|
Name |
Accession |
Description |
Interval |
E-value |
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
1-1314 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 2578.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1 MASTTLGVKVDDLLRSRLKDAATRLERTPHWLIKQAIFAYLEKIEHGQLPPELSGHTGSADLADGAAVEQEeDGASHPFL 80
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADTPA-EEPHQPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 81 EFAQNVQPQSVLRAAITAAYRRPEPECVPFLLGQARLPANLAGDVQAMAGKLVETLRTKSKGGG----VEGLIHEFSLSS 156
Cdd:PRK11809 80 EFAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGragmVQGLLQEFSLSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 157 QEGVALMCLAEALLRIPDRATRDALIRDKISKGDWKSHVGQAPSLFVNAATWGLMITGKLVTTNSETGLSSALTRLIGKG 236
Cdd:PRK11809 160 QEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 237 GEPLIRKGVDMAMRLMGEQFVTGENISEALANSRKYEARGFRYSYDMLGEAATTEADAQRYYASYEQAIHAIGKAAGGRG 316
Cdd:PRK11809 240 GEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 317 IYEGPGISIKLSALHARYSRSQQERAMSELLPRVRSLAVLARRYDIGLNIDAEEADRLEISLDLLEALCFDPELAGWNGI 396
Cdd:PRK11809 320 IYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 397 GFVVQAYQKRCPFVIDYIVDLARRSRHRIMVRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLGAPDA 476
Cdd:PRK11809 400 GFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 477 VYPQFATHNAHTLSAIYHLAGNNYYPGQYEFQCLHGMGEPLYEEVTGR---DKLNRPCRVYAPVGTHETLLAYLVRRLLE 553
Cdd:PRK11809 480 IYPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKvadGKLNRPCRIYAPVGTHETLLAYLVRRLLE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 554 NGANTSFVNRIADENVAIKDLIADPVDEASKIV----PLGAPHAKIPLPRNLFGAERLNSMGLDLSNEHRLASLSSALLA 629
Cdd:PRK11809 560 NGANTSFVNRIADTSLPLDELVADPVEAVEKLAqqegQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 630 SAHHPWRAAPMLEDnEIAVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLE 709
Cdd:PRK11809 640 SAHQKWQAAPMLED-PVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLME 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 710 AQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNT 789
Cdd:PRK11809 719 AQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNS 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 790 VLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLDPEGKPI 869
Cdd:PRK11809 799 VLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPI 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 870 PLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGP 949
Cdd:PRK11809 879 PLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGP 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 950 VIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGG--AQGTFVPPTLIELDSIDELKREVFGPVLHVVRYRRNQLDKLLEQI 1027
Cdd:PRK11809 959 VIDAEAKANIERHIQAMRAKGRPVFQAARENSEdwQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQI 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1028 RTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQRLLATRPAGlpkSL 1107
Cdd:PRK11809 1039 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPED---AL 1115
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1108 ADALivDAPQAGANGDNRGGDNPSAALTAYRDWLIgEQQPVLAARVDGYLSHVLAGATAVLSGPTGERNTYTLGARGTVL 1187
Cdd:PRK11809 1116 AVTL--ARQDAEYPVDAQLRAALLAPLTALREWAA-EREPELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVL 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1188 CIASTASGARVQFAAALATGNRALF-EGAAGEQLVSQLPAALKSYASVKK---SADTPFDAVLFEGDSDELLALVKEVAK 1263
Cdd:PRK11809 1193 CLADTEQDALTQLAAVLAVGSQALWpDDALHRALVAALPAAVQARIQLAKdwqLADQPFDAVLFHGDSDQLRALCEQVAQ 1272
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|.
gi 1024315852 1264 RAGPIVSVQGVAaraleSGDDDYALERLLTERSVSVNTAAAGGNANLMTIG 1314
Cdd:PRK11809 1273 RDGPIVSVQGFA-----RGETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
78-1314 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 2094.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 78 PFLEFAQNVQPQSVLRAAITAAYRRPEPECVPFLLGQARLPANLAGDVQAMAGKLVETLRTKSKGGGVEGLIHEFSLSSQ 157
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTGVEALLQEYSLSSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 158 EGVALMCLAEALLRIPDRATRDALIRDKISKGDWKSHVGQAPSLFVNAATWGLMITGKLVTTNSETGLSSALTRLIGKGG 237
Cdd:PRK11905 81 EGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIARLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 238 EPLIRKGVDMAMRLMGEQFVTGENISEALANSRKYEARGFRYSYDMLGEAATTEADAQRYYASYEQAIHAIGKAAGGRGI 317
Cdd:PRK11905 161 EPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 318 YEGPGISIKLSALHARYSRSQQERAMSELLPRVRSLAVLARRYDIGLNIDAEEADRLEISLDLLEALCFDPELAGWNGIG 397
Cdd:PRK11905 241 YDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 398 FVVQAYQKRCPFVIDYIVDLARRSRHRIMVRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLGAPDAV 477
Cdd:PRK11905 321 FVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 478 YPQFATHNAHTLSAIYHLAGNNYypgQYEFQCLHGMGEPLYEEVTGRDKLNRPCRVYAPVGTHETLLAYLVRRLLENGAN 557
Cdd:PRK11905 401 YPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGAN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 558 TSFVNRIADENVAIKDLIADPVDEASKIVplGAPHAKIPLPRNLFGAERLNSMGLDLSNEHRLASLSSALLASAHHPWRA 637
Cdd:PRK11905 478 SSFVNRIVDENVPVEELIADPVEKVAAMG--VAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAAKTWHA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 638 APMLEDNEiAVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMG 717
Cdd:PRK11905 556 APLLAGGD-VDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFA 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 718 LVVREAGKSLANAVAEIREAIDFLRYYSTQIRNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQ 797
Cdd:PRK11905 635 LAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQ 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 798 TPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpeGKPIPLIAETGG 877
Cdd:PRK11905 715 TPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GPPVPLIAETGG 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 878 QNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKR 957
Cdd:PRK11905 792 QNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQA 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 958 GIDAHVAAMREKGRKVEQLPMPEGGAQGTFVPPTLIELDSIDELKREVFGPVLHVVRYRRNQLDKLLEQIRTTGYGLTLG 1037
Cdd:PRK11905 872 NIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFG 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1038 IHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQRLLATRPAglpksladaliVDAPQ 1117
Cdd:PRK11905 952 LHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPT-----------PIPPA 1020
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1118 AGANgdnrggdNPSAALTAYRDWLIGEQQPVLAARVDGYLSHVLAGATAVLSGPTGERNTYTLGARGTVLCIASTASGAR 1197
Cdd:PRK11905 1021 HESV-------DTDAAARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVADTEEALL 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1198 VQFAAALATGNRALFEGAAG-EQLVSQLPAALKSYASVKKS--ADTPFDAVLFEGDSDELLALVKEVAKRAGPIVSVQGV 1274
Cdd:PRK11905 1094 RQLAAALATGNVAVVAADSGlAAALADLPGLVAARIDWTQDweADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAA 1173
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|
gi 1024315852 1275 aaraleSGDDDYALERLLTERSVSVNTAAAGGNANLMTIG 1314
Cdd:PRK11905 1174 ------EPTDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
80-1095 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1611.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 80 LEFAQNVQPQSVLRAAITAAYRRPEPECVPFLLGQARLPANLAGDVQAMAGKLVETLRTKSKG-GGVEGLIHEFSLSSQE 158
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKlGGIDAFLQEYSLSTEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 159 GVALMCLAEALLRIPDRATRDALIRDKISKGDWKSHVGQAPSLFVNAATWGLMITGKLVTTNSETG--LSSALTRLIGKG 236
Cdd:PRK11904 81 GIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADgtPSGVLKRLVNRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 237 GEPLIRKGVDMAMRLMGEQFVTGENISEALANSRKYEARGFRYSYDMLGEAATTEADAQRYYASYEQAIHAIGKAAGGRG 316
Cdd:PRK11904 161 GEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 317 IYEGPGISIKLSALHARYSRSQQERAMSELLPRVRSLAVLARRYDIGLNIDAEEADRLEISLDLLEALCFDPELAGWNGI 396
Cdd:PRK11904 241 LPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 397 GFVVQAYQKRCPFVIDYIVDLARRSRHRIMVRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLGAPDA 476
Cdd:PRK11904 321 GLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 477 VYPQFATHNAHTLSAIYHLAGNnyypGQYEFQCLHGMGEPLYEEVtgRDKLNRPCRVYAPVGTHETLLAYLVRRLLENGA 556
Cdd:PRK11904 401 IYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDAL--LDAPGIPCRIYAPVGSHKDLLPYLVRRLLENGA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 557 NTSFVNRIADENVAIKDLIADPVDEASKivPLGAPHAKIPLPRNLFGAERLNSMGLDLSNEHRLASLSSALLASAHHPWR 636
Cdd:PRK11904 475 NSSFVHRLVDPDVPIEELVADPVEKLRS--FETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 637 AAPMLedneIAVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLM 716
Cdd:PRK11904 553 AGPII----NGEGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELI 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 717 GLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNEFSNDTHRPlGPV--------------VCISPWNFPLAIFMGQVAA 782
Cdd:PRK11904 629 ALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLP-GPTgesnelrlhgrgvfVCISPWNFPLAIFLGQVAA 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 783 ALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRl 862
Cdd:PRK11904 708 ALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAAR- 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 863 dpEGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDR 942
Cdd:PRK11904 787 --DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRL 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 943 LSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGGAQGTFVPPTLIELDSIDELKREVFGPVLHVVRYRRNQLDK 1022
Cdd:PRK11904 865 LSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDK 944
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024315852 1023 LLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQRL 1095
Cdd:PRK11904 945 VIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRF 1017
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
78-1311 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1570.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 78 PFLEFAQNVQPQSVLRAAITAAYRRPEPECVPFLLGQARLPANLAGDVQAMAGKLVETLRTKSKGGGVEGLIHEFSLSSQ 157
Cdd:COG4230 2 PFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 158 EGVALMCLAEALLRIPDRATRDALIRDKISKGDWKSHVGQAPSLFVNAATWGLMITGKLVTTNSETGLSSALTRLIGKGG 237
Cdd:COG4230 82 EALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 238 EPLIRKGVDMAMRLMGEQFVTGENISEALANSRKYEARGFRYSYDMLGEAATTEADAQRYYASYEQAIHAIGKAAGGRGI 317
Cdd:COG4230 162 RPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGSG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 318 YEGPGISIKLSALHARYSRSQQERAMSELLPRVRSLAVLARRYDIGLNIDAEEADRLEISLDLLEALCFDPELAGWNGIG 397
Cdd:COG4230 242 GPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 398 FVVQAYQKRCPFVIDYIVDLARRSRHRIMVRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLGAPDAV 477
Cdd:COG4230 322 GGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 478 YPQFATHNAHTLSAIYHLAGNNYYPGQYEFQCLHGMGEPLYEEVtGRDKLNRPCRVYAPVGTHETLLAYLVRRLLENGAN 557
Cdd:COG4230 402 QPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQV-GRGKLGRPCRIYAPVGSHEDLLAYLVRRLLENGAN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 558 TSFVNRIADENVAIKDLIADPVDEASKIVplGAPHAKIPLPRNLFGAERLNSMGLDLSNEHRLASLSSALLASAHHPWRA 637
Cdd:COG4230 481 SSFVNRIADEDVPVEELIADPVEKARALG--GAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 638 APMLeDNEIAVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMG 717
Cdd:COG4230 559 APLI-AGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMA 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 718 LVVREAGKSLANAVAEIREAIDFLRYYSTQIRNEFSNDT-HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:COG4230 638 LLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAE 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRldpEGKPIPLIAETG 876
Cdd:COG4230 718 QTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR---DGPIVPLIAETG 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAK 956
Cdd:COG4230 795 GQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEAR 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 957 RGIDAHVAAMREKGRKVEQLPMPEGGAQGTFVPPTLIELDSIDELKREVFGPVLHVVRYRRNQLDKLLEQIRTTGYGLTL 1036
Cdd:COG4230 875 ANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATGYGLTL 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1037 GIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQRLLATRPaglpksladaLIVDAP 1116
Cdd:COG4230 955 GVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERT----------VTVNTT 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1117 QAGANgdnrggdnpsAALTAYRDWLIGeqqpvlaarvdgylshvlAGATAVLSGPTGERNTYTLGARGTVLCIASTASGA 1196
Cdd:COG4230 1025 AAGGN----------ASLLALGDWLAS------------------LLGALTLPGPTGERNTLTLRPRGRVLCLADSLEAL 1076
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1197 RVQFAAALATGNRALFegaAGEQLVSQLPAALksyasvkksaDTPFDAVLFEGdsdELLALVKEVAKRAGPIVSVQGVaa 1276
Cdd:COG4230 1077 LAQLAAALATGNRAVV---AADLALAGLPAVL----------LPPFDAVLFEG---RLRALRQALAARDGAIVPVIDA-- 1138
|
1210 1220 1230
....*....|....*....|....*....|....*
gi 1024315852 1277 ralesgddDYALERLLTErsvsvntaaAGGNANLM 1311
Cdd:COG4230 1139 --------GYDLERLLEE---------AGGNASLM 1156
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
600-1100 |
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: 714.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 600 NLFGAERLNSMGLDLSNEHRLASLSSALLASAHHPWRAAPMLEDNEIAVGAARDVRNPADHRDLVGTVVEATSEHVSAAL 679
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 680 AHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNEFSNDTHRP 759
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 760 LGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRT 839
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 840 RAVMFTGSTEVARLINKTLSNRLDPegkPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQED 919
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 920 VADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGGA--QGTFVPPTLIELDS 997
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRAcqHGTFVAPTLFELDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 998 IDELKREVFGPVLHVVRYRRNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGE 1077
Cdd:TIGR01238 398 IAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQ 477
|
490 500
....*....|....*....|...
gi 1024315852 1078 GLSGTGPKAGGALYLQRLLATRP 1100
Cdd:TIGR01238 478 GLSGTGPKAGGPHYLYRLTQVQY 500
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
556-1104 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 696.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 556 ANTSFVNRIADENVaikdliadpvdeaskivPLGAPHAKIPLPRnlfgaerlnsmgldlsnehrlaslssallasaHHPW 635
Cdd:cd07125 1 ANSSFVNRIFDLEV-----------------PLEALADALKAFD--------------------------------EKEW 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 636 RAAPMLEDNEIAVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTL 715
Cdd:cd07125 32 EAIPIINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGEL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 716 MGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNEFS-----------NDTH-RPLGPVVCISPWNFPLAIFMGQVAAA 783
Cdd:cd07125 112 IALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 784 LAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRld 863
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAER-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 864 pEGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRL 943
Cdd:cd07125 270 -DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 944 SIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGgaQGTFVPPTLIELDSIDELKREVFGPVLHVVRYRRNQLDKL 1023
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDG--NGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1024 LEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQRLLATRPAGL 1103
Cdd:cd07125 427 IEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSL 506
|
.
gi 1024315852 1104 P 1104
Cdd:cd07125 507 N 507
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
115-1111 |
0e+00 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 676.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 115 ARLPANLAGDVQAMAGKLVETLRtKSKGGGVEGLIHEFSLSSQEGVALMCLAEALLRIPDRATRDALIRDKISKgdwksh 194
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIR-AAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 195 vgqAPSLFVNAATWGLMITgklvttnsetglssaltrLIGKGGEPLIRKGVDMAMRLMGEQFVTGENISEALANSRKYEA 274
Cdd:COG0506 76 ---SPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 275 RGFRYSYDMLGEAATTEADAQRYYASYEQAIHAIGKAAggrgiYEGPGISIKLSALHARYSRSQQERAMSELLPRVRSLA 354
Cdd:COG0506 135 KGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 355 VLARRYDIGLNIDAEEADRLEISLDLLEALCFDPELAGWNGIGFVVQAYQKRCPFVIDYIVDLARRSRHRIMVRLVKGAY 434
Cdd:COG0506 210 RAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 435 WDTEIKRAQVDGLeGYPVYTRKIYTDVSYLACAKKLLGAPDAVYPQFATHNAHTLSAIYHLAG-NNYYPGQYEFQCLHGM 513
Cdd:COG0506 290 WDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGeRGRPPDRFEFQMLYGM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 514 GEPLYEEVTGRDK--LNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADENVAIKDLIADPVDEASkiVPLGAP 591
Cdd:COG0506 369 GEDLQRALAAVDGgrLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAA--LAAPTP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 592 HAKIPLPRNLFGAERLNSMGLDLSNEHRLASLSSALLASAHHPWRAAPMLEDNEIAVGAARDVRNPADHRDLVGTVVEAT 671
Cdd:COG0506 447 PPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 672 SEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNE 751
Cdd:COG0506 527 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAA 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 752 F-------SNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPG 824
Cdd:COG0506 607 AppppppgGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLV 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 825 DGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLDPEGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSA 904
Cdd:COG0506 687 LGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASA 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 905 GQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPE-GGA 983
Cdd:COG0506 767 SASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLvPGL 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 984 QGTFVPPTLIELDSIDELKREVFGPVLHVVRYRRNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRN 1063
Cdd:COG0506 847 LTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGG 926
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*...
gi 1024315852 1064 VIGAVVGVQPFGGEGLSGTGPKAGGALYLQRLLATRPAGLPKSLADAL 1111
Cdd:COG0506 927 GGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAA 974
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
265-563 |
1.77e-153 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 463.50 E-value: 1.77e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 265 ALANSRKYEARGFRYSYDMLGEAATTEADAQRYYASYEQAIHAIGKAAGGRGIYEGPGISIKLSALHARYSRSQQERAMS 344
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 345 ELLPRVRSLAVLARRYDIGLNIDAEEADRLEISLDLLEALCFDPELAGWNGIGFVVQAYQKRCPFVIDYIVDLARRSRHR 424
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 425 IMVRLVKGAYWDTEIKRAQVdGLEGYPVYTRKIYTDVSYLACAKKLLGAPDAVYPQFATHNAHTLSAIYHLAG-NNYYPG 503
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEeLGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 504 QYEFQCLHGMGEPLYEEVTGRDklnRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNR 563
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAAG---YRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
635-1096 |
3.00e-147 |
|
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: 455.50 E-value: 3.00e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 635 WRAAPMLE-DNEIAVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMH 713
Cdd:cd07083 16 GRAYPLVIgGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 714 TLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRN-------------EFSNDTHRPLGPVVCISPWNFPLAIFMGQV 780
Cdd:cd07083 96 ELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRlrypavevvpypgEDNESFYVGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 781 AAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSN 860
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 861 RLDPEGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNP 940
Cdd:cd07083 256 LAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 941 DRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGgaQGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYRRN 1018
Cdd:cd07083 336 EENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEG--EGYFVAPTVVEEVPPKAriAQEEIFGPVLSVIRYKDD 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024315852 1019 QLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQRLL 1096
Cdd:cd07083 414 DFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFL 491
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
653-1093 |
3.51e-127 |
|
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: 402.37 E-value: 3.51e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07124 49 ESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRYYSTQIRN-----------EFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 801
Cdd:cd07124 129 DVAEAIDFLEYYAREMLRlrgfpvemvpgEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 802 AAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLDPEGKPIPLIAETGGQNAM 881
Cdd:cd07124 209 AAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 882 IVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDA 961
Cdd:cd07124 289 IVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 962 HVAAMREKGRKVEQLPMPEGGAQGTFVPPTLIE-LDSIDEL-KREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIH 1039
Cdd:cd07124 369 YIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFAdVPPDHRLaQEEIFGPVLAVIKAK--DFDEALEIANDTEYGLTGGVF 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1024315852 1040 TRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQ 1093
Cdd:cd07124 447 SRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLL 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
649-1089 |
1.85e-120 |
|
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: 383.32 E-value: 1.85e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:COG1012 20 GETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NAVAEIREAIDFLRYYSTQIR------------NEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:COG1012 99 EARGEVDRAADFLRYYAGEARrlygetipsdapGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETG 876
Cdd:COG1012 179 QTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVTLELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAK 956
Cdd:COG1012 253 GKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 957 RGIDAHVAAMREKGRKVEQLPMPEGGAQGTFVPPTLIE-LDSIDEL-KREVFGPVLHVVRYRRnqLDKLLEQIRTTGYGL 1034
Cdd:COG1012 333 ERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLAdVTPDMRIaREEIFGPVLSVIPFDD--EEEAIALANDTEYGL 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1024315852 1035 TLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGvQPFGGEGLSGTGPKAGGA 1089
Cdd:COG1012 411 AASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGRE 464
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
653-1087 |
6.08e-114 |
|
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: 364.93 E-value: 6.08e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:pfam00171 10 EVINPATG-EVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRYYSTQIR-----------NEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 801
Cdd:pfam00171 89 EVDRAIDVLRYYAGLARrldgetlpsdpGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 802 AAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAM 881
Cdd:pfam00171 169 ALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 882 IVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDA 961
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 962 HVAAMREKGRKVEqLPMPEGGAQGTFVPPTLIE-LDSIDEL-KREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIH 1039
Cdd:pfam00171 323 YVEDAKEEGAKLL-TGGEAGLDNGYFVEPTVLAnVTPDMRIaQEEIFGPVLSVIRF--KDEEEAIEIANDTEYGLAAGVF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1024315852 1040 TRIDETIAHVISRAHVGNIYVNRNVIGAVVGVqPFGGEGLSGTGPKAG 1087
Cdd:pfam00171 400 TSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFGREGG 446
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
687-1099 |
2.61e-110 |
|
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: 354.21 E-value: 2.61e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 687 PIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIR------------NEFSN 754
Cdd:cd07078 12 KAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARrlhgevipspdpGELAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 755 DTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALV 834
Cdd:cd07078 92 VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 835 ADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVL 914
Cdd:cd07078 172 SHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 915 CLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGGAQGTFVPPTLIE 994
Cdd:cd07078 246 LVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 995 -LDSIDEL-KREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRiDETIAH-VISRAHVGNIYVNRNVIGAVVGv 1071
Cdd:cd07078 326 dVDPDMPIaQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTR-DLERALrVAERLEAGTVWINDYSVGAEPS- 401
|
410 420
....*....|....*....|....*...
gi 1024315852 1072 QPFGGEGLSGTGpKAGGALYLQRLLATR 1099
Cdd:cd07078 402 APFGGVKQSGIG-REGGPYGLEEYTEPK 428
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
656-1093 |
6.22e-110 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 356.17 E-value: 6.22e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 656 NPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIR 735
Cdd:PRK03137 56 NPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 736 EAIDFLRYYSTQI---------------RNEFSndtHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 800
Cdd:PRK03137 136 EAIDFLEYYARQMlkladgkpvesrpgeHNRYF---YIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 801 IAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINkTLSNRLDPEGKPIP-LIAETGGQN 879
Cdd:PRK03137 213 IAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIY-ERAAKVQPGQIWLKrVIAEMGGKD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 880 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSiDVGPVIDLDAKRGI 959
Cdd:PRK03137 292 AIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 960 DAHVAAMREKGRKVeqLPMPEGGAQGTFVPPTLI-ELDSIDEL-KREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLG 1037
Cdd:PRK03137 371 MSYIEIGKEEGRLV--LGGEGDDSKGYFIQPTIFaDVDPKARImQEEIFGPVVAFIKAK--DFDHALEIANNTEYGLTGA 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1038 IHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQ 1093
Cdd:PRK03137 447 VISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
656-1099 |
5.46e-107 |
|
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: 348.01 E-value: 5.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 656 NPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIR 735
Cdd:TIGR01237 52 NPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 736 EAIDFLRYYSTQI--------RNEFSNDTHR----PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 803
Cdd:TIGR01237 132 EAIDFMEYYARQMielakgkpVNSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 804 QAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSnRLDPEGKPIP-LIAETGGQNAMI 882
Cdd:TIGR01237 212 KFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAA-KVQPGQKHLKrVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 883 VDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAH 962
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 963 VAAMREKGRKVeqLPMPEGGAQGTFVPPTLI-ELDSIDEL-KREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHT 1040
Cdd:TIGR01237 371 IEIGKAEGRLV--SGGCGDDSKGYFIGPTIFaDVDRKARLaQEEIFGPVVAFIRAS--DFDEALEIANNTEYGLTGGVIS 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024315852 1041 RIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLQRLLATR 1099
Cdd:TIGR01237 447 NNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAK 505
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
646-1088 |
4.00e-90 |
|
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: 300.32 E-value: 4.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 646 IAVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGK 725
Cdd:cd07097 10 VAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 726 SLANAVAEIREAIDFLRYYSTQ-----------IRNEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAK 793
Cdd:cd07097 90 TLPEARGEVTRAGQIFRYYAGEalrlsgetlpsTRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 794 PAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRldpeGKPIPLia 873
Cdd:cd07097 170 PAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR----GARVQL-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 874 ETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDL 953
Cdd:cd07097 244 EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 954 DAKRGIDAHVAAMREKGRKV----EQLPMPEGgaqGTFVPPTLIElDSIDEL---KREVFGPVLHVVRYRrnQLDKLLEQ 1026
Cdd:cd07097 324 RQLEKDLRYIEIARSEGAKLvyggERLKRPDE---GYYLAPALFA-GVTNDMriaREEIFGPVAAVIRVR--DYDEALAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1027 IRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVqPFGGEGLSGTGPKAGG 1088
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQG 458
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
687-1087 |
2.46e-84 |
|
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: 280.27 E-value: 2.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 687 PIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIR------------NEFSN 754
Cdd:cd06534 8 KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADklggpelpspdpGGEAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 755 DTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALV 834
Cdd:cd06534 88 VRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 835 ADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVL 914
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 915 CLQEDVADRTLEMLTGamreLSVGNPDRLSIdvgpvidldakrgidahvaaMREkgrkveqlpmpeggaqgtfvpptlie 994
Cdd:cd06534 242 LVHESIYDEFVEKLVT----VLVDVDPDMPI--------------------AQE-------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 995 ldsidelkrEVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRiDETIAH-VISRAHVGNIYVNRNVIGAVVGvQP 1073
Cdd:cd06534 272 ---------EIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTR-DLNRALrVAERLRAGTVYINDSSIGVGPE-AP 338
|
410
....*....|....
gi 1024315852 1074 FGGEGLSGTGPKAG 1087
Cdd:cd06534 339 FGGVKNSGIGREGG 352
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
647-1090 |
6.87e-84 |
|
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: 283.08 E-value: 6.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 647 AVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKS 726
Cdd:cd07131 11 ASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 727 LANAVAEIREAIDFLRYYS------------TQIRNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKP 794
Cdd:cd07131 91 LAEGRGDVQEAIDMAQYAAgegrrlfgetvpSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 795 AEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRldpeGKPIPLiaE 874
Cdd:cd07131 171 AEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP----NKRVAL--E 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 875 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLD 954
Cdd:cd07131 245 MGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 955 AKRGIDAHVAAMREKGRKVE---QLPMPEGGAQGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYrrNQLDKLLEQIRT 1029
Cdd:cd07131 325 QLEKVLNYNEIGKEEGATLLlggERLTGGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEV--SSLEEAIEIAND 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1030 TGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVqPFGGEGLSGTG-PKAGGAL 1090
Cdd:cd07131 403 TEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGhREAGTTA 463
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
654-1083 |
2.72e-83 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 280.09 E-value: 2.72e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAE 733
Cdd:cd07103 1 VINPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 734 IREAIDFLRYYSTQIRNEF------SNDTHR------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 801
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYgrtipsPAPGKRilvikqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 802 AAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAM 881
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV----KRVSL--ELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 882 IVDSSALAEQVVADVLQSSFDSAGQRC-SALRVLClQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGID 960
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 961 AHVAAMREKGRKVEQlpmpeGG----AQGTFVPPTLIE--LDSIDELKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGL 1034
Cdd:cd07103 313 ALVEDAVAKGAKVLT-----GGkrlgLGGYFYEPTVLTdvTDDMLIMNEETFGPVAPIIPFD--TEDEVIARANDTPYGL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1024315852 1035 TLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVvgVQPFGGEGLSGTG 1083
Cdd:cd07103 386 AAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
653-1087 |
8.26e-83 |
|
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: 279.83 E-value: 8.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHRDLVgTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07086 16 TSRNPANGEPIA-RVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRY------------YSTQIRNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 800
Cdd:cd07086 95 EVQEMIDICDYavglsrmlygltIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 801 IAAQAVRILREA----GVPAGAVQLLPGDGEtVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpeGKPIpliAETG 876
Cdd:cd07086 175 TAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRVL---LELG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAK 956
Cdd:cd07086 248 GNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 957 RGIDAHVAAMREKGRKVEQLP-MPEGGAQGTFVPPTLIEL--DSIDELKREVFGPVLHVVRYrrNQLDKLLEQIRTTGYG 1033
Cdd:cd07086 328 EKYLNAIEIAKSQGGTVLTGGkRIDGGEPGNYVEPTIVTGvtDDARIVQEETFAPILYVIKF--DSLEEAIAINNDVPQG 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1034 LTLGIHTRIDETIAHVISRA--HVGNIYVNRNVIGAVVGVqPFGGEGLSGTGPKAG 1087
Cdd:cd07086 406 LSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
645-1094 |
3.82e-77 |
|
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: 265.22 E-value: 3.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 645 EIAVGAARDVRNPADHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLL------EAQMHTLMGl 718
Cdd:cd07123 41 EVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgkyryELNAATMLG- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 719 vvreAGKslaNAV-AEIR---EAIDFLR---YYSTQI---------RNEFSNDTHRPL-GPVVCISPWNFPlAIfMGQVA 781
Cdd:cd07123 120 ----QGK---NVWqAEIDaacELIDFLRfnvKYAEELyaqqplsspAGVWNRLEYRPLeGFVYAVSPFNFT-AI-GGNLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 782 AALA-AGNTVLAKPAEqTPLIAAQAV-RILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLS 859
Cdd:cd07123 191 GAPAlMGNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 860 NRLDpEGKPIP-LIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVG 938
Cdd:cd07123 270 ENLD-RYRTYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 939 NPDRLSIDVGPVIDldaKRGIDAHVAAMrEKGRKVEQLPMPEGG----AQGTFVPPTLIELDSIDE--LKREVFGPVLHV 1012
Cdd:cd07123 349 DPDDFSNFMGAVID---EKAFDRIKGYI-DHAKSDPEAEIIAGGkcddSVGYFVEPTVIETTDPKHklMTEEIFGPVLTV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1013 VRYRRNQLDKLLEQIRTTG-YGLTLGIHTRIDETI--AHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGA 1089
Cdd:cd07123 425 YVYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIreATDALRNAAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSP 504
|
....*
gi 1024315852 1090 LYLQR 1094
Cdd:cd07123 505 LNLLR 509
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
649-1062 |
2.89e-75 |
|
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: 257.96 E-value: 2.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:cd07088 12 GETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NAVAEIREAIDFLRYYSTQIR--------NEFSNDT----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:cd07088 91 LARVEVEFTADYIDYMAEWARriegeiipSDRPNENififKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETG 876
Cdd:cd07088 171 ETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVSLELG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAK 956
Cdd:cd07088 245 GKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 957 RGIDAHVAAMREKGRKVEQlpmpeGGAQ-----GTFVPPTLIE-LDSIDEL-KREVFGPVLHVVRYrrNQLDKLLEQIRT 1029
Cdd:cd07088 325 DKVEEMVERAVEAGATLLT-----GGKRpegekGYFYEPTVLTnVRQDMEIvQEEIFGPVLPVVKF--SSLDEAIELAND 397
|
410 420 430
....*....|....*....|....*....|...
gi 1024315852 1030 TGYGLTLGIHTRIDETIAHVISRAHVGNIYVNR 1062
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
653-1083 |
5.33e-73 |
|
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: 251.11 E-value: 5.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07145 2 EVRNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLR---YYSTQIRNEFSN-------------DTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:cd07145 81 EVERTIRLFKlaaEEAKVLRGETIPvdayeynerriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKtlsnRLDPEGKPIplIAETG 876
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIAS----KAGGTGKKV--ALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAK 956
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 957 RGIDAHVAAMREKGRKVEQlpmpeGGA--QGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYrrNQLDKLLEQIRTTGY 1032
Cdd:cd07145 315 ERMENLVNDAVEKGGKILY-----GGKrdEGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKV--KDDEEAVEIANSTEY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1024315852 1033 GLTLGIHTRiDETIAHVISRA-HVGNIYVN---RNVIGAVvgvqPFGGEGLSGTG 1083
Cdd:cd07145 388 GLQASVFTN-DINRALKVARElEAGGVVINdstRFRWDNL----PFGGFKKSGIG 437
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
687-1087 |
2.39e-72 |
|
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: 249.39 E-value: 2.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 687 PIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYS------------TQIRNEFSN 754
Cdd:cd07114 35 GAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAgladkiegavipVDKGDYLNF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 755 DTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALV 834
Cdd:cd07114 115 TRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 835 ADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVL 914
Cdd:cd07114 195 EHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 915 CLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKV----EQLPMPEGGAqGTFVPP 990
Cdd:cd07114 269 LVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVltggERPSGADLGA-GYFFEP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 991 TLIELDSIDE--LKREVFGPVLHVVRYRRNqlDKLLEQIRTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVN---RNV 1064
Cdd:cd07114 348 TILADVTNDMriAQEEVFGPVLSVIPFDDE--EEAIALANDSEYGLAAGIWTR-DLARAHRVARAiEAGTVWVNtyrALS 424
|
410 420
....*....|....*....|...
gi 1024315852 1065 IGAvvgvqPFGGEGLSGTGPKAG 1087
Cdd:cd07114 425 PSS-----PFGGFKDSGIGRENG 442
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
653-1083 |
6.81e-72 |
|
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: 247.89 E-value: 6.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07149 2 EVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFL--------RYYSTQI--------RNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:cd07149 81 EVDRAIETLrlsaeeakRLAGETIpfdaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRldpegkpiPLIAETG 876
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--------KVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SALRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA 955
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 956 KRGIDAHVAAMREKGRKVEQlpmpEGGAQGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYRRnqLDKLLEQIRTTGYG 1033
Cdd:cd07149 312 AERIEEWVEEAVEGGARLLT----GGKRDGAILEPTVLTDVPPDMkvVCEEVFAPVVSLNPFDT--LDEAIAMANDSPYG 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1034 LTLGIHTRIDETIAHVISRAHVGNIYVNrNVIGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07149 386 LQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
654-1083 |
5.37e-69 |
|
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: 239.77 E-value: 5.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA- 732
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRYYSTQIR----------NEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 801
Cdd:cd07093 80 DIPRAAANFRFFADYILqldgesypqdGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 802 AAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAM 881
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 882 IVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDA 961
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 962 HVAAMREKGRKV------EQLPMPEGGAqgtFVPPTLIE-LDSIDEL-KREVFGPVLHVVRYrrNQLDKLLEQIRTTGYG 1033
Cdd:cd07093 314 YVELARAEGATIltgggrPELPDLEGGY---FVEPTVITgLDNDSRVaQEEIFGPVVTVIPF--DDEEEAIELANDTPYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1024315852 1034 LTLGIHTRiDETIAHVISRA-HVGNIYVN----RNVigavvgVQPFGGEGLSGTG 1083
Cdd:cd07093 389 LAAYVWTR-DLGRAHRVARRlEAGTVWVNcwlvRDL------RTPFGGVKASGIG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
687-1089 |
1.28e-68 |
|
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: 237.94 E-value: 1.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 687 PIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAE-------IREAIDFLRYYSTQIRNEFSND---- 755
Cdd:cd07095 14 PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEvaamagkIDISIKAYHERTGERATPMAQGravl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 756 THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETvGAALVA 835
Cdd:cd07095 94 RHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRET-GEALAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 836 DPRTRAVMFTGSTEVARLINKTLSNRldPEgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLC 915
Cdd:cd07095 173 HEGIDGLLFTGSAATGLLLHRQFAGR--PG---KILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 916 LQED-VADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAK-RGIDAHVAAMREKGRKVeqLPMPEGGAQGTFVPPTLI 993
Cdd:cd07095 248 VPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAaRYLLAQQDLLALGGEPL--LAMERLVAGTAFLSPGII 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 994 ELDSIDEL-KREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAvVGVQ 1072
Cdd:cd07095 326 DVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA-SSTA 402
|
410
....*....|....*...
gi 1024315852 1073 PFGGEGLSGTG-PKAGGA 1089
Cdd:cd07095 403 PFGGVGLSGNHrPSAYYA 420
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
654-1083 |
1.82e-68 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 237.81 E-value: 1.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPAdHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAE 733
Cdd:cd07106 1 VINPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 734 IREAIDFLRYYsTQIRNE----FSNDT------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 803
Cdd:cd07106 80 VGGAVAWLRYT-ASLDLPdeviEDDDTrrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 804 QAVRILREAgVPAGAVQLLPGDGEtVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIV 883
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 884 DSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPV---IDLDAKRGId 960
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVqnkMQYDKVKEL- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 961 ahVAAMREKGRKVEQLPMPEGGaQGTFVPPTLIelDSIDELKR----EVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTL 1036
Cdd:cd07106 310 --VEDAKAKGAKVLAGGEPLDG-PGYFIPPTIV--DDPPEGSRivdeEQFGPVLPVLKYS--DEDEVIARANDSEYGLGA 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1024315852 1037 GIHTRiDETIA-HVISRAHVGNIYVNRnvIGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07106 383 SVWSS-DLERAeAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
689-1083 |
4.80e-68 |
|
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: 236.27 E-value: 4.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 689 WQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLR------------YYSTQIRNEFSNDT 756
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILReaaglprrpegeILPSDVPGKESMVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 757 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP-----LIAaqavRILREAGVPAGAVQLLPGDGETVGA 831
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPKGVLNVVPGGGSEIGD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 832 ALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SA 910
Cdd:cd07104 172 ALVEHPRVRMISFTGSTAVGRHIGELAGRHL----KKVAL--ELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICmAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 911 LRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQlpmpEGGAQGTFVPP 990
Cdd:cd07104 246 GRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLT----GGTYEGLFYQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 991 TLieLDSIDE----LKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVI- 1065
Cdd:cd07104 321 TV--LSDVTPdmpiFREEIFGPVAPVIPFD--DDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVn 396
|
410
....*....|....*....
gi 1024315852 1066 -GAVVgvqPFGGEGLSGTG 1083
Cdd:cd07104 397 dEPHV---PFGGVKASGGG 412
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
655-1099 |
2.29e-67 |
|
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: 234.81 E-value: 2.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 655 RNPADHRDlVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEI 734
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 735 REAIDFLRYYSTQI-----------RNEFSND----THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 799
Cdd:cd07099 80 LLALEAIDWAARNAprvlaprkvptGLLMPNKkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 800 LIAAQAVRILREAGVPAGAVQLLPGDGETvGAALVaDPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQN 879
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGSVATGRKVMAAAAERL------IPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 880 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGI 959
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 960 DAHVAAMREKGRKVeQLPMPEGGAQGTFVPPT-LIELD-SIDELKREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLG 1037
Cdd:cd07099 312 RRHVDDAVAKGAKA-LTGGARSNGGGPFYEPTvLTDVPhDMDVMREETFGPVLPVMPV--ADEDEAIALANDSRYGLSAS 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1038 IHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGpKAGGALYLQRLLATR 1099
Cdd:cd07099 389 VFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPK 449
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
653-1083 |
4.51e-67 |
|
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: 234.77 E-value: 4.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQAT-PVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAV 731
Cdd:cd07082 19 EVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 732 AEIREAIDFLRY-----------YST------------QIRNEfsndthrPLGPVVCISPWNFPLAIFMGQVAAALAAGN 788
Cdd:cd07082 98 KEVDRTIDYIRDtieelkrldgdSLPgdwfpgtkgkiaQVRRE-------PLGVVLAIGPFNYPLNLTVSKLIPALIMGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 789 TVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTlsnrldpeGKP 868
Cdd:cd07082 171 TVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ--------HPM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 869 IPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVG 948
Cdd:cd07082 243 KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 949 PVIDLDAKRGIDAHVAAMREKGRKVEQlpmPEGGAQGTFVPPTLIELDSiDELK---REVFGPVLHVVRYrrNQLDKLLE 1025
Cdd:cd07082 323 PLIDPKSADFVEGLIDDAVAKGATVLN---GGGREGGNLIYPTLLDPVT-PDMRlawEEPFGPVLPIIRV--NDIEEAIE 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1026 QIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVN----RNvigavVGVQPFGGEGLSGTG 1083
Cdd:cd07082 397 LANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRG-----PDHFPFLGRKDSGIG 453
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
654-1087 |
9.16e-66 |
|
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: 230.32 E-value: 9.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPiwQATPVDaRADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAE 733
Cdd:cd07146 3 VRNPYTG-EVVGTVPAGTEEALREALALAASYRS--TLTRYQ-RSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 734 IREAIDFLRYYSTQIRNE----FSND-----------THR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQ 797
Cdd:cd07146 79 VGRAADVLRFAAAEALRDdgesFSCDltangkarkifTLRePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 798 TPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRldpegkpiPLIAETGG 877
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 878 QNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKR 957
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 958 GIDAHVAAMREKGRKVeqlpMPEGGAQGTFVPPTLieLDSIDE----LKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYG 1033
Cdd:cd07146 311 QIENRVEEAIAQGARV----LLGNQRQGALYAPTV--LDHVPPdaelVTEETFGPVAPVIRVK--DLDEAIAISNSTAYG 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1024315852 1034 LTLGIHTRIDETIAHVISRAHVGNIYVNrNVIGAVVGVQPFGGEGLSGTGPKAG 1087
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
656-1087 |
1.06e-65 |
|
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: 230.02 E-value: 1.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 656 NPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAV-AEI 734
Cdd:cd07115 3 NPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 735 REAIDFLRYYS----------TQIRNEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 803
Cdd:cd07115 82 PRAADTFRYYAgwadkiegevIPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 804 QAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIV 883
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNL----KRVSL--ELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 884 DSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHV 963
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 964 AAMREKGRKVEQlpmpeGG----AQGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYRRNQldkllEQIRT---TGYGL 1034
Cdd:cd07115 316 DVGREEGARLLT-----GGkrpgARGFFVEPTIFAAVPPEMriAQEEIFGPVVSVMRFRDEE-----EALRIangTEYGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1024315852 1035 TLGIHTRiDETIAH-VISRAHVGNIYVnrNVIGAVVGVQPFGGEGLSGTGPKAG 1087
Cdd:cd07115 386 AAGVWTR-DLGRAHrVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
653-1087 |
2.59e-65 |
|
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: 229.79 E-value: 2.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDA--RADCLARAADLLEAQMHTLMGLVVREAGKSL-AN 729
Cdd:cd07091 22 PTINPATE-EVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPreRGRLLNKLADLIERDRDELAALESLDNGKPLeES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 730 AVAEIREAIDFLRYY----------STQIRNEFSNDTHR-PLGpvVC--ISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:cd07091 101 AKGDVALSIKCLRYYagwadkiqgkTIPIDGNFLAYTRRePIG--VCgqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINK--TLSNRldpegKPIPLiaE 874
Cdd:cd07091 179 QTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEaaAKSNL-----KKVTL--E 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 875 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLD 954
Cdd:cd07091 252 LGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 955 AKRGIDAHVaamrEKGrKVEQLPMPEGGAQ----GTFVPPTlIELDSIDEL---KREVFGPVLHVVRYrrNQLDKLLEQI 1027
Cdd:cd07091 332 QFDKILSYI----ESG-KKEGATLLTGGERhgskGYFIQPT-VFTDVKDDMkiaKEEIFGPVVTILKF--KTEDEVIERA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1028 RTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVNR-NVIGAVVgvqPFGGEGLSGTGPKAG 1087
Cdd:cd07091 404 NDTEYGLAAGVFTK-DINKALRVSRAlKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
653-1083 |
1.18e-64 |
|
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: 226.93 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07094 2 DVHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLR---YYSTQIRNE-------FSNDTHR------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:cd07094 81 EVDRAIDTLRlaaEEAERIRGEeipldatQGSDNRLawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLsnrldpegkPIPLIA-ET 875
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA---------GGKRIAlEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 876 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA 955
Cdd:cd07094 232 GGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 956 KRGIDAHVAAMREKGRKVeqlpMPEGGAQGTFVPPTLIELDSIDEL--KREVFGPVLHVVRYrrNQLDKLLEQIRTTGYG 1033
Cdd:cd07094 312 AERVERWVEEAVEAGARL----LCGGERDGALFKPTVLEDVPRDTKlsTEETFGPVVPIIRY--DDFEEAIRIANSTDYG 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1034 LTLGIHTRIDETIAHVISRAHVGNIYVNRNVIgAVVGVQPFGGEGLSGTG 1083
Cdd:cd07094 386 LQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
662-1089 |
1.34e-64 |
|
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: 226.79 E-value: 1.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 662 DLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFL 741
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 742 RYYS---TQIRNEF--------SNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP-----LIAaqa 805
Cdd:cd07152 82 HEAAglpTQPQGEIlpsapgrlSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggvVIA--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 806 vRILREAGVPAGAVQLLPGDGEtVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIVDS 885
Cdd:cd07152 159 -RLFEEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHL----KKVSL--ELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 886 SALAEQVVADVLQSSFDSAGQRC-SALRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVA 964
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 965 AMREKGRKVEQlpmpeGG-AQGTFVPPTLI-----ELDSIDElkrEVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGI 1038
Cdd:cd07152 310 DSVAAGARLEA-----GGtYDGLFYRPTVLsgvkpGMPAFDE---EIFGPVAPVTVFD--SDEEAVALANDTEYGLSAGI 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1039 HTRIDETIAHVISRAHVGNIYVN-RNVIGAVVGvqPFGGEGLSGTGPKAGGA 1089
Cdd:cd07152 380 ISRDVGRAMALADRLRTGMLHINdQTVNDEPHN--PFGGMGASGNGSRFGGP 429
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
145-256 |
1.38e-64 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 213.91 E-value: 1.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 145 VEGLIHEFSLSSQEGVALMCLAEALLRIPDRATRDALIRDKISKGDWKSHVGQAPSLFVNAATWGLMITGKLVTTNSETG 224
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 1024315852 225 LSSALTRLIGKGGEPLIRKGVDMAMRLMGEQF 256
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
654-1083 |
1.79e-64 |
|
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: 226.73 E-value: 1.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPADHRdLVGTVVEATSEHVSAALAHAVAAAPIW--QATPVDaRADCLARAADLLEAQMHTLMGLVVREAGKSLANAV 731
Cdd:cd07109 1 VFDPSTGE-VFARIARGGAADVDRAVQAARRAFESGwlRLSPAE-RGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 732 AEIREAIDFLRYYSTQIrNEFSNDT------------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 799
Cdd:cd07109 79 ADVEAAARYFEYYGGAA-DKLHGETiplgpgyfvytvREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 800 LIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQN 879
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 880 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGnPDRLSIDVGPVIDLDAKRGI 959
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 960 DAHVAAMREKGRKV----EQLPMPEGGaqGTFVPPTLI-ELDSIDELKR-EVFGPVLHVVryrrnQLDKLLEQIRT---T 1030
Cdd:cd07109 311 EGFVARARARGARIvaggRIAEGAPAG--GYFVAPTLLdDVPPDSRLAQeEIFGPVLAVM-----PFDDEAEAIALangT 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1024315852 1031 GYGLTLGIHTRiDETIAHVISRA-HVGNIYVNRnvIGAVVGVQ-PFGGEGLSGTG 1083
Cdd:cd07109 384 DYGLVAGVWTR-DGDRALRVARRlRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
645-1083 |
1.87e-63 |
|
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: 224.50 E-value: 1.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 645 EIAVGAARDVRNPADhRDLVGTVVEATSEHVSAALAHAVAA--APIWQATPVDARADCLARAADLLEAQMHTLMGLVVRE 722
Cdd:cd07119 8 EAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 723 AGKSLANAVAEIREAIDFLRYYSTQIRNE-----------FSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVL 791
Cdd:cd07119 87 TGKTLRESEIDIDDVANCFRYYAGLATKEtgevydvpphvISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 792 AKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPL 871
Cdd:cd07119 167 IKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV----KKVAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 872 iaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVI 951
Cdd:cd07119 243 --ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 952 DLDAKRGIDAHVAAMREKGRKVE---QLPMPEGGAQGTFVPPTLIelDSIDE----LKREVFGPVLHVVRYRRNQldkll 1024
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVcggKRPTGDELAKGYFVEPTIF--DDVDRtmriVQEEIFGPVLTVERFDTEE----- 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024315852 1025 EQIRT---TGYGLTLGIHTRiDETIAH-VISRAHVGNIYVNRnvIGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07119 394 EAIRLandTPYGLAGAVWTK-DIARANrVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
654-1086 |
7.70e-63 |
|
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: 221.85 E-value: 7.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPAdHRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSL-ANAVA 732
Cdd:cd07108 1 VINPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRYY---STQIRNE--------FSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 801
Cdd:cd07108 80 EAAVLADLFRYFgglAGELKGEtlpfgpdvLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 802 AAQAVRILREAgVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAM 881
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 882 IVDSSALAEQVVADVLQSS-FDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGID 960
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 961 AHVA-AMREKGRKVEQL-PMPEGG--AQGTFVPPTLI-ELDSIDELKR-EVFGPVLHVVRYrrNQLDKLLEQIRTTGYGL 1034
Cdd:cd07108 313 GYIDlGLSTSGATVLRGgPLPGEGplADGFFVQPTIFsGVDNEWRLAReEIFGPVLCAIPW--KDEDEVIAMANDSHYGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1035 TLGIHTRIDETIAHVISRAHVGNIYVNRNViGAVVGvQPFGGEGLSGTGPKA 1086
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQGG-GQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
652-1088 |
1.76e-62 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 220.66 E-value: 1.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 652 RDVRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAV 731
Cdd:cd07150 1 FDDLNPADG-SVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 732 AEIREAIDFLRYYSTQIRN------------EFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 799
Cdd:cd07150 80 FETTFTPELLRAAAGECRRvrgetlpsdspgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 800 LIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQN 879
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHL----KKITL--ELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 880 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGI 959
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 960 DAHVAAMREKGRKVeqlpMPEGGAQGTFVPPTLIE--LDSIDELKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLG 1037
Cdd:cd07150 314 KRQVEDAVAKGAKL----LTGGKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPAK--DAEEALELANDTEYGLSAA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1024315852 1038 IHTRiDETIA-HVISRAHVGNIYVNRNVI--GAVVgvqPFGGEGLSGTGpKAGG 1088
Cdd:cd07150 388 ILTN-DLQRAfKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGG 436
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
653-1083 |
3.33e-61 |
|
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: 217.77 E-value: 3.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07085 19 DVYNPATGE-VIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIR---EAIDF--------LRYYSTQIRNEFsnDTH---RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 798
Cdd:cd07085 98 DVLrglEVVEFacsiphllKGEYLENVARGI--DTYsyrQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 799 PLIAAQAVRILREAGVPAGAVQLLPGDGETVGaALVADPRTRAVMFTGSTEVARLINKTLSNRldpeGKPIplIAETGGQ 878
Cdd:cd07085 176 PGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEYIYERAAAN----GKRV--QALGGAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 879 NAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRG 958
Cdd:cd07085 249 NHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKER 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 959 IDAHVA-AMRE------KGRKVEqlpmPEGGAQGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYrrNQLDKLLEQIRT 1029
Cdd:cd07085 329 IEGLIEsGVEEgaklvlDGRGVK----VPGYENGNFVGPTILDNVTPDMkiYKEEIFGPVLSIVRV--DTLDEAIAIINA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1024315852 1030 TGYGLTLGIHTRIDETIAHVISRAHVGNIYVnrNV-IGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07085 403 NPYGNGAAIFTRSGAAARKFQREVDAGMVGI--NVpIPVPLAFFSFGGWKGSFFG 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
654-1083 |
1.13e-60 |
|
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: 215.57 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIW-QATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07089 1 VINPATE-EVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 -EIREAIDFLRYYSTQIRN---EFSND-------------THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPA 795
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSfpwEFDLPvpalrggpgrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 796 EQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaET 875
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 876 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA 955
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 956 KRGIDAHVAAMREKG-RKVEQLPMPEGGAQGTFVPPTLieLDSIDE----LKREVFGPVLHVVRYrrnqlDKLLEQIR-- 1028
Cdd:cd07089 314 RDRVEGYIARGRDEGaRLVTGGGRPAGLDKGFYVEPTL--FADVDNdmriAQEEIFGPVLVVIPY-----DDDDEAVRia 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1029 -TTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGvqPFGGEGLSGTG 1083
Cdd:cd07089 387 nDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDA--PFGGYKQSGLG 440
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
649-1093 |
1.78e-60 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 216.48 E-value: 1.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHRDLVgTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:PLN02278 39 GKTFPVYNPATGEVIA-NVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NAVAEIREAIDFLRYYSTQIRNEFSN-------DT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:PLN02278 118 EAIGEVAYGASFLEYFAEEAKRVYGDiipspfpDRrllvlKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETG 876
Cdd:PLN02278 198 LTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV----KRVSL--ELG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SALRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA 955
Cdd:PLN02278 272 GNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 956 KRGIDAHVAAMREKGRKVEQlpmpeGGAQ----GTFVPPTLIELDSIDEL--KREVFGPVLHVVRYRRNQldkllEQIR- 1028
Cdd:PLN02278 351 VQKVESHVQDAVSKGAKVLL-----GGKRhslgGTFYEPTVLGDVTEDMLifREEVFGPVAPLTRFKTEE-----EAIAi 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1029 --TTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGvqPFGGEGLSGTG---PKAGGALYLQ 1093
Cdd:PLN02278 421 anDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLGregSKYGIDEYLE 488
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
653-1088 |
3.06e-60 |
|
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: 214.76 E-value: 3.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHRDLVgTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07130 15 TSISPANGEPIA-RVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRY--------YSTQIRNEFSNdtHR------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 798
Cdd:cd07130 94 EVQEMIDICDFavglsrqlYGLTIPSERPG--HRmmeqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 799 PL--IAAQAV--RILREAGVPAGAVQLLPGDGEtVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpeGKpipLIAE 874
Cdd:cd07130 172 PLtaIAVTKIvaRVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---GR---SLLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 875 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLD 954
Cdd:cd07130 245 LGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 955 AKRGIDAHVAAMREKGRKVEQlpmpeGGAQ----GTFVPPTLIELDSIDEL-KREVFGPVLHVVRYrrNQLDKLLEQIRT 1029
Cdd:cd07130 325 AVDNYLAAIEEAKSQGGTVLF-----GGKVidgpGNYVEPTIVEGLSDAPIvKEETFAPILYVLKF--DTLEEAIAWNNE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024315852 1030 TGYGLTLGIHTRIDETIAHVISRA--HVGNIYVNRNVIGAVVGvQPFGGEGLSGTGPKAGG 1088
Cdd:cd07130 398 VPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
649-1083 |
7.98e-60 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 213.23 E-value: 7.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHRDLvGTVVEATSEHVSAALAHAVAAAP--IWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKS 726
Cdd:cd07112 1 GETFATINPATGRVL-AEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 727 LANAVA-EIREAIDFLRYYSTQI-----------RNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKP 794
Cdd:cd07112 80 ISDALAvDVPSAANTFRWYAEAIdkvygevaptgPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 795 AEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLInktLSNRLDPEGKPIPLiaE 874
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRF---LEYSGQSNLKRVWL--E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 875 TGGQNAMIV-----DSSALAEQVVAdvlqSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGP 949
Cdd:cd07112 235 CGGKSPNIVfadapDLDAAAEAAAA----GIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 950 VIDLDAKRGIDAHVAAMREKGRKV----EQLpMPEGGaqGTFVPPTLIE-LDSIDELKR-EVFGPVLHVVRYrrNQLDKL 1023
Cdd:cd07112 311 LVSEAHFDKVLGYIESGKAEGARLvaggKRV-LTETG--GFFVEPTVFDgVTPDMRIAReEIFGPVLSVITF--DSEEEA 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024315852 1024 LEQIRTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVnrNVIGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07112 386 VALANDSVYGLAASVWTS-DLSRAHRVARRlRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
689-1087 |
6.10e-58 |
|
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: 207.55 E-value: 6.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 689 WQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNEF--------------SN 754
Cdd:cd07101 34 WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERLLkprrrrgaipvltrTT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 755 DTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALV 834
Cdd:cd07101 114 VNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 835 AdpRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVL 914
Cdd:cd07101 194 D--NADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 915 CLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVeqL----PMPEGGAqgTFVPP 990
Cdd:cd07101 266 YVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATV--LaggrARPDLGP--YFYEP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 991 TLieLDSIDE----LKREVFGPVLHVVRYRRnqLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIG 1066
Cdd:cd07101 342 TV--LTGVTEdmelFAEETFGPVVSIYRVAD--DDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAA 417
|
410 420
....*....|....*....|..
gi 1024315852 1067 AVVGVQ-PFGGEGLSGTGPKAG 1087
Cdd:cd07101 418 AWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
687-1083 |
1.28e-57 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 205.77 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 687 PIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYS---------TQIRNEFSND-- 755
Cdd:cd07100 13 LAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenaeafladEPIETDAGKAyv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 756 THRPLGPVVCISPWNFPLAifmgQV----AAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVgA 831
Cdd:cd07100 93 RYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQV-E 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 832 ALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SA 910
Cdd:cd07100 168 AIIADPRVRGVTLTGSERAGRAVAAEAGKNL----KKSVL--ELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCiAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 911 LRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEqlpmpEGGAQ----GT 986
Cdd:cd07100 242 KRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLL-----LGGKRpdgpGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 987 FVPPTLI-----ELDSIDElkrEVFGPVLHVVRYRRNQldkllEQIR---TTGYGLTLGIHTRIDETIAHVISRAHVGNI 1058
Cdd:cd07100 316 FYPPTVLtdvtpGMPAYDE---ELFGPVAAVIKVKDEE-----EAIAlanDSPFGLGGSVFTTDLERAERVARRLEAGMV 387
|
410 420
....*....|....*....|....*...
gi 1024315852 1059 YVNrnvigAVVGVQ---PFGGEGLSGTG 1083
Cdd:cd07100 388 FIN-----GMVKSDprlPFGGVKRSGYG 410
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
653-1083 |
1.58e-57 |
|
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: 206.58 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAG--KSLANA 730
Cdd:cd07138 17 DVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGapITLARA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 731 V------AEIREAIDFLRYYSTQIRNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQ 804
Cdd:cd07138 96 AqvglgiGHLRAAADALKDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAII 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 805 AVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIVD 884
Cdd:cd07138 176 LAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTV----KRVAL--ELGGKSANIIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 885 SSALAEQVVADVLQSSFDSAGQRCSAL-RVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHV 963
Cdd:cd07138 250 DDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 964 AAMREKGRKVEQ--LPMPEGGAQGTFVPPTLI-ELDSIDELKR-EVFGPVLHVVRYrrnqlDKLLEQIRT---TGYGLTL 1036
Cdd:cd07138 329 QKGIEEGARLVAggPGRPEGLERGYFVKPTVFaDVTPDMTIAReEIFGPVLSIIPY-----DDEDEAIAIandTPYGLAG 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1024315852 1037 GIHTRIDETIAHVISRAHVGNIYVNrnviGAVVGVQ-PFGGEGLSGTG 1083
Cdd:cd07138 404 YVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
654-1083 |
2.42e-57 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 206.00 E-value: 2.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAE 733
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 734 IREAIDFLRYYS----------TQIRNEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIA 802
Cdd:cd07090 80 IDSSADCLEYYAglaptlsgehVPLPGGSFAYTRRePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 803 AQAVRILREAGVPAGAVQLLPGDGETvGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMI 882
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 883 VDSSALAEQVVADVLQSSFDSAGQRCS-ALRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDA 961
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 962 HVAAMREKGRKV----EQLPMPEGGAQGTFVPPTLieLDSIDE----LKREVFGPVLHVVRYRRNqlDKLLEQIRTTGYG 1033
Cdd:cd07090 312 YIESAKQEGAKVlcggERVVPEDGLENGFYVSPCV--LTDCTDdmtiVREEIFGPVMSILPFDTE--EEVIRRANDTTYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1034 LTLGIHTRiDETIAH-VISRAHVGNIYVNR-NVIGAVVgvqPFGGEGLSGTG 1083
Cdd:cd07090 388 LAAGVFTR-DLQRAHrVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
649-1081 |
4.04e-57 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 206.35 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADhrdlvGTVV----EATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAG 724
Cdd:PRK09457 14 GEAFESRNPVS-----GEVLwqgnDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 725 KSLANAVAEI-----REAIDFLRYY--STQIRNEFSNDT----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAK 793
Cdd:PRK09457 89 KPLWEAATEVtaminKIAISIQAYHerTGEKRSEMADGAavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 794 PAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETvGAALVADPRTRAVMFTGSTEVARLINKTLSNRldPEgkpIPLIA 873
Cdd:PRK09457 169 PSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQ--PE---KILAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 874 ETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCS-ALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRlsiD----VG 948
Cdd:PRK09457 243 EMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDA---EpqpfMG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 949 PVIDLDAKRGIDAHVAAMREKGRKVeQLPMPEGGAQGTFVPPTLIELDSIDEL-KREVFGPVLHVVRYrrNQLDKLLEQI 1027
Cdd:PRK09457 320 AVISEQAAQGLVAAQAQLLALGGKS-LLEMTQLQAGTGLLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDFDEAIRLA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1024315852 1028 RTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAvVGVQPFGGEGLSG 1081
Cdd:PRK09457 397 NNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
689-1087 |
6.03e-57 |
|
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: 204.88 E-value: 6.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 689 WQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNeFSNDTHRPLGP------ 762
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLART-LHGDSYNNLGDdmlglv 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 763 -------VVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVA 835
Cdd:cd07118 116 lrepigvVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 836 DPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLC 915
Cdd:cd07118 196 HPDVDMVSFTGSTRVGKAIAAAAARNL----KKVSL--ELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 916 LQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKV----EQLPmpegGAQGTFVPPT 991
Cdd:cd07118 270 VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLllggERLA----SAAGLFYQPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 992 LIE--LDSIDELKREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVv 1069
Cdd:cd07118 346 IFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP- 422
|
410
....*....|....*...
gi 1024315852 1070 gVQPFGGEGLSGTGPKAG 1087
Cdd:cd07118 423 -ELPFGGFKQSGIGRELG 439
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
649-1083 |
1.46e-56 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 205.50 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:PRK09407 31 GPTREVTAPFTGE-PLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NAVAEIREAIDFLRYYSTQIRNEF--------------SNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKP 794
Cdd:PRK09407 110 HAFEEVLDVALTARYYARRAPKLLaprrragalpvltkTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 795 AEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVAdpRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAE 874
Cdd:PRK09407 190 DSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAGRRL------IGFSLE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 875 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLD 954
Cdd:PRK09407 262 LGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 955 AKRGIDAHVAAMREKGRKVEQ--LPMPEGGAqgTFVPPTLieLDSIDE---LKR-EVFGPVLHVVRYRRnqLDKLLEQIR 1028
Cdd:PRK09407 342 QLETVSAHVDDAVAKGATVLAggKARPDLGP--LFYEPTV--LTGVTPdmeLAReETFGPVVSVYPVAD--VDEAVERAN 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1029 TTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQ-PFGGEGLSGTG 1083
Cdd:PRK09407 416 DTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
653-1093 |
2.67e-56 |
|
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: 203.79 E-value: 2.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHrDLVGTVVEATSEHVSAALAHAVAA-APIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSL-ANA 730
Cdd:cd07144 26 KTVNPSTG-EVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 731 VAEIREAIDFLRYYS---TQIRNE-FSNDT-------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 799
Cdd:cd07144 105 LGDLDEIIAVIRYYAgwaDKIQGKtIPTSPnklaytlHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 800 LIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQN 879
Cdd:cd07144 185 LSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL----KAVTL--ECGGKS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 880 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELS-VGNPDRLSIDVGPVIDLDAKRG 958
Cdd:cd07144 259 PALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkVGSPFDDDTVVGPQVSKTQYDR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 959 IDAHVAAMREKGRKV--EQLPMPEGGAQGTFVPPTlIELDSIDE---LKREVFGPVLHVVRYRRNqlDKLLEQIRTTGYG 1033
Cdd:cd07144 339 VLSYIEKGKKEGAKLvyGGEKAPEGLGKGYFIPPT-IFTDVPQDmriVKEEIFGPVVVISKFKTY--EEAIKKANDTTYG 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024315852 1034 LTLGIHTRiDETIAHVISR-AHVGNIYVNRNVIGAvVGVqPFGGEGLSGTGP---KAGGALYLQ 1093
Cdd:cd07144 416 LAAAVFTK-DIRRAHRVAReLEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRelgEYGLETYTQ 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
689-1087 |
9.01e-56 |
|
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: 201.95 E-value: 9.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 689 WQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANA-VAEIREAIDFLRYYS---TQIRNE--------FSNDT 756
Cdd:cd07142 59 WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYYAgwaDKIHGMtlpadgphHVYTL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 757 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVAD 836
Cdd:cd07142 139 HEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 837 PRTRAVMFTGSTEVARLINKTLSNrldPEGKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCL 916
Cdd:cd07142 219 MDVDKVAFTGSTEVGKIIMQLAAK---SNLKPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 917 QEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKV----EQLpmpegGAQGTFVPPTL 992
Cdd:cd07142 294 HESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLitggDRI-----GSKGYYIQPTI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 993 IElDSIDELK---REVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVN-RNVIGA 1067
Cdd:cd07142 369 FS-DVKDDMKiarDEIFGPVQSILKFK--TVDEVIKRANNSKYGLAAGVFSK-NIDTANTLSRAlKAGTVWVNcYDVFDA 444
|
410 420
....*....|....*....|
gi 1024315852 1068 VVgvqPFGGEGLSGTGPKAG 1087
Cdd:cd07142 445 SI---PFGGYKMSGIGREKG 461
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
649-1087 |
1.81e-55 |
|
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: 201.22 E-value: 1.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHRdLVGTVVEATSEHVSAALAHAVAA--APIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKS 726
Cdd:cd07143 21 GGTVKVYNPSTGK-LITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 727 -LANAVAEIREAIDFLRYYS------------TQIRnEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAK 793
Cdd:cd07143 100 fGTAKRVDVQASADTFRYYGgwadkihgqvieTDIK-KLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 794 PAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRldpEGKPIPLia 873
Cdd:cd07143 179 PSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS---NLKKVTL-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 874 ETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGP-VID 952
Cdd:cd07143 254 ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPqVSQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 953 LDAKRgIDAHVAAMREKGRKVEqLPMPEGGAQGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYRRNQldKLLEQIRTT 1030
Cdd:cd07143 334 IQYER-IMSYIESGKAEGATVE-TGGKRHGNEGYFIEPTIFTDVTEDMkiVKEEIFGPVVAVIKFKTEE--EAIKRANDS 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024315852 1031 GYGLTLGIHTRIDETIAHVISRAHVGNIYVN-RNVIGAVVgvqPFGGEGLSGTGPKAG 1087
Cdd:cd07143 410 TYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
653-1083 |
2.24e-55 |
|
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: 200.49 E-value: 2.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHRdLVGTVVEATSEHVSAALAHAVAA--APIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAG---KSL 727
Cdd:cd07139 17 DVVSPATEE-VVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGmpiSWS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 728 ANAVAEIreAIDFLRYYSTQIRNeFSNDTHR-------------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKP 794
Cdd:cd07139 96 RRAQGPG--PAALLRYYAALARD-FPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 795 AEQTPLIAAQAVRILREAGVPAGAVQLLPGDGEtVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaE 874
Cdd:cd07139 173 SPETPLDAYLLAEAAEEAGLPPGVVNVVPADRE-VGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL----ARVTL--E 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 875 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSAL-RVLCLQEDvADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDL 953
Cdd:cd07139 246 LGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVPRSR-YDEVVEALAAAVAALKVGDPLDPATQIGPLASA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 954 DAKRGIDAHVAAMREKG-RKVEQLPMPEGGAQGTFVPPTLI-ELDSIDELKR-EVFGPVLHVVRYrrnqlDKLLEQIRT- 1029
Cdd:cd07139 325 RQRERVEGYIAKGRAEGaRLVTGGGRPAGLDRGWFVEPTLFaDVDNDMRIAQeEIFGPVLSVIPY-----DDEDDAVRIa 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024315852 1030 --TGYGLTLGIHTRIDETIAHVISRAHVGNIYVNrnviGAVVGVQ-PFGGEGLSGTG 1083
Cdd:cd07139 400 ndSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG 452
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
654-1083 |
2.67e-55 |
|
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: 199.91 E-value: 2.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAE 733
Cdd:cd07107 1 VINPATGQ-VLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 734 IREAIDFLRYYSTQIrNEFSNDT------------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 801
Cdd:cd07107 80 VMVAAALLDYFAGLV-TELKGETipvggrnlhytlREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 802 AAQAVRILREAgVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAM 881
Cdd:cd07107 159 ALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGI----KHVTL--ELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 882 IV----DSSALAEQVVADVlqsSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA-K 956
Cdd:cd07107 232 IVfpdaDPEAAADAAVAGM---NFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQyD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 957 RGIDAHVAAMREKGRKVEQLPMPEG--GAQGTFVPPT-LIELDSIDELKR-EVFGPVLHVVRYRrnQLDKLLEQIRTTGY 1032
Cdd:cd07107 309 RVMHYIDSAKREGARLVTGGGRPEGpaLEGGFYVEPTvFADVTPGMRIAReEIFGPVLSVLRWR--DEAEMVAQANGVEY 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1024315852 1033 GLTLGIHTRiDETIAH-VISRAHVGNIYVN---RNVIGAvvgvqPFGGEGLSGTG 1083
Cdd:cd07107 387 GLTAAIWTN-DISQAHrTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
653-1083 |
6.35e-55 |
|
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: 199.07 E-value: 6.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07151 13 DVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 E-------IREAIDF-LRYYSTQIRNEFSNDTHR----PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP- 799
Cdd:cd07151 92 EwgaamaiTREAATFpLRMEGRILPSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPi 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 800 ----LIAaqavRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTlsnrldpEGKPIPLIA-E 874
Cdd:cd07151 172 tgglLLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGEL-------AGRHLKKVAlE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 875 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLD 954
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 955 AKRGIDAHVAAMREKGRKVEQlpmpEGGAQGTFVPPT-LIELDSIDELKR-EVFGPVLHVVRYRRNqlDKLLEQIRTTGY 1032
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLV----GGEAEGNVLEPTvLSDVTNDMEIAReEIFGPVAPIIKADDE--EEALELANDTEY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1024315852 1033 GLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVqPFGGEGLSGTG 1083
Cdd:cd07151 395 GLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
656-1062 |
1.69e-54 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 197.47 E-value: 1.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 656 NPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIR 735
Cdd:cd07102 2 SPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 736 EAIDFLRYYSTQIRNEFSND------------THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 803
Cdd:cd07102 81 GMLERARYMISIAEEALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 804 QAVRILREAGVPAGAVQLLPGDGETvGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIV 883
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRF------IKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 884 DSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHV 963
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 964 AAMREKGRKVEqLPM---PEGGAQGTFVPPT-LIELD-SIDELKREVFGPVLHVVRYRRNqlDKLLEQIRTTGYGLTLGI 1038
Cdd:cd07102 314 ADAIAKGARAL-IDGalfPEDKAGGAYLAPTvLTNVDhSMRVMREETFGPVVGIMKVKSD--AEAIALMNDSEYGLTASV 390
|
410 420
....*....|....*....|....
gi 1024315852 1039 HTRIDETIAHVISRAHVGNIYVNR 1062
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
654-1083 |
3.32e-54 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 196.80 E-value: 3.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 654 VRNPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAE 733
Cdd:cd07110 1 VINPATEA-TIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 734 IREAIDFLRYYSTQIR--------------NEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 798
Cdd:cd07110 80 VDDVAGCFEYYADLAEqldakaeravplpsEDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 799 PLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQ 878
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDI----KPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 879 NAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRG 958
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 959 IDAHVAAMREKG-RKVEQLPMPEGGAQGTFVPPTLI---ELDSidELKR-EVFGPVLHVVRYRRNqlDKLLEQIRTTGYG 1033
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRRPAHLEKGYFIAPTVFadvPTDS--RIWReEIFGPVLCVRSFATE--DEAIALANDSEYG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1024315852 1034 LTLGIHTRIDETIAHVISRAHVGNIYVNRNvigAVVGVQ-PFGGEGLSGTG 1083
Cdd:cd07110 390 LAAAVISRDAERCDRVAEALEAGIVWINCS---QPCFPQaPWGGYKRSGIG 437
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
649-1081 |
1.14e-53 |
|
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 274486 Cd Length: 484 Bit Score: 196.09 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHRDLvGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:TIGR03240 12 GESFASRNPATQEVL-WQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVIARETGKPLW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NAVAEI-----REAIDfLRYYSTQIrNEFSNDT--------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPA 795
Cdd:TIGR03240 91 ETRTEVasmigKVAIS-IKAYHERT-GESENPMpdgravlrHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 796 EQTPLIAAQAVRILREAGVPAGAVQLLPGDGETvGAALVADPRTRAVMFTGSTEVARLINKTLSNRldPEgkpIPLIAET 875
Cdd:TIGR03240 169 ELTPWVAEETVKLWEKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFGGR--PE---KILALEM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 876 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCS-ALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSID-VGPVIDL 953
Cdd:TIGR03240 243 GGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTcARRLLVPDGAQGDAFLARLVEVAERLTVGAWDAEPQPfMGAVISL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 954 DA-KRGIDAHVAAMREKGRKVEQLPMPEGGAqgTFVPPTLIELDSIDEL-KREVFGPVLHVVRYrrNQLDKLLEQIRTTG 1031
Cdd:TIGR03240 323 RAaQRLLAAQAKLLALGGKSLLEMRQLDPGA--AFLTPGIIDVTGVAELpDEEHFGPLLQVIRY--TDFDEAIAIANNTR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1024315852 1032 YGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAvVGVQPFGGEGLSG 1081
Cdd:TIGR03240 399 FGLSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
664-1083 |
2.68e-53 |
|
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: 194.08 E-value: 2.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 664 VGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA-EIREAIDFLR 742
Cdd:cd07092 10 IATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdELPGAVDNFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 743 YYSTQIR-------NEFSNDT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILR 810
Cdd:cd07092 90 FFAGAARtlegpaaGEYLPGHtsmirREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 811 EaGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIVDSSALAE 890
Cdd:cd07092 170 E-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTL----KRVHL--ELGGKAPVIVFDDADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 891 QVVADVLQSSFDSAGQRC-SALRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREK 969
Cdd:cd07092 243 AAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 970 GRKVEQLPMPEGgaQGTFVPPTLI-ELDSIDEL-KREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRiDETIA 1047
Cdd:cd07092 322 ARVLTGGRRAEG--PGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSVWTR-DVGRA 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 1024315852 1048 HVISRA-HVGNIYVNRNviGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07092 397 MRLSARlDFGTVWVNTH--IPLAAEMPHGGFKQSGYG 431
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
687-1083 |
5.35e-53 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 192.41 E-value: 5.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 687 PIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYY---STQIRNEFSNDTH------ 757
Cdd:cd07105 14 PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAaslITQIIGGSIPSDKpgtlam 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 758 ---RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLL---PGDGETVGA 831
Cdd:cd07105 94 vvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEVVE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 832 ALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SA 910
Cdd:cd07105 174 ALIAHPAVRKVNFTGSTRVGRIIAETAAKHL----KPVLL--ELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICmST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 911 LRVLcLQEDVADRTLEMLTGAMRELSVGNPdrlsiDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGGAQGTFVPP 990
Cdd:cd07105 248 ERII-VHESIADEFVEKLKAAAEKLFAGPV-----VLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 991 TLieLDSIDELKR----EVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVNrnvi 1065
Cdd:cd07105 322 TI--LDNVTPDMDiyseESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR-DLARALAVAKRiESGAVHIN---- 392
|
410 420
....*....|....*....|.
gi 1024315852 1066 GAVVGVQ---PFGGEGLSGTG 1083
Cdd:cd07105 393 GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
653-1087 |
6.82e-53 |
|
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: 193.77 E-value: 6.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKslanAVA 732
Cdd:cd07111 40 PTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK----PIR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIRE-----AIDFLRYYSTQIR-NEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAV 806
Cdd:cd07111 115 ESRDcdiplVARHFYHHAGWAQlLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 807 RILREAGVPAGAVQLLPGDGETvGAALVADPRTRAVMFTGSTEVARLINKTLSNrldpEGKPIPLiaETGGQNAMIVDSS 886
Cdd:cd07111 195 EICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAG----TGKKLSL--ELGGKSPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 887 ALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAM 966
Cdd:cd07111 268 ADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 967 REKGRKVEQ--LPMPeggAQGTFVPPTLIE-LDSIDELKR-EVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRI 1042
Cdd:cd07111 348 RAEGADVFQpgADLP---SKGPFYPPTLFTnVPPASRIAQeEIFGPVLVVLTFR--TAKEAVALANNTPYGLAASVWSEN 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1024315852 1043 DETIAHVISRAHVGNIYVN-RNVIGAVVgvqPFGGEGLSGTGPKAG 1087
Cdd:cd07111 423 LSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFGREGG 465
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
689-1087 |
3.26e-52 |
|
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: 191.79 E-value: 3.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 689 WQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANA-VAEIREAIDFLRYY---STQIR--------NEFSNDT 756
Cdd:cd07141 63 WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYagwADKIHgktipmdgDFFTYTR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 757 HRPLGpvVC--ISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALV 834
Cdd:cd07141 143 HEPVG--VCgqIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAIS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 835 ADPRTRAVMFTGSTEVARLINKTL--SNRldpegKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALR 912
Cdd:cd07141 221 SHPDIDKVAFTGSTEVGKLIQQAAgkSNL-----KRVTL--ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 913 VLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQlpmpeGGA----QGTFV 988
Cdd:cd07141 294 RTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLEC-----GGKrhgdKGYFI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 989 PPTLIElDSIDEL---KREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTR-IDETIaHVISRAHVGNIYVNrnv 1064
Cdd:cd07141 369 QPTVFS-DVTDDMriaKEEIFGPVQQIFKFK--TIDEVIERANNTTYGLAAAVFTKdIDKAI-TFSNALRAGTVWVN--- 441
|
410 420
....*....|....*....|....
gi 1024315852 1065 IGAVVGVQ-PFGGEGLSGTGPKAG 1087
Cdd:cd07141 442 CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
697-1061 |
5.76e-52 |
|
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: 190.25 E-value: 5.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 697 RADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNE-----------FSNDTHRPLGPVVC 765
Cdd:cd07120 44 RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEagrmiepepgsFSLVLREPMGVAGI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 766 ISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREA-GVPAGAVQLLPGDGETVGAALVADPRTRAVMF 844
Cdd:cd07120 124 IVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 845 TGSTEVARLINKTLSNRLdpegKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRT 924
Cdd:cd07120 204 TGSTATGRAIMAAAAPTL----KRLGL--ELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 925 LEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKV--EQLPMPEGGAQGTFVPPTLIELD--SIDE 1000
Cdd:cd07120 278 RDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVvlRGGPVTEGLAKGAFLRPTLLEVDdpDADI 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1001 LKREVFGPVLHVVRYRRNqlDKLLEQIRTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVN 1061
Cdd:cd07120 358 VQEEIFGPVLTLETFDDE--AEAVALANDTDYGLAASVWTR-DLARAMRVARAiRAGTVWIN 416
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
649-1083 |
1.02e-51 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 190.12 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:PRK13473 16 GEKQPVYNPATG-EVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NAVA-EIREAIDFLRYYSTQIRN-------EFSNDtH------RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKP 794
Cdd:PRK13473 95 LALNdEIPAIVDVFRFFAGAARClegkaagEYLEG-HtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 795 AEQTPLIAAQAVRILREAgVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSnrldPEGKPIPLiaE 874
Cdd:PRK13473 174 SEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA----DSVKRTHL--E 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 875 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLd 954
Cdd:PRK13473 247 LGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISA- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 955 AKRgidAHVAAMREKGRKVEQLPMPEGGA----QGTFVPPTLI-ELDSIDEL-KREVFGPVLHVVRYRrnQLDKLLEQIR 1028
Cdd:PRK13473 326 AHR---DRVAGFVERAKALGHIRVVTGGEapdgKGYYYEPTLLaGARQDDEIvQREVFGPVVSVTPFD--DEDQAVRWAN 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1029 TTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVNRNVIgaVVGVQPFGGEGLSGTG 1083
Cdd:PRK13473 401 DSDYGLASSVWTR-DVGRAHRVSARlQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
653-1089 |
3.20e-51 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 188.80 E-value: 3.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADhRDLVGTVVEATSEHV-SAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA-NA 730
Cdd:cd07113 18 DITNPAT-EQVIASVASATEADVdAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHlSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 731 VAEIREAIDFLRYY---STQIRNE-------------FSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAK 793
Cdd:cd07113 97 AFEVGQSANFLRYFagwATKINGEtlapsipsmqgerYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 794 PAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGEtVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLia 873
Cdd:cd07113 177 PSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDL----TRVTL-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 874 ETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDL 953
Cdd:cd07113 250 ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 954 DAKRGIDAHVAAMREKGRKV----EQLPMPeggaqGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYRRNqlDKLLEQI 1027
Cdd:cd07113 330 PHFDKVCSYLDDARAEGDEIvrggEALAGE-----GYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDE--EELIQLI 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024315852 1028 RTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVN-RNVIGAVVgvqPFGGEGLSGTGPKAGGA 1089
Cdd:cd07113 403 NDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIGREFGSA 462
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
653-1083 |
3.26e-51 |
|
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: 187.84 E-value: 3.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHRDlVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:cd07147 2 EVTNPYTGEV-VARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRYY---STQIRNEFSN-DTHR------------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:cd07147 81 EVARAIDTFRIAaeeATRIYGEVLPlDISArgegrqglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGETvGAALVADPRTRAVMFTGSTEVARLInKTLSNRldpegKPIPLiaETG 876
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-----KKVVL--ELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SALRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA 955
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 956 KRGIDAHVAAMREKGRKVeqlpMPEGGAQGTFVPPTLIE-LDSIDEL-KREVFGPVLHVVRYRRnqLDKLLEQIRTTGYG 1033
Cdd:cd07147 311 AERVEGWVNEAVDAGAKL----LTGGKRDGALLEPTILEdVPPDMEVnCEEVFGPVVTVEPYDD--FDEALAAVNDSKFG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1024315852 1034 LTLGIHTRIDETIAHVISRAHVGNIyvnrnVIGAV----VGVQPFGGEGLSGTG 1083
Cdd:cd07147 385 LQAGVFTRDLEKALRAWDELEVGGV-----VINDVptfrVDHMPYGGVKDSGIG 433
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
653-1083 |
7.21e-51 |
|
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: 187.55 E-value: 7.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHRDLVgTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAV- 731
Cdd:cd07559 19 DNYNPVNGKVLC-EIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 732 AEIREAIDFLRYYSTQIR------NEFSNDT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 800
Cdd:cd07559 98 ADIPLAIDHFRYFAGVIRaqegslSEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 801 IAAQAVRILREAgVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNA 880
Cdd:cd07559 178 SILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------IPVTLELGGKSP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 881 MIVDSSALAEqvvadvlQSSFDSA------------GQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVG 948
Cdd:cd07559 251 NIFFDDAMDA-------DDDFDDKaeegqlgfafnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 949 PVIDLDAKRGIDAHVAAMREKGRKV----EQLPMPeGGAQGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYRRNqlDK 1022
Cdd:cd07559 324 AQVSKDQLEKILSYVDIGKEEGAEVltggERLTLG-GLDKGYFYEPTLIKGGNNDMriFQEEIFGPVLAVITFKDE--EE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024315852 1023 LLEQIRTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVN-RNVIGAVVgvqPFGGEGLSGTG 1083
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTR-DINRALRVARGiQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
696-1093 |
5.11e-48 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 180.02 E-value: 5.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 696 ARADCLARAADLLEAQMHTLMGLVVREAGKSLA-NAVAEIREAIDFLRYY----------STQIRNEFSNDT-HRPLGPV 763
Cdd:PLN02766 83 ERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAAAGLLRYYagaadkihgeTLKMSRQLQGYTlKEPIGVV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 764 VCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVM 843
Cdd:PLN02766 163 GHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 844 FTGSTEVARLINKTL--SNRldpegKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVA 921
Cdd:PLN02766 243 FTGSTEVGRKIMQAAatSNL-----KQVSL--ELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 922 DRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVaamrEKGRKvEQLPMPEGGA----QGTFVPPTlIELDS 997
Cdd:PLN02766 316 DEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYI----EHGKR-EGATLLTGGKpcgdKGYYIEPT-IFTDV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 998 IDEL---KREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVnrNVIGAVVGVQP 1073
Cdd:PLN02766 390 TEDMkiaQDEIFGPVMSLMKFK--TVEEAIKKANNTKYGLAAGIVTK-DLDVANTVSRSiRAGTIWV--NCYFAFDPDCP 464
|
410 420
....*....|....*....|...
gi 1024315852 1074 FGGEGLSGTGPKAG-GAL--YLQ 1093
Cdd:PLN02766 465 FGGYKMSGFGRDQGmDALdkYLQ 487
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
715-1093 |
2.11e-47 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 175.69 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 715 LMGLVVREAGKSLANAVAEIREAIDFL--------RYYSTQIRNEFSNDT----HRPLGPVVCISPWNFPLAIFMGQVAA 782
Cdd:PRK10090 15 ISALIVEEGGKIQQLAEVEVAFTADYIdymaewarRYEGEIIQSDRPGENillfKRALGVTTGILPWNFPFFLIARKMAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 783 ALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRL 862
Cdd:PRK10090 95 ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 863 dpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNP-D 941
Cdd:PRK10090 175 ------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPaE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 942 RLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGGAqGTFVPPTLIeLD---SIDELKREVFGPVLHVVRYrrN 1018
Cdd:PRK10090 249 RNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGK-GYYYPPTLL-LDvrqEMSIMHEETFGPVLPVVAF--D 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1019 QLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQP-FGGEGLSGTGPKAGGALYLQ 1093
Cdd:PRK10090 325 TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAgWRKSGIGGADGKHGLHEYLQ 400
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
649-1093 |
4.16e-47 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 176.64 E-value: 4.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:PRK11241 25 GEVIDVTNPANG-DKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NAVAEIREAIDFLRYYSTQIRNEFSnDT-------------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPA 795
Cdd:PRK11241 104 EAKGEISYAASFIEWFAEEGKRIYG-DTipghqadkrliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 796 EQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaET 875
Cdd:PRK11241 183 SQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI----KKVSL--EL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 876 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA 955
Cdd:PRK11241 257 GGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 956 KRGIDAHVAAMREKGRKVEQLPMPEgGAQGTFVPPT-LIEL-DSIDELKREVFGPVLHVVRYRRNqlDKLLEQIRTTGYG 1033
Cdd:PRK11241 337 VAKVEEHIADALEKGARVVCGGKAH-ELGGNFFQPTiLVDVpANAKVAKEETFGPLAPLFRFKDE--ADVIAQANDTEFG 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024315852 1034 LTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGvqPFGG---EGLSGTGPKAGGALYLQ 1093
Cdd:PRK11241 414 LAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYLE 474
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
649-1083 |
3.46e-46 |
|
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: 173.79 E-value: 3.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHRDLvGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:cd07117 15 GETIDSYNPANGETL-SEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NAVA-EIREAIDFLRYYSTQIR------NEFSNDT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:cd07117 94 ETRAvDIPLAADHFRYFAGVIRaeegsaNMIDEDTlsivlREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAgVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETG 876
Cdd:cd07117 174 TTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------IPATLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAK 956
Cdd:cd07117 247 GKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 957 RGIDAHVAAMREKGRKV---EQLPMPEGGAQGTFVPPTLIEldSIDELKR----EVFGPVLHVVRYRRNqlDKLLEQIRT 1029
Cdd:cd07117 327 DKILSYVDIAKEEGAKIltgGHRLTENGLDKGFFIEPTLIV--NVTNDMRvaqeEIFGPVATVIKFKTE--DEVIDMAND 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1030 TGYGLTLGIHTRiDETIAHVISRA-HVGNIYVNR-NVIGAVVgvqPFGGEGLSGTG 1083
Cdd:cd07117 403 SEYGLGGGVFTK-DINRALRVARAvETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
689-1087 |
4.33e-46 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 175.00 E-value: 4.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 689 WQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAV-AEIREAIDFLRYY---STQIR--------NEFSNDT 756
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMFARLFRYYagwADKIHgltvpadgPHHVQTL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 757 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVAD 836
Cdd:PLN02466 193 HEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 837 PRTRAVMFTGSTEVARLINKTLSNRldpEGKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCL 916
Cdd:PLN02466 273 MDVDKLAFTGSTDTGKIVLELAAKS---NLKPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 917 QEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA--------KRGIDAHvAAMREKGRKVeqlpmpegGAQGTFV 988
Cdd:PLN02466 348 HERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQfekilryiKSGVESG-ATLECGGDRF--------GSKGYYI 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 989 PPTLIElDSIDEL---KREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIHTRIDETiAHVISRA-HVGNIYVN-RN 1063
Cdd:PLN02466 419 QPTVFS-NVQDDMliaQDEIFGPVQSILKF--KDLDEVIRRANNTRYGLAAGVFTQNLDT-ANTLSRAlRVGTVWVNcFD 494
|
410 420
....*....|....*....|....
gi 1024315852 1064 VIGAVVgvqPFGGEGLSGTGPKAG 1087
Cdd:PLN02466 495 VFDAAI---PFGGYKMSGIGREKG 515
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
656-1087 |
1.12e-44 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 170.01 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 656 NPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIR 735
Cdd:PLN02315 40 NPANNQ-PIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 736 EAIDFLRY---YSTQIR---------NEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 803
Cdd:PLN02315 119 EIIDMCDFavgLSRQLNgsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 804 QAVRI----LREAGVPAGAVQLLPGdGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpeGKpipLIAETGGQN 879
Cdd:PLN02315 199 AMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GK---CLLELSGNN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 880 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGI 959
Cdd:PLN02315 272 AIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 960 DAHVAAMREKGRKVEQlpmpeGGA----QGTFVPPTLIELD-SIDELKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGL 1034
Cdd:PLN02315 352 EKGIEIIKSQGGKILT-----GGSaiesEGNFVQPTIVEISpDADVVKEELFGPVLYVMKFK--TLEEAIEINNSVPQGL 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1024315852 1035 TLGIHTRIDETIAHVI--SRAHVGNIYVNRNVIGAVVGvQPFGGEGLSGTGPKAG 1087
Cdd:PLN02315 425 SSSIFTRNPETIFKWIgpLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
649-1083 |
2.52e-43 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 165.44 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 649 GAARDVRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLA 728
Cdd:PRK13252 21 GETFEVINPATG-EVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 729 NA-VAEIREAIDFLRYY----------STQIRNEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 796
Cdd:PRK13252 100 ETsVVDIVTGADVLEYYaglapalegeQIPLRGGSFVYTRRePLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 797 QTPLIAAQAVRILREAGVPAGAVQLLPGDGEtVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegKPIPLiaETG 876
Cdd:PRK13252 180 VTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL----KEVTM--ELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 877 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCS-ALRVLcLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA 955
Cdd:PRK13252 253 GKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAH 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 956 KRGIDAHVAAMREKGRKV----EQLPmPEGGAQGTFVPPTLIElDSIDEL---KREVFGPVLHVVRYRRNqlDKLLEQIR 1028
Cdd:PRK13252 332 RDKVLGYIEKGKAEGARLlcggERLT-EGGFANGAFVAPTVFT-DCTDDMtivREEIFGPVMSVLTFDDE--DEVIARAN 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1029 TTGYGLTLGIHTRiDETIAH-VISRAHVGNIYVnrNVIGAVVGVQPFGGEGLSGTG 1083
Cdd:PRK13252 408 DTEYGLAAGVFTA-DLSRAHrVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
656-1083 |
7.62e-42 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 160.67 E-value: 7.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 656 NPADHRdLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIR 735
Cdd:PRK09406 7 NPATGE-TVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 736 EAIDFLRYYSTQIRNEFSNDT--------------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 801
Cdd:PRK09406 86 KCAKGFRYYAEHAEALLADEPadaaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 802 AAQAVRILREAGVPAGAVQ-LLPGDGETvgAALVADPRTRAVMFTGSTEVARLINKTLSNRLDPEgkpiplIAETGGQNA 880
Cdd:PRK09406 166 ALYLADLFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKT------VLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 881 MIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGID 960
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 961 AHVAAMREKGRKV----EQlpmPEGgaQGTFVPPTLIElDSIDELK---REVFGPVLHVvrYRRNQLDKLLEQIRTTGYG 1033
Cdd:PRK09406 318 KQVDDAVAAGATIlcggKR---PDG--PGWFYPPTVIT-DITPDMRlytEEVFGPVASL--YRVADIDEAIEIANATTFG 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1034 LTLGIHTRIDETIAHVISRAHVGNIYVNrnviGAVVGVQ--PFGGEGLSGTG 1083
Cdd:PRK09406 390 LGSNAWTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
757-1083 |
1.14e-41 |
|
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: 159.23 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 757 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAgVPAGAVQLLPGDGEtVGAALVAD 836
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-VATALLAE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 837 PRTRaVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCL 916
Cdd:cd07087 176 PFDH-IFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 917 QEDVADRTLEMLTGAMRELsVGNPDRLSIDVGPVIDldakrgiDAHVAAMRE--KGRKVEQlpmpeGG---AQGTFVPPT 991
Cdd:cd07087 249 HESIKDELIEELKKAIKEF-YGEDPKESPDYGRIIN-------ERHFDRLASllDDGKVVI-----GGqvdKEERYIAPT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 992 LIELDSIDE--LKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVV 1069
Cdd:cd07087 316 ILDDVSPDSplMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAI 393
|
330
....*....|....
gi 1024315852 1070 GVQPFGGEGLSGTG 1083
Cdd:cd07087 394 PNLPFGGVGNSGMG 407
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
693-1083 |
2.93e-41 |
|
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: 158.74 E-value: 2.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 693 PVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIR----------------NEFSNDT 756
Cdd:cd07148 42 PAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGqlggreipmgltpasaGRIAFTT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 757 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGEtVGAALVAD 836
Cdd:cd07148 122 REPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 837 PRTRAVMFTGSTEVARLINKTLSnrldpEGKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCL 916
Cdd:cd07148 201 PRVAFFSFIGSARVGWMLRSKLA-----PGTRCAL--EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 917 QEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQlpmpeGGAQ--GTFVPPTLIe 994
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLC-----GGKRlsDTTYAPTVL- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 995 LDSIDELK---REVFGPVlhVVRYRRNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNViGAVVGV 1071
Cdd:cd07148 348 LDPPRDAKvstQEIFGPV--VCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHT-AFRVDW 424
|
410
....*....|..
gi 1024315852 1072 QPFGGEGLSGTG 1083
Cdd:cd07148 425 MPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
653-1056 |
5.79e-41 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 158.51 E-value: 5.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADHrDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:TIGR01722 19 PVTNPATN-EVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRY---YSTQIRNEFSNDTHR---------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 800
Cdd:TIGR01722 98 DVARGLEVVEHacgVNSLLKGETSTQVATrvdvysirqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 801 IAAQAVRILREAGVPAGAVQLLPGDGETVGaALVADPRTRAVMFTGSTEVARLINKTLSNrldpEGKPIPliAETGGQNA 880
Cdd:TIGR01722 178 AAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTTGSA----HGKRVQ--ALGGAKNH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 881 MIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQeDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGID 960
Cdd:TIGR01722 251 MVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLV-GAADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 961 AHVAAMREKGRKV---EQLPMPEGGAQGTFVPPTLIE--LDSIDELKREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLT 1035
Cdd:TIGR01722 330 SLIAGGAAEGAEVlldGRGYKVDGYEEGNWVGPTLLErvPPTMKAYQEEIFGPVLCVLEA--DTLEEAIALINASPYGNG 407
|
410 420
....*....|....*....|....
gi 1024315852 1036 LGIHTR---IDETIAHVISRAHVG 1056
Cdd:TIGR01722 408 TAIFTRdgaAARRFQHEIEVGQVG 431
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
656-1087 |
7.50e-41 |
|
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: 157.85 E-value: 7.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 656 NPADHRDLvGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAV-AEI 734
Cdd:cd07098 2 DPATGQHL-GSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 735 R---EAIDFL-----RYYSTQIRNEFSNDTHR-------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 799
Cdd:cd07098 81 LvtcEKIRWTlkhgeKALRPESRPGGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 800 LIAAQAVRILREA----GVPAGAVQLLPGDGETvGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAET 875
Cdd:cd07098 161 WSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 876 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDA 955
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 956 KRGIDAHVAAMREKGRKV----EQLPMPEgGAQGTFVPPTLIeLDSIDELK---REVFGPVLHVVRYrrNQLDKLLEQIR 1028
Cdd:cd07098 314 FDRLEELVADAVEKGARLlaggKRYPHPE-YPQGHYFPPTLL-VDVTPDMKiaqEEVFGPVMVVMKA--SDDEEAVEIAN 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024315852 1029 TTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAG 1087
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
667-1083 |
1.41e-40 |
|
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: 157.23 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 667 VVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAV-AEIREAIDFLRYYS 745
Cdd:cd07116 32 VPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 746 TQIR------NEFSNDT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAgV 814
Cdd:cd07116 112 GCIRaqegsiSEIDENTvayhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-L 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 815 PAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQvva 894
Cdd:cd07116 191 PPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI------IPVTLELGGKSPNIFFADVMDAD--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 895 dvlQSSFDSA-----------GQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHV 963
Cdd:cd07116 262 ---DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 964 AAMREKGRKV----EQLPMPEGGAQGTFVPPTLIELDSIDELKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIH 1039
Cdd:cd07116 339 DIGKEEGAEVltggERNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFK--DEEEALEIANDTLYGLGAGVW 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1024315852 1040 TRiDETIAHVISRA-HVGNIYVnrNVIGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07116 417 TR-DGNTAYRMGRGiQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
690-1087 |
1.70e-40 |
|
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: 157.27 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 690 QATPVDaRADCLARAADLLEAQMHTLMGLVVREAGKSLANAV-AEIREAIDFLRYY----------STQIRNEFSND--- 755
Cdd:cd07140 63 KMNARD-RGRLMYRLADLMEEHQEELATIESLDSGAVYTLALkTHVGMSIQTFRYFagwcdkiqgkTIPINQARPNRnlt 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 756 -THR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAAL 833
Cdd:cd07140 142 lTKRePIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 834 VADPRTRAVMFTGSTEVARLINKT--LSNRldpegKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSAL 911
Cdd:cd07140 222 SDHPDVRKLGFTGSTPIGKHIMKScaVSNL-----KKVSL--ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 912 RVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPvidldakRGIDAHVAAMRE-------KGRKVE----QLPMPe 980
Cdd:cd07140 295 GRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP-------QNHKAHLDKLVEycergvkEGATLVyggkQVDRP- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 981 ggaqGTFVPPTLIElDSIDEL---KREVFGPVLHVVRYRRNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGN 1057
Cdd:cd07140 367 ----GFFFEPTVFT-DVEDHMfiaKEESFGPIMIISKFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGT 441
|
410 420 430
....*....|....*....|....*....|
gi 1024315852 1058 IYVNRNVIGAVVGvqPFGGEGLSGTGPKAG 1087
Cdd:cd07140 442 VFVNTYNKTDVAA--PFGGFKQSGFGKDLG 469
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
635-1061 |
5.08e-39 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 153.35 E-value: 5.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 635 WRAAPMledneiavGAARDVRNPADHrDLVGTVVEATSEHVSAALAH-----AVAAAPIWQATPVDARADCLARAADLLE 709
Cdd:PLN02467 16 WREPVL--------GKRIPVVNPATE-ETIGDIPAATAEDVDAAVEAarkafKRNKGKDWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 710 AQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIR--------------NEF-SNDTHRPLGPVVCISPWNFPLA 774
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEaldakqkapvslpmETFkGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 775 IFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADPRTRAVMFTGSTEVARLI 854
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 855 NKTLSnrldPEGKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRE 934
Cdd:PLN02467 247 MTAAA----QMVKPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 935 LSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGrkVEQL---PMPEGGAQGTFVPPTLI-ELDSIDELKR-EVFGPV 1009
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEG--ATILcggKRPEHLKKGFFIEPTIItDVTTSMQIWReEVFGPV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1010 LHVVRYRRNqlDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVN 1061
Cdd:PLN02467 399 LCVKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
671-1061 |
6.82e-39 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 152.60 E-value: 6.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 671 TSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRY------- 743
Cdd:PLN00412 51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYtaeegvr 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 744 ------------YSTQIRNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILRE 811
Cdd:PLN00412 131 ilgegkflvsdsFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 812 AGVPAGAVQLLPGDGETVGAALVADPRTRAVMFT-GSTEVArlINKtlsnrldpEGKPIPLIAETGGQNAMIVDSSALAE 890
Cdd:PLN00412 211 AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA--ISK--------KAGMVPLQMELGGKDACIVLEDADLD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 891 QVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRlSIDVGPVIDLDAKRGIDAHVAAMREKG 970
Cdd:PLN00412 281 LAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDAKEKG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 971 RKVEQlpmpEGGAQGTFVPPTLieLDSIDELKR----EVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIHTR-IDET 1045
Cdd:PLN00412 360 ATFCQ----EWKREGNLIWPLL--LDNVRPDMRiaweEPFGPVLPVIRI--NSVEEGIHHCNASNFGLQGCVFTRdINKA 431
|
410
....*....|....*..
gi 1024315852 1046 IAhvISRA-HVGNIYVN 1061
Cdd:PLN00412 432 IL--ISDAmETGTVQIN 446
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
690-1083 |
5.64e-37 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 146.96 E-value: 5.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 690 QATPVdARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAE-IREAIDFLRYYSTQI-----------RNEFSNDTH 757
Cdd:PRK09847 77 LSSPA-KRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDdIPGAARAIRWYAEAIdkvygevattsSHELAMIVR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 758 RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADP 837
Cdd:PRK09847 156 EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 838 RTRAVMFTGSTEVARlinKTLSNRLDPEGKPIPLiaETGGQNAMIV--DSSALaEQVVADVLQSSFDSAGQRCSALRVLC 915
Cdd:PRK09847 236 DIDAIAFTGSTRTGK---QLLKDAGDSNMKRVWL--EAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 916 LQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDldakrgiDAHVAAMR---EKGRKVEQLPMP--EGGAQGTFVPP 990
Cdd:PRK09847 310 LEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLID-------CAHADSVHsfiREGESKGQLLLDgrNAGLAAAIGPT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 991 TLIELDSIDELKR-EVFGPVLHVVRYRRNQldKLLEQIRTTGYGLTLGIHTRiDETIAHVISRA-HVGNIYVNRNVIGAV 1068
Cdd:PRK09847 383 IFVDVDPNASLSReEIFGPVLVVTRFTSEE--QALQLANDSQYGLGAAVWTR-DLSRAHRMSRRlKAGSVFVNNYNDGDM 459
|
410
....*....|....*
gi 1024315852 1069 vgVQPFGGEGLSGTG 1083
Cdd:PRK09847 460 --TVPFGGYKQSGNG 472
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
689-1088 |
3.25e-36 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 143.14 E-value: 3.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 689 WQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKS--------LANAVAEIREAIDFLRYY---------------S 745
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPaaevdlteILPVLSEINHAIKHLKKWmkpkrvrtplllfgtK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 746 TQIRNEfsndthrPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAgVPAGAVQLLPGD 825
Cdd:cd07134 94 SKIRYE-------PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 826 GEtVGAALVADPRTRaVMFTGSTEVARLI----NKTLSnrldpegkPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSF 901
Cdd:cd07134 166 AE-VAQALLELPFDH-IFFTGSPAVGKIVmaaaAKHLA--------SVTL--ELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 902 DSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRL-SIDVGPVIDLDAKRGIDAHVAAMREKGRKVEqlpmpE 980
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVE-----F 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 981 GG---AQGTFVPPTLIE---LDSiDELKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAH 1054
Cdd:cd07134 309 GGqfdAAQRYIAPTVLTnvtPDM-KIMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTS 385
|
410 420 430
....*....|....*....|....*....|....
gi 1024315852 1055 VGNIYVNRNVIGAVVGVQPFGGEGLSGTGpKAGG 1088
Cdd:cd07134 386 SGGVVVNDVVLHFLNPNLPFGGVNNSGIG-SYHG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
687-1089 |
1.03e-35 |
|
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: 141.99 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 687 PIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRY----YSTQIRNEFSN-------- 754
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARafviYSYRIPHEPGNhlgqglkq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 755 DTHR---PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAG-VPAGAVQLLPGDGETvG 830
Cdd:cd07084 93 QSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-M 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 831 AALVADPRTRAVMFTGSTEVARLInktlsnRLDPegKPIPLIAETGGQNAMIVDSSALAEQVVAD-VLQSSFDSAGQRCS 909
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVAEKL------ALDA--KQARIYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTACSGQKCT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 910 ALRVLCLQEDVADR-TLEMLTGAMRELSVGnpdrlSIDVGPVIDLDakrgIDAHVAAMREKGRKV------EQLPMPEGG 982
Cdd:cd07084 244 AQSMLFVPENWSKTpLVEKLKALLARRKLE-----DLLLGPVQTFT----TLAMIAHMENLLGSVllfsgkELKNHSIPS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 983 AQGTFVPPTLI----ELDSIDEL-KREVFGPVLHVVRYRRNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHV-G 1056
Cdd:cd07084 315 IYGACVASALFvpidEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVaG 394
|
410 420 430
....*....|....*....|....*....|....
gi 1024315852 1057 NIY-VNRNVIGAVVGVQPFGGEGLSGTGPKAGGA 1089
Cdd:cd07084 395 RTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGP 428
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
757-1083 |
4.18e-35 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 140.05 E-value: 4.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 757 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAgVPAGAVQLLPGDGETVGAALvaD 836
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 837 PRTRAVMFTGSTEVARLI----NKTLSnrldpegkpiPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALR 912
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIaeaaAKHLT----------PVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 913 -VLClQEDVADRTLEMLTGAMRELSVGNPDRLSiDVGPVI-DLDAKRgidAHVAAMREKGRKVEQLPMpegGAQGTFVPP 990
Cdd:cd07135 253 yVLV-DPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVnPRHFNR---LKSLLDTTKGKVVIGGEM---DEATRFIPP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 991 TLIELDSIDE--LKREVFGPVLHVVRYRR-NQLDKLLEQIRTTgygLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGA 1067
Cdd:cd07135 325 TIVSDVSWDDslMSEELFGPVLPIIKVDDlDEAIKVINSRDTP---LALYIFTDDKSEIDHILTRTRSGGVVINDTLIHV 401
|
330
....*....|....*.
gi 1024315852 1068 VVGVQPFGGEGLSGTG 1083
Cdd:cd07135 402 GVDNAPFGGVGDSGYG 417
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
653-1040 |
1.28e-31 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 132.56 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 653 DVRNPADhRDLVGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVA 732
Cdd:PLN02419 132 DVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 733 EIREAIDFLRY-----------YSTQIRNEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 800
Cdd:PLN02419 211 DIFRGLEVVEHacgmatlqmgeYLPNVSNGVDTYSIRePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 801 IAAQAVRILREAGVPAGAVQLLPGDGETVGaALVADPRTRAVMFTGSTEVARLINKtlsnRLDPEGKPIPliAETGGQNA 880
Cdd:PLN02419 291 ASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYA----RAAAKGKRIQ--SNMGAKNH 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 881 MIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVA---DRTLEMlTGAMRELSVGNPDrlsIDVGPVIDLDAKR 957
Cdd:PLN02419 364 GLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVER-AKALKVTCGSEPD---ADLGPVISKQAKE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 958 GIDAHVAAMREKGRKV----EQLPMPeGGAQGTFVPPTLIE--LDSIDELKREVFGPVLhvVRYRRNQLDKLLEQIRTTG 1031
Cdd:PLN02419 440 RICRLIQSGVDDGAKLlldgRDIVVP-GYEKGNFIGPTILSgvTPDMECYKEEIFGPVL--VCMQANSFDEAISIINKNK 516
|
....*....
gi 1024315852 1032 YGLTLGIHT 1040
Cdd:PLN02419 517 YGNGAAIFT 525
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
656-1061 |
2.76e-31 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 129.21 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 656 NPADHRDLvGTVVEATSEHVSAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIR 735
Cdd:PRK13968 13 NPATGEQL-SVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 736 EAIDFLRYYS-----------TQIRNEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQ 804
Cdd:PRK13968 92 KSANLCDWYAehgpamlkaepTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 805 AVRILREAGVPAGAVQLLPGDGETVgAALVADPRTRAVMFTGSTEVARLINKTLSNRLDpegkpiPLIAETGGQNAMIVD 884
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALK------KCVLELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 885 SSALAEQVVADVLQSSFDSAGQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVA 964
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 965 AMREKGRKVeQLPMPEGGAQGTFVPPTLIE--LDSIDELKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRI 1042
Cdd:PRK13968 325 ATLAEGARL-LLGGEKIAGAGNYYAPTVLAnvTPEMTAFREELFGPVAAITVAK--DAEHALELANDSEFGLSATIFTTD 401
|
410
....*....|....*....
gi 1024315852 1043 DETIAHVISRAHVGNIYVN 1061
Cdd:PRK13968 402 ETQARQMAARLECGGVFIN 420
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
759-1083 |
2.73e-30 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 126.68 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 759 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIaAQAVRILREAGVPAGAVQLLPGdGETVGAALVADPR 838
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT-SKLMAKLLTKYLDPSYVRVIEG-GVEVTTELLKEPF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 839 TRaVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQE 918
Cdd:PTZ00381 187 DH-IFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 919 DVADRTLEMLTGAMRELSVGNPDRlSIDVGPVIDldaKRGIDAHVAAMREKGRKVEQlpmpeGGAQGT---FVPPTLIEL 995
Cdd:PTZ00381 260 SIKDKFIEALKEAIKEFFGEDPKK-SEDYSRIVN---EFHTKRLAELIKDHGGKVVY-----GGEVDIenkYVAPTIIVN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 996 DSIDE--LKREVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQP 1073
Cdd:PTZ00381 331 PDLDSplMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLP 408
|
330
....*....|
gi 1024315852 1074 FGGEGLSGTG 1083
Cdd:PTZ00381 409 FGGVGNSGMG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
756-1083 |
3.36e-30 |
|
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: 125.29 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 756 THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGvPAGAVQLLPGDGEtVGAALVA 835
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF-DEDEVAVVTGGAD-VAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 836 DPRTRaVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALR-VL 914
Cdd:cd07133 176 LPFDH-LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDyVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 915 CLQEDVaDRTLEMLTGAMREL---SVGNPDRLSIdvgpvIDldakrgiDAH-------VAAMREKGRKVEQL-PMPEGGA 983
Cdd:cd07133 249 VPEDKL-EEFVAAAKAAVAKMyptLADNPDYTSI-----IN-------ERHyarlqglLEDARAKGARVIELnPAGEDFA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 984 QGTFVPPTLIeLDSIDELK---REVFGPVLHVVRYRRnqLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYV 1060
Cdd:cd07133 316 ATRKLPPTLV-LNVTDDMRvmqEEIFGPILPILTYDS--LDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTI 392
|
330 340
....*....|....*....|...
gi 1024315852 1061 NRNVIGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07133 393 NDTLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
689-1040 |
2.11e-28 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 120.34 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 689 WQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRN--------EFSNDT---- 756
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgswldariDPADPDrqpl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 757 --------HRPLGPVVCISPWNFPLAIFM--GQVAAALAAGNTVLAK--PA--EQTPLIAAQAVRILREAGVPAGAVQLL 822
Cdd:cd07129 95 prpdlrrmLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhpGTSELVARAIRAALRATGLPAGVFSLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 823 PGDGETVGAALVADPRTRAVMFTGSTEVARLINKTLSNRldPEgkPIPLIAETGGQNAMIVDSSALAEQV--VADVLQSS 900
Cdd:cd07129 175 QGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAAR--PE--PIPFYAELGSVNPVFILPGALAERGeaIAQGFVGS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 901 FD-SAGQRCSALRVLCLQEDVA-DRTLEMLTGAMRElsvgnpdrlsidVGPVIDLDA--KRGIDAHVAAMREKGrKVEQL 976
Cdd:cd07129 251 LTlGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAA------------APAQTMLTPgiAEAYRQGVEALAAAP-GVRVL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024315852 977 PMPEGGAQGTFVPPTLIELDSIDELKR-----EVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHT 1040
Cdd:cd07129 318 AGGAAAEGGNQAAPTLFKVDAAAFLADpalqeEVFGPASLVVRYD--DAAELLAVAEALEGQLTATIHG 384
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
718-1059 |
3.26e-24 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 107.97 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 718 LVVREAGKSLANAVAEIREAIDFLRYYS-TQIR-------------NEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAA 783
Cdd:cd07126 87 LIQRVAPKSDAQALGEVVVTRKFLENFAgDQVRflarsfnvpgdhqGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 784 LAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALV-ADPRTraVMFTGSTEVA-RLINKTlsnr 861
Cdd:cd07126 167 LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANPRM--TLFTGSSKVAeRLALEL---- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 862 ldpEGKpipLIAETGGQNAMIVDSSALAEQVVADVL-QSSFDSAGQRCSALRVLCLQEDVADRTLE---MLTGAMRELSv 937
Cdd:cd07126 241 ---HGK---VKLEDAGFDWKILGPDVSDVDYVAWQCdQDAYACSGQKCSAQSILFAHENWVQAGILdklKALAEQRKLE- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 938 gnpdrlSIDVGPVIDLDAKRgIDAHVAAMRE-KGRKVE---------QLPMPEGGAQGT--FVP-PTLIELDSIDELKRE 1004
Cdd:cd07126 314 ------DLTIGPVLTWTTER-ILDHVDKLLAiPGAKVLfggkpltnhSIPSIYGAYEPTavFVPlEEIAIEENFELVTTE 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1024315852 1005 VFGPVLHVVRYRRNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIY 1059
Cdd:cd07126 387 VFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
759-1083 |
5.97e-23 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 103.74 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 759 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAgVPAGAVQLLPGDGETVGAALvaDPR 838
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL--DQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 839 TRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQE 918
Cdd:cd07136 177 FDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 919 DVADRTLEMLTGAMRELSVGNPdRLSIDVGPVIDldakrgiDAH---VAAMREKGRKVeqlpmpEGG---AQGTFVPPTL 992
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDP-LESPDYGRIIN-------EKHfdrLAGLLDNGKIV------FGGntdRETLYIEPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 993 ieLDSIDE----LKREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAV 1068
Cdd:cd07136 317 --LDNVTWddpvMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLA 392
|
330
....*....|....*
gi 1024315852 1069 VGVQPFGGEGLSGTG 1083
Cdd:cd07136 393 NPYLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
759-1083 |
7.17e-22 |
|
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: 100.18 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 759 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILrEAGVPAGAVQLLPGdGETVGAALVaDPR 838
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEG-GVPETTALL-EQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 839 TRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDS-AGQRCSALRVLCLQ 917
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 918 EDVADRTLEMLTGAMRELSVGNPdRLSIDVGPVID----------LDAKRGIDA--HVAAMREKGRKVEqlpmpeggaqg 985
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENP-KESKDLSRIVNshhfqrlsrlLDDPSVADKivHGGERDEKNLYIE----------- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 986 tfvpPTLI---ELDSIdELKREVFGPVLHVVRYRRnqLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNR 1062
Cdd:cd07137 320 ----PTILldpPLDSS-IMTEEIFGPLLPIITVKK--IEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFND 392
|
330 340
....*....|....*....|.
gi 1024315852 1063 NVIGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07137 393 TVVQYAIDTLPFGGVGESGFG 413
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
748-1083 |
1.31e-21 |
|
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: 99.60 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 748 IRNEfsndthrPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEqtplIAAQAVRILREagvpagavqLLP---- 823
Cdd:cd07132 96 IYKE-------PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE----VSPATAKLLAE---------LIPkyld 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 824 ---------GDGETvgaALVADPRTRAVMFTGSTEVARLI----NKTLSnrldpegkpiPLIAETGGQNAMIVDSSALAE 890
Cdd:cd07132 156 kecypvvlgGVEET---TELLKQRFDYIFYTGSTSVGKIVmqaaAKHLT----------PVTLELGGKSPCYVDKSCDID 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 891 QVVADVLQSSFDSAGQRCSALR-VLCLQEdVADRTLEMLTGAMRELsVGNPDRLSIDVGPVIDldakrgiDAH---VAAM 966
Cdd:cd07132 223 VAARRIAWGKFINAGQTCIAPDyVLCTPE-VQEKFVEALKKTLKEF-YGEDPKESPDYGRIIN-------DRHfqrLKKL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 967 REKGRKVeqlpmpEGG--AQGT-FVPPTLI----ELDSIdeLKREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIH 1039
Cdd:cd07132 294 LSGGKVA------IGGqtDEKErYIAPTVLtdvkPSDPV--MQEEIFGPILPIVTV--NNLDEAIEFINSREKPLALYVF 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1024315852 1040 TRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTG 1083
Cdd:cd07132 364 SNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
759-1094 |
3.25e-20 |
|
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: 95.80 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 759 PLGPV-VCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGV-PAGAVQLLPGDGETVGAALvaD 836
Cdd:cd07128 143 PRRGVaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHL--G 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 837 PRTrAVMFTGSTEVARLInKTLSNRLDpegKPIPLIAETGGQNAMIvdssaLAEQVVADvlQSSFD------------SA 904
Cdd:cd07128 221 EQD-VVAFTGSAATAAKL-RAHPNIVA---RSIRFNAEADSLNAAI-----LGPDATPG--TPEFDlfvkevaremtvKA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 905 GQRCSALRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKV-----EQLPMP 979
Cdd:cd07128 289 GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVfggpdRFEVVG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 980 EGGAQGTFVPPTLIELDSIDELKR----EVFGPVLHVVRYRrnQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRA-- 1053
Cdd:cd07128 369 ADAEKGAFFPPTLLLCDDPDAATAvhdvEAFGPVATLMPYD--SLAEAIELAARGRGSLVASVVTNDPAFARELVLGAap 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1024315852 1054 HVGNIYV-NRNVIGAVVG---VQP---FGGEGLSGTGPKAGG----ALYLQR 1094
Cdd:cd07128 447 YHGRLLVlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGGlrgvKHYMQR 498
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
759-1083 |
1.51e-19 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 93.64 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 759 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAqavriLREAGVP----AGAVQLLPGdGETVGAALV 834
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPkyldSKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 835 aDPRTRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALA---EQVVADVLQSSFDS-AGQRCSA 910
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 911 LRVLCLQEDVADRTLEMLTGAMRELSVGNPDRLSidvgpvidlDAKRGIDAHvAAMREKG----RKVeQLPMPEGG---A 983
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRESK---------SMARILNKK-HFQRLSNllkdPRV-AASIVHGGsidE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 984 QGTFVPPTLI---ELDSiDELKREVFGPVLHVVRYRRnqLDKLLEQIRTTGYGLTLGIHTRiDETIA-HVISRAHVGNIY 1059
Cdd:PLN02203 324 KKLFIEPTILlnpPLDS-DIMTEEIFGPLLPIITVKK--IEDSIAFINSKPKPLAIYAFTN-NEKLKrRILSETSSGSVT 399
|
330 340
....*....|....*....|....
gi 1024315852 1060 VNRNVIGAVVGVQPFGGEGLSGTG 1083
Cdd:PLN02203 400 FNDAIIQYACDSLPFGGVGESGFG 423
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
90-137 |
1.22e-17 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 77.50 E-value: 1.22e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1024315852 90 SVLRAAITAAYRRPEPECVPFLLGQARLPANLAGDVQAMAGKLVETLR 137
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
761-1094 |
3.13e-17 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 86.68 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 761 GPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGV-PAGAVQLLPGDGETVGAALVAdprT 839
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQP---F 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 840 RAVMFTGSTEVARLInktlsnRLDPE--GKPIPLIAETGGQNAMI-----VDSSALAEQVVADVLQSSFDSAGQRCSALR 912
Cdd:PRK11903 227 DVVSFTGSAETAAVL------RSHPAvvQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQKCTAIR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 913 VLCLQEDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREK------GRKVEQLPMPEGGAqgT 986
Cdd:PRK11903 301 RIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQaevlfdGGGFALVDADPAVA--A 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 987 FVPPTLIELDSIDELKR----EVFGPVLHVVRYRRnqLDKLLEQIRTTGYGLTLGIHTRIDETIAHVI-------SRAHV 1055
Cdd:PRK11903 379 CVGPTLLGASDPDAATAvhdvEVFGPVATLLPYRD--AAHALALARRGQGSLVASVYSDDAAFLAAAAleladshGRVHV 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1024315852 1056 GNIYVNRNVIGAVVgVQP---FGGEGLSGTGPKAGG----ALYLQR 1094
Cdd:PRK11903 457 ISPDVAALHTGHGN-VMPqslHGGPGRAGGGEELGGlralAFYHRR 501
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
759-1087 |
1.07e-15 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 81.63 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 759 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILrEAGVPAGAVQLLPGDGETVGAALvaDPR 838
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 839 TRAVMFTGSTEVARLINKTLSNRLdpegkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFD-SAGQRCSALRVLCLQ 917
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 918 EDVADRTLEMLTGAMRELSVGNPDRlSIDVGPVIDldaKRGIDAHVAAMREKGRKVEQLPMPEGGAQGTFVPPTL---IE 994
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVN---STHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTIlldVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 995 LDSIDeLKREVFGPVLHVVRYrrNQLDKLLEQIRTTGYGLTLGIHT---RIDETIAHVISrahVGNIYVNRNVIGAVVGV 1071
Cdd:PLN02174 339 LDSLI-MSEEIFGPLLPILTL--NNLEESFDVIRSRPKPLAAYLFThnkKLKERFAATVS---AGGIVVNDIAVHLALHT 412
|
330
....*....|....*.
gi 1024315852 1072 QPFGGEGLSGTGPKAG 1087
Cdd:PLN02174 413 LPFGGVGESGMGAYHG 428
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-72 |
2.30e-13 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 66.00 E-value: 2.30e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024315852 2 ASTTLGVKVDDLLRSRLKDAATRLERTPHWLIKQAIFAYLEKIEHGQLPPELsghtGSADLADGAAVEQEE 72
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQE----GLAAADAGEFVSHEE 67
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
758-1090 |
4.20e-12 |
|
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: 70.59 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 758 RPLGPVVCISP---WNFPLAIFmgqvaAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAG---AVQLLPGD--GETV 829
Cdd:cd07127 194 RGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGfdpNLVTLAADtpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 830 GAALVADPRTRAVMFTGSTevarlinkTLSNRLDPEGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCS 909
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSN--------AFGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 910 ALRVLCLQED---------VADRTLEMLTGAMRELsVGNPDRLSIDVGPVIDLDAKRGIdAHVAAMREKGRKVEQLPMPE 980
Cdd:cd07127 341 TPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI-AEARQLGEVLLASEAVAHPE 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 981 gGAQGTFVPPTLIELDSIDE--LKREVFGPVLHVVRYRR--NQLDKLLEQIRTTGyGLTLGIHTRIDETIAHVISRAHVG 1056
Cdd:cd07127 419 -FPDARVRTPLLLKLDASDEaaYAEERFGPIAFVVATDStdHSIELARESVREHG-AMTVGVYSTDPEVVERVQEAALDA 496
|
330 340 350
....*....|....*....|....*....|....*.
gi 1024315852 1057 NIYVNRNVIGAVVGVQPFGGEGLSGTG--PKAGGAL 1090
Cdd:cd07127 497 GVALSINLTGGVFVNQSAAFSDFHGTGanPAANAAL 532
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
759-940 |
1.36e-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: 58.77 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 759 PLGPVVCISPWNFPLAIfMGQVAAALAAGNTVLAKPAEQTPlIAAQAVRILREAGVPAG----AVQLLPGDGETVGAALV 834
Cdd:cd07077 100 PIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkiLVLYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 835 ADPRTRAVMFTGSTEVARLINKTlsnrldpeGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQS-SFDSAGqrCSALRV 913
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSkFFDQNA--CASEQN 247
|
170 180
....*....|....*....|....*..
gi 1024315852 914 LCLQEDVADRTLEMLTGAMRELSVGNP 940
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLKLVVEGLKVP 274
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-45 |
4.50e-08 |
|
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar proteins; This family includes the N-terminal ribbon-helix-helix (RHH) domain of Shewanella oneidensis CopA(SO), a newly identified type II antitoxin, as well as the N-terminal RHH domain of Escherichia coli PutA flavoprotein, among other similar proteins, many of which are as yet uncharacterized. CopA(SO) is a typical RHH antitoxin that includes an ordered N-terminal domain (CopA(SO)-N) and a disordered C-terminal domain (CopA(SO)-C). Biophysical investigation indicates allosteric effects of CopA(SO)-N on CopA(SO)-C; DNA binding of CopA(SO)-N appears to induce CopA(SO)-C to fold and self-associate the C-terminal domain. The multifunctional E. coli proline utilization A (PutA) flavoprotein functions as a membrane-associated proline catabolic enzyme as well as a transcriptional repressor of the proline utilization genes putA and putP. The N-terminal domain of PutA is a transcriptional regulator with an RHH fold; structure studies show that it forms a homodimer to bind one DNA duplex. This family also includes orphan antitoxin ParD2, an antitoxin component of a non-functional type II toxin-antitoxin (TA system); it does not neutralize the effect of any of the RelE or ParE toxins.
Pssm-ID: 409023 Cd Length: 44 Bit Score: 50.45 E-value: 4.50e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1024315852 4 TTLGVKVDDLLRSRLKDAATRLERTPHWLIKQAIFAYLEKIE 45
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREE 42
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
210-554 |
4.74e-07 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 53.94 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 210 LMITGKLVTtNSETGLSSALTRLIGKGGEPLIRKGVdmamrlmGEQFVTGENISEALANSRKYEARGFRYSYDMLGEAAT 289
Cdd:PLN02681 50 LCAIGPLVD-LGEWLLTSPLMVLGRAIVLALVKATF-------YSHFCAGEDAEEAARTVRRLWELGLGGILDYAAEDAG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 290 TEADAQRYYASYEQAIHAIGKAAGGRGIyegpgISIKLSAL--------------------------------------- 330
Cdd:PLN02681 122 DNAACDRNLEKFLAAIRAAATLPPSSSS-----AAVKITALcppsllervsdllrwqdrdpngklpwkqwsfplfadssp 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 331 --HARYSR----SQQERAMSELLPRVRSLAVLARRYDIGLNIDAEEA------DRleISLDLLEALCFDPELAgwngIGF 398
Cdd:PLN02681 197 lyHATSEPepltAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYTslqpaiDY--ITYDLAREFNKGKDRP----IVY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 399 V-VQAYQKRCPFVIDYIVDLARRSRHRIMVRLVKGAYWDTEIKRAQVDGLEGyPVYTRKIYTDVSYLACAKKLL----GA 473
Cdd:PLN02681 271 GtYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAEFLLekasNG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 474 PDAVYpqFATHNAHTLSAIYHLA---GNNYYPGQYEFQCLHGMGEPLYEEVtgrdkLNRPCRV--YAPVGTHETLLAYLV 548
Cdd:PLN02681 350 DGEVM--LATHNVESGELAAAKMnelGLHKGDPRVQFAQLLGMSDNLSFGL-----GNAGFRVskYLPYGPVEEVIPYLL 422
|
....*.
gi 1024315852 549 RRLLEN 554
Cdd:PLN02681 423 RRAEEN 428
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
759-1085 |
1.72e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 48.80 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 759 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPG-----DGETvGAAL 833
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGwidnpSIEL-AQRL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 834 VADPRTRAVMFTGSTEVARLINKTlsnrldpeGKpiPLIAETGGQNAMIVDSSALAEQVVADVLQS-SFDSaGQRCSALR 912
Cdd:cd07081 174 MKFPGIGLLLATGGPAVVKAAYSS--------GK--PAIGVGAGNTPVVIDETADIKRAVQSIVKSkTFDN-GVICASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 913 VLCLQEDVADRTLEMLTGAMRELSVGNPDRlsiDVGPVI--DLDAKRGIdahvaamrekgrkVEQLPMPEGGAQGTFVPP 990
Cdd:cd07081 243 SVIVVDSVYDEVMRLFEGQGAYKLTAEELQ---QVQPVIlkNGDVNRDI-------------VGQDAYKIAAAAGLKVPQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 991 T----LIELDSIDE---LKREVFGPVLHVVRYRR--NQLDKLLEQIRTTGYGLTLGIHTRIDETIAHV------------ 1049
Cdd:cd07081 307 EtrilIGEVTSLAEhepFAHEKLSPVLAMYRAANfaDADAKALALKLEGGCGHTSAMYSDNIKAIENMnqfanamktsrf 386
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1024315852 1050 -----ISRAHVGNIYVNRNVIGAVVGVQPFGGEGLS-GTGPK 1085
Cdd:cd07081 387 vkngpCSQGGLGDLYNFRGWPSMTLGCGTWGGNSVSeNVGPK 428
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
758-1061 |
9.83e-05 |
|
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: 46.33 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 758 RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGA----VQLLPGDGETVGAAL 833
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGApeglIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 834 VADPRTRAVMFTGSTEVARLINKTlsnrldpeGKPIplIAETGGQNAMIVDSSALAEQVVADVLQS-SFDSaGQRCSALR 912
Cdd:cd07122 174 MKHPDVDLILATGGPGMVKAAYSS--------GKPA--IGVGPGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 913 VLCLQEDVADRTLEMLtgamrelsvgnpdrlsidvgpvidldAKRGidAHVAAMREKgRKVEQLPMPEGG---------- 982
Cdd:cd07122 243 SVIVDDEIYDEVRAEL--------------------------KRRG--AYFLNEEEK-EKLEKALFDDGGtlnpdivgks 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 983 AQ------GTFVPPT----LIELDSIDE---LKREVFGPVLHVVRYR--RNQLDKLLEQIRTTGYGLTLGIHTRIDETIA 1047
Cdd:cd07122 294 AQkiaelaGIEVPEDtkvlVAEETGVGPeepLSREKLSPVLAFYRAEdfEEALEKARELLEYGGAGHTAVIHSNDEEVIE 373
|
330
....*....|....
gi 1024315852 1048 HVISRAHVGNIYVN 1061
Cdd:cd07122 374 EFALRMPVSRILVN 387
|
|
| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-42 |
2.50e-04 |
|
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins; This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.
Pssm-ID: 409020 Cd Length: 42 Bit Score: 39.80 E-value: 2.50e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1024315852 4 TTLGVKVDDLLRSRLKDAATRLERTPHWLIKQAIFAYLE 42
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLE 39
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1168-1228 |
3.30e-04 |
|
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: 44.88 E-value: 3.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024315852 1168 LSGPTGERNTYTLGARGTVLCIA------STASGarvQFAAALATGNRALFEGAagEQlvSQLPAAL 1228
Cdd:cd07125 153 LPGPTGELNGLELHGRGVFVCISpwnfplAIFTG---QIAAALAAGNTVIAKPA--EQ--TPLIAAR 212
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
781-937 |
3.80e-04 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 44.67 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 781 AAALA--AGNTVL---AKPAEQTPLIAAQAVR-ILREAGVPAGAVQLLPG-DGETVGAALVAD-------PRtravmftG 846
Cdd:PRK00197 133 AAALClkSGNAVIlrgGSEAIHSNRALVAVIQeALEEAGLPADAVQLVETtDRAAVGELLKLDgyvdviiPR-------G 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 847 StevARLINKTLSN-RldpegkpIPLIaETG-GQNAMIVDSSA---LAEQVVadvlqssFDSAGQR---CSALRVLCLQE 918
Cdd:PRK00197 206 G---AGLIRRVVENaT-------VPVI-EHGdGICHIYVDESAdldKALKIV-------LNAKTQRpsvCNALETLLVHE 267
|
170
....*....|....*....
gi 1024315852 919 DVADRTLEMLTGAMRELSV 937
Cdd:PRK00197 268 AIAEEFLPKLAEALAEAGV 286
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1163-1208 |
1.25e-03 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 43.26 E-value: 1.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024315852 1163 GATAVLSGPTGERNTYTLGARGTVLCIastaS----------GarvQFAAALATGN 1208
Cdd:PRK11904 665 GAPEKLPGPTGESNELRLHGRGVFVCI----SpwnfplaiflG---QVAAALAAGN 713
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
527-1120 |
5.35e-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: 41.40 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 527 LNRPCRVYAPVGTHETLLAyLVRRLLENGANTSFV---NRIADENVAIKDLIAD------PVDEASkiVPLGAPHAKIPL 597
Cdd:COG3321 787 LADGVRVFLEVGPGPVLTG-LVRQCLAAAGDAVVLpslRRGEDELAQLLTALAQlwvagvPVDWSA--LYPGRGRRRVPL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 598 PRNLFGAERLNSMGLDLSNEHRLASLSSALLASAHHPWRAAPMLEDNEIAVGAARDVRNPADHRDLVGTVVEATSEHVsa 677
Cdd:COG3321 864 PTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAA-- 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 678 ALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLVVREAGKSLANAVAEIREAIDFLRYYSTQIRNEFSNDTH 757
Cdd:COG3321 942 LLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAAL 1021
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 758 RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADP 837
Cdd:COG3321 1022 LALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAA 1101
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 838 RTRAVMFTGSTEVARLINKTLSNRLDPEGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQ 917
Cdd:COG3321 1102 LAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALAL 1181
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 918 EDVADRTLEMLTGAMRELSVGNPDRLSIDVGPVIDLDAKRGIDAHVAAMREKGRKVEQLPMPEGGAQGTFVPPTLIELDS 997
Cdd:COG3321 1182 AAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAA 1261
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024315852 998 IDELKREVFGPVLHVVRYRRNQLDKLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGE 1077
Cdd:COG3321 1262 LALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAAL 1341
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1024315852 1078 GLSGTGPKAGGALYLQRLLATRPAGLPKSLADALIVDAPQAGA 1120
Cdd:COG3321 1342 ALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
4-45 |
9.29e-03 |
|
Predicted DNA-binding protein with an HTH domain [General function prediction only];
Pssm-ID: 443745 Cd Length: 76 Bit Score: 36.42 E-value: 9.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1024315852 4 TTLGVKVDDLLRSRLKDAATRLERTPHWLIKQAIFAYLEKIE 45
Cdd:COG4710 2 KMLSIRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
|
|
| |
