCRYYA-QQVVTLPAPT-----QAAPLVCISPWNFPLAIFVGQLSAALAAGRCVLAKPALATPLTAALAVELMHA 740
Cdd:COG3321 844 gvpVDWSALYPgRGRRRVPLPTypfqrEDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAA 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 741 AGIPRAALQLLPGRGGSVGQTLARDPRIGGVLFTGSTDVARGLARWLAERGAGPEPCLIAETGGQNAMIVDSSALLEQVV 820
Cdd:COG3321 924 AALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALA 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 821 QDVLVSAFDSAGQRCSALRVLCVQRDIAEPLLTMLKDAMGELRIGDPAALATDIGPVIDNAARDALEAHVARMQAAGRGV 900
Cdd:COG3321 1004 LLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAA 1083
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 901 FRVPLPPACENGSFVAPTLIEIDGIGDVGREVFGPILHVLRFDAEGLDRLIASINATGYGLTGGLHSRIDETVERVVAGL 980
Cdd:COG3321 1084 LALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAAL 1163
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 981 RVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLHRLLGTAQLDPAALGLVAPAEPAAALGVLAAWARQRGDSAL 1060
Cdd:COG3321 1164 AAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAA 1243
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500091462 1061 AARCAEDGARSLAGCHcALPGPTGEANTLRFVGRGVVLCVADSAPALLAQLAAALATGNSALFEAGAAAYRVAAELPSAL 1140
Cdd:COG3321 1244 AVAALAAAAAALLAAL-AALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALA 1322
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500091462 1141 GGWLGVRGHGPDPVFAVALFDGDTEAEWLLRRRLAERPGPLVAVLRADGAGRYPLHRLVAERVV 1204
Cdd:COG3321 1323 AALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| |
