|
Name |
Accession |
Description |
Interval |
E-value |
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
1-1309 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 2574.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1 MASTTLGVKVDDLLRSRLKDAASRLERTPHWLIKQAIFAYLERIEHGQLPPELSGHTGAADLSDSHADGDEDGAPHPFLE 80
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADTPAEEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 81 FAQNVQPQSVLRAAITAAYRRPEPECVPFLIGEARLPASLAPDVQSMAAGLVEALREKSSGGG----VEGLIHEFSLSSQ 156
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGragmVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 157 EGVALMCLAEALLRIPDRATRDALIRDKISKGDWRSHVGHAPSLFVNAATWGLMITGKLVTTNSEAGLSSALTRLIGKGG 236
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 237 EPLIRKGVDMAMRLMGEQFVTGETISEALANSRKYEARGFRYSYDMLGEAATTEEDALRYYASYEQAIHAIGKAAGGRGI 316
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 317 YEGPGISIKLSALHARYSRSQQERTMVELLPRVRSLALLARRYDIGLNIDAEEADRLELSLDLLEALCFDPELAGWNGIG 396
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 397 FVVQAYQKRCPFVIDYLVDLARRSRHRLMIRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLAAPDAV 476
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 477 YPQFATHNAYTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEEVTGR---DKLNRPCRVYAPVGTHETLLAYLVRRLLEN 553
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKvadGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 554 GANTSFVNRIADKTVSVKELVADPLDEAAKVV----PLGAPHEKIPLPRELYGASRVNSMGLDLSNEHRLASLSSALLAS 629
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAqqegQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLAS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 630 AHHPWRAAPMLAdDALEHAAPRDVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEA 709
Cdd:PRK11809 641 AHQKWQAAPMLE-DPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 710 QMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTV 789
Cdd:PRK11809 720 QMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSV 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 790 LAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLDPDGKPIP 869
Cdd:PRK11809 800 LAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIP 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 870 LIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPV 949
Cdd:PRK11809 880 LIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPV 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 950 IDADAKRTIDAHIAAMKDKGHAVTQLAMPDAC--AQGTFVPPTIIEIGNVDELKREVFGPVLHVVRYRRSGLDKLLEQIR 1027
Cdd:PRK11809 960 IDAEAKANIERHIQAMRAKGRPVFQAARENSEdwQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQIN 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1028 ATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLPRLLATRPAGLPRSLE 1107
Cdd:PRK11809 1040 ASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAVTL 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1108 ASLVADAPQEGETRDNPSAALTALRDWLIEQrEPALAARCDGYLSHVLAGATAVLSGPTGERNTYTLGARGTVLCIAATA 1187
Cdd:PRK11809 1120 ARQDAEYPVDAQLRAALLAPLTALREWAAER-EPELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADTE 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1188 SGARAQFAAVLATGNRALFaGAAGEALAAALPASLKAQAGVR-----KQADAAFDAVLFEGDSDELLALVKEVAQRPGPI 1262
Cdd:PRK11809 1199 QDALTQLAAVLAVGSQALW-PDDALHRALVAALPAAVQARIQlakdwQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPI 1277
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*..
gi 1943257567 1263 VSVQGVAAgafengGDEDYALERLLTERSVSVNTAAAGGNANLMTIG 1309
Cdd:PRK11809 1278 VSVQGFAR------GETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
77-1309 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 2074.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 77 PFLEFAQNVQPQSVLRAAITAAYRRPEPECVPFLIGEARLPASLAPDVQSMAAGLVEALREKSSGGGVEGLIHEFSLSSQ 156
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTGVEALLQEYSLSSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 157 EGVALMCLAEALLRIPDRATRDALIRDKISKGDWRSHVGHAPSLFVNAATWGLMITGKLVTTNSEAGLSSALTRLIGKGG 236
Cdd:PRK11905 81 EGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIARLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 237 EPLIRKGVDMAMRLMGEQFVTGETISEALANSRKYEARGFRYSYDMLGEAATTEEDALRYYASYEQAIHAIGKAAGGRGI 316
Cdd:PRK11905 161 EPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 317 YEGPGISIKLSALHARYSRSQQERTMVELLPRVRSLALLARRYDIGLNIDAEEADRLELSLDLLEALCFDPELAGWNGIG 396
Cdd:PRK11905 241 YDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 397 FVVQAYQKRCPFVIDYLVDLARRSRHRLMIRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLAAPDAV 476
Cdd:PRK11905 321 FVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 477 YPQFATHNAYTLAAIYHLAGQNYypgQYEFQCLHGMGEPLYEEVTGRDKLNRPCRVYAPVGTHETLLAYLVRRLLENGAN 556
Cdd:PRK11905 401 YPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGAN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 557 TSFVNRIADKTVSVKELVADPLDEAAKVVplGAPHEKIPLPRELYGASRVNSMGLDLSNEHRLASLSSALLASAHHPWRA 636
Cdd:PRK11905 478 SSFVNRIVDENVPVEELIADPVEKVAAMG--VAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAAKTWHA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 637 APMLADDALEHAApRDVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMG 716
Cdd:PRK11905 556 APLLAGGDVDGGT-RPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFA 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 717 LIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQ 796
Cdd:PRK11905 635 LAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQ 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 797 TPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdGKPIPLIAETGG 876
Cdd:PRK11905 715 TPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GPPVPLIAETGG 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 877 QNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKR 956
Cdd:PRK11905 792 QNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQA 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 957 TIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPPTIIEIGNVDELKREVFGPVLHVVRYRRSGLDKLLEQIRATGYGLTLG 1036
Cdd:PRK11905 872 NIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFG 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1037 IHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLPRLLATRPAGLPRSLEASLVAdapq 1116
Cdd:PRK11905 952 LHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPIPPAHESVDTD---- 1027
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1117 egetrdnpsAALTALRDWLIEQREPALAARCDGYLSHVLAGATAVLSGPTGERNTYTLGARGTVLCIAATASGARAQFAA 1196
Cdd:PRK11905 1028 ---------AAARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVADTEEALLRQLAA 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1197 VLATGNRALFAGAAGEALAAALPASLKAQAGVRKQ---ADAAFDAVLFEGDSDELLALVKEVAQRPGPIVSVQGVaagaf 1273
Cdd:PRK11905 1099 ALATGNVAVVAADSGLAAALADLPGLVAARIDWTQdweADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAA----- 1173
|
1210 1220 1230
....*....|....*....|....*....|....*.
gi 1943257567 1274 enGGDEDYALERLLTERSVSVNTAAAGGNANLMTIG 1309
Cdd:PRK11905 1174 --EPTDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
79-1094 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1589.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 79 LEFAQNVQPQSVLRAAITAAYRRPEPECVPFLIGEARLPASLAPDVQSMAAGLVEALREKSSG-GGVEGLIHEFSLSSQE 157
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKlGGIDAFLQEYSLSTEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 158 GVALMCLAEALLRIPDRATRDALIRDKISKGDWRSHVGHAPSLFVNAATWGLMITGKLVTTNSEAG--LSSALTRLIGKG 235
Cdd:PRK11904 81 GIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADgtPSGVLKRLVNRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 236 GEPLIRKGVDMAMRLMGEQFVTGETISEALANSRKYEARGFRYSYDMLGEAATTEEDALRYYASYEQAIHAIGKAAGGRG 315
Cdd:PRK11904 161 GEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 316 IYEGPGISIKLSALHARYSRSQQERTMVELLPRVRSLALLARRYDIGLNIDAEEADRLELSLDLLEALCFDPELAGWNGI 395
Cdd:PRK11904 241 LPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 396 GFVVQAYQKRCPFVIDYLVDLARRSRHRLMIRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLAAPDA 475
Cdd:PRK11904 321 GLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 476 VYPQFATHNAYTLAAIYHLAGQnyypGQYEFQCLHGMGEPLYEEVtgRDKLNRPCRVYAPVGTHETLLAYLVRRLLENGA 555
Cdd:PRK11904 401 IYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDAL--LDAPGIPCRIYAPVGSHKDLLPYLVRRLLENGA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 556 NTSFVNRIADKTVSVKELVADPLDEAAKvvPLGAPHEKIPLPRELYGASRVNSMGLDLSNEHRLASLSSALLASAHHPWR 635
Cdd:PRK11904 475 NSSFVHRLVDPDVPIEELVADPVEKLRS--FETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 636 AAPMLADDalehAAPRDVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLM 715
Cdd:PRK11904 553 AGPIINGE----GEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELI 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 716 GLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDEFSNDTHRPlGPV--------------VCISPWNFPLAIFMGQVAA 781
Cdd:PRK11904 629 ALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLP-GPTgesnelrlhgrgvfVCISPWNFPLAIFLGQVAA 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 782 ALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRl 861
Cdd:PRK11904 708 ALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAAR- 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 862 dpDGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDR 941
Cdd:PRK11904 787 --DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRL 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 942 LSADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPPTIIEIGNVDELKREVFGPVLHVVRYRRSGLDK 1021
Cdd:PRK11904 865 LSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDK 944
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943257567 1022 LLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLPRL 1094
Cdd:PRK11904 945 VIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRF 1017
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
77-1306 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1548.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 77 PFLEFAQNVQPQSVLRAAITAAYRRPEPECVPFLIGEARLPASLAPDVQSMAAGLVEALREKSSGGGVEGLIHEFSLSSQ 156
Cdd:COG4230 2 PFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 157 EGVALMCLAEALLRIPDRATRDALIRDKISKGDWRSHVGHAPSLFVNAATWGLMITGKLVTTNSEAGLSSALTRLIGKGG 236
Cdd:COG4230 82 EALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 237 EPLIRKGVDMAMRLMGEQFVTGETISEALANSRKYEARGFRYSYDMLGEAATTEEDALRYYASYEQAIHAIGKAAGGRGI 316
Cdd:COG4230 162 RPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGSG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 317 YEGPGISIKLSALHARYSRSQQERTMVELLPRVRSLALLARRYDIGLNIDAEEADRLELSLDLLEALCFDPELAGWNGIG 396
Cdd:COG4230 242 GPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 397 FVVQAYQKRCPFVIDYLVDLARRSRHR----LMIRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLAA 472
Cdd:COG4230 322 GGVGQAVQAYAKALLLVLDLLARRRRRrrrrLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 473 PDAVYPQFATHNAYTLAAIYHLAGQnyypGQYEFQCLHGMGEPLYEEVtGRDKLNRPCRVYAPVGTHETLLAYLVRRLLE 552
Cdd:COG4230 402 QPAFAPQFATHAAATAAAAAAAGGG----GEFEFQCLHGMGEYLYDQV-GRGKLGRPCRIYAPVGSHEDLLAYLVRRLLE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 553 NGANTSFVNRIADKTVSVKELVADPLDEAAKVVplGAPHEKIPLPRELYGASRVNSMGLDLSNEHRLASLSSALLASAHH 632
Cdd:COG4230 477 NGANSSFVNRIADEDVPVEELIADPVEKARALG--GAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAAAAEK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 633 PWRAAPMLADDALEhAAPRDVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMH 712
Cdd:COG4230 555 QWQAAPLIAGEAAS-GEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRA 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 713 TLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDEFSNDT-HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLA 791
Cdd:COG4230 634 ELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 792 KPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRldpDGKPIPLI 871
Cdd:COG4230 714 KPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR---DGPIVPLI 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 872 AETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVID 951
Cdd:COG4230 791 AETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVID 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 952 ADAKRTIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPPTIIEIGNVDELKREVFGPVLHVVRYRRSGLDKLLEQIRATGY 1031
Cdd:COG4230 871 AEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATGY 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1032 GLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLPRLLATRPAGLPRsleaslv 1111
Cdd:COG4230 951 GLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNT------- 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1112 adAPQEGEtrdnpsAALTALRDWLIEQrepalaarcdgylshvlaGATAVLSGPTGERNTYTLGARGTVLCIAATASGAR 1191
Cdd:COG4230 1024 --TAAGGN------ASLLALGDWLASL------------------LGALTLPGPTGERNTLTLRPRGRVLCLADSLEALL 1077
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1192 AQFAAVLATGNRALFagaagealaaalpASLKAQAGVRKQADAAFDAVLFEGdsdELLALVKEVAQRPGPIVSVQGVaag 1271
Cdd:COG4230 1078 AQLAAALATGNRAVV-------------AADLALAGLPAVLLPPFDAVLFEG---RLRALRQALAARDGAIVPVIDA--- 1138
|
1210 1220 1230
....*....|....*....|....*....|....*
gi 1943257567 1272 afenggdeDYALERLLTErsvsvntaaAGGNANLM 1306
Cdd:COG4230 1139 --------GYDLERLLEE---------AGGNASLM 1156
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
599-1099 |
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: 704.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 599 ELYGASRVNSMGLDLSNEHRLASLSSALLASAHHPWRAAPMLADDALEHAAPRDVRNPADLRDIVGTVSEATPEEVGAAL 678
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 679 AHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDEFSNDTHRP 758
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 759 LGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRT 838
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 839 RAVMFTGSTEVARLINKTLSSRLDPdgkPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDD 918
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 919 VADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPD--ACAQGTFVPPTIIEIGN 996
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDsrACQHGTFVAPTLFELDD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 997 VDELKREVFGPVLHVVRYRRSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGE 1076
Cdd:TIGR01238 398 IAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQ 477
|
490 500
....*....|....*....|...
gi 1943257567 1077 GLSGTGPKAGGALYLPRLLATRP 1099
Cdd:TIGR01238 478 GLSGTGPKAGGPHYLYRLTQVQY 500
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
555-1104 |
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: 678.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 555 ANTSFVNRIADKTVsvkelvadplDEAAKVVPLGAPHEKiplprelygasrvnsmgldlsnehrlaslssallasahhPW 634
Cdd:cd07125 1 ANSSFVNRIFDLEV----------PLEALADALKAFDEK---------------------------------------EW 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 635 RAAPMLADDALEHAAPRDVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTL 714
Cdd:cd07125 32 EAIPIINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGEL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 715 MGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDEFS-----------NDTH-RPLGPVVCISPWNFPLAIFMGQVAAA 782
Cdd:cd07125 112 IALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 783 LAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLD 862
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 863 PDgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRL 942
Cdd:cd07125 272 PI---LPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 943 SADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPDAcaQGTFVPPTIIEIGNVDELKREVFGPVLHVVRYRRSGLDKL 1022
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDG--NGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1023 LEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLPRLLATRPAGL 1102
Cdd:cd07125 427 IEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSL 506
|
..
gi 1943257567 1103 PR 1104
Cdd:cd07125 507 NT 508
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
114-1110 |
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: 670.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 114 ARLPASLAPDVQSMAAGLVEALREKSsGGGVEGLIHEFSLSSQEGVALMCLAEALLRIPDRATRDALIRDKISkgdwrsh 193
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAAP-EGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 194 vgHAPSLFVNAATWGLMITgklvttnseaglssaltrLIGKGGEPLIRKGVDMAMRLMGEQFVTGETISEALANSRKYEA 273
Cdd:COG0506 75 --KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 274 RGFRYSYDMLGEAATTEEDALRYYASYEQAIHAIGKAAggrgiYEGPGISIKLSALHARYSRSQQERTMVELLPRVRSLA 353
Cdd:COG0506 135 KGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 354 LLARRYDIGLNIDAEEADRLELSLDLLEALCFDPELAGWNGIGFVVQAYQKRCPFVIDYLVDLARRSRHRLMIRLVKGAY 433
Cdd:COG0506 210 RAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 434 WDTEIKRAQVDGLeGYPVYTRKIYTDVSYLACAKKLLAAPDAVYPQFATHNAYTLAAIYHLAGQ-NYYPGQYEFQCLHGM 512
Cdd:COG0506 290 WDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQMLYGM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 513 GEPLYEEVTGRDK--LNRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNRIADKTVSVKELVADPLDEAAKVVPLGAP 590
Cdd:COG0506 369 GEDLQRALAAVDGgrLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPP 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 591 HekIPLPRELYGASRVNSMGLDLSNEHRLASLSSALLASAHHPWRAAPMLADDALEHAAPRDVRNPADLRDIVGTVSEAT 670
Cdd:COG0506 449 P--PPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 671 PEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDE 750
Cdd:COG0506 527 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAA 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 751 F-------SNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPG 823
Cdd:COG0506 607 AppppppgGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLV 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 824 NGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLDPDGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSA 903
Cdd:COG0506 687 LGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASA 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 904 GQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPD-ACA 982
Cdd:COG0506 767 SASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLvPGL 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 983 QGTFVPPTIIEIGNVDELKREVFGPVLHVVRYRRSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRN 1062
Cdd:COG0506 847 LTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGG 926
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*...
gi 1943257567 1063 VIGAVVGVQPFGGEGLSGTGPKAGGALYLPRLLATRPAGLPRSLEASL 1110
Cdd:COG0506 927 GGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAA 974
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
264-562 |
3.50e-153 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 462.73 E-value: 3.50e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 264 ALANSRKYEARGFRYSYDMLGEAATTEEDALRYYASYEQAIHAIGKAAGGRGIYEGPGISIKLSALHARYSRSQQERTMV 343
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 344 ELLPRVRSLALLARRYDIGLNIDAEEADRLELSLDLLEALCFDPELAGWNGIGFVVQAYQKRCPFVIDYLVDLARRSRHR 423
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 424 LMIRLVKGAYWDTEIKRAQVdGLEGYPVYTRKIYTDVSYLACAKKLLAAPDAVYPQFATHNAYTLAAIYHLAGQ-NYYPG 502
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 503 QYEFQCLHGMGEPLYEEVTGRDklnRPCRVYAPVGTHETLLAYLVRRLLENGANTSFVNR 562
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAAG---YRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
634-1095 |
5.89e-142 |
|
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: 441.25 E-value: 5.89e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 634 WRAAPMLADDALEHAAPRDVR-NPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMH 712
Cdd:cd07083 16 GRAYPLVIGGEWVDTKERMVSvSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 713 TLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRD-------------EFSNDTHRPLGPVVCISPWNFPLAIFMGQV 779
Cdd:cd07083 96 ELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRlrypavevvpypgEDNESFYVGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 780 AAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSS 859
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 860 RLDPDGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNP 939
Cdd:cd07083 256 LAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 940 DRLSADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPDacAQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYRRS 1017
Cdd:cd07083 336 EENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLE--GEGYFVAPTVVEEVPPKAriAQEEIFGPVLSVIRYKDD 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1943257567 1018 GLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLPRLL 1095
Cdd:cd07083 414 DFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFL 491
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
652-1092 |
3.20e-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: 3.20e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07124 49 ESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYYSAQIR-----------DEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 800
Cdd:cd07124 129 DVAEAIDFLEYYAREMLrlrgfpvemvpGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 801 AAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLDPDGKPIPLIAETGGQNAM 880
Cdd:cd07124 209 AAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 881 IVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDA 960
Cdd:cd07124 289 IVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 961 HIAAMKDKGHAVTQLAMPDACAQGTFVPPTIieIGNVDELKR----EVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLG 1036
Cdd:cd07124 369 YIEIGKSEGRLLLGGEVLELAAEGYFVQPTI--FADVPPDHRlaqeEIFGPVLAVIKAK--DFDEALEIANDTEYGLTGG 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1037 IHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLP 1092
Cdd:cd07124 445 VFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLL 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
652-1088 |
1.53e-118 |
|
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: 377.93 E-value: 1.53e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:COG1012 24 DVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYYSAQIR------------DEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:COG1012 103 EVDRAADFLRYYAGEARrlygetipsdapGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNA 879
Cdd:COG1012 183 SALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVTLELGGKNP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 880 MIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTID 959
Cdd:COG1012 257 AIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 960 AHIAAMKDKGHAVtqLAMPDAC--AQGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGL 1033
Cdd:COG1012 337 AYIEDAVAEGAEL--LTGGRRPdgEGGYFVEPTVLA--DVTPdmriAREEIFGPVLSVIPFD--DEEEAIALANDTEYGL 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1943257567 1034 TLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGvQPFGGEGLSGTGPKAGGA 1088
Cdd:COG1012 411 AASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGRE 464
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
652-1086 |
2.63e-112 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 360.31 E-value: 2.63e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:pfam00171 10 EVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYYSAQIR-----------DEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 800
Cdd:pfam00171 89 EVDRAIDVLRYYAGLARrldgetlpsdpGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 801 AAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAM 880
Cdd:pfam00171 169 ALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 881 IVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDA 960
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 961 HIAAMKDKGHAVTQLAMPDaCAQGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLG 1036
Cdd:pfam00171 323 YVEDAKEEGAKLLTGGEAG-LDNGYFVEPTVLA--NVTPdmriAQEEIFGPVLSVIRF--KDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1037 IHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVqPFGGEGLSGTGPKAG 1086
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFGREGG 446
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
655-1091 |
8.17e-107 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 347.69 E-value: 8.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIR 734
Cdd:PRK03137 56 NPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 735 EAVDFLRYYSAQ------------IRDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 802
Cdd:PRK03137 136 EAIDFLEYYARQmlkladgkpvesRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 803 QAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINkTLSSRLDPDGKPIP-LIAETGGQNAMI 881
Cdd:PRK03137 216 KFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIY-ERAAKVQPGQIWLKrVIAEMGGKDAIV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 882 VDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRlSADVGPVIDADAKRTIDAH 961
Cdd:PRK03137 295 VDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSY 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 962 IAAMKDKGHAVTQLAMPDacAQGTFVPPTIieIGNVDELKR----EVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGI 1037
Cdd:PRK03137 374 IEIGKEEGRLVLGGEGDD--SKGYFIQPTI--FADVDPKARimqeEIFGPVVAFIKAK--DFDHALEIANNTEYGLTGAV 447
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1943257567 1038 HTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYL 1091
Cdd:PRK03137 448 ISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYL 501
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
655-1098 |
1.35e-106 |
|
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: 346.85 E-value: 1.35e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIR 734
Cdd:TIGR01237 52 NPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 735 EAVDFLRYYSAQIRD--------EFSNDTHR----PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 802
Cdd:TIGR01237 132 EAIDFMEYYARQMIElakgkpvnSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 803 QAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTlSSRLDPDGKPIP-LIAETGGQNAMI 881
Cdd:TIGR01237 212 KFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFER-AAKVQPGQKHLKrVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 882 VDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAH 961
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 962 IAAMKDKGHAVtqLAMPDACAQGTFVPPTIieIGNVDELKR----EVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGI 1037
Cdd:TIGR01237 371 IEIGKAEGRLV--SGGCGDDSKGYFIGPTI--FADVDRKARlaqeEIFGPVVAFIRA--SDFDEALEIANNTEYGLTGGV 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943257567 1038 HTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLPRLLATR 1098
Cdd:TIGR01237 445 ISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAK 505
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
686-1082 |
7.33e-106 |
|
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: 341.88 E-value: 7.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 686 PIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIR------------DEFSN 753
Cdd:cd07078 12 KAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARrlhgevipspdpGELAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 754 DTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALV 833
Cdd:cd07078 92 VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 834 ADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVL 913
Cdd:cd07078 172 SHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 914 CLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPPTIIE 993
Cdd:cd07078 246 LVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFVPPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 994 igNVDE----LKREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTRiDETIAH-VISHAHVGNIYVNRNVIGAVV 1068
Cdd:cd07078 326 --DVDPdmpiAQEEIFGPVLPVIPFKD--EEEAIELANDTEYGLAAGVFTR-DLERALrVAERLEAGTVWINDYSVGAEP 400
|
410
....*....|....
gi 1943257567 1069 GvQPFGGEGLSGTG 1082
Cdd:cd07078 401 S-APFGGVKQSGIG 413
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
648-1087 |
8.66e-89 |
|
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: 296.47 E-value: 8.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 648 AAPRDVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLP 727
Cdd:cd07097 13 GDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 728 NAIAEIREAVDFLRYYSAQ-----------IRDEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 795
Cdd:cd07097 93 EARGEVTRAGQIFRYYAGEalrlsgetlpsTRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 796 QTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRldpdGKPIPLiaETG 875
Cdd:cd07097 173 LTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR----GARVQL--EMG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 876 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAK 955
Cdd:cd07097 247 GKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 956 RTIDAHIAAMKDKGHAVT----QLAMPDacaQGTFVPPTIIEigNVDELKR----EVFGPVLHVVRYRrsGLDKLLEQIR 1027
Cdd:cd07097 327 EKDLRYIEIARSEGAKLVyggeRLKRPD---EGYYLAPALFA--GVTNDMRiareEIFGPVAAVIRVR--DYDEALAIAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1028 ATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVqPFGGEGLSGTGPKAGG 1087
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQG 458
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
652-1089 |
1.59e-82 |
|
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: 279.23 E-value: 1.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07131 17 DSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDfLRYYSA-------------QIRDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 798
Cdd:cd07131 97 DVQEAID-MAQYAAgegrrlfgetvpsELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 799 LIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLssrldpdGKPIPLIA-ETGGQ 877
Cdd:cd07131 176 ACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETC-------ARPNKRVAlEMGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 878 NAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRT 957
Cdd:cd07131 249 NPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 958 IDAHIAAMKDKGHAV---TQLAMPDACAQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYG 1032
Cdd:cd07131 329 VLNYNEIGKEEGATLllgGERLTGGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEV--SSLEEAIEIANDTEYG 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1943257567 1033 LTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVqPFGGEGLSGTG-PKAGGAL 1089
Cdd:cd07131 407 LSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGhREAGTTA 463
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
652-1086 |
3.21e-82 |
|
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: 278.29 E-value: 3.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRDIVgTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07086 16 TSRNPANGEPIA-RVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYYSAQIR------------DEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:cd07086 95 EVQEMIDICDYAVGLSRmlygltipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDA----GVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdGKPIpliAETG 875
Cdd:cd07086 175 TAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRVL---LELG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 876 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAK 955
Cdd:cd07086 248 GNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 956 RTIDAHIA-AMKDKGHAVTQLAMPDACAQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYG 1032
Cdd:cd07086 328 EKYLNAIEiAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDAriVQEETFAPILYVIKF--DSLEEAIAINNDVPQG 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1033 LTLGIHTRIDETIAHVISHA--HVGNIYVNRNVIGAVVGVqPFGGEGLSGTGPKAG 1086
Cdd:cd07086 406 LSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
653-1082 |
2.19e-81 |
|
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: 274.69 E-value: 2.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADLRdIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAE 732
Cdd:cd07103 1 VINPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 733 IREAVDFLRYYSAQIR--------DEFSND----THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 800
Cdd:cd07103 80 VDYAASFLEWFAEEARriygrtipSPAPGKrilvIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 801 AAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAM 880
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV----KRVSL--ELGGNAPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 881 IVDSSALAEQVVADVLQSSFDSAGQRC-SALRVLClQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTID 959
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 960 AHIAAMKDKG-HAVTQLAMPDacAQGTFVPPTIIEIGNVDEL--KREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLG 1036
Cdd:cd07103 313 ALVEDAVAKGaKVLTGGKRLG--LGGYFYEPTVLTDVTDDMLimNEETFGPVAPIIPF--DTEDEVIARANDTPYGLAAY 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1943257567 1037 IHTRIDETIAHVISHAHVGNIYVNRNVIGAVvgVQPFGGEGLSGTG 1082
Cdd:cd07103 389 VFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
686-1086 |
2.64e-81 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 271.41 E-value: 2.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 686 PIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDEFSNDT---------- 755
Cdd:cd06534 8 KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELpspdpggeay 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 --HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALV 833
Cdd:cd06534 88 vrREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 834 ADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVL 913
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 914 CLQDDVADRTLTMLKGamrelalgnpdrLSADVGPvidadakrtidahiaamkdkghavtqlAMPdacaqgtfvpptiie 993
Cdd:cd06534 242 LVHESIYDEFVEKLVT------------VLVDVDP---------------------------DMP--------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 994 ignvdELKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTRiDETIAH-VISHAHVGNIYVNRNVIGAVVGvQP 1072
Cdd:cd06534 268 -----IAQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTR-DLNRALrVAERLRAGTVYINDSSIGVGPE-AP 338
|
410
....*....|....
gi 1943257567 1073 FGGEGLSGTGPKAG 1086
Cdd:cd06534 339 FGGVKNSGIGREGG 352
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
652-1082 |
9.20e-72 |
|
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: 247.65 E-value: 9.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLrDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07145 2 EVRNPANG-EVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLR---YYSAQIRDEFSN-------------DTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 795
Cdd:cd07145 81 EVERTIRLFKlaaEEAKVLRGETIPvdayeynerriafTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 796 QTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLInktlSSRLDPDGKPIplIAETG 875
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI----ASKAGGTGKKV--ALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 876 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAK 955
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 956 RTIDAHIAAMKDKGHAVTQLAMPDacaQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYRRSglDKLLEQIRATGYGL 1033
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKRD---EGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDD--EEAVEIANSTEYGL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1943257567 1034 TLGIHTRiDETIAHVISHA-HVGNIYVN---RNVIGAVvgvqPFGGEGLSGTG 1082
Cdd:cd07145 390 QASVFTN-DINRALKVARElEAGGVVINdstRFRWDNL----PFGGFKKSGIG 437
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
651-1093 |
1.59e-70 |
|
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: 246.34 E-value: 1.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 651 RDVRNPADLRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLL------EAQMHTLMGlivreAGK 724
Cdd:cd07123 48 GKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLsgkyryELNAATMLG-----QGK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 725 slpNAI-AEIR---EAVDFLR---YYSAQI---------RDEFSNDTHRPL-GPVVCISPWNFPlAIfMGQVAAALA-AG 786
Cdd:cd07123 123 ---NVWqAEIDaacELIDFLRfnvKYAEELyaqqplsspAGVWNRLEYRPLeGFVYAVSPFNFT-AI-GGNLAGAPAlMG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 787 NTVLAKPAEqTPLIAAQAV-RLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLDpDG 865
Cdd:cd07123 198 NVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLD-RY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 866 KPIP-LIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSAL-RV---LCLQDDVADRTLTMLKgamrELALGNPD 940
Cdd:cd07123 276 RTYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAAsRAyvpESLWPEVKERLLEELK----EIKMGDPD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 941 RLSADVGPVIDADAKRTIDAHI-AAMKDKGHAVTQLAMPDAcAQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYRRS 1017
Cdd:cd07123 352 DFSNFMGAVIDEKAFDRIKGYIdHAKSDPEAEIIAGGKCDD-SVGYFVEPTVIETTDPKHklMTEEIFGPVLTVYVYPDS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1018 GLDKLLEQIRATG-YGLTLGIHTRiD----ETIAHVISHAhVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAGGALYLP 1092
Cdd:cd07123 431 DFEETLELVDTTSpYALTGAIFAQ-DrkaiREATDALRNA-AGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLL 508
|
.
gi 1943257567 1093 R 1093
Cdd:cd07123 509 R 509
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
652-1082 |
8.22e-70 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 242.12 E-value: 8.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07149 2 EVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFL--------RYYSAQI--------RDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 795
Cdd:cd07149 81 EVDRAIETLrlsaeeakRLAGETIpfdaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 796 QTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRldpdgkpiPLIAETG 875
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--------KVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 876 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SALRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADA 954
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 955 KRTIDAHIAAMKDKGHAVTQLAMPDacaqGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYRRsgLDKLLEQIRATG 1030
Cdd:cd07149 312 AERIEEWVEEAVEGGARLLTGGKRD----GAILEPTVLT--DVPPdmkvVCEEVFAPVVSLNPFDT--LDEAIAMANDSP 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1031 YGLTLGIHTRIDETIAHVISHAHVGNIYVNrNVIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07149 384 YGLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
652-1061 |
3.92e-69 |
|
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: 240.63 E-value: 3.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07088 16 DVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYYSAQIR--------DEFSNDT----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:cd07088 95 EVEFTADYIDYMAEWARriegeiipSDRPNENififKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNA 879
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVSLELGGKAP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 880 MIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTID 959
Cdd:cd07088 249 AIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 960 AHIAAMKDKGHAVTQLAMPDACAQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTL 1035
Cdd:cd07088 329 EMVERAVEAGATLLTGGKRPEGEKGYFYEPTV--LTNVRQdmeiVQEEIFGPVLPVVKF--SSLDEAIELANDSEYGLTS 404
|
410 420
....*....|....*....|....*.
gi 1943257567 1036 GIHTRIDETIAHVISHAHVGNIYVNR 1061
Cdd:cd07088 405 YIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
654-1082 |
1.11e-68 |
|
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: 238.66 E-value: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 654 RNPADLRDiVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEI 733
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 734 REAVDFLRYYSAQI----RDEFSND-----------THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 798
Cdd:cd07099 80 LLALEAIDWAARNAprvlAPRKVPTgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 799 LIAAQAVRLLRDAGVPAGAVQLLPGNGETvGAALVaDSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQN 878
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGSVATGRKVMAAAAERL------IPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 879 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTI 958
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKG-HAVTQLAmpDACAQGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYGL 1033
Cdd:cd07099 312 RRHVDDAVAKGaKALTGGA--RSNGGGPFYEPTVLT--DVPHdmdvMREETFGPVLPVMPV--ADEDEAIALANDSRYGL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1943257567 1034 TLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07099 386 SASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
653-1082 |
7.39e-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: 236.27 E-value: 7.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAE 732
Cdd:cd07106 1 VINPAT-GEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 733 IREAVDFLRYYsAQIRDE----FSNDT------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 802
Cdd:cd07106 80 VGGAVAWLRYT-ASLDLPdeviEDDDTrrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 803 QAVRLLRDAgVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIV 882
Cdd:cd07106 159 KLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 883 DSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHI 962
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 963 AAMKDKGHAVTQLAMPDaCAQGTFVPPTIieIGNVDELKR----EVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIH 1038
Cdd:cd07106 311 EDAKAKGAKVLAGGEPL-DGPGYFIPPTI--VDDPPEGSRivdeEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1943257567 1039 TRiDETIA-HVISHAHVGNIYVNRnvIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07106 386 SS-DLERAeAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
653-1082 |
5.15e-67 |
|
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: 234.00 E-value: 5.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSL------ 726
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPItlartr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 727 --PNAIAEIREAVDFLRYYSAQI---RDEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 800
Cdd:cd07093 80 diPRAAANFRFFADYILQLDGESypqDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 801 AAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAM 880
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 881 IVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDA 960
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 961 HIAAMKDKGHAVT---QLAMPDACAQGTFVPPTIIE-IGNVDEL-KREVFGPVLHVVRYRRSglDKLLEQIRATGYGLTL 1035
Cdd:cd07093 314 YVELARAEGATILtggGRPELPDLEGGYFVEPTVITgLDNDSRVaQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1036 GIHTRiDETIAHVISHA-HVGNIYVN----RNVigavvgVQPFGGEGLSGTG 1082
Cdd:cd07093 392 YVWTR-DLGRAHRVARRlEAGTVWVNcwlvRDL------RTPFGGVKASGIG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
686-1088 |
2.62e-66 |
|
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: 231.01 E-value: 2.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 686 PIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNA-------IAEIREAVDFLRYYSAQIRDEFSND---- 754
Cdd:cd07095 14 PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAqtevaamAGKIDISIKAYHERTGERATPMAQGravl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 755 THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETvGAALVA 834
Cdd:cd07095 94 RHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRET-GEALAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 835 DSRTRAVMFTGSTEVARLINKTLSsrldpdGKPIPLIA-ETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCS-ALRV 912
Cdd:cd07095 173 HEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTcARRL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 913 LCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGhAVTQLAMPDACAQGTFVPPTII 992
Cdd:cd07095 247 IVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALG-GEPLLAMERLVAGTAFLSPGII 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 993 EIGNVDEL-KREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAvVGVQ 1071
Cdd:cd07095 326 DVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGA-SSTA 402
|
410
....*....|....*...
gi 1943257567 1072 PFGGEGLSGTG-PKAGGA 1088
Cdd:cd07095 403 PFGGVGLSGNHrPSAYYA 420
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
652-1086 |
2.66e-66 |
|
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: 232.48 E-value: 2.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDA--RADCLARAADLLEAQMHTLMGLIVREAGKSLP-N 728
Cdd:cd07091 22 PTINPAT-EEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPreRGRLLNKLADLIERDRDELAALESLDNGKPLEeS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 729 AIAEIREAVDFLRYYSA----------QIRDEFSNDTHR-PLGpvVC--ISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 795
Cdd:cd07091 101 AKGDVALSIKCLRYYAGwadkiqgktiPIDGNFLAYTRRePIG--VCgqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 796 QTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKT-LSSRLdpdgKPIPLiaET 874
Cdd:cd07091 179 QTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAaAKSNL----KKVTL--EL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 875 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADA 954
Cdd:cd07091 253 GGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 955 KRTIDAHIAAMKDKG-HAVTQLAMPDacAQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIRAT 1029
Cdd:cd07091 333 FDKILSYIESGKKEGaTLLTGGERHG--SKGYFIQPTV--FTDVKDdmkiAKEEIFGPVVTILKF--KTEDEVIERANDT 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1943257567 1030 GYGLTLGIHTRiDETIAHVISHA-HVGNIYVNR-NVIGAVVgvqPFGGEGLSGTGPKAG 1086
Cdd:cd07091 407 EYGLAAGVFTK-DINKALRVSRAlKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
653-1086 |
9.01e-66 |
|
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: 230.52 E-value: 9.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADlRDIVGTVSEATPEEVGAALAHAVA--AAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI 730
Cdd:cd07114 1 SINPAT-GEPWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 731 AEIREAVDFLRYYSAQIR------------DEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 798
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADkiegavipvdkgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 799 LIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQN 878
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 879 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTI 958
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKGHAVT---QLAMPDACAQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYRRSglDKLLEQIRATGYGL 1033
Cdd:cd07114 314 ERYVARAREEGARVLtggERPSGADLGAGYFFEPTILADVTNDMriAQEEVFGPVLSVIPFDDE--EEAIALANDSEYGL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1943257567 1034 TLGIHTRiDETIAHVISHA-HVGNIYVN---RNVIGAvvgvqPFGGEGLSGTGPKAG 1086
Cdd:cd07114 392 AAGIWTR-DLARAHRVARAiEAGTVWVNtyrALSPSS-----PFGGFKDSGIGRENG 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
652-1082 |
3.42e-65 |
|
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: 229.38 E-value: 3.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRdIVGTVSEATPEEVGAALAHAVAAAPIWQAT-PVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI 730
Cdd:cd07082 19 EVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 731 AEIREAVDFLRY-----------YS------------AQIRDEfsndthrPLGPVVCISPWNFPLAIFMGQVAAALAAGN 787
Cdd:cd07082 98 KEVDRTIDYIRDtieelkrldgdSLpgdwfpgtkgkiAQVRRE-------PLGVVLAIGPFNYPLNLTVSKLIPALIMGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 788 TVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSrldpdgkp 867
Cdd:cd07082 171 TVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 868 IPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVG 947
Cdd:cd07082 243 KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 948 PVIDADAKRTIDAHIAAMKDKGHAVTQlamPDACAQGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYrrSGLDKLL 1023
Cdd:cd07082 323 PLIDPKSADFVEGLIDDAVAKGATVLN---GGGREGGNLIYPTLLD--PVTPdmrlAWEEPFGPVLPIIRV--NDIEEAI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943257567 1024 EQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVN----RNvigavVGVQPFGGEGLSGTG 1082
Cdd:cd07082 396 ELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRG-----PDHFPFLGRKDSGIG 453
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
144-255 |
1.14e-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: 214.29 E-value: 1.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 144 VEGLIHEFSLSSQEGVALMCLAEALLRIPDRATRDALIRDKISKGDWRSHVGHAPSLFVNAATWGLMITGKLVTTNSEAG 223
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 1943257567 224 LSSALTRLIGKGGEPLIRKGVDMAMRLMGEQF 255
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
655-1086 |
7.99e-64 |
|
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: 224.63 E-value: 7.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNA-IAEI 733
Cdd:cd07115 3 NPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 734 REAVDFLRYYSA----------QIRDEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 802
Cdd:cd07115 82 PRAADTFRYYAGwadkiegeviPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 803 QAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIV 882
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNL----KRVSL--ELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 883 DSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHI 962
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 963 -AAMKDKGHAVTQLAMPDacAQGTFVPPTIIEigNVDELKR----EVFGPVLHVVRYRRSglDKLLEQIRATGYGLTLGI 1037
Cdd:cd07115 316 dVGREEGARLLTGGKRPG--ARGFFVEPTIFA--AVPPEMRiaqeEIFGPVVSVMRFRDE--EEALRIANGTEYGLAAGV 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1038 HTRiDETIAHVISHA-HVGNIYVnrNVIGAVVGVQPFGGEGLSGTGPKAG 1086
Cdd:cd07115 390 WTR-DLGRAHRVAAAlKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
652-1082 |
3.10e-63 |
|
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: 223.55 E-value: 3.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07085 19 DVYNPAT-GEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIR---EAVDF--------LRYYSAQIRDEFsnDTH---RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 797
Cdd:cd07085 98 DVLrglEVVEFacsiphllKGEYLENVARGI--DTYsyrQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 798 PLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGaALVADSRTRAVMFTGSTEVARLINKTLSSRldpdGKPIplIAETGGQ 877
Cdd:cd07085 176 PGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEYIYERAAAN----GKRV--QALGGAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 878 NAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRT 957
Cdd:cd07085 249 NHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKER 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 958 IDAHIAAMKDKGHAVT---QLAMPDACAQGTFVPPTIIEigNV----DELKREVFGPVLHVVRYRRsgLDKLLEQIRATG 1030
Cdd:cd07085 329 IEGLIESGVEEGAKLVldgRGVKVPGYENGNFVGPTILD--NVtpdmKIYKEEIFGPVLSIVRVDT--LDEAIAIINANP 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1943257567 1031 YGLTLGIHTRIDETIAHVISHAHVGNIYVnrNV-IGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07085 405 YGNGAAIFTRSGAAARKFQREVDAGMVGI--NVpIPVPLAFFSFGGWKGSFFG 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
653-1086 |
4.00e-62 |
|
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: 219.54 E-value: 4.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPiwQATPVDaRADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAE 732
Cdd:cd07146 3 VRNPYT-GEVVGTVPAGTEEALREALALAASYRS--TLTRYQ-RSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 733 IREAVDFLRYYSAQI-RDE---FSND-----------THR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQ 796
Cdd:cd07146 79 VGRAADVLRFAAAEAlRDDgesFSCDltangkarkifTLRePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 797 TPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRldpdgkpiPLIAETGG 876
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 877 QNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKR 956
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 957 TIDAHIAAMKDKGHAVtqlaMPDACAQGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYRrsGLDKLLEQIRATGYG 1032
Cdd:cd07146 311 QIENRVEEAIAQGARV----LLGNQRQGALYAPTVLD--HVPPdaelVTEETFGPVAPVIRVK--DLDEAIAISNSTAYG 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1943257567 1033 LTLGIHTRIDETIAHVISHAHVGNIYVNrNVIGAVVGVQPFGGEGLSGTGPKAG 1086
Cdd:cd07146 383 LSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
651-1082 |
2.58e-61 |
|
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: 218.33 E-value: 2.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 651 RDVRNPADlRDIVGTVSEATPEEVGAALAHAVAA--APIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPN 728
Cdd:cd07119 15 RDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 729 AIAEIREAVDFLRYYSAQIRDE-----------FSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 797
Cdd:cd07119 94 SEIDIDDVANCFRYYAGLATKEtgevydvpphvISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 798 PLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQ 877
Cdd:cd07119 174 PLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV----KKVAL--ELGGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 878 NAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRT 957
Cdd:cd07119 248 NPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 958 IDAHIAAMKDKGHAVT---QLAMPDACAQGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYRRSglDKLLEQIRATG 1030
Cdd:cd07119 328 VLSYIQLGKEEGARLVcggKRPTGDELAKGYFVEPTIFD--DVDRtmriVQEEIFGPVLTVERFDTE--EEAIRLANDTP 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1943257567 1031 YGLTLGIHTRiDETIAH-VISHAHVGNIYVNRnvIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07119 404 YGLAGAVWTK-DIARANrVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
688-1082 |
2.86e-61 |
|
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: 216.63 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 688 WQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLR------------YYSAQIRDEFSNDT 755
Cdd:cd07104 16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILReaaglprrpegeILPSDVPGKESMVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP-----LIAaqavRLLRDAGVPAGAVQLLPGNGETVGA 830
Cdd:cd07104 96 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPKGVLNVVPGGGSEIGD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 831 ALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SA 909
Cdd:cd07104 172 ALVEHPRVRMISFTGSTAVGRHIGELAGRHL----KKVAL--ELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICmAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 910 LRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHAVtqlaMPDACAQGTFVPP 989
Cdd:cd07104 246 GRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL----LTGGTYEGLFYQP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 990 TIieIGNVDE----LKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVI- 1064
Cdd:cd07104 321 TV--LSDVTPdmpiFREEIFGPVAPVIPFD--DDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVn 396
|
410
....*....|....*....
gi 1943257567 1065 -GAVVgvqPFGGEGLSGTG 1082
Cdd:cd07104 397 dEPHV---PFGGVKASGGG 412
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
653-1082 |
5.30e-61 |
|
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: 216.33 E-value: 5.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADLRDIvGTVSEATPEEVGAALAHAVAAAPIW--QATPVDaRADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI 730
Cdd:cd07109 1 VFDPSTGEVF-ARIARGGAADVDRAVQAARRAFESGwlRLSPAE-RGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 731 AEIREAVDFLRYYSAQIrDEFSNDT------------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 798
Cdd:cd07109 79 ADVEAAARYFEYYGGAA-DKLHGETiplgpgyfvytvREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 799 LIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQN 878
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 879 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGnPDRLSADVGPVIDADAKRTI 958
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKG-HAVTQ-LAMPDACAQGTFVPPTIieIGNV---DELKR-EVFGPVLHVVRYRrsGLDKLLEQIRATGYG 1032
Cdd:cd07109 311 EGFVARARARGaRIVAGgRIAEGAPAGGYFVAPTL--LDDVppdSRLAQeEIFGPVLAVMPFD--DEAEAIALANGTDYG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1033 LTLGIHTRiDETIAHVISHA-HVGNIYVNRnvIGAVVGVQ-PFGGEGLSGTG 1082
Cdd:cd07109 387 LVAGVWTR-DGDRALRVARRlRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
652-1082 |
1.02e-60 |
|
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: 215.76 E-value: 1.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07094 2 DVHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLR---YYSAQIRDE-------FSNDTHR------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 795
Cdd:cd07094 81 EVDRAIDTLRlaaEEAERIRGEeipldatQGSDNRLawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 796 QTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLssrldpdgkPIPLIA-ET 874
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA---------GGKRIAlEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 875 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADA 954
Cdd:cd07094 232 GGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 955 KRTIDAHIAAMKDKGHAVTQLAMPDacaqGTFVPPTIIEIGNVDEL--KREVFGPVLHVVRYRRsgLDKLLEQIRATGYG 1032
Cdd:cd07094 312 AERVERWVEEAVEAGARLLCGGERD----GALFKPTVLEDVPRDTKlsTEETFGPVVPIIRYDD--FEEAIRIANSTDYG 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1033 LTLGIHTRIDETIAHVISHAHVGNIYVNRNVIgAVVGVQPFGGEGLSGTG 1082
Cdd:cd07094 386 LQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
653-1085 |
7.47e-60 |
|
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: 213.38 E-value: 7.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSL-PNAIA 731
Cdd:cd07108 1 VINPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYY---SAQIRDE--------FSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLI 800
Cdd:cd07108 80 EAAVLADLFRYFgglAGELKGEtlpfgpdvLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 801 AAQAVRLLRDAgVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAM 880
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 881 IVDSSALAEQVVADVLQSS-FDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTID 959
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 960 AHIAAMKDKGHA--VTQLAMP--DACAQGTFVPPTII-EIGNVDELKR-EVFGPVLHVVRYrrSGLDKLLEQIRATGYGL 1033
Cdd:cd07108 313 GYIDLGLSTSGAtvLRGGPLPgeGPLADGFFVQPTIFsGVDNEWRLAReEIFGPVLCAIPW--KDEDEVIAMANDSHYGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1943257567 1034 TLGIHTRiDETIAHVISHA-HVGNIYVNRNViGAVVGvQPFGGEGLSGTGPKA 1085
Cdd:cd07108 391 AAYVWTR-DLGRALRAAHAlEAGWVQVNQGG-GQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
663-1086 |
1.19e-59 |
|
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: 212.55 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 663 VGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRY 742
Cdd:cd07101 9 LGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 743 YSAQIRDEF--------------SNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLL 808
Cdd:cd07101 89 YARRAERLLkprrrrgaipvltrTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 809 RDAGVPAGAVQLLPGNGETVGAALVAdsRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALA 888
Cdd:cd07101 169 IEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 889 EQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDK 968
Cdd:cd07101 241 DKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 969 GHAVTQ--LAMPDAcaqGT-FVPPTIIEigNVDE----LKREVFGPVLHVvrYRRSGLDKLLEQIRATGYGLTLGIHTRI 1041
Cdd:cd07101 321 GATVLAggRARPDL---GPyFYEPTVLT--GVTEdmelFAEETFGPVVSI--YRVADDDEAIELANDTDYGLNASVWTRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1943257567 1042 DETIAHVISHAHVGNIYVNRNVIGAVVGVQ-PFGGEGLSGTGPKAG 1086
Cdd:cd07101 394 GARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
653-1082 |
4.95e-59 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 210.95 E-value: 4.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIW-QATPVDARADCLARAADLLEAQMHTLMGLIVREAGKS------ 725
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmtara 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 726 --LPNAIAEIREAVDFLRYYSAQIRDEFSNDT---------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPA 794
Cdd:cd07089 80 mqVDGPIGHLRYFADLADSFPWEFDLPVPALRggpgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 795 EQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaET 874
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 875 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADA 954
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 955 KRTIDAHIAAMKDKG-HAVTQLAMPDACAQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYRrsGLDkllEQIR-- 1027
Cdd:cd07089 314 RDRVEGYIARGRDEGaRLVTGGGRPAGLDKGFYVEPTL--FADVDNdmriAQEEIFGPVLVVIPYD--DDD---EAVRia 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1028 -ATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGvqPFGGEGLSGTG 1082
Cdd:cd07089 387 nDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDA--PFGGYKQSGLG 440
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
652-1087 |
6.44e-59 |
|
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: 210.91 E-value: 6.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRDIVgTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07130 15 TSISPANGEPIA-RVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRY--------YSAQIRDEFSNdtHR------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 797
Cdd:cd07130 94 EVQEMIDICDFavglsrqlYGLTIPSERPG--HRmmeqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 798 PL--IAAQAV--RLLRDAGVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdGKpipLIAE 873
Cdd:cd07130 172 PLtaIAVTKIvaRVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---GR---SLLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 874 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDAD 953
Cdd:cd07130 245 LGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 954 AKRTIDAHIAAMKDKGHAV----TQLAMPdacaqGTFVPPTIIEIGNVDEL-KREVFGPVLHVVRYrrSGLDKLLEQIRA 1028
Cdd:cd07130 325 AVDNYLAAIEEAKSQGGTVlfggKVIDGP-----GNYVEPTIVEGLSDAPIvKEETFAPILYVLKF--DTLEEAIAWNNE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943257567 1029 TGYGLTLGIHTRIDETIAHVISHA--HVGNIYVNRNVIGAVVGvQPFGGEGLSGTGPKAGG 1087
Cdd:cd07130 398 VPQGLSSSIFTTDLRNAFRWLGPKgsDCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
686-1082 |
2.19e-58 |
|
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: 208.08 E-value: 2.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 686 PIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYS----AQIRDEFSND------- 754
Cdd:cd07100 13 LAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenaeAFLADEPIETdagkayv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 755 THRPLGPVVCISPWNFPLAifmgQV----AAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVgA 830
Cdd:cd07100 93 RYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLIDSDQV-E 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 831 ALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SA 909
Cdd:cd07100 168 AIIADPRVRGVTLTGSERAGRAVAAEAGKNL----KKSVL--ELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCiAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 910 LRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKG-HAVTQLAMPDacAQGTFVP 988
Cdd:cd07100 242 KRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLGGKRPD--GPGAFYP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 989 PTIIEigNVDE----LKREVFGPVLHVvrYRRSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNrnvi 1064
Cdd:cd07100 319 PTVLT--DVTPgmpaYDEELFGPVAAV--IKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN---- 390
|
410 420
....*....|....*....|.
gi 1943257567 1065 gAVVGVQ---PFGGEGLSGTG 1082
Cdd:cd07100 391 -GMVKSDprlPFGGVKRSGYG 410
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
652-1082 |
2.28e-58 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 209.00 E-value: 2.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRdIVGTVSEATPEEVGAALAHAVAAAP--IWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNA 729
Cdd:cd07112 5 ATINPATGR-VLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 730 IA-EIREAVDFLRYYSAQI-----------RDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 797
Cdd:cd07112 84 LAvDVPSAANTFRWYAEAIdkvygevaptgPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 798 PLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLInktLSSRLDPDGKPIPLiaETGGQ 877
Cdd:cd07112 164 PLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRF---LEYSGQSNLKRVWL--ECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 878 NAMIV-----DSSALAEQVVAdvlqSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDA 952
Cdd:cd07112 239 SPNIVfadapDLDAAAEAAAA----GIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 953 DAKRTIDAHIAAMKDKGHAVT---QLAMPDacAQGTFVPPTIIE-IGNVDELKR-EVFGPVLHVVRYrrSGLDKLLEQIR 1027
Cdd:cd07112 315 AHFDKVLGYIESGKAEGARLVaggKRVLTE--TGGFFVEPTVFDgVTPDMRIAReEIFGPVLSVITF--DSEEEAVALAN 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1028 ATGYGLTLGIHTRiDETIAHVISHA-HVGNIYVnrNVIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07112 391 DSVYGLAASVWTS-DLSRAHRVARRlRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
651-1087 |
3.36e-58 |
|
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: 208.34 E-value: 3.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 651 RDVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI 730
Cdd:cd07150 1 FDDLNPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 731 AEIREAVDFLRYYSAQIR------------DEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 798
Cdd:cd07150 80 FETTFTPELLRAAAGECRrvrgetlpsdspGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 799 LIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQN 878
Cdd:cd07150 160 VIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHL----KKITL--ELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 879 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTI 958
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKGHAVtqlaMPDACAQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLT 1034
Cdd:cd07150 314 KRQVEDAVAKGAKL----LTGGKYDGNFYQPTV--LTDVTPdmriFREETFGPVTSVIPA--KDAEEALELANDTEYGLS 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1035 LGIHTRiDETIA-HVISHAHVGNIYVNRNVI--GAVVgvqPFGGEGLSGTGpKAGG 1087
Cdd:cd07150 386 AAILTN-DLQRAfKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGG 436
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
661-1088 |
4.02e-58 |
|
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: 207.92 E-value: 4.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 661 DIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFL 740
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 741 RYYSA-----------QIRDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP-----LIAaqa 804
Cdd:cd07152 82 HEAAGlptqpqgeilpSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggvVIA--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 805 vRLLRDAGVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIVDS 884
Cdd:cd07152 159 -RLFEEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHL----KKVSL--ELGGKNALIVLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 885 SALAEQVVADVLQSSFDSAGQRC-SALRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIA 963
Cdd:cd07152 231 DADLDLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 964 AMKDKGHAVTQlampDACAQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHT 1039
Cdd:cd07152 310 DSVAAGARLEA----GGTYDGLFYRPTV--LSGVKPgmpaFDEEIFGPVAPVTVF--DSDEEAVALANDTEYGLSAGIIS 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1040 RIDETIAHVISHAHVGNIYVN-RNVIGAVVGvqPFGGEGLSGTGPKAGGA 1088
Cdd:cd07152 382 RDVGRAMALADRLRTGMLHINdQTVNDEPHN--PFGGMGASGNGSRFGGP 429
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
635-1082 |
4.58e-58 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 210.12 E-value: 4.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 635 RAAPMLADDALEHAAPRDVRNPADLRDIvGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTL 714
Cdd:PRK09407 18 RLRRLTARVDGAAGPTREVTAPFTGEPL-ATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 715 MGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIRDEF--------------SNDTHRPLGPVVCISPWNFPLAIFMGQVA 780
Cdd:PRK09407 97 LDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLaprrragalpvltkTTELRQPKGVVGVISPWNYPLTLAVSDAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 781 AALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVAdsRTRAVMFTGSTEVARLINKTLSSR 860
Cdd:PRK09407 177 PALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAGRR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 861 LdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPD 940
Cdd:PRK09407 255 L------IGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 941 RLSADVGPVIDADAKRTIDAHIAAMKDKGHAVtqL----AMPDAcaqGT-FVPPTIIEigNVDE---LKR-EVFGPVLHV 1011
Cdd:PRK09407 329 DYSADMGSLISEAQLETVSAHVDDAVAKGATV--LaggkARPDL---GPlFYEPTVLT--GVTPdmeLAReETFGPVVSV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1012 vrYRRSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQ-PFGGEGLSGTG 1082
Cdd:PRK09407 402 --YPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
669-1080 |
5.54e-58 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 208.66 E-value: 5.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 669 ATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNA-------IAEIREAVDFLR 741
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAatevtamINKIAISIQAYH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 742 YYSAQIRDEFSNDT----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGA 817
Cdd:PRK09457 114 ERTGEKRSEMADGAavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 818 VQLLPGNGETvGAALVADSRTRAVMFTGSTEVARLINKTLSSRldPDgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQ 897
Cdd:PRK09457 194 LNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQ--PE---KILALEMGGNNPLVIDEVADIDAAVHLIIQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 898 SSFDSAGQRCS-ALRVLCLQDDVADRTLTMLKGAMRELALGNPDrlsAD----VGPVIDADAKRTIDAHIAAMKDKGhAV 972
Cdd:PRK09457 268 SAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRWD---AEpqpfMGAVISEQAAQGLVAAQAQLLALG-GK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 973 TQLAMPDACAQGTFVPPTIIEIGNVDEL-KREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISH 1051
Cdd:PRK09457 344 SLLEMTQLQAGTGLLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLE 421
|
410 420
....*....|....*....|....*....
gi 1943257567 1052 AHVGNIYVNRNVIGAvVGVQPFGGEGLSG 1080
Cdd:PRK09457 422 IRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
652-1082 |
2.21e-57 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 207.24 E-value: 2.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:PLN02278 43 PVYNPAT-GEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYYSAQIRDEFSN-------DT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKRVYGDiipspfpDRrllvlKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNA 879
Cdd:PLN02278 202 TALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV----KRVSL--ELGGNAP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 880 MIVDSSALAEQVVADVLQSSFDSAGQRC-SALRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTI 958
Cdd:PLN02278 276 FIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKGhAVTQLAMPDACAQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYRRSGldkllEQIR---ATGY 1031
Cdd:PLN02278 355 ESHVQDAVSKG-AKVLLGGKRHSLGGTFYEPTV--LGDVTEdmliFREEVFGPVAPLTRFKTEE-----EAIAianDTEA 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1943257567 1032 GLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGvqPFGGEGLSGTG 1082
Cdd:PLN02278 427 GLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
652-1082 |
1.09e-56 |
|
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: 204.27 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNA-- 729
Cdd:cd07138 17 DVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLAra 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 730 ------IAEIREAVDFLRYYSAQIRDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQ 803
Cdd:cd07138 96 aqvglgIGHLRAAADALKDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAII 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 804 AVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSsrldPDGKPIPLiaETGGQNAMIVD 883
Cdd:cd07138 176 LAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA----DTVKRVAL--ELGGKSANIIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 884 SSALAEQVVADVLQSSFDSAGQRCSAL-RVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHI 962
Cdd:cd07138 250 DDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 963 -AAMKDKGHAVT-QLAMPDACAQGTFVPPTIieIGNVD---ELKR-EVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLG 1036
Cdd:cd07138 329 qKGIEEGARLVAgGPGRPEGLERGYFVKPTV--FADVTpdmTIAReEIFGPVLSIIPYD--DEDEAIAIANDTPYGLAGY 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1943257567 1037 IHTRIDETIAHVISHAHVGNIYVNrnviGAVVGVQ-PFGGEGLSGTG 1082
Cdd:cd07138 405 VWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
688-1086 |
3.86e-56 |
|
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: 202.18 E-value: 3.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 688 WQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIR----DEFSN---DT----- 755
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARtlhgDSYNNlgdDMlglvl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVAD 835
Cdd:cd07118 117 REPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 836 SRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCL 915
Cdd:cd07118 197 PDVDMVSFTGSTRVGKAIAAAAARNL----KKVSL--ELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 916 QDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPPTIieIG 995
Cdd:cd07118 271 HESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTI--FT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 996 NVDE----LKREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVvgVQ 1071
Cdd:cd07118 349 DVTPdmaiAREEIFGPVLSVLTFDT--VDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--EL 424
|
410
....*....|....*
gi 1943257567 1072 PFGGEGLSGTGPKAG 1086
Cdd:cd07118 425 PFGGFKQSGIGRELG 439
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
654-1080 |
6.18e-54 |
|
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: 196.86 E-value: 6.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 654 RNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEI 733
Cdd:TIGR03240 18 RNPAT-QEVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVIARETGKPLWETRTEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 734 REAVD----FLRYYsAQIRDEFSNDT--------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIA 801
Cdd:TIGR03240 97 ASMIGkvaiSIKAY-HERTGESENPMpdgravlrHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPSELTPWVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 802 AQAVRLLRDAGVPAGAVQLLPGNGETvGAALVADSRTRAVMFTGSTEVARLINKTLSSRldPDgkpIPLIAETGGQNAMI 881
Cdd:TIGR03240 176 EETVKLWEKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFGGR--PE---KILALEMGGNNPLI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 882 VDSSALAEQVVADVLQSSFDSAGQRCS-ALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSAD-VGPVIDADAKRTID 959
Cdd:TIGR03240 250 VDEVADIDAAVHHIIQSAFISAGQRCTcARRLLVPDGAQGDAFLARLVEVAERLTVGAWDAEPQPfMGAVISLRAAQRLL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 960 AHIAAMKDKGhAVTQLAMPDACAQGTFVPPTIIEIGNVDEL-KREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIH 1038
Cdd:TIGR03240 330 AAQAKLLALG-GKSLLEMRQLDPGAAFLTPGIIDVTGVAELpDEEHFGPLLQVIRY--TDFDEAIAIANNTRFGLSAGLL 406
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1943257567 1039 TRIDETIAHVISHAHVGNIYVNRNVIGAvVGVQPFGGEGLSG 1080
Cdd:TIGR03240 407 SDDRELYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
688-1086 |
3.19e-53 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 194.63 E-value: 3.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 688 WQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNA-IAEIREAVDFLRYYsAQIRDEFSNDT----------- 755
Cdd:cd07142 59 WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYY-AGWADKIHGMTlpadgphhvyt 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 -HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVA 834
Cdd:cd07142 138 lHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIAS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 835 DSRTRAVMFTGSTEVARLINKTLS-SRLdpdgKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVL 913
Cdd:cd07142 218 HMDVDKVAFTGSTEVGKIIMQLAAkSNL----KPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 914 CLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGhAVTQLAMPDACAQGTFVPPTIie 993
Cdd:cd07142 292 FVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEG-ATLITGGDRIGSKGYYIQPTI-- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 994 IGNV-DELK---REVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVN-RNVIGAVV 1068
Cdd:cd07142 369 FSDVkDDMKiarDEIFGPVQSILKF--KTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI 446
|
410
....*....|....*...
gi 1943257567 1069 gvqPFGGEGLSGTGPKAG 1086
Cdd:cd07142 447 ---PFGGYKMSGIGREKG 461
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
653-1082 |
3.63e-53 |
|
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: 193.67 E-value: 3.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADLRdIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAE 732
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 733 IREAVDFLRYYSAQIRD------EFSND----THR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIA 801
Cdd:cd07090 80 IDSSADCLEYYAGLAPTlsgehvPLPGGsfayTRRePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 802 AQAVRLLRDAGVPAGAVQLLPGNGETvGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMI 881
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 882 VDSSALAEQVVADVLQSSFDSAGQRCS-ALRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDA 960
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 961 HIAAMKDKGHAV----TQLAMPDACAQGTFVPPTIIEiGNVDEL---KREVFGPVLHVVRYRrsGLDKLLEQIRATGYGL 1033
Cdd:cd07090 312 YIESAKQEGAKVlcggERVVPEDGLENGFYVSPCVLT-DCTDDMtivREEIFGPVMSILPFD--TEEEVIRRANDTTYGL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1943257567 1034 TLGIHTRiDETIAH-VISHAHVGNIYVNR-NVIGAVVgvqPFGGEGLSGTG 1082
Cdd:cd07090 389 AAGVFTR-DLQRAHrVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
652-1082 |
8.83e-53 |
|
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: 193.18 E-value: 8.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAA--APIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGksLPNA 729
Cdd:cd07139 17 DVVSPAT-EEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENG--MPIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 730 IAEIRE---AVDFLRYYSAQIRDeFSNDTHR-------------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKP 793
Cdd:cd07139 94 WSRRAQgpgPAALLRYYAALARD-FPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 794 AEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaE 873
Cdd:cd07139 173 SPETPLDAYLLAEAAEEAGLPPGVVNVVPADRE-VGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL----ARVTL--E 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 874 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSAL-RVLC---LQDDVADRtltmLKGAMRELALGNPDRLSADVGPV 949
Cdd:cd07139 246 LGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVprsRYDEVVEA----LAAAVAALKVGDPLDPATQIGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 950 IDADAKRTIDAHIAAMKDKGhavTQLAM----PDACAQGTFVPPTIieIGNVDELKR----EVFGPVLHVVRYRrsGLDK 1021
Cdd:cd07139 322 ASARQRERVEGYIAKGRAEG---ARLVTgggrPAGLDRGWFVEPTL--FADVDNDMRiaqeEIFGPVLSVIPYD--DEDD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1022 LLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNrnviGAVVGVQ-PFGGEGLSGTG 1082
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG 452
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
655-1061 |
9.46e-53 |
|
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: 192.46 E-value: 9.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIR 734
Cdd:cd07102 2 SPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 735 EAVDFLRYYSAQIRDEFSND------------THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 802
Cdd:cd07102 81 GMLERARYMISIAEEALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 803 QAVRLLRDAGVPAGAVQLLPGNGETvGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIV 882
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRF------IKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 883 DSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHI 962
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 963 AAMKDKGhAVTQLAM---PDACAQGTFVPPTIIEigNVDE----LKREVFGPVLHVvrYRRSGLDKLLEQIRATGYGLTL 1035
Cdd:cd07102 314 ADAIAKG-ARALIDGalfPEDKAGGAYLAPTVLT--NVDHsmrvMREETFGPVVGI--MKVKSDAEAIALMNDSEYGLTA 388
|
410 420
....*....|....*....|....*.
gi 1943257567 1036 GIHTRIDETIAHVISHAHVGNIYVNR 1061
Cdd:cd07102 389 SVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
686-1082 |
9.69e-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: 191.64 E-value: 9.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 686 PIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSA---QIRDEFSNDTH------ 756
Cdd:cd07105 14 PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASlitQIIGGSIPSDKpgtlam 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 757 ---RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLL---PGNGETVGA 830
Cdd:cd07105 94 vvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEVVE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 831 ALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SA 909
Cdd:cd07105 174 ALIAHPAVRKVNFTGSTRVGRIIAETAAKHL----KPVLL--ELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICmST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 910 LRVLcLQDDVADRTLTMLKGAMRELALGnpdrlSADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPP 989
Cdd:cd07105 248 ERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGTSMPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 990 TIIEigNVDELKR----EVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHTRiDETIAHVISHA-HVGNIYVNrnvi 1064
Cdd:cd07105 322 TILD--NVTPDMDiyseESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR-DLARALAVAKRiESGAVHIN---- 392
|
410 420
....*....|....*....|.
gi 1943257567 1065 GAVVGVQ---PFGGEGLSGTG 1082
Cdd:cd07105 393 GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
653-1082 |
1.64e-52 |
|
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: 191.82 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAE 732
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 733 IREAVDFLRYYSAQIRD-----------EFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIA 801
Cdd:cd07107 80 VMVAAALLDYFAGLVTElkgetipvggrNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 802 AQAVRLLRDAgVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMI 881
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGI----KHVTL--ELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 882 V----DSSALAEQVVADVlqsSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRT 957
Cdd:cd07107 233 VfpdaDPEAAADAAVAGM---NFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 958 IDAHIAAMKDKG-HAVTQLAMPD--ACAQGTFVPPTIieIGNVDELKR----EVFGPVLHVVRYRrsGLDKLLEQIRATG 1030
Cdd:cd07107 310 VMHYIDSAKREGaRLVTGGGRPEgpALEGGFYVEPTV--FADVTPGMRiareEIFGPVLSVLRWR--DEAEMVAQANGVE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1031 YGLTLGIHTRiDETIAH-VISHAHVGNIYVN---RNVIGAvvgvqPFGGEGLSGTG 1082
Cdd:cd07107 386 YGLTAAIWTN-DISQAHrTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
653-1082 |
2.81e-52 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 191.03 E-value: 2.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 653 VRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAE 732
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 733 IREAVDFLRYYSAQIRD--------------EFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 797
Cdd:cd07110 80 VDDVAGCFEYYADLAEQldakaeravplpseDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 798 PLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSrldpDGKPIPLiaETGGQ 877
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ----DIKPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 878 NAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRT 957
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 958 IDAHIAAMKDKG-HAVTQLAMPDACAQGTFVPPTIIEIGNVD-ELKR-EVFGPVLHVVRYRRSglDKLLEQIRATGYGLT 1034
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRRPAHLEKGYFIAPTVFADVPTDsRIWReEIFGPVLCVRSFATE--DEAIALANDSEYGLA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1943257567 1035 LGIHTRIDETIAHVISHAHVGNIYVNRNvigAVVGVQ-PFGGEGLSGTG 1082
Cdd:cd07110 392 AAVISRDAERCDRVAEALEAGIVWINCS---QPCFPQaPWGGYKRSGIG 437
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
652-1086 |
2.03e-51 |
|
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: 189.54 E-value: 2.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAA-APIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSL-PNA 729
Cdd:cd07144 26 KTVNPST-GEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 730 IAEIREAVDFLRYYSAQIrDEFSNDT------------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 797
Cdd:cd07144 105 LGDLDEIIAVIRYYAGWA-DKIQGKTiptspnklaytlHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 798 PLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQ 877
Cdd:cd07144 184 PLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL----KAVTL--ECGGK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 878 NAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRE-LALGNPDRLSADVGPVIDADAKR 956
Cdd:cd07144 258 SPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKTQYD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 957 TIDAHIAAMKDKGH--AVTQLAMPDACAQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIRATG 1030
Cdd:cd07144 338 RVLSYIEKGKKEGAklVYGGEKAPEGLGKGYFIPPTI--FTDVPQdmriVKEEIFGPVVVISKF--KTYEEAIKKANDTT 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1943257567 1031 YGLTLGIHTRiDETIAH-VISHAHVGNIYVNRNVIGAvVGVqPFGGEGLSGTGPKAG 1086
Cdd:cd07144 414 YGLAAAVFTK-DIRRAHrVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
647-1086 |
2.42e-51 |
|
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: 189.28 E-value: 2.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 647 HAAPRDVRNPADlRDIVGTVSEATPEEVGAALAHAVAA--APIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGK 724
Cdd:cd07143 20 HGGTVKVYNPST-GKLITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 725 SLPNAIA-EIREAVDFLRYYSA-------QIRD----EFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAK 792
Cdd:cd07143 99 TFGTAKRvDVQASADTFRYYGGwadkihgQVIEtdikKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 793 PAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRldpDGKPIPLia 872
Cdd:cd07143 179 PSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS---NLKKVTL-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 873 ETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDA 952
Cdd:cd07143 254 ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 953 DAKRTIDAHIAAmkDKGHAVTQLAMPDACA-QGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYRRSglDKLLEQIR 1027
Cdd:cd07143 334 IQYERIMSYIES--GKAEGATVETGGKRHGnEGYFIEPTI--FTDVTEdmkiVKEEIFGPVVAVIKFKTE--EEAIKRAN 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943257567 1028 ATGYGLTLGIHTRiDETIAHVISHA-HVGNIYVN-RNVIGAVVgvqPFGGEGLSGTGPKAG 1086
Cdd:cd07143 408 DSTYGLAAAVFTN-NINNAIRVANAlKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
663-1082 |
1.80e-50 |
|
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: 185.61 E-value: 1.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 663 VGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA-EIREAVDFLR 741
Cdd:cd07092 10 IATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdELPGAVDNFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 742 YYSAQIRD-------EFSNDT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLR 809
Cdd:cd07092 90 FFAGAARTlegpaagEYLPGHtsmirREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 810 DaGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIVDSSALAE 889
Cdd:cd07092 170 E-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTL----KRVHL--ELGGKAPVIVFDDADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 890 QVVADVLQSSFDSAGQRC-SALRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDK 968
Cdd:cd07092 243 AAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 969 GHAVTQLAMPDacAQGTFVPPTII-EIGNVDEL-KREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTRiDETIA 1046
Cdd:cd07092 322 ARVLTGGRRAE--GPGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPFDD--EDEAIELANDVEYGLASSVWTR-DVGRA 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 1943257567 1047 HVISHA-HVGNIYVNRNviGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07092 397 MRLSARlDFGTVWVNTH--IPLAAEMPHGGFKQSGYG 431
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
652-1082 |
2.41e-50 |
|
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: 185.59 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKS------ 725
Cdd:cd07151 13 DVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTrikani 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 726 -LPNAIAEIREAVDF-LRYYSAQIRDEFSNDTHR----PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP- 798
Cdd:cd07151 92 eWGAAMAITREAATFpLRMEGRILPSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPi 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 799 ----LIAaqavRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLssrldpdGKPIPLIA-E 873
Cdd:cd07151 172 tgglLLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELA-------GRHLKKVAlE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 874 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDAD 953
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 954 AKRTIDAHIAAMKDKGhAVTQLAMPdacAQGTFVPPTII-EIGNVDELKR-EVFGPVLHVVRYRrsGLDKLLEQIRATGY 1031
Cdd:cd07151 321 QVDGLLDKIEQAVEEG-ATLLVGGE---AEGNVLEPTVLsDVTNDMEIAReEIFGPVAPIIKAD--DEEEALELANDTEY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1943257567 1032 GLTLGIHTRIDE---TIAHVISHA--HVGNIYVNR--NVigavvgvqPFGGEGLSGTG 1082
Cdd:cd07151 395 GLSGAVFTSDLErgvQFARRIDAGmtHINDQPVNDepHV--------PFGGEKNSGLG 444
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
646-1086 |
3.16e-50 |
|
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: 185.68 E-value: 3.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 646 EHAAPRDVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKs 725
Cdd:cd07111 34 ENRKSFPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 726 lpnAIAEIRE-----AVDFLRYYS--AQIRD-EFSNdtHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQT 797
Cdd:cd07111 112 ---PIRESRDcdiplVARHFYHHAgwAQLLDtELAG--WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 798 PLIAAQAVRLLRDAGVPAGAVQLLPGNGETvGAALVADSRTRAVMFTGSTEVARLINKTLSSrldpDGKPIPLiaETGGQ 877
Cdd:cd07111 187 PLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAG----TGKKLSL--ELGGK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 878 NAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRT 957
Cdd:cd07111 260 SPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 958 IDAHIAAMKDKGHAVTQlamPDAC--AQGTFVPPTIIEigNVDELKR----EVFGPVLHVVRYRRsgLDKLLEQIRATGY 1031
Cdd:cd07111 340 IRELVEEGRAEGADVFQ---PGADlpSKGPFYPPTLFT--NVPPASRiaqeEIFGPVLVVLTFRT--AKEAVALANNTPY 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1032 GLTLGIHTRIDETIAHVISHAHVGNIYVN-RNVIGAVVgvqPFGGEGLSGTGPKAG 1086
Cdd:cd07111 413 GLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFGREGG 465
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
696-1060 |
1.02e-49 |
|
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: 183.70 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 696 RADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIR-----------DEFSNDTHRPLGPVVC 764
Cdd:cd07120 44 RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARteagrmiepepGSFSLVLREPMGVAGI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 765 ISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDA-GVPAGAVQLLPGNGETVGAALVADSRTRAVMF 843
Cdd:cd07120 124 IVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 844 TGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRT 923
Cdd:cd07120 204 TGSTATGRAIMAAAAPTL----KRLGL--ELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 924 LTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHI-AAMKDKGHAVTQL-AMPDACAQGTFVPPTIIEIGNVDE-- 999
Cdd:cd07120 278 RDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVeRAIAAGAEVVLRGgPVTEGLAKGAFLRPTLLEVDDPDAdi 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1000 LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHTRiDETIAHVISHA-HVGNIYVN 1060
Cdd:cd07120 358 VQEEIFGPVLTLETF--DDEAEAVALANDTDYGLAASVWTR-DLARAMRVARAiRAGTVWIN 416
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
688-1086 |
1.38e-49 |
|
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: 184.09 E-value: 1.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 688 WQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKS-LPNAIAEIREAVDFLRYYSA---QIR--------DEFSNDT 755
Cdd:cd07141 63 WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPfSKSYLVDLPGAIKVLRYYAGwadKIHgktipmdgDFFTYTR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 HRPLGpvVC--ISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALV 833
Cdd:cd07141 143 HEPVG--VCgqIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAIS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 834 ADSRTRAVMFTGSTEVARLINKTLS-SRLdpdgKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRV 912
Cdd:cd07141 221 SHPDIDKVAFTGSTEVGKLIQQAAGkSNL----KRVTL--ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 913 LCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGhavTQL-----AMPDacaQGTFV 987
Cdd:cd07141 295 TFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKKEG---AKLecggkRHGD---KGYFI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 988 PPTIieIGNV-DEL---KREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTR-IDETIaHVISHAHVGNIYVNrn 1062
Cdd:cd07141 369 QPTV--FSDVtDDMriaKEEIFGPVQQIFKFKT--IDEVIERANNTTYGLAAAVFTKdIDKAI-TFSNALRAGTVWVN-- 441
|
410 420
....*....|....*....|....*
gi 1943257567 1063 vIGAVVGVQ-PFGGEGLSGTGPKAG 1086
Cdd:cd07141 442 -CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
648-1082 |
6.38e-49 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 181.65 E-value: 6.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 648 AAPRDVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLP 727
Cdd:PRK13473 16 GEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 728 NAIA-EIREAVDFLRYYSAQIRD-------EFSNDtH------RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKP 793
Cdd:PRK13473 95 LALNdEIPAIVDVFRFFAGAARClegkaagEYLEG-HtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 794 AEQTPLIAAQAVRLLRDAgVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaE 873
Cdd:PRK13473 174 SEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSV----KRTHL--E 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 874 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDAD 953
Cdd:PRK13473 247 LGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 954 AKRTIDAHIAAMKDKGHA--VTQLAMPDacAQGTFVPPTII-EIGNVDEL-KREVFGPVLHVVRYrrSGLDKLLEQIRAT 1029
Cdd:PRK13473 327 HRDRVAGFVERAKALGHIrvVTGGEAPD--GKGYYYEPTLLaGARQDDEIvQREVFGPVVSVTPF--DDEDQAVRWANDS 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1943257567 1030 GYGLTLGIHTRiDETIAH-VISHAHVGNIYVNRNVIgaVVGVQPFGGEGLSGTG 1082
Cdd:PRK13473 403 DYGLASSVWTR-DVGRAHrVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
652-1082 |
6.46e-49 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 181.29 E-value: 6.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRdIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07147 2 EVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYYSAQIRD---------------EFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 795
Cdd:cd07147 81 EVARAIDTFRIAAEEATRiygevlpldisargeGRQGLVRRfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 796 QTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETvGAALVADSRTRAVMFTGSTEVARLInKTLSSRldpdgKPIPLiaETG 875
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-----KKVVL--ELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 876 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRC-SALRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADA 954
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 955 KRTIDAHIAAMKDKGHAVTQLAMPDacaqGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYRRsgLDKLLEQIRATG 1030
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGKRD----GALLEPTILE--DVPPdmevNCEEVFGPVVTVEPYDD--FDEALAAVNDSK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1031 YGLTLGIHTRIDETIAHVISHAHVGNIyvnrnVIGAV----VGVQPFGGEGLSGTG 1082
Cdd:cd07147 383 FGLQAGVFTRDLEKALRAWDELEVGGV-----VINDVptfrVDHMPYGGVKDSGIG 433
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
652-1088 |
7.48e-49 |
|
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: 181.49 E-value: 7.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAA-APIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKS--LPN 728
Cdd:cd07113 18 DITNPAT-EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSihLSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 729 AIaEIREAVDFLRYY---SAQIRDE-------------FSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLA 791
Cdd:cd07113 97 AF-EVGQSANFLRYFagwATKINGEtlapsipsmqgerYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 792 KPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLINKTLSSrldpDGKPIPLi 871
Cdd:cd07113 176 KPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAAS----DLTRVTL- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 872 aETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVID 951
Cdd:cd07113 250 -ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLAN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 952 ADAKRTIDAHIAAMKDKGHAVtqLAMPDACAQ-GTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYRRSglDKLLEQIRA 1028
Cdd:cd07113 329 QPHFDKVCSYLDDARAEGDEI--VRGGEALAGeGYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDE--EELIQLIND 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943257567 1029 TGYGLTLGIHTRIDETIAHVISHAHVGNIYVN-RNVIGAVVgvqPFGGEGLSGTGPKAGGA 1088
Cdd:cd07113 405 TPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIGREFGSA 462
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
652-1091 |
1.29e-48 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 181.26 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:PRK11241 29 DVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYYSAQIRDEFSnDT-------------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 798
Cdd:PRK11241 108 EISYAASFIEWFAEEGKRIYG-DTipghqadkrliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 799 LIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARlinkTLSSRLDPDGKPIPLiaETGGQN 878
Cdd:PRK11241 187 FSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGR----QLMEQCAKDIKKVSL--ELGGNA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 879 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTI 958
Cdd:PRK11241 261 PFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKGHAVTQLAMPDACAqGTFVPPTIIE--IGNVDELKREVFGPVLHVVRYRRSglDKLLEQIRATGYGLTLG 1036
Cdd:PRK11241 341 EEHIADALEKGARVVCGGKAHELG-GNFFQPTILVdvPANAKVAKEETFGPLAPLFRFKDE--ADVIAQANDTEFGLAAY 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1943257567 1037 IHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGvqPFGG---EGLSGTGPKAGGALYL 1091
Cdd:PRK11241 418 FYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
652-1082 |
5.24e-48 |
|
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: 179.08 E-value: 5.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRdIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI- 730
Cdd:cd07559 19 DNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 731 AEIREAVDFLRYYSAQIR------DEFSNDT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:cd07559 98 ADIPLAIDHFRYFAGVIRaqegslSEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAgVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNA 879
Cdd:cd07559 178 SILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------IPVTLELGGKSP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 880 MIVDSSALAEqvvadvlQSSFDSA------------GQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVG 947
Cdd:cd07559 251 NIFFDDAMDA-------DDDFDDKaeegqlgfafnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 948 PVIDADAKRTIDAHIAAMKDKGHAVT---QLAMPDACAQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYRRSglDKL 1022
Cdd:cd07559 324 AQVSKDQLEKILSYVDIGKEEGAEVLtggERLTLGGLDKGYFYEPTLIKGGNNDMriFQEEIFGPVLAVITFKDE--EEA 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1023 LEQIRATGYGLTLGIHTRiDETIAHVISHA-HVGNIYVN-RNVIGAVVgvqPFGGEGLSGTG 1082
Cdd:cd07559 402 IAIANDTEYGLGGGVWTR-DINRALRVARGiQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
695-1086 |
1.92e-47 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 178.09 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 695 ARADCLARAADLLEAQMHTLMGLIVREAGKSLP-NAIAEIREAVDFLRYYsAQIRDEFSNDT------------HRPLGP 761
Cdd:PLN02766 83 ERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAAAGLLRYY-AGAADKIHGETlkmsrqlqgytlKEPIGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 762 VVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAV 841
Cdd:PLN02766 162 VGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 842 MFTGSTEVARLINKTLS-SRLdpdgKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVA 920
Cdd:PLN02766 242 SFTGSTEVGRKIMQAAAtSNL----KQVSL--ELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 921 DRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGhaVTQLAMPDACA-QGTFVPPTIIEigNVDE 999
Cdd:PLN02766 316 DEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREG--ATLLTGGKPCGdKGYYIEPTIFT--DVTE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1000 ----LKREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTRiDETIAHVISHA-HVGNIYVnrNVIGAVVGVQPFG 1074
Cdd:PLN02766 392 dmkiAQDEIFGPVMSLMKFKT--VEEAIKKANNTKYGLAAGIVTK-DLDVANTVSRSiRAGTIWV--NCYFAFDPDCPFG 466
|
410
....*....|..
gi 1943257567 1075 GEGLSGTGPKAG 1086
Cdd:PLN02766 467 GYKMSGFGRDQG 478
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
652-1082 |
3.37e-44 |
|
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: 168.02 E-value: 3.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:cd07117 19 DSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 -EIREAVDFLRYYSAQIRDE------FSNDT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:cd07117 98 vDIPLAADHFRYFAGVIRAEegsanmIDEDTlsivlREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAgVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNA 879
Cdd:cd07117 178 SLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------IPATLELGGKSA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 880 MIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTID 959
Cdd:cd07117 251 NIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKIL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 960 AHIAAMKDKGHAVT---QLAMPDACAQGTFVPPTIIEigNVDELKR----EVFGPVLHVVRYRRSglDKLLEQIRATGYG 1032
Cdd:cd07117 331 SYVDIAKEEGAKILtggHRLTENGLDKGFFIEPTLIV--NVTNDMRvaqeEIFGPVATVIKFKTE--DEVIDMANDSEYG 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1033 LTLGIHTRiDETIAHVISHA-HVGNIYVNR-NVIGAVVgvqPFGGEGLSGTG 1082
Cdd:cd07117 407 LGGGVFTK-DINRALRVARAvETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
655-1086 |
4.42e-44 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 168.47 E-value: 4.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADLRDIvGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIR 734
Cdd:PLN02315 40 NPANNQPI-AEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 735 EAVDFLRY---YSAQ-----IRDEFSN----DTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAA 802
Cdd:PLN02315 119 EIIDMCDFavgLSRQlngsiIPSERPNhmmmEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 803 QAVRL----LRDAGVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdGKpipLIAETGGQN 878
Cdd:PLN02315 199 AMTKLvaevLEKNNLPGAIFTSFCGGAE-IGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GK---CLLELSGNN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 879 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTI 958
Cdd:PLN02315 272 AIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKGHAVTqLAMPDACAQGTFVPPTIIEIG-NVDELKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGI 1037
Cdd:PLN02315 352 EKGIEIIKSQGGKIL-TGGSAIESEGNFVQPTIVEISpDADVVKEELFGPVLYVMKFK--TLEEAIEINNSVPQGLSSSI 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1943257567 1038 HTRIDETIAHVI--SHAHVGNIYVNRNVIGAVVGvQPFGGEGLSGTGPKAG 1086
Cdd:PLN02315 429 FTRNPETIFKWIgpLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
688-1086 |
1.60e-43 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 167.29 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 688 WQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI-AEIREAVDFLRYYsAQIRDEFSNDT----------- 755
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMFARLFRYY-AGWADKIHGLTvpadgphhvqt 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 -HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVA 834
Cdd:PLN02466 192 lHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALAS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 835 DSRTRAVMFTGSTEVARLINKtLSSRldPDGKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLC 914
Cdd:PLN02466 272 HMDVDKLAFTGSTDTGKIVLE-LAAK--SNLKPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 915 LQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGhAVTQLAMPDACAQGTFVPPTIIEi 994
Cdd:PLN02466 347 VHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESG-ATLECGGDRFGSKGYYIQPTVFS- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 995 gNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHTRIDETiAHVISHA-HVGNIYVN-RNVIGAVV 1068
Cdd:PLN02466 425 -NVQDdmliAQDEIFGPVQSILKF--KDLDEVIRRANNTRYGLAAGVFTQNLDT-ANTLSRAlRVGTVWVNcFDVFDAAI 500
|
410
....*....|....*...
gi 1943257567 1069 gvqPFGGEGLSGTGPKAG 1086
Cdd:PLN02466 501 ---PFGGYKMSGIGREKG 515
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
743-1082 |
3.06e-42 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 160.77 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 743 YSAQIRDEfsndthrPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAgVPAGAVQLLP 822
Cdd:cd07087 92 AKAYVIPE-------PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 823 GnGETVGAALVA---DSrtraVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSS 899
Cdd:cd07087 164 G-GVEVATALLAepfDH----IFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 900 FDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELaLGNPDRLSADVGPVIDAD-AKRtidahIAAMKDKGHAVTQlamP 978
Cdd:cd07087 233 FLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINERhFDR-----LASLLDDGKVVIG---G 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 979 DACAQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGN 1056
Cdd:cd07087 304 QVDKEERYIAPTILDDVSPDSplMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGG 381
|
330 340
....*....|....*....|....*.
gi 1943257567 1057 IYVNRNVIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07087 382 VCVNDVLLHAAIPNLPFGGVGNSGMG 407
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
652-1082 |
2.20e-41 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 159.66 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI- 730
Cdd:PRK13252 25 EVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 731 AEIREAVDFLRYYSA----------QIRDEFSNDTHR-PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:PRK13252 104 VDIVTGADVLEYYAGlapalegeqiPLRGGSFVYTRRePLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAGVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgKPIPLiaETGGQNA 879
Cdd:PRK13252 184 TALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL----KEVTM--ELGGKSP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 880 MIVDSSALAEQVVADVLQSSFDSAGQRCS-ALRVLcLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTI 958
Cdd:PRK13252 257 LIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKG-------HAVTqlamPDACAQGTFVPPTIIeIGNVDEL---KREVFGPVLHVVRYRRSglDKLLEQIRA 1028
Cdd:PRK13252 336 LGYIEKGKAEGarllcggERLT----EGGFANGAFVAPTVF-TDCTDDMtivREEIFGPVMSVLTFDDE--DEVIARAND 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1943257567 1029 TGYGLTLGIHTRiDETIAH-VISHAHVGNIYVnrNVIGAVVGVQPFGGEGLSGTG 1082
Cdd:PRK13252 409 TEYGLAAGVFTA-DLSRAHrVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
652-1075 |
3.85e-41 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 158.89 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:TIGR01722 19 PVTNPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIR---EAVDFLRYYSAQIRDEFSNDTHR---------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:TIGR01722 98 DVArglEVVEHACGVNSLLKGETSTQVATrvdvysirqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAGVPAGAVQLLPGNGETVGaALVADSRTRAVMFTGSTEVARLINKTLSSrldpDGKPIPliAETGGQNA 879
Cdd:TIGR01722 178 AAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIGRYIHTTGSA----HGKRVQ--ALGGAKNH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 880 MIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDvADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTID 959
Cdd:TIGR01722 251 MVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 960 AHIAAMKDKGHAVT---QLAMPDACAQGTFVPPTIIE--IGNVDELKREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLT 1034
Cdd:TIGR01722 330 SLIAGGAAEGAEVLldgRGYKVDGYEEGNWVGPTLLErvPPTMKAYQEEIFGPVLCVLEA--DTLEEAIALINASPYGNG 407
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1943257567 1035 LGIHTRIDETIAHVISHAHVGNIYVNRNvIGAVVGVQPFGG 1075
Cdd:TIGR01722 408 TAIFTRDGAAARRFQHEIEVGQVGVNVP-IPVPLPYFSFTG 447
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
714-1091 |
2.94e-40 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 154.51 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 714 LMGLIVREAGKSLPNAIAEIREAVDFL--------RYYSAQIRDEFSNDT----HRPLGPVVCISPWNFPLAIFMGQVAA 781
Cdd:PRK10090 15 ISALIVEEGGKIQQLAEVEVAFTADYIdymaewarRYEGEIIQSDRPGENillfKRALGVTTGILPWNFPFFLIARKMAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 782 ALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRL 861
Cdd:PRK10090 95 ALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAAAAKNI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 862 dpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNP-D 940
Cdd:PRK10090 175 ------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPaE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 941 RLSADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPDAcAQGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYrr 1016
Cdd:PRK10090 249 RNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE-GKGYYYPPTLLL--DVRQemsiMHEETFGPVLPVVAF-- 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1017 SGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQP-FGGEGLSGTGPKAGGALYL 1091
Cdd:PRK10090 324 DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAgWRKSGIGGADGKHGLHEYL 399
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
655-1082 |
3.60e-39 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 152.58 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIR 734
Cdd:PRK09406 7 NPAT-GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 735 EAVDFLRYYsAQIRDEFSNDT---------------HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:PRK09406 86 KCAKGFRYY-AEHAEALLADEpadaaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAGVPAGAVQ-LLPGNGETvgAALVADSRTRAVMFTGSTEVARLINKTLSSRLDPDgkpiplIAETGGQN 878
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKT------VLELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 879 AMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTI 958
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 959 DAHIAAMKDKGHAV----TQLAMPdacaqGTFVPPTII-----EIGNVDElkrEVFGPVLHVvrYRRSGLDKLLEQIRAT 1029
Cdd:PRK09406 317 EKQVDDAVAAGATIlcggKRPDGP-----GWFYPPTVItditpDMRLYTE---EVFGPVASL--YRVADIDEAIEIANAT 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1943257567 1030 GYGLTLGIHTRIDETIAHVISHAHVGNIYVNrnviGAVVGVQ--PFGGEGLSGTG 1082
Cdd:PRK09406 387 TFGLGSNAWTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
652-1082 |
1.92e-38 |
|
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: 150.26 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADLRDI--VGTVSEATPEEVGAALAHAVAAAPIWqaTPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNA 729
Cdd:cd07148 2 EVVNPFDLKPIgeVPTVDWAAIDKALDTAHALFLDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 730 IAEIREAVDFLRYYSAQIRD----EFSND------------THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKP 793
Cdd:cd07148 80 KVEVTRAIDGVELAADELGQlggrEIPMGltpasagriaftTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 794 AEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGEtVGAALVADSRTRAVMFTGSTEVARLinktLSSRLDPdGKPIPLiaE 873
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWM----LRSKLAP-GTRCAL--E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 874 TGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVID-A 952
Cdd:cd07148 232 HGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRpR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 953 DAKRTIDAHIAAMKDKGHAVTQLA-MPDACAQGTFV--PPTIIEIGnvdelKREVFGPVLHVVRYRRsgLDKLLEQIRAT 1029
Cdd:cd07148 312 EVDRVEEWVNEAVAAGARLLCGGKrLSDTTYAPTVLldPPRDAKVS-----TQEIFGPVVCVYSYDD--LDEAIAQANSL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1943257567 1030 GYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNViGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07148 385 PVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHT-AFRVDWMPFAGRRQSGYG 436
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
634-1060 |
3.64e-38 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 150.65 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 634 WRAAPmladdaleHAAPRDVRNPADlRDIVGTVSEATPEEVGAALAH-----AVAAAPIWQATPVDARADCLARAADLLE 708
Cdd:PLN02467 16 WREPV--------LGKRIPVVNPAT-EETIGDIPAATAEDVDAAVEAarkafKRNKGKDWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 709 AQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSAQIR--------------DEF-SNDTHRPLGPVVCISPWNFPLA 773
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEaldakqkapvslpmETFkGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 774 IFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLI 853
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 854 NKTLSsrldPDGKPIPLiaETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRE 933
Cdd:PLN02467 247 MTAAA----QMVKPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 934 LALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHAV-TQLAMPDACAQGTFVPPTII-EIGNVDELKR-EVFGPVLH 1010
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATIlCGGKRPEHLKKGFFIEPTIItDVTTSMQIWReEVFGPVLC 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1943257567 1011 VVRYRRSglDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVN 1060
Cdd:PLN02467 401 VKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
666-1082 |
5.97e-38 |
|
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: 149.52 E-value: 5.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 666 VSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI-AEIREAVDFLRYYS 744
Cdd:cd07116 32 VPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 745 AQIR------DEFSNDT-----HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAgV 813
Cdd:cd07116 112 GCIRaqegsiSEIDENTvayhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-L 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 814 PAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQvva 893
Cdd:cd07116 191 PPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI------IPVTLELGGKSPNIFFADVMDAD--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 894 dvlQSSFDSA-----------GQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHI 962
Cdd:cd07116 262 ---DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 963 AAMKDKGHAV----TQLAMPDACAQGTFVPPTIIEIGNVDELKREVFGPVLHVVRYRRSglDKLLEQIRATGYGLTLGIH 1038
Cdd:cd07116 339 DIGKEEGAEVltggERNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFKDE--EEALEIANDTLYGLGAGVW 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1943257567 1039 TRiDETIAHVISHA-HVGNIYVnrNVIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07116 417 TR-DGNTAYRMGRGiQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
655-1086 |
2.09e-37 |
|
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: 147.45 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADLRDIvGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNA-IAEI 733
Cdd:cd07098 2 DPATGQHL-GSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 734 REAVDFLRYYSA--------QIRDEFSNDTHR-------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTP 798
Cdd:cd07098 81 LVTCEKIRWTLKhgekalrpESRPGGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 799 LIAAQAVRLLRDA----GVPAGAVQLLPGNGETvGAALVADSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAET 874
Cdd:cd07098 161 WSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 875 GGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADA 954
Cdd:cd07098 234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 955 KRTIDAHIAAMKDKGHAVTQLAMPDAC---AQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYrrSGLDKLLEQIR 1027
Cdd:cd07098 314 FDRLEELVADAVEKGARLLAGGKRYPHpeyPQGHYFPPTL--LVDVTPdmkiAQEEVFGPVMVVMKA--SDDEEAVEIAN 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1943257567 1028 ATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFGGEGLSGTGPKAG 1086
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
655-1086 |
2.88e-37 |
|
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: 147.64 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADlRDIVGTVSEATPEEVGAALAHAVAA---APIWQATPVDaRADCLARAADLLEAQMHTLMGLIVREAGKSLPNAI- 730
Cdd:cd07140 27 NPTD-GSVICKVSLATVEDVDRAVAAAKEAfenGEWGKMNARD-RGRLMYRLADLMEEHQEELATIESLDSGAVYTLALk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 731 AEIREAVDFLRYYS---------------AQIRDEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAE 795
Cdd:cd07140 105 THVGMSIQTFRYFAgwcdkiqgktipinqARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 796 QTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKtlsSRLDPDGKPIPLiaETG 875
Cdd:cd07140 185 VTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMK---SCAVSNLKKVSL--ELG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 876 GQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPvidadak 955
Cdd:cd07140 260 GKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 956 RTIDAHI--------AAMKDKGHAV---TQLAMPdacaqGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYRRSGLD 1020
Cdd:cd07140 333 QNHKAHLdklveyceRGVKEGATLVyggKQVDRP-----GFFFEPTVFT--DVEDhmfiAKEESFGPIMIISKFDDGDVD 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 1021 KLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGvqPFGGEGLSGTGPKAG 1086
Cdd:cd07140 406 GVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLG 469
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
689-1082 |
7.90e-37 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 146.58 E-value: 7.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 689 QATPVdARADCLARAADLLEAQMHTLMGLIVREAGK--------SLPNAIAEIR---EAVDFLRYYSAQI-RDEFSNDTH 756
Cdd:PRK09847 77 LSSPA-KRKAVLNKLADLMEAHAEELALLETLDTGKpirhslrdDIPGAARAIRwyaEAIDKVYGEVATTsSHELAMIVR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 757 RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGAALVADS 836
Cdd:PRK09847 156 EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 837 RTRAVMFTGSTEVARlinKTLSSRLDPDGKPIPLiaETGGQNAMIV--DSSALaEQVVADVLQSSFDSAGQRCSALRVLC 914
Cdd:PRK09847 236 DIDAIAFTGSTRTGK---QLLKDAGDSNMKRVWL--EAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 915 LQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHA-VTQLAMPDACAQGtfvPPTIIE 993
Cdd:PRK09847 310 LEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLlLDGRNAGLAAAIG---PTIFVD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 994 IGNVDELKR-EVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHTRiDETIAHVISHA-HVGNIYVNRNVIGAVvgVQ 1071
Cdd:PRK09847 387 VDPNASLSReEIFGPVLVVTRF--TSEEQALQLANDSQYGLGAAVWTR-DLSRAHRMSRRlKAGSVFVNNYNDGDM--TV 461
|
410
....*....|.
gi 1943257567 1072 PFGGEGLSGTG 1082
Cdd:PRK09847 462 PFGGYKQSGNG 472
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
666-1060 |
1.27e-36 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 145.67 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 666 VSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRYYSA 745
Cdd:PLN00412 47 VQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 746 Q-----------IRDEF-SNDTHR-------PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVR 806
Cdd:PLN00412 127 EgvrilgegkflVSDSFpGNERNKycltskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 807 LLRDAGVPAGAVQLLPGNGETVGAALVADSRTRAVMFT-GSTEVArlINKTLSSrldpdgkpIPLIAETGGQNAMIVDSS 885
Cdd:PLN00412 207 CFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA--ISKKAGM--------VPLQMELGGKDACIVLED 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 886 ALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRlSADVGPVIDADAKRTIDAHIAAM 965
Cdd:PLN00412 277 ADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDITPVVSESSANFIEGLVMDA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 966 KDKGHAVTQlampDACAQGTFVPPTIIEigNVDELKR----EVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTR- 1040
Cdd:PLN00412 356 KEKGATFCQ----EWKREGNLIWPLLLD--NVRPDMRiaweEPFGPVLPVIRIN--SVEEGIHHCNASNFGLQGCVFTRd 427
|
410 420
....*....|....*....|.
gi 1943257567 1041 IDETIAhvISHA-HVGNIYVN 1060
Cdd:PLN00412 428 INKAIL--ISDAmETGTVQIN 446
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
688-1087 |
5.99e-36 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 142.37 E-value: 5.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 688 WQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKS--------LPNAIAEIREAVDFLRYY---------------S 744
Cdd:cd07134 14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPaaevdlteILPVLSEINHAIKHLKKWmkpkrvrtplllfgtK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 745 AQIRDEfsndthrPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAgVPAGAVQLLPGN 824
Cdd:cd07134 94 SKIRYE-------PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 825 GETVGAALvaDSRTRAVMFTGSTEVARLI----NKTLSSrldpdgkpIPLiaETGGQNAMIVDSSALAEQVVADVLQSSF 900
Cdd:cd07134 166 AEVAQALL--ELPFDHIFFTGSPAVGKIVmaaaAKHLAS--------VTL--ELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 901 DSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRL-SADVGPVIDADAKRTIDAHIAAMKDKGHAVTQLAMPD 979
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 980 ACaqGTFVPPTIIEigNVDE----LKREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVG 1055
Cdd:cd07134 314 AA--QRYIAPTVLT--NVTPdmkiMQEEIFGPVLPIITYED--LDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSG 387
|
410 420 430
....*....|....*....|....*....|..
gi 1943257567 1056 NIYVNRNVIGAVVGVQPFGGEGLSGTGpKAGG 1087
Cdd:cd07134 388 GVVVNDVVLHFLNPNLPFGGVNNSGIG-SYHG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
686-1096 |
9.35e-34 |
|
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: 136.21 E-value: 9.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 686 PIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIREAVDFLRY----YSAQIRDEFSN-------- 753
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARafviYSYRIPHEPGNhlgqglkq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 754 DTHR---PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAG-VPAGAVQLLPGNGETvG 829
Cdd:cd07084 93 QSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-M 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 830 AALVADSRTRAVMFTGSTEVARlinktlssRLDPDGKPIPLIAETGGQNAMIVDSSALAEQVVAD-VLQSSFDSAGQRCS 908
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVAE--------KLALDAKQARIYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTACSGQKCT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 909 ALR-VLCLQDDVADRTLTMLKGAMRELALGnpdrlSADVGPVIdadaKRTIDAHIAAMKDKG-----------HAVTQLA 976
Cdd:cd07084 244 AQSmLFVPENWSKTPLVEKLKALLARRKLE-----DLLLGPVQ----TFTTLAMIAHMENLLgsvllfsgkelKNHSIPS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 977 MPDAC-AQGTFVPptIIEIGNVDEL-KREVFGPVLHVVRYRRSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHV 1054
Cdd:cd07084 315 IYGACvASALFVP--IDEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1943257567 1055 -GNIYVNRNVIGavvGVQPFGGEGLSGTGPKAGGALYLPRLLA 1096
Cdd:cd07084 393 aGRTYAILRGRT---GVAPNQNHGGGPAADPRGAGIGGPEAIK 432
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
756-1082 |
4.73e-33 |
|
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: 133.88 E-value: 4.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAgVPAGAVQLLPGNGETVGAALvaD 835
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 836 SRTRAVMFTGSTEVARLI----NKTLSsrldpdgkpiPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALR 911
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIaeaaAKHLT----------PVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 912 -VLClQDDVADRTLTMLKGAMRELALGNPDRLSaDVGPVI-DADAKRtidahIAAMKD--KGHAVTQLAMPDAcaqGTFV 987
Cdd:cd07135 253 yVLV-DPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVnPRHFNR-----LKSLLDttKGKVVIGGEMDEA---TRFI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 988 PPTIIEIGNVDE--LKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIG 1065
Cdd:cd07135 323 PPTIVSDVSWDDslMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIH 400
|
330
....*....|....*..
gi 1943257567 1066 AVVGVQPFGGEGLSGTG 1082
Cdd:cd07135 401 VGVDNAPFGGVGDSGYG 417
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
652-1039 |
4.89e-33 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 136.80 E-value: 4.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 652 DVRNPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIA 731
Cdd:PLN02419 132 DVINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 732 EIREAVDFLRYY----SAQIRDEFSN-----DTH---RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPL 799
Cdd:PLN02419 211 DIFRGLEVVEHAcgmaTLQMGEYLPNvsngvDTYsirEPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 800 IAAQAVRLLRDAGVPAGAVQLLPGNGETVGaALVADSRTRAVMFTGSTEVARLInktlSSRLDPDGKPIPliAETGGQNA 879
Cdd:PLN02419 291 ASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHI----YARAAAKGKRIQ--SNMGAKNH 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 880 MIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVA--DRTLTMLKGAMRELALGNPDrlsADVGPVIDADAKRT 957
Cdd:PLN02419 364 GLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKswEDKLVERAKALKVTCGSEPD---ADLGPVISKQAKER 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 958 IDAHIAAMKDKGHAV----TQLAMPdACAQGTFVPPTIIE--IGNVDELKREVFGPVLhvVRYRRSGLDKLLEQIRATGY 1031
Cdd:PLN02419 441 ICRLIQSGVDDGAKLlldgRDIVVP-GYEKGNFIGPTILSgvTPDMECYKEEIFGPVL--VCMQANSFDEAISIINKNKY 517
|
....*...
gi 1943257567 1032 GLTLGIHT 1039
Cdd:PLN02419 518 GNGAAIFT 525
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
758-1082 |
1.58e-30 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 127.45 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 758 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLrDAGVPAGAVQLLPGnGETVGAALVaDSR 837
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEG-GVEVTTELL-KEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 838 TRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQD 917
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 918 DVADRTLTMLKGAMRELaLGNPDRLSADVGPVIDADAKRTIDAHIAAMKDK----GHA-VTQLampdacaqgtFVPPTII 992
Cdd:PTZ00381 260 SIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGKvvygGEVdIENK----------YVAPTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 993 EIGNVDE--LKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGV 1070
Cdd:PTZ00381 329 VNPDLDSplMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
330
....*....|..
gi 1943257567 1071 QPFGGEGLSGTG 1082
Cdd:PTZ00381 407 LPFGGVGNSGMG 418
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
655-1060 |
5.54e-30 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 125.36 E-value: 5.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 655 NPADlRDIVGTVSEATPEEVGAALAHAVAAAPIWQATPVDARADCLARAADLLEAQMHTLMGLIVREAGKSLPNAIAEIR 734
Cdd:PRK13968 13 NPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 735 EAVDFLRYYS----AQIRDE---FSND----THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQ 803
Cdd:PRK13968 92 KSANLCDWYAehgpAMLKAEptlVENQqaviEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 804 AVRLLRDAGVPAGAVQLLPGNGETVgAALVADSRTRAVMFTGSTEVARLINKTLSSRLDpdgkpiPLIAETGGQNAMIVD 883
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALK------KCVLELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 884 SSALAEQVVADVLQSSFDSAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIA 963
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 964 AMKDKGhAVTQLAMPDACAQGTFVPPTIieIGNVDE----LKREVFGPVLHVVRYRRSglDKLLEQIRATGYGLTLGIHT 1039
Cdd:PRK13968 325 ATLAEG-ARLLLGGEKIAGAGNYYAPTV--LANVTPemtaFREELFGPVAAITVAKDA--EHALELANDSEFGLSATIFT 399
|
410 420
....*....|....*....|.
gi 1943257567 1040 RIDETIAHVISHAHVGNIYVN 1060
Cdd:PRK13968 400 TDETQARQMAARLECGGVFIN 420
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
755-1082 |
2.17e-28 |
|
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: 119.90 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 755 THRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGvPAGAVQLLPGNGEtVGAALVA 834
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF-DEDEVAVVTGGAD-VAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 835 ---DSrtraVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALR 911
Cdd:cd07133 176 lpfDH----LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 912 -VLCLQDDVaDRTLTMLKGAMRELA---LGNPDRLSadvgpVIDADAKRTIDAHIAAMKDKGHAVTQLAMPDACAQGT-F 986
Cdd:cd07133 246 yVLVPEDKL-EEFVAAAKAAVAKMYptlADNPDYTS-----IINERHYARLQGLLEDARAKGARVIELNPAGEDFAATrK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 987 VPPTIIEigNVDE----LKREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRN 1062
Cdd:cd07133 320 LPPTLVL--NVTDdmrvMQEEIFGPILPILTYDS--LDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDT 395
|
330 340
....*....|....*....|
gi 1943257567 1063 VIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07133 396 LLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
688-1039 |
2.06e-27 |
|
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: 117.26 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 688 WQATPVDARADCLARAADLLEAQMHTLMGLIVREAGksLPNAIAE---------IREAVDFLR---YYSAQIRDEFSNDT 755
Cdd:cd07129 15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgelgrttgqLRLFADLVRegsWLDARIDPADPDRQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 ----------HRPLGPVVCISPWNFPLAIFM--GQVAAALAAGNTVLAK--PA--EQTPLIAAQAVRLLRDAGVPAGAVQ 819
Cdd:cd07129 93 plprpdlrrmLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhpGTSELVARAIRAALRATGLPAGVFS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 820 LLPGNGETVGAALVADSRTRAVMFTGSTEVARLINKTLSSRLDpdgkPIPLIAETGGQNAMIVDSSALAEQV--VADVLQ 897
Cdd:cd07129 173 LLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGSVNPVFILPGALAERGeaIAQGFV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 898 SSFD-SAGQRCSA--LrVLCLQDDVADRTLTMLKGAMRElalgnpdrlsADVGPVIDADAKRTIDAHIAAMKDKGHAVTq 974
Cdd:cd07129 249 GSLTlGAGQFCTNpgL-VLVPAGPAGDAFIAALAEALAA----------APAQTMLTPGIAEAYRQGVEALAAAPGVRV- 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 975 LAMPDACAQGTFVPPTIIEI-----GNVDELKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHT 1039
Cdd:cd07129 317 LAGGAAAEGGNQAAPTLFKVdaaafLADPALQEEVFGPASLVVRYD--DAAELLAVAEALEGQLTATIHG 384
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
756-1082 |
9.04e-24 |
|
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: 106.15 E-value: 9.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 756 HRPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEqtplIAAQAVRLLRDagvpagavqLLP------------- 822
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE----VSPATAKLLAE---------LIPkyldkecypvvlg 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 823 GNGETvgaALVADSRTRAVMFTGSTEVARLI----NKTLSsrldpdgkpiPLIAETGGQNAMIVDSSALAEQVVADVLQS 898
Cdd:cd07132 165 GVEET---TELLKQRFDYIFYTGSTSVGKIVmqaaAKHLT----------PVTLELGGKSPCYVDKSCDIDVAARRIAWG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 899 SFDSAGQRCSALR-VLClQDDVADRTLTMLKGAMRELaLGNPDRLSADVGPVIDADAKRTIDAHIAAMKdkghavtqLAM 977
Cdd:cd07132 232 KFINAGQTCIAPDyVLC-TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGK--------VAI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 978 PDACAQGT-FVPPTIIEigNVDE----LKREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHA 1052
Cdd:cd07132 302 GGQTDEKErYIAPTVLT--DVKPsdpvMQEEIFGPILPIVTVN--NLDEAIEFINSREKPLALYVFSNNKKVINKILSNT 377
|
330 340 350
....*....|....*....|....*....|
gi 1943257567 1053 HVGNIYVNRNVIGAVVGVQPFGGEGLSGTG 1082
Cdd:cd07132 378 SSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
758-1082 |
7.06e-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: 103.35 E-value: 7.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 758 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAgVPAGAVQLLPGNGETVGAALvaDSR 837
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQELL--DQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 838 TRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCSALRVLCLQD 917
Cdd:cd07136 177 FDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 918 DVADRTLTMLKGAMRELALGNPdRLSADVGPVIDadakrtiDAH---IAAMKDKGHAVTQlamPDACAQGTFVPPTIIEI 994
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDP-LESPDYGRIIN-------EKHfdrLAGLLDNGKIVFG---GNTDRETLYIEPTILDN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 995 GNVDE--LKREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQP 1072
Cdd:cd07136 320 VTWDDpvMQEEIFGPILPVLTYDT--LDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLP 397
|
330
....*....|
gi 1943257567 1073 FGGEGLSGTG 1082
Cdd:cd07136 398 FGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
758-1082 |
6.28e-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: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 758 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLrDAGVPAGAVQLLPGnGETVGAALVaDSR 837
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEG-GVPETTALL-EQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 838 TRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDS-AGQRCSALRVLCLQ 916
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 917 DDVADRTLTMLKGAMRELALGNPdRLSADVGPVIDadaKRTIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPPTIIEIGN 996
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENP-KESKDLSRIVN---SHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEPTILLDPP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 997 VDEL--KREVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIYVNRNVIGAVVGVQPFG 1074
Cdd:cd07137 328 LDSSimTEEIFGPLLPIITVK--KIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFG 405
|
....*...
gi 1943257567 1075 GEGLSGTG 1082
Cdd:cd07137 406 GVGESGFG 413
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
717-1058 |
9.64e-22 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 100.65 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 717 LIVREAGKSLPNAIAEIREAVDFLRYYSA-QIR-------------DEFSNDTHRPLGPVVCISPWNFPLAIFMGQVAAA 782
Cdd:cd07126 87 LIQRVAPKSDAQALGEVVVTRKFLENFAGdQVRflarsfnvpgdhqGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 783 LAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGETVGaALVADSRTRAVMFTGSTEVARLINKTLSSRLD 862
Cdd:cd07126 167 LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPRMTLFTGSSKVAERLALELHGKVK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 863 pdgkpipliAETGGQNAMIVDSSALAEQVVADVL-QSSFDSAGQRCSALRVLCLQDDVADrtltmlKGAMRELALGNPDR 941
Cdd:cd07126 246 ---------LEDAGFDWKILGPDVSDVDYVAWQCdQDAYACSGQKCSAQSILFAHENWVQ------AGILDKLKALAEQR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 942 LSAD--VGPVIDADAKRTIDaHI--------AAMKDKGHAVTQLAMPDACAQ----GTFVP-PTIIEIGNVDELKREVFG 1006
Cdd:cd07126 311 KLEDltIGPVLTWTTERILD-HVdkllaipgAKVLFGGKPLTNHSIPSIYGAyeptAVFVPlEEIAIEENFELVTTEVFG 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1007 PVLHVVRYRRSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVISHAHVGNIY 1058
Cdd:cd07126 390 PFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
758-1082 |
4.51e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 89.02 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 758 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAqavrlLRDAGVP----AGAVQLLPGnGETVGAALV 833
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPkyldSKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 834 aDSRTRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALA---EQVVADVLQSSFDS-AGQRCSA 909
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 910 LRVLCLQDDVADRTLTMLKGAMRELALGNPDRlSADVGPVIDadaKRTIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPP 989
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRE-SKSMARILN---KKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFIEP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 990 TIIEIGNVDE--LKREVFGPVLHVVRYRRsgLDKLLEQIRATGYGLTLGIHTRiDETIA-HVISHAHVGNIYVNRNVIGA 1066
Cdd:PLN02203 331 TILLNPPLDSdiMTEEIFGPLLPIITVKK--IEDSIAFINSKPKPLAIYAFTN-NEKLKrRILSETSSGSVTFNDAIIQY 407
|
330
....*....|....*.
gi 1943257567 1067 VVGVQPFGGEGLSGTG 1082
Cdd:PLN02203 408 ACDSLPFGGVGESGFG 423
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
89-136 |
1.03e-16 |
|
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: 74.81 E-value: 1.03e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1943257567 89 SVLRAAITAAYRRPEPECVPFLIGEARLPASLAPDVQSMAAGLVEALR 136
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
758-1087 |
9.00e-16 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 81.93 E-value: 9.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 758 PLGPV-VCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGV-PAGAVQLLPGNgetVGAALVAD 835
Cdd:cd07128 143 PRRGVaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 836 SRTRAVMFTGSTEVARLInktlssRLDPD--GKPIPLIAETGGQNAMIvdssaLAEQVVADvlQSSFD------------ 901
Cdd:cd07128 220 GEQDVVAFTGSAATAAKL------RAHPNivARSIRFNAEADSLNAAI-----LGPDATPG--TPEFDlfvkevaremtv 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 902 SAGQRCSALRVLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHAVtqLAMPDAC 981
Cdd:cd07128 287 KAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVV--FGGPDRF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 982 A-------QGTFVPPTIIEIGNVDELKR----EVFGPVLHVVRYRrsGLDKLLEQIRATGYGLTLGIHTRIDETIAHVIS 1050
Cdd:cd07128 365 EvvgadaeKGAFFPPTLLLCDDPDAATAvhdvEAFGPVATLMPYD--SLAEAIELAARGRGSLVASVVTNDPAFARELVL 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1943257567 1051 HA--HVGNIYV-NRNVIGAVVG---VQP---FGGEGLSGTGPKAGG 1087
Cdd:cd07128 443 GAapYHGRLLVlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGG 488
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
758-1086 |
3.07e-15 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 80.09 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 758 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAgAVQLLPGNGETVGAALvaDSR 837
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 838 TRAVMFTGSTEVARLINKTLSSRLdpdgkpIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFD-SAGQRCSALRVLCLQ 916
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 917 DDVADRTLTMLKGAMRELALGNPDRlSADVGPVIDADAkrtIDAHIAAMKDKGHAVTQLAMPDACAQGTFVPPTIIEIGN 996
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTH---FDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 997 VDEL--KREVFGPVLHVVRYrrSGLDKLLEQIRATGYGLTLGIHT---RIDETIAHVIShahVGNIYVNRNVIGAVVGVQ 1071
Cdd:PLN02174 339 LDSLimSEEIFGPLLPILTL--NNLEESFDVIRSRPKPLAAYLFThnkKLKERFAATVS---AGGIVVNDIAVHLALHTL 413
|
330
....*....|....*
gi 1943257567 1072 PFGGEGLSGTGPKAG 1086
Cdd:PLN02174 414 PFGGVGESGMGAYHG 428
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
760-1015 |
1.37e-14 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 78.21 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 760 GPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGV-PAGAVQLLPGNGETVGAALVADSrt 838
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFD-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 839 rAVMFTGSTEVARLInktlssRLDPD--GKPIPLIAETGGQNAMI-----VDSSALAEQVVADVLQSSFDSAGQRCSALR 911
Cdd:PRK11903 228 -VVSFTGSAETAAVL------RSHPAvvQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQKCTAIR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 912 VLCLQDDVADRTLTMLKGAMRELALGNPDRLSADVGPVIDADAKRTIDAHIAAMKDKGHAV---TQLAMPDA-CAQGTFV 987
Cdd:PRK11903 301 RIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLfdgGGFALVDAdPAVAACV 380
|
250 260 270
....*....|....*....|....*....|..
gi 1943257567 988 PPTIIEIGNVDELKR----EVFGPVLHVVRYR 1015
Cdd:PRK11903 381 GPTLLGASDPDAATAvhdvEVFGPVATLLPYR 412
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-52 |
4.12e-12 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 62.53 E-value: 4.12e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1943257567 2 ASTTLGVKVDDLLRSRLKDAASRLERTPHWLIKQAIFAYLERIEHGQLPPE 52
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQ 51
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
757-1089 |
9.03e-09 |
|
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: 59.80 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 757 RPLGPVVCISP---WNFPLAIFmgqvaAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAG---AVQLLPGN--GETV 828
Cdd:cd07127 194 RGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVQVAREVLAEAGfdpNLVTLAADtpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 829 GAALVADSRTRAVMFTGSTevarlinkTLSSRLDPDGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQSSFDSAGQRCS 908
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSN--------AFGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 909 ALRVLCLQDD---------VADRTLTMLKGAMRELaLGNPDRLSADVGPVIDADAKRTIdAHIAAMKDKGHAVTQLAMPD 979
Cdd:cd07127 341 TPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI-AEARQLGEVLLASEAVAHPE 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 980 AcAQGTFVPPTIIEIGNVDE--LKREVFGPVLHVVRYRRS--GLDKLLEQIRATGyGLTLGIHTRIDETIAHVISHAHVG 1055
Cdd:cd07127 419 F-PDARVRTPLLLKLDASDEaaYAEERFGPIAFVVATDSTdhSIELARESVREHG-AMTVGVYSTDPEVVERVQEAALDA 496
|
330 340 350
....*....|....*....|....*....|....*.
gi 1943257567 1056 NIYVNRNVIGAVVGVQPFGGEGLSGTG--PKAGGAL 1089
Cdd:cd07127 497 GVALSINLTGGVFVNQSAAFSDFHGTGanPAANAAL 532
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-45 |
3.12e-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: 50.83 E-value: 3.12e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1943257567 4 TTLGVKVDDLLRSRLKDAASRLERTPHWLIKQAIFAYLERIE 45
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREE 42
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
758-939 |
6.00e-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: 56.46 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 758 PLGPVVCISPWNFPLAIfMGQVAAALAAGNTVLAKPAEQTPlIAAQAVRLLRDAGVPAG----AVQLLPGNGETVGAALV 833
Cdd:cd07077 100 PIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkiLVLYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 834 ADSRTRAVMFTGSTEVARLINKTlssrldpdGKPIPLIAETGGQNAMIVDSSALAEQVVADVLQS-SFDSAGqrCSALRV 912
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSkFFDQNA--CASEQN 247
|
170 180
....*....|....*....|....*..
gi 1943257567 913 LCLQDDVADRTLTMLKGAMRELALGNP 939
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLKLVVEGLKVP 274
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
337-553 |
6.78e-07 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 53.55 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 337 QQERTMVELLPRVRSLALLARRYDIGLNIDAEEA------DRLELSLdlleALCFDPelAGWNGIGFV-VQAYQKRCPfv 409
Cdd:PLN02681 210 EEERLLELAHERLQKLCERAAQLGVPLLIDAEYTslqpaiDYITYDL----AREFNK--GKDRPIVYGtYQAYLKDAR-- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 410 iDYLVDLARRSRHR---LMIRLVKGAYWDTEIKRAQVDGLEGyPVYTRKIYTDVSYLACAKKLLAA----PDAVYpqFAT 482
Cdd:PLN02681 282 -ERLRLDLERSEREgvpLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAEFLLEKasngDGEVM--LAT 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943257567 483 HNAYTLAAIYHLA---GQNYYPGQYEFQCLHGMGEPLYEEVtgrdkLNRPCRV--YAPVGTHETLLAYLVRRLLEN 553
Cdd:PLN02681 358 HNVESGELAAAKMnelGLHKGDPRVQFAQLLGMSDNLSFGL-----GNAGFRVskYLPYGPVEEVIPYLLRRAEEN 428
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
758-1084 |
2.01e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 51.88 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 758 PLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGAVQLLPGNGET----VGAALV 833
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNpsieLAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 834 ADSRTRAVMFTGSTEVARLINKTlssrldpdGKPipLIAETGGQNAMIVDSSALAEQVVADVLQS-SFDSaGQRCSALRV 912
Cdd:cd07081 175 KFPGIGLLLATGGPAVVKAAYSS--------GKP--AIGVGAGNTPVVIDETADIKRAVQSIVKSkTFDN-GVICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 913 LCLQDDVADRTLTMLKGAMRELALGNPdrlSADVGPVI--DADAKRTIdahiaamkdkghaVTQLAMPDACAQGTFVPPT 990
Cdd:cd07081 244 VIVVDSVYDEVMRLFEGQGAYKLTAEE---LQQVQPVIlkNGDVNRDI-------------VGQDAYKIAAAAGLKVPQE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 991 ----IIEIGNVDE---LKREVFGPVLHVVRYRR--SGLDKLLEQIRATGYGLTLGIHTRIDETIAHV------------- 1048
Cdd:cd07081 308 trilIGEVTSLAEhepFAHEKLSPVLAMYRAANfaDADAKALALKLEGGCGHTSAMYSDNIKAIENMnqfanamktsrfv 387
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1943257567 1049 ----ISHAHVGNIYVNRNVIGAVVGVQPFGGEGLS-GTGPK 1084
Cdd:cd07081 388 kngpCSQGGLGDLYNFRGWPSMTLGCGTWGGNSVSeNVGPK 428
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
757-1060 |
2.50e-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: 48.26 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 757 RPLGPVVCISPWNFPLAIFMGQVAAALAAGNTVLAKPAEQTPLIAAQAVRLLRDAGVPAGA----VQLLPGNGETVGAAL 832
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGApeglIQWIEEPSIELTQEL 173
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 833 VADSRTRAVMFTGSTEVARLinkTLSSrldpdGKPIplIAETGGQNAMIVDSSALAEQVVADVLQS-SFDSaGQRCSALR 911
Cdd:cd07122 174 MKHPDVDLILATGGPGMVKA---AYSS-----GKPA--IGVGPGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQ 242
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 912 VLCLQDDVADRTLTMLK--GA----------MRELALGNPDRLSADvgpVIDADAkrtidAHIAAMKdkghavtqlampd 979
Cdd:cd07122 243 SVIVDDEIYDEVRAELKrrGAyflneeekekLEKALFDDGGTLNPD---IVGKSA-----QKIAELA------------- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943257567 980 acaqGTFVPPT----IIEIGNVDE---LKREVFGPVLHVVRYR--RSGLDKLLEQIRATGYGLTLGIHTRIDETIAHVIS 1050
Cdd:cd07122 302 ----GIEVPEDtkvlVAEETGVGPeepLSREKLSPVLAFYRAEdfEEALEKARELLEYGGAGHTAVIHSNDEEVIEEFAL 377
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330
....*....|
gi 1943257567 1051 HAHVGNIYVN 1060
Cdd:cd07122 378 RMPVSRILVN 387
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| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-43 |
1.96e-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: 40.18 E-value: 1.96e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1943257567 4 TTLGVKVDDLLRSRLKDAASRLERTPHWLIKQAIFAYLER 43
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLER 40
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| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
1162-1203 |
1.14e-03 |
|
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: 42.95 E-value: 1.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1943257567 1162 LSGPTGERNTYTLGARGTVLCIA------ATASGaraQFAAVLATGNR 1203
Cdd:cd07125 153 LPGPTGELNGLELHGRGVFVCISpwnfplAIFTG---QIAAALAAGNT 197
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| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
4-45 |
2.36e-03 |
|
Predicted DNA-binding protein with an HTH domain [General function prediction only];
Pssm-ID: 443745 Cd Length: 76 Bit Score: 37.96 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1943257567 4 TTLGVKVDDLLRSRLKDAASRLERTPHWLIKQAIFAYLERIE 45
Cdd:COG4710 2 KMLSIRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
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|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1157-1202 |
4.67e-03 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 41.34 E-value: 4.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1943257567 1157 GATAVLSGPTGERNTYTLGARGTVLCIA------ATASGaraQFAAVLATGN 1202
Cdd:PRK11904 665 GAPEKLPGPTGESNELRLHGRGVFVCISpwnfplAIFLG---QVAAALAAGN 713
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