|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1-1044 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1899.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 1 MISSIQEPNALRKRLQAFYRADEKSHVRYLVEKSELSADSKNIIYNIAKQIVEKIRGNK--LGIIDSFIQQYSLSNDEGV 78
Cdd:PRK11904 3 GIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKkkLGGIDAFLQEYSLSTEEGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 79 ALMCLAESLLRIPDDYTIDELIKDKIANQEWNKHLGRSSSLFVNASTWSLIIGSSILR-NNEEDSKFYHIISRLLKNLGE 157
Cdd:PRK11904 83 ALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKlDKKADGTPSGVLKRLVNRLGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 158 PIIRKAVKQAISILGKHFIVGETIAKALESVKSDDYSKYLCSFDMLGESACKVEDAEEYFNLYMHAIKAIGEAADINDCF 237
Cdd:PRK11904 163 PVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADLP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 238 KSQGVSIKLSSLHSRYEFSQFGNIAEELRAKLLELCHEAKKYNISLCIDAEESERLEMSLVLFEQLRLDDSLSKWEGLGL 317
Cdd:PRK11904 243 ARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 318 AVQAYQKRALSVLDFVEDVAIRSKHKIMVRLVKGAYWDSEIKRTQELGLIGYPVFTRKSHTDVCYLACAQKLLSKENHFY 397
Cdd:PRK11904 323 AVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAIY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 398 PCFGTHNAYTFATIIELADknHPGFEFQRLHGMGKSLYDYAISelATSINCRIYAPVGKHSDLLPYLIRRLLENGANSSF 477
Cdd:PRK11904 403 PQFATHNAHTVAAILEMAG--HRGFEFQRLHGMGEALYDALLD--APGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 478 VNQVNDSDVKIEELVSDPLEKVKSLEYEPHPSIPLPRDIFGEERKNSLGMDISDSIAVSQFANDVREFSEKKWQVGPIID 557
Cdd:PRK11904 479 VHRLVDPDVPIEELVADPVEKLRSFETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPIIN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 558 GksfldNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIV 637
Cdd:PRK11904 559 G-----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVR 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 638 EAGKILSDAIAEVREAIDFLRYYAMIAKNELNDWKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGN 717
Cdd:PRK11904 634 EAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGN 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 718 AVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIVPL 797
Cdd:PRK11904 714 TVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPL 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 798 IAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPII 877
Cdd:PRK11904 794 IAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVI 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 878 DKASIDMLTKHTEKISRDEdtNLLSKVPMDTNSYNGYFFPPYIYEIQKISQLKQEVFGPILHIIRFNKSQLNEVISDINN 957
Cdd:PRK11904 874 DAEAKANLDAHIERMKREA--RLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAINA 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 958 TGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFSIEKVVSVNTTACG 1037
Cdd:PRK11904 952 TGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNTTAAG 1031
|
....*..
gi 1571382267 1038 GNITLAC 1044
Cdd:PRK11904 1032 GNASLLS 1038
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
1-1031 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1495.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 1 MISSIQEPNALRKRLQAFYRADEKSHVRYLVEKSELSADSKNIIYNIAKQIVEKIRGNKLG-IIDSFIQQYSLSNDEGVA 79
Cdd:PRK11905 5 FAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGtGVEALLQEYSLSSQEGVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 80 LMCLAESLLRIPDDYTIDELIKDKIANQEWNKHLGRSSSLFVNASTWSLIIGSSILrNNEEDSKFYHIISRLLKNLGEPI 159
Cdd:PRK11905 85 LMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLL-STVNDRGLSAALTRLIARLGEPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 160 IRKAVKQAISILGKHFIVGETIAKALESVKSDDYSKYLCSFDMLGESACKVEDAEEYFNLYMHAIKAIGEAADINDCFKS 239
Cdd:PRK11905 164 IRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGVYDG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 240 QGVSIKLSSLHSRYEFSQFGNIAEELRAKLLELCHEAKKYNISLCIDAEESERLEMSLVLFEQLRLDDSLSKWEGLGLAV 319
Cdd:PRK11905 244 PGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIGFVV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 320 QAYQKRALSVLDFVEDVAIRSKHKIMVRLVKGAYWDSEIKRTQELGLIGYPVFTRKSHTDVCYLACAQKLLSKENHFYPC 399
Cdd:PRK11905 324 QAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVIYPQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 400 FGTHNAYTFATIIELADKNHPgFEFQRLHGMGKSLYDYAISELATSINCRIYAPVGKHSDLLPYLIRRLLENGANSSFVN 479
Cdd:PRK11905 404 FATHNAQTLAAIYELAGGKGD-FEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVN 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 480 QVNDSDVKIEELVSDPLEKVKSLEYEPHPSIPLPRDIFGEERKNSLGMDISDSIAVSQFANDVREFSEKKWQVGPIIDGK 559
Cdd:PRK11905 483 RIVDENVPVEELIADPVEKVAAMGVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLAGG 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 560 SFLDNAEftEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEA 639
Cdd:PRK11905 563 DVDGGTR--PVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 640 GKILSDAIAEVREAIDFLRYYAMIAKNELNDWKKLPgptgednfiffegRGVFLCISPWNFPLAIFIGQVSAALAAGNAV 719
Cdd:PRK11905 641 GKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKP-------------LGPVVCISPWNFPLAIFTGQIAAALVAGNTV 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 720 LAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIVPLIA 799
Cdd:PRK11905 708 LAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLIA 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 800 ETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDK 879
Cdd:PRK11905 788 ETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDA 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 880 ASIDMLTKHTEKIsRDEDTnLLSKVPMDTNSYNGYFFPPYIYEIQKISQLKQEVFGPILHIIRFNKSQLNEVISDINNTG 959
Cdd:PRK11905 868 EAQANIEAHIEAM-RAAGR-LVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATG 945
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1571382267 960 YGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFSIEKVVSV 1031
Cdd:PRK11905 946 YGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPI 1017
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
1-1046 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1276.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 1 MISSIQEPNALRKRLQAFYRADEKSHVRYLVEKSELSADSKNIIYNIAKQIVEKIRGNKLGIIDSFIQQYSLSNDEGVAL 80
Cdd:COG4230 6 FAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLSSEALA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 81 MCLAESLLRIPDDYTIDELIKDKIANQEWNKHLGRSSSLFVNASTWSLIIGSSILRNNEEDSKFYHIISRLLKNLGEPII 160
Cdd:COG4230 86 LLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRLGRPGI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 161 RKAVKQAISILGKHFIVGETIAKALESVKSDDYSKYLCSFDMLGESACKVEDAEEYFNLYMHAIKAIGEAADINDCFKSQ 240
Cdd:COG4230 166 RRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGSGGPGP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 241 GVSIKLSSLHSRYEFSQFGNIAEELRAKLLELCHEAKKYNISLCIDAEESERLEMSLVLFEQLRLDDSLSKWEGLGLAVQ 320
Cdd:COG4230 246 SISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 321 AYQKRALSVLDFVEDVAIRSKHKIMVRLVKGAYWDSEIKRTQELGLIGYPVFTRKSHTDVCYLACAQKLLSKENHFYPCF 400
Cdd:COG4230 326 QAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAAQPAF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 401 GTHNAYTFATIIELADKNHPGFEFQRLHGMGKSLYDYA-ISELATSINCRIYAPVGKHSDLLPYLIRRLLENGANSSFVN 479
Cdd:COG4230 406 APQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDqVGRGKLGRPCRIYAPVGSHEDLLAYLVRRLLENGANSSFVN 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 480 QVNDSDVKIEELVSDPLEKVKSLEYEPHPSIPLPRDIFGEERKNSLGMDISDSIAVSQFANDVREFSEKKWQVGPIIDGK 559
Cdd:COG4230 486 RIADEDVPVEELIADPVEKARALGGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQAAPLIAGE 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 560 SflDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEA 639
Cdd:COG4230 566 A--ASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 640 GKILSDAIAEVREAIDFLRYYAMIAKNELNDWKKLpgptgednfiffEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAV 719
Cdd:COG4230 644 GKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVL------------RGRGVFVCISPWNFPLAIFTGQVAAALAAGNTV 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 720 LAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIVPLIA 799
Cdd:COG4230 712 LAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLIA 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 800 ETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDK 879
Cdd:COG4230 792 ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDA 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 880 ASIDMLTKHTEKISRDEdtNLLSKVPMDTNSYNGYFFPPYIYEIQKISQLKQEVFGPILHIIRFNKSQLNEVISDINNTG 959
Cdd:COG4230 872 EARANLEAHIERMRAEG--RLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATG 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 960 YGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFSIEKVVSVNTTACGGN 1039
Cdd:COG4230 950 YGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTAAGGN 1029
|
....*..
gi 1571382267 1040 ITLACLD 1046
Cdd:COG4230 1030 ASLLALG 1036
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
4-1022 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1216.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 4 SIQEPNALRKRLQAFYRADEKSHVRYLVEKSELSADSKNIIYNIAKQIVEKIR-----GNKLGIIDSFIQQYSLSNDEGV 78
Cdd:PRK11809 84 QILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRnqksaGGRAGMVQGLLQEFSLSSQEGV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 79 ALMCLAESLLRIPDDYTIDELIKDKIANQEWNKHLGRSSSLFVNASTWSLII-GSSILRNNEedSKFYHIISRLLKNLGE 157
Cdd:PRK11809 164 ALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFtGKLVSTHNE--ASLSSSLNRIIGKSGE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 158 PIIRKAVKQAISILGKHFIVGETIAKALESVKSDDYSKYLCSFDMLGESACKVEDAEEYFNLYMHAIKAIGEAADINDCF 237
Cdd:PRK11809 242 PLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGIY 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 238 KSQGVSIKLSSLHSRYEFSQFGNIAEELRAKLLELCHEAKKYNISLCIDAEESERLEMSLVLFEQLRLDDSLSKWEGLGL 317
Cdd:PRK11809 322 EGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGF 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 318 AVQAYQKRALSVLDFVEDVAIRSKHKIMVRLVKGAYWDSEIKRTQELGLIGYPVFTRKSHTDVCYLACAQKLLSKENHFY 397
Cdd:PRK11809 402 VIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLIY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 398 PCFGTHNAYTFATIIELADKN-HPG-FEFQRLHGMGKSLYDYAISELAT-SIN--CRIYAPVGKHSDLLPYLIRRLLENG 472
Cdd:PRK11809 482 PQFATHNAHTLAAIYHLAGQNyYPGqYEFQCLHGMGEPLYEQVVGKVADgKLNrpCRIYAPVGTHETLLAYLVRRLLENG 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 473 ANSSFVNQVNDSDVKIEELVSDPLEKVKSLEYE------PHPSIPLPRDIFGEERKNSLGMDISDSIAVSQFANDVREFS 546
Cdd:PRK11809 562 ANTSFVNRIADTSLPLDELVADPVEAVEKLAQQegqlglPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLASA 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 547 EKKWQVGPIIDGKsfLDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEE 626
Cdd:PRK11809 642 HQKWQAAPMLEDP--VAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEA 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 627 RMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNEL-NDWKKLPGPTgednfiffegrgvfLCISPWNFPLAIF 705
Cdd:PRK11809 720 QMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFdNDTHRPLGPV--------------VCISPWNFPLAIF 785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 706 IGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINR 785
Cdd:PRK11809 786 TGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQR 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 786 MLASR---DGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELK 862
Cdd:PRK11809 866 NLAGRldpQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECR 945
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 863 IGDPIQLSTDIGPIID---KASIDmltKHTEKISRDEDTNLLSKVPMDTNSYNGYFFPPYIYEIQKISQLKQEVFGPILH 939
Cdd:PRK11809 946 MGNPDRLSTDIGPVIDaeaKANIE---RHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSFDELKREVFGPVLH 1022
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 940 IIRFNKSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNY 1019
Cdd:PRK11809 1023 VVRYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLY 1102
|
...
gi 1571382267 1020 LQR 1022
Cdd:PRK11809 1103 LYR 1105
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
473-1042 |
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: 825.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 473 ANSSFVNQVNDSDVKIEelvsdplekvksleyephpsiplprdifgeerknslgmdisdsiavsQFANDVREFSEKKWQV 552
Cdd:cd07125 1 ANSSFVNRIFDLEVPLE-----------------------------------------------ALADALKAFDEKEWEA 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 553 GPIIDGKsFLDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELI 632
Cdd:cd07125 34 IPIINGE-ETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 633 YILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELNDWKkLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAA 712
Cdd:cd07125 113 ALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPE-LPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 713 LAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDG 792
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 793 PIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTD 872
Cdd:cd07125 272 PILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 873 IGPIIDKASIDMLTKHTEKISRDEdtNLLSKVPMDTNsyNGYFFPPYIYEIQKISQLKQEVFGPILHIIRFNKSQLNEVI 952
Cdd:cd07125 352 VGPLIDKPAGKLLRAHTELMRGEA--WLIAPAPLDDG--NGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEAI 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 953 SDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFSIEKVVSVN 1032
Cdd:cd07125 428 EDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLN 507
|
570
....*....|
gi 1571382267 1033 TTACGGNITL 1042
Cdd:cd07125 508 TTAAGGNPSL 517
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
35-1039 |
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: 674.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 35 ELSADSKNIIYNIAKQIVEKIRGNKLGIIDSFIQQYSLSNDEGVALMCLAESLLRIPDDYTIDELIKDKIAnqewnkhlg 114
Cdd:COG0506 4 ALDEALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 115 RSSSLFVNASTWSLIIGssilrnneedskfyhiisrLLKNLGEPIIRKAVKQAISILGKHFIVGETIAKALESVKSDDYS 194
Cdd:COG0506 75 KSPSFLVNASTWGLMLT-------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 195 KYLCSFDMLGESACKVEDAEEYFNLYMHAIKAIGEAADINDcfksqGVSIKLSSLHSRYEFSQFGNIAEELRAKLLELCH 274
Cdd:COG0506 136 GYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAGVDRP-----GVSVKLSALGPRYSPAQRERVVEELLERLRPLAR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 275 EAKKYNISLCIDAEESERLEMSLVLFEQLRLDDSLSKWEGLGLAVQAYQKRALSVLDFVEDVAIRSKHKIMVRLVKGAYW 354
Cdd:COG0506 211 AAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAYW 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 355 DSEIKRTQELGLiGYPVFTRKSHTDVCYLACAQKLLSKENHFYPCFGTHNAYTFATIIELADKN---HPGFEFQRLHGMG 431
Cdd:COG0506 291 DPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGERgrpPDRFEFQMLYGMG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 432 KSLYDYAISELATSIN-CRIYAPVGKHSDLLPYLIRRLLENGANSSFVNQVNDSDV-KIEELVSDPLEKVKSLEYEPHPS 509
Cdd:COG0506 370 EDLQRALAAVDGGRLLlYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEdLLEFPREPPRFLAALAAPTPPPP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 510 IPLPRDIFGEERKNSLGMDISDSIAVSQFANDVREFSEKKWQVGPIIDGKsflDNAEFTEVVNPAHLENVIGEVSSATSA 589
Cdd:COG0506 450 PPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAA---AAAAAAVAVVPAAAAAVVAAAAAAAAA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 590 QALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELN 669
Cdd:COG0506 527 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAA 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 670 DWKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLH 749
Cdd:COG0506 607 APPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLV 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 750 LIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRS 829
Cdd:COG0506 687 LGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASA 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 830 GGQRCSALRVLFIQEDIAEKQIKMIcnAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPMDTN 909
Cdd:COG0506 767 SASLLSLLALLLLDADLVILLLALA--AAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVP 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 910 SYNGYFFPPYIYEIQKISQLKQEVFGPILHIIRFNKSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYIN 989
Cdd:COG0506 845 GLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGG 924
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|
gi 1571382267 990 RNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFSIEKVVSVNTTACGGN 1039
Cdd:COG0506 925 GGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAA 974
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
515-1024 |
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: 590.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 515 DIFGEERKNSLGMDISDSIAVSQFANDVREFSEKKWQVGPIIDGKsFLDNAEFTEVVNPAHLENVIGEVSSATSAQALNA 594
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHS-YKADGEAQPVTNPADRRDIVGQVFHANLAHVQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 595 LEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELndwkkl 674
Cdd:TIGR01238 80 IDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVL------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 675 pgptGEDNFiffEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGD 754
Cdd:TIGR01238 154 ----GEFSV---ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 755 GWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRC 834
Cdd:TIGR01238 227 GADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 835 SALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPMDTNSYNGY 914
Cdd:TIGR01238 307 SALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 915 FFPPYIYEIQKISQLKQEVFGPILHIIRFNKSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIG 994
Cdd:TIGR01238 387 FVAPTLFELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVG 466
|
490 500 510
....*....|....*....|....*....|
gi 1571382267 995 AAVGTQPFGGRGLSGTGPKAGGPNYLQRFS 1024
Cdd:TIGR01238 467 AVVGVQPFGGQGLSGTGPKAGGPHYLYRLT 496
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
542-1032 |
1.39e-166 |
|
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: 499.03 E-value: 1.39e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 542 VREFSEKKWQVGPIIDGKSFLDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAA 621
Cdd:cd07083 8 LRRVKEEFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 622 DLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELNDWKKLPGPTGEDNFIFFEGRGVFLCISPWNFP 701
Cdd:cd07083 88 DLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 702 LAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQ 781
Cdd:cd07083 168 VAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 782 IINRMLAS---RDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAA 858
Cdd:cd07083 248 KIYEAAARlapGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 859 QELKIGDPIQLSTDIGPIIDKASIDMLTKHTEkISRDEDTNLLSkvpMDTNSYNGYFFPPYIYEIQ--KISQLKQEVFGP 936
Cdd:cd07083 328 ERLSVGPPEENGTDLGPVIDAEQEAKVLSYIE-HGKNEGQLVLG---GKRLEGEGYFVAPTVVEEVppKARIAQEEIFGP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 937 ILHIIRFNKSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGG 1016
Cdd:cd07083 404 VLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGG 483
|
490
....*....|....*.
gi 1571382267 1017 PNYLQRFSIEKVVSVN 1032
Cdd:cd07083 484 PHYLRRFLEMKAVAER 499
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
551-1033 |
6.14e-143 |
|
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: 437.81 E-value: 6.14e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 551 QVGPIIDGKSfLDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKE 630
Cdd:cd07124 32 EYPLVIGGKE-VRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 631 LIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAknELNDWKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVS 710
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREM--LRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 711 AALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRmLASR 790
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE-RAAK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 791 DGP----IVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDP 866
Cdd:cd07124 268 VQPgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 867 IQLSTDIGPIIDKASIDMLTKHTEkISRDEDTnLLSKVPMDTNSYNGYFFPPYIYE-IQKISQL-KQEVFGPILHIIRFN 944
Cdd:cd07124 348 EDPEVYMGPVIDKGARDRIRRYIE-IGKSEGR-LLLGGEVLELAAEGYFVQPTIFAdVPPDHRLaQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 945 ksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFS 1024
Cdd:cd07124 426 --DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFM 503
|
....*....
gi 1571382267 1025 IEKVVSVNT 1033
Cdd:cd07124 504 QPKTVTENF 512
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
551-1033 |
1.05e-133 |
|
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: 412.60 E-value: 1.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 551 QVGPIIDGKS-FLDNAEFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMK 629
Cdd:COG1012 5 EYPLFIGGEWvAAASGETFDVINPATGE-VLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 630 ELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKnelndwkKLPGPT------GEDNFIFFEGRGVFLCISPWNFPLA 703
Cdd:COG1012 84 ELAALLTLETGKPLAEARGEVDRAADFLRYYAGEAR-------RLYGETipsdapGTRAYVRREPLGVVGAITPWNFPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 704 IFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQII 783
Cdd:COG1012 157 LAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 784 NRMLASRdgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKI 863
Cdd:COG1012 237 AAAAAEN---LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 864 GDPIQLSTDIGPIIDKASIDMLTKHTEkISRDEDTNLLS--KVPMDTnsyNGYFFPPYIYEI----QKISQlkQEVFGPI 937
Cdd:COG1012 314 GDPLDPGTDMGPLISEAQLERVLAYIE-DAVAEGAELLTggRRPDGE---GGYFVEPTVLADvtpdMRIAR--EEIFGPV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 938 LHIIRFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRnQIGAAVGTQPFGGRGLSGTGPKaGGP 1017
Cdd:COG1012 388 LSVIPF--DDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWIND-GTTGAVPQAPFGGVKQSGIGRE-GGR 463
|
490
....*....|....*.
gi 1571382267 1018 NYLQRFSIEKVVSVNT 1033
Cdd:COG1012 464 EGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
563-1029 |
5.04e-127 |
|
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: 394.21 E-value: 5.04e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 563 DNAEFTEVVNPAHlENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKI 642
Cdd:pfam00171 4 SESETIEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 643 LSDAIAEVREAIDFLRYYAMIAKNElnDWKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAK 722
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRL--DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 723 PAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETG 802
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN---LKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 803 GLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASI 882
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 883 DMLTKHTEKiSRDEDTNLLskVPMDTNSYNGYFFPPYIYE-IQKISQL-KQEVFGPILHIIRFNKsqLNEVISDINNTGY 960
Cdd:pfam00171 318 ERVLKYVED-AKEEGAKLL--TGGEAGLDNGYFVEPTVLAnVTPDMRIaQEEIFGPVLSVIRFKD--EEEAIEIANDTEY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1571382267 961 GLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVgTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVV 1029
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAD-GLPFGGFKQSGFG-REGGPYGLEEYTEVKTV 459
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
183-480 |
7.36e-124 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 379.91 E-value: 7.36e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 183 KALESVKSDdysKYLCSFDMLGESACKVEDAEEYFNLYMHAIKAIGEAADINDCFKSQGVSIKLSSLHSRYEFSQFGNIA 262
Cdd:pfam01619 3 KTIEKLRKQ---GYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 263 EELRAKLLELCHEAKKYNISLCIDAEESERLEMSLVLFEQLRLDDSLSKWEGLGLAVQAYQKRALSVLDFVEDVAIRSKH 342
Cdd:pfam01619 80 AELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 343 KIMVRLVKGAYWDSEIKRTQElGLIGYPVFTRKSHTDVCYLACAQKLLSKENHFYPCFGTHNAYTFATIIELADK---NH 419
Cdd:pfam01619 160 PLGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElgiPP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1571382267 420 PGFEFQRLHGMGKSLYDyaisELATS-INCRIYAPVGKHSDLLPYLIRRLLENGANSSFVNQ 480
Cdd:pfam01619 239 RRFEFQQLYGMGDNLSF----ALVAAgYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
594-1031 |
2.48e-123 |
|
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: 383.87 E-value: 2.48e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 594 ALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKnELNDWKK 673
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLAR-RLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 674 LPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPG 753
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 754 DGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQR 833
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEN---LKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 834 CSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPMDTNsyNG 913
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGG--KG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 914 YFFPPYIYE----IQKISQlkQEVFGPILHIIRFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYIN 989
Cdd:cd07078 317 YFVPPTVLTdvdpDMPIAQ--EEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1571382267 990 RNQIGaAVGTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd07078 393 DYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTVTI 432
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
555-1030 |
1.14e-111 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 355.78 E-value: 1.14e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 555 IIDGKSfLDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYI 634
Cdd:PRK03137 40 IIGGER-ITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 635 LIVEAGKILSDAIAEVREAIDFLRYYA--MIaknELNDWKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAA 712
Cdd:PRK03137 119 LVKEAGKPWAEADADTAEAIDFLEYYArqML---KLADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 713 LAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRmLASRDG 792
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE-RAAKVQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 793 P----IVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQ 868
Cdd:PRK03137 275 PgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 869 lSTDIGPIIDKASIDMLTKHTEkISRDEDTNLLSKvpmDTNSYNGYFFPPYIY-EIQKISQLKQ-EVFGPILHIIRFnkS 946
Cdd:PRK03137 355 -NAYMGPVINQASFDKIMSYIE-IGKEEGRLVLGG---EGDDSKGYFIQPTIFaDVDPKARIMQeEIFGPVVAFIKA--K 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 947 QLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFSIE 1026
Cdd:PRK03137 428 DFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQA 507
|
....
gi 1571382267 1027 KVVS 1030
Cdd:PRK03137 508 KTVS 511
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
554-1032 |
1.11e-110 |
|
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: 353.40 E-value: 1.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 554 PIIDGKsFLDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIY 633
Cdd:TIGR01237 35 LVINGE-RVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 634 ILIVEAGKILSDAIAEVREAIDFLRYYA--MI--AKNELNDWKKlpgptGEDNFIFFEGRGVFLCISPWNFPLAIFIGQV 709
Cdd:TIGR01237 114 LLVKEVGKPWNEADAEVAEAIDFMEYYArqMIelAKGKPVNSRE-----GETNQYVYTPTGVTVVISPWNFPFAIMVGMT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 710 SAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMlAS 789
Cdd:TIGR01237 189 VAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFER-AA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 790 RDGP----IVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGD 865
Cdd:TIGR01237 268 KVQPgqkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 866 PIQLSTDIGPIIDKASIDMLTKHTEkISRDEDTNLLSKVPMDTnsyNGYFFPPYIY-EIQKISQLKQ-EVFGPILHIIRf 943
Cdd:TIGR01237 348 PDSADVYVGPVIDQKSFNKIMEYIE-IGKAEGRLVSGGCGDDS---KGYFIGPTIFaDVDRKARLAQeEIFGPVVAFIR- 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 944 nKSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRF 1023
Cdd:TIGR01237 423 -ASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALF 501
|
....*....
gi 1571382267 1024 SIEKVVSVN 1032
Cdd:TIGR01237 502 MQAKTVTEM 510
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
596-1031 |
4.11e-97 |
|
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: 311.86 E-value: 4.11e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 596 EIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKnELNDWKKLP 675
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLAD-KLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 676 GPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDG 755
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 756 WYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCS 835
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAEN---LKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 836 ALRVLFIQEDIAEKQIKMICnaaqelkigdpiQLSTDIGPiidkasiDMltkhteKIsrdedtnllskvpmdtnsyngyf 915
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------TVLVDVDP-------DM------PI----------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 916 fppyiyeiqkisqLKQEVFGPILHIIRFNksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGa 995
Cdd:cd06534 269 -------------AQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG- 332
|
410 420 430
....*....|....*....|....*....|....*.
gi 1571382267 996 AVGTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd06534 333 VGPEAPFGGVKNSGIG-REGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
556-1032 |
2.10e-94 |
|
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: 308.51 E-value: 2.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKsFLDNA--EFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIY 633
Cdd:cd07131 3 IGGE-WVDSAsgETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 634 ILIVEAGKILSDAIAEVREAIDFLRYYAmiaknelNDWKKLPGPT------GEDNFIFFEGRGVFLCISPWNFPLAIFIG 707
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAA-------GEGRRLFGETvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 708 QVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRML 787
Cdd:cd07131 155 KIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 788 ASrdgPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPI 867
Cdd:cd07131 235 AR---PNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 868 QLSTDIGPIIDKASIDMLTKHTEkISRDEDTNLL--SKVPMDTNSYNGYFFPPYIYEI--QKISQLKQEVFGPILHIIRF 943
Cdd:cd07131 312 DEETDMGPLINEAQLEKVLNYNE-IGKEEGATLLlgGERLTGGGYEKGYFVEPTVFTDvtPDMRIAQEEIFGPVVALIEV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 944 nkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTqPFGGRGLSGTGPKAGGPNYLQRF 1023
Cdd:cd07131 391 --SSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGTTALDAF 467
|
....*....
gi 1571382267 1024 SIEKVVSVN 1032
Cdd:cd07131 468 TEWKAVYVD 476
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
556-1031 |
1.49e-90 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 298.01 E-value: 1.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKsFLDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYIL 635
Cdd:cd07097 5 IDGE-WVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 636 IVEAGKILSDAIAEVREAIDFLRYYAMIAKnelndwkKLPG----PTGEDNFIFF--EGRGVFLCISPWNFPLAIFIGQV 709
Cdd:cd07097 84 TREEGKTLPEARGEVTRAGQIFRYYAGEAL-------RLSGetlpSTRPGVEVETtrEPLGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 710 SAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLAS 789
Cdd:cd07097 157 APALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 790 RDGPIVpliAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQL 869
Cdd:cd07097 237 RGARVQ---LEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 870 STDIGPIIDKASIDMLTKHTEkISRDEDTNLLS---KVPMDTnsyNGYFFPPYIYE----IQKISQlkQEVFGPILHIIR 942
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIE-IARSEGAKLVYggeRLKRPD---EGYYLAPALFAgvtnDMRIAR--EEIFGPVAAVIR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 943 FNksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGaaVGTQ-PFGGRGLSGTGPKAGGPNYLQ 1021
Cdd:cd07097 388 VR--DYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEAALE 463
|
490
....*....|
gi 1571382267 1022 RFSIEKVVSV 1031
Cdd:cd07097 464 FYTTIKTVYV 473
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
570-1031 |
5.65e-90 |
|
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: 295.50 E-value: 5.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAE 649
Cdd:cd07103 1 VINPATGE-VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 650 VREAIDFLRYYAMIAKNELNDwkKLPGPTGeDNFIFFEGR--GVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQT 727
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYGR--TIPSPAP-GKRILVIKQpvGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 728 PIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGlNA- 806
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADT---VKRVSLELGG-NAp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 807 MIVDSSALLEQVTKDVLISAFRSGGQRC-SALRVlFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDML 885
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCvCANRI-YVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 886 TKHTE-------KI----SRDEDtnllskvpmdtnsyNGYFFPPYIyeiqkISQ-------LKQEVFGPILHIIRFnkSQ 947
Cdd:cd07103 312 EALVEdavakgaKVltggKRLGL--------------GGYFYEPTV-----LTDvtddmliMNEETFGPVAPIIPF--DT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 948 LNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVgtQPFGGRGLSGTGpKAGGPNYLQRFSIEK 1027
Cdd:cd07103 371 EDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLG-REGGKEGLEEYLETK 447
|
....
gi 1571382267 1028 VVSV 1031
Cdd:cd07103 448 YVSL 451
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
569-1015 |
7.73e-88 |
|
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: 290.62 E-value: 7.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 569 EVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIA 648
Cdd:cd07086 16 TSRNPANGE-PIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDfLRYYAmiakneLNDWKKLPGPT------GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAK 722
Cdd:cd07086 95 EVQEMID-ICDYA------VGLSRMLYGLTipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 723 PAEQTPIIAYEAVKILHEA----GIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIvplI 798
Cdd:cd07086 168 PSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRV---L 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 799 AETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIID 878
Cdd:cd07086 244 LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLIN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 879 KASIDMLTKHTEKIsRDEDTNLL--SKVPmdTNSYNGYFFPPYIYEI--QKISQLKQEVFGPILHIIRFnkSQLNEVISD 954
Cdd:cd07086 324 QAAVEKYLNAIEIA-KSQGGTVLtgGKRI--DGGEPGNYVEPTIVTGvtDDARIVQEETFAPILYVIKF--DSLEEAIAI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1571382267 955 INNTGYGLTFSLQSRVQSQI-DLISKKIS-VGNVYINRNQIGAAVGTqPFGGRGLSGTGPKAG 1015
Cdd:cd07086 399 NNDVPQGLSSSIFTEDLREAfRWLGPKGSdCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
556-1029 |
8.07e-83 |
|
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: 276.84 E-value: 8.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKsFLDNA--EFTEVVNPAHlENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIY 633
Cdd:cd07088 2 INGE-FVPSSsgETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 634 ILIVEAGKILSDAIAEVREAIDFLRYYAmiaknelnDWKK------LPG-PTGEDNFIFFEGRGVFLCISPWNFPLAIFI 706
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMA--------EWARriegeiIPSdRPNENIFIFKVPIGVVAGILPWNFPFFLIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 707 GQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrM 786
Cdd:cd07088 152 RKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKI--M 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 787 LASRDGpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDP 866
Cdd:cd07088 230 EAAAEN-ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 867 IQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLL---SKVPMDtnsyNGYFFPPYIYEI--QKISQLKQEVFGPILHII 941
Cdd:cd07088 309 FDAATDMGPLVNEAALDKVEEMVER-AVEAGATLLtggKRPEGE----KGYFYEPTVLTNvrQDMEIVQEEIFGPVLPVV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 942 RFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRnqiGAAVGTQPF-GGRGLSGTGpKAGGPNYL 1020
Cdd:cd07088 384 KF--SSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINR---ENFEAMQGFhAGWKKSGLG-GADGKHGL 457
|
....*....
gi 1571382267 1021 QRFSIEKVV 1029
Cdd:cd07088 458 EEYLQTKVV 466
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
555-1032 |
8.85e-82 |
|
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: 274.06 E-value: 8.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 555 IIDGKSFLDNAEFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKW-QNVSAEERAKCLEKAADLLEERMKELIY 633
Cdd:cd07082 5 LINGEWKESSGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWwPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 634 ILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELNDWKKLPGPTGEDNFIFFEGR---GVFLCISPWNFPLAIFIGQVS 710
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRReplGVVLAIGPFNYPLNLTVSKLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 711 AALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMlasr 790
Cdd:cd07082 164 PALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ---- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 791 dGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLS 870
Cdd:cd07082 240 -HPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 871 TDIGPIIDKASIDMLTKHTE-----------KISRDEDTnllskvpmdtnsyngYFFPPYIYEIQKISQL-KQEVFGPIL 938
Cdd:cd07082 319 VDITPLIDPKSADFVEGLIDdavakgatvlnGGGREGGN---------------LIYPTLLDPVTPDMRLaWEEPFGPVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 939 HIIRFNksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRN-QIGaaVGTQPFGGRGLSGTGpKAGGP 1017
Cdd:cd07082 384 PIIRVN--DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcQRG--PDHFPFLGRKDSGIG-TQGIG 458
|
490
....*....|....*
gi 1571382267 1018 NYLQRFSIEKVVSVN 1032
Cdd:cd07082 459 DALRSMTRRKGIVIN 473
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
569-1011 |
1.45e-81 |
|
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: 273.07 E-value: 1.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 569 EVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIA 648
Cdd:cd07145 2 EVRNPANGE-VIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRYYAMIAKNELNDWKKLPGPTGEDNFIFFEGR---GVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAE 725
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFTVRepiGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 726 QTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrmlASRDGPIVPLIA-ETGGL 804
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI----ASKAGGTGKKVAlELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 805 NAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDM 884
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 885 LTKHTEKiSRDEDTNLLSKVPMDtnsyNGYFFPPYIYEIQKISQ--LKQEVFGPILHIIRFNKSqlNEVISDINNTGYGL 962
Cdd:cd07145 317 MENLVND-AVEKGGKILYGGKRD----EGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDD--EEAVEIANSTEYGL 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1571382267 963 TFSLQSRVQSQIDLISKKISVGNVYINrNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:cd07145 390 QASVFTNDINRALKVARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGIG 437
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
568-1029 |
9.17e-81 |
|
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: 270.62 E-value: 9.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 568 TEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI 647
Cdd:cd07149 1 IEVISPYDGE-VIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 AEVREAIDFLRYYAMIAKNelndwkkLPG--------PTGEDNFIFF--EGRGVFLCISPWNFPLAIFIGQVSAALAAGN 717
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKR-------LAGetipfdasPGGEGRIGFTirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 718 AVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMlasrdGPIVPL 797
Cdd:cd07149 153 AVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARK-----AGLKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 798 IAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPII 877
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 878 DKasidmltKHTEKISR------DEDTNLLSKvpmdtNSYNGYFFPPYIYE-IQKISQL-KQEVFGPILHIIRFnkSQLN 949
Cdd:cd07149 308 SE-------AEAERIEEwveeavEGGARLLTG-----GKRDGAILEPTVLTdVPPDMKVvCEEVFAPVVSLNPF--DTLD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 950 EVISDINNTGYGLTFSLQSRvqsQIDLI---SKKISVGNVYIN-----RnqigaaVGTQPFGGRGLSGTGPKagGPnylq 1021
Cdd:cd07149 374 EAIAMANDSPYGLQAGVFTN---DLQKAlkaARELEVGGVMINdsstfR------VDHMPYGGVKESGTGRE--GP---- 438
|
490
....*....|...
gi 1571382267 1022 RFSIE-----KVV 1029
Cdd:cd07149 439 RYAIEemteiKLV 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
570-1011 |
1.77e-77 |
|
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: 261.73 E-value: 1.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIA- 648
Cdd:cd07093 1 NFNPATGE-VLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRYYAMIAKNElnDWKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTP 728
Cdd:cd07093 80 DIPRAAANFRFFADYILQL--DGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 729 IIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMI 808
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN---LKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 809 VDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKAsidmltkH 888
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE-------H 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 889 TEK------ISRDEDTNLLS--KVPMDTNSYNGYFFPPYIYEIQKISQ--LKQEVFGPILHIIRFNKSqlNEVISDINNT 958
Cdd:cd07093 308 LEKvlgyveLARAEGATILTggGRPELPDLEGGYFVEPTVITGLDNDSrvAQEEIFGPVVTVIPFDDE--EEAIELANDT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1571382267 959 GYGLTFSLQSRVQSQIDLISKKISVGNVYIN----RNQigaavgTQPFGGRGLSGTG 1011
Cdd:cd07093 386 PYGLAAYVWTRDLGRAHRVARRLEAGTVWVNcwlvRDL------RTPFGGVKASGIG 436
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
570-1015 |
5.89e-77 |
|
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: 260.18 E-value: 5.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI 647
Cdd:cd07114 1 SINPATGE-PWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 AEVREAIDFLRYYAMIAKnelndwkKLPG---PTGED---NFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLA 721
Cdd:cd07114 80 AQVRYLAEWYRYYAGLAD-------KIEGaviPVDKGdylNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 722 KPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAET 801
Cdd:cd07114 153 KPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN---LAPVTLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 802 GGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKAS 881
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 882 IDMLTKHTEkISRDEDTNLLS--KVPMDTNSYNGYFFPPYIYEIQKISQ--LKQEVFGPILHIIRFNKSQlnEVISDINN 957
Cdd:cd07114 310 LEKVERYVA-RAREEGARVLTggERPSGADLGAGYFFEPTILADVTNDMriAQEEVFGPVLSVIPFDDEE--EAIALAND 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571382267 958 TGYGLTFSLQSRVQSQIDLISKKISVGNVYIN---RNQIGAavgtqPFGGRGLSGTGPKAG 1015
Cdd:cd07114 387 SEYGLAAGIWTRDLARAHRVARAIEAGTVWVNtyrALSPSS-----PFGGFKDSGIGRENG 442
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
568-1029 |
9.61e-74 |
|
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: 251.20 E-value: 9.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 568 TEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI 647
Cdd:cd07094 1 LDVHNPYDGE-VIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 AEVREAIDFLRYYAMIAKNELNDWKKLPGPTGEDN-FIFF--EGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPA 724
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNrLAWTirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 725 EQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrmlaSRDGPIVPLIAETGGL 804
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL-----RANAGGKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 805 NAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDM 884
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 885 LTKHTEKISRDEDTNLLSkvpmdtNSYNGYFFPPYIYEIQKISQL--KQEVFGPILHIIRFNksQLNEVISDINNTGYGL 962
Cdd:cd07094 315 VERWVEEAVEAGARLLCG------GERDGALFKPTVLEDVPRDTKlsTEETFGPVVPIIRYD--DFEEAIRIANSTDYGL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1571382267 963 TFSLQSRVQSQIDLISKKISVGNVYINRNQIgAAVGTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVV 1029
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG-REGVPYAMEEMTEEKTV 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
594-1031 |
9.74e-73 |
|
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: 247.83 E-value: 9.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 594 ALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELNdwKK 673
Cdd:cd07104 5 AYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG--EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 674 LPGPT-GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPI-----IAyeavKILHEAGIPKNV 747
Cdd:cd07104 83 LPSDVpGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVtggllIA----EIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 748 LHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRmLASRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAF 827
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGE-LAGRHLKKVAL--ELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 828 RSGGQRC-SALRVLfIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLLSKvpm 906
Cdd:cd07104 236 LHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVED-AVAAGARLLTG--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 907 dtNSYNGYFFPPYIY-------EIqkisqLKQEVFGPILHIIRFNKSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISK 979
Cdd:cd07104 311 --GTYEGLFYQPTVLsdvtpdmPI-----FREEIFGPVAPVIPFDDDE--EAVELANDTEYGLSAAVFTRDLERAMAFAE 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1571382267 980 KISVGNVYINRNQIGAAVgTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd07104 382 RLETGMVHINDQTVNDEP-HVPFGGVKASGGG-RFGGPASLEEFTEWQWITV 431
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
569-1031 |
2.06e-72 |
|
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: 247.63 E-value: 2.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 569 EVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIA 648
Cdd:cd07150 2 DDLNPADGS-VYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRYYAMIAKNELNdwKKLP-GPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQT 727
Cdd:cd07150 81 ETTFTPELLRAAAGECRRVRG--ETLPsDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 728 PIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAqiinRMLASRDGPIVPLIA-ETGGLNA 806
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRHLKKITlELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 807 MIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLT 886
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 887 KHTEKiSRDEDTNLLSKvpmdtNSYNGYFFPPYIYE--IQKISQLKQEVFGPILHIIRFNKSQlnEVISDINNTGYGLTF 964
Cdd:cd07150 315 RQVED-AVAKGAKLLTG-----GKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPAKDAE--EALELANDTEYGLSA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1571382267 965 SLQSRVQSQIDLISKKISVGNVYINRNQI--GAAVgtqPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd07150 387 AILTNDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSMEEFTELKWITV 451
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
554-1024 |
1.13e-71 |
|
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: 247.89 E-value: 1.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 554 PIIDGKSFLDNAEFTEVVNPAHLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMK-ELI 632
Cdd:cd07123 34 PLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRyELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 633 YILIVEAGK------IlsDAIAEVreaIDFLRYYAMIAKnELNDWKKLPGPTGEDNFIFFEG-RGVFLCISPWNFPlAIf 705
Cdd:cd07123 114 AATMLGQGKnvwqaeI--DAACEL---IDFLRFNVKYAE-ELYAQQPLSSPAGVWNRLEYRPlEGFVYAVSPFNFT-AI- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 706 IGQVSAALA-AGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQT----- 779
Cdd:cd07123 186 GGNLAGAPAlMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTfkslw 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 780 AQIINRMLASRDGPivPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQ 859
Cdd:cd07123 266 KQIGENLDRYRTYP--RIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 860 ELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKISRDEDTNLL-------SKvpmdtnsynGYFFPPYIYEIQ--KISQLK 930
Cdd:cd07123 344 EIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEAEIIaggkcddSV---------GYFVEPTVIETTdpKHKLMT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 931 QEVFGPILHIIRFNKSQLNEVISDINNTG-YGLTFSLQSRVQSQIDLISKKI--SVGNVYINRNQIGAAVGTQPFGGRGL 1007
Cdd:cd07123 415 EEIFGPVLTVYVYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDALrnAAGNFYINDKPTGAVVGQQPFGGARA 494
|
490
....*....|....*..
gi 1571382267 1008 SGTGPKAGGPNYLQRFS 1024
Cdd:cd07123 495 SGTNDKAGSPLNLLRWV 511
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
556-1021 |
1.95e-71 |
|
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: 245.58 E-value: 1.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKSFldnaeftEVVNPAHlENVIGEVSSATSAQALNALEIAHGAF--TKWQNVSAEERAKCLEKAADLLEERMKELIY 633
Cdd:cd07091 16 VSGKTF-------PTINPAT-EEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDRDELAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 634 ILIVEAGKILSDAI-AEVREAIDFLRYYAMIAKnelndwkKLPGPT--GEDNFIFF---EGRGVFLCISPWNFPLAIFIG 707
Cdd:cd07091 88 LESLDNGKPLEESAkGDVALSIKCLRYYAGWAD-------KIQGKTipIDGNFLAYtrrEPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 708 QVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRML 787
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 788 ASRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPI 867
Cdd:cd07091 241 AKSNLKKVTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 868 QLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLL--SKVPMDtnsyNGYFFPPYIY----EIQKISqlKQEVFGPILHII 941
Cdd:cd07091 319 DPDTFQGPQVSKAQFDKILSYIES-GKKEGATLLtgGERHGS----KGYFIQPTVFtdvkDDMKIA--KEEIFGPVVTIL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 942 RFNKSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINR-NQIGAAVgtqPFGGRGLSGTGPKAGG---P 1017
Cdd:cd07091 392 KFKTED--EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELGEeglE 466
|
....
gi 1571382267 1018 NYLQ 1021
Cdd:cd07091 467 EYTQ 470
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
570-1031 |
5.70e-71 |
|
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: 243.20 E-value: 5.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAE 649
Cdd:cd07106 1 VINPATGE-VFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 650 VREAIDFLRYYAMIAknelndwkkLPGPTGEDNFiffEGR--------GVFLCISPWNFPLAIFIGQVSAALAAGNAVLA 721
Cdd:cd07106 80 VGGAVAWLRYTASLD---------LPDEVIEDDD---TRRvelrrkplGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 722 KPAEQTPIIAYEAVKILHEAgIPKNVLHLIPGDGwYLGKTLV--PDnrISGVAFTGSTQTAQiinRMLASRDGPIVPLIA 799
Cdd:cd07106 148 KPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGD-ELGPALTshPD--IRKISFTGSTATGK---KVMASAAKTLKRVTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 800 ETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDK 879
Cdd:cd07106 221 ELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 880 ASIDMLTKHTEKISRDEDTNLLSKVPMDTnsyNGYFFPPYI-YEIQKISQL-KQEVFGPILHIIRFnkSQLNEVISDINN 957
Cdd:cd07106 301 MQYDKVKELVEDAKAKGAKVLAGGEPLDG---PGYFIPPTIvDDPPEGSRIvDEEQFGPVLPVLKY--SDEDEVIARAND 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1571382267 958 TGYGLTFSLQSRVQSQIDLISKKISVGNVYInrNQIGAAVGTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd07106 376 SEYGLGASVWSSDLERAEAVARRLEAGTVWI--NTHGALDPDAPFGGHKQSGIG-VEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
571-1024 |
2.78e-70 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 241.74 E-value: 2.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 571 VNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEV 650
Cdd:cd07099 1 RNPATGE-VLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 651 REAIDFLRYYAMIAKNELNDWKKLPGPT--GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTP 728
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVPTGLLmpNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 729 IIAYEAVKILHEAGIPKNVLHLIPGDGwYLGKTLVpDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMI 808
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALI-DAGVDKVAFTGSVATGRKVMAAAAER---LIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 809 VDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKH 888
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 889 -TEKISR-------DEDTNLlskvpmdtnsyNGYFFPPYIY--EIQKISQLKQEVFGPILHIIRFNksQLNEVISDINNT 958
Cdd:cd07099 315 vDDAVAKgakaltgGARSNG-----------GGPFYEPTVLtdVPHDMDVMREETFGPVLPVMPVA--DEDEAIALANDS 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1571382267 959 GYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGpKAGGPNYLQRFS 1024
Cdd:cd07099 382 RYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFC 446
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
568-1031 |
2.90e-70 |
|
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: 241.49 E-value: 2.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 568 TEVVNPAHLEnVIGEVSSATSAQALNALEIAhGAFTKwqNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI 647
Cdd:cd07146 1 LEVRNPYTGE-VVGTVPAGTEEALREALALA-ASYRS--TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 AEVREAIDFLRYYAMIAKNElnDWKKLP---GPTGEDNFIFF--EGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAK 722
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRD--DGESFScdlTANGKARKIFTlrEPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 723 PAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDgpivpLIAETG 802
Cdd:cd07146 155 PSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKR-----QLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 803 GLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASI 882
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 883 DMLTKHTEKISRDEDTNLLSkvpmdtNSYNGYFFPPYIYE-IQKISQL-KQEVFGPILHIIRFnkSQLNEVISDINNTGY 960
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLG------NQRQGALYAPTVLDhVPPDAELvTEETFGPVAPVIRV--KDLDEAIAISNSTAY 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571382267 961 GLTFSLQSRVQSQIDLISKKISVGNVYINrNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd07146 382 GLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
558-1011 |
3.02e-70 |
|
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: 241.74 E-value: 3.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 558 GKSFldnaeftEVVNPAHlENVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKELIYIL 635
Cdd:cd07112 1 GETF-------ATINPAT-GRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 636 IVEAGKILSDAIA-EVREAIDFLRYYAmiaknELNDwkKLPG---PTGEDN--FIFFEGRGVFLCISPWNFPLAIFIGQV 709
Cdd:cd07112 73 TLDMGKPISDALAvDVPSAANTFRWYA-----EAID--KVYGevaPTGPDAlaLITREPLGVVGAVVPWNFPLLMAAWKI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 710 SAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrMLAS 789
Cdd:cd07112 146 APALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRF--LEYS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 790 RDGPIVPLIAETGGLNAMIV-DSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQ 868
Cdd:cd07112 224 GQSNLKRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 869 LSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLLSKVPMDTNSYNGYFFPPYIYE----IQKISQlkQEVFGPILHIIRFN 944
Cdd:cd07112 304 PATRMGALVSEAHFDKVLGYIES-GKAEGARLVAGGKRVLTETGGFFVEPTVFDgvtpDMRIAR--EEIFGPVLSVITFD 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1571382267 945 KSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYInrNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:cd07112 381 SEE--EAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
570-1011 |
7.80e-70 |
|
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: 240.60 E-value: 7.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAF-TKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIA 648
Cdd:cd07109 1 VFDPSTGE-VFARIARGGAADVDRAVQAARRAFeSGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRYYAMIAKnelndwkKLPG---PTGEDNFIF--FEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKP 723
Cdd:cd07109 80 DVEAAARYFEYYGGAAD-------KLHGetiPLGPGYFVYtvREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 724 AEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGG 803
Cdd:cd07109 153 AEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN---VVPVTLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 804 LNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGdPIQLSTDIGPIIDKASID 883
Cdd:cd07109 230 KSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 884 MLTKHTEkISRDEDTNLLSK--VPMDTNSyNGYFFPPYIYEI----QKISQlkQEVFGPILHIIRFnkSQLNEVISDINN 957
Cdd:cd07109 309 RVEGFVA-RARARGARIVAGgrIAEGAPA-GGYFVAPTLLDDvppdSRLAQ--EEIFGPVLAVMPF--DDEAEAIALANG 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1571382267 958 TGYGLTFSLQSRVQSQIDLISKKISVGNVYInrNQIGAAVGTQ-PFGGRGLSGTG 1011
Cdd:cd07109 383 TDYGLVAGVWTRDGDRALRVARRLRAGQVFV--NNYGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
570-1031 |
6.26e-69 |
|
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: 238.03 E-value: 6.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKIL-SDAIA 648
Cdd:cd07108 1 VINPATGQ-VIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRYYAMIAkNELndwKKLPGPTGEDNFIFF--EGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQ 726
Cdd:cd07108 80 EAAVLADLFRYFGGLA-GEL---KGETLPFGPDVLTYTvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 727 TPIIAYEAVKILHEAgIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNA 806
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR---LIPVSLELGGKSP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 807 MIVDSSALLEQVTKDVLISA-FRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDML 885
Cdd:cd07108 232 MIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 886 TKH-TEKISRDEDTNLL-SKVPMDTNSYNGYFFPPYIYE-IQKISQLKQ-EVFGPILHIIRFnkSQLNEVISDINNTGYG 961
Cdd:cd07108 312 CGYiDLGLSTSGATVLRgGPLPGEGPLADGFFVQPTIFSgVDNEWRLAReEIFGPVLCAIPW--KDEDEVIAMANDSHYG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 962 LTFSLQSRVQSQIDLISKKISVGNVYINRNqiGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd07108 390 LAAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLGREASLEGMLEHFTQKKTVNI 457
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
590-1009 |
1.00e-68 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 236.78 E-value: 1.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 590 QALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVReaidflryyAMIAKNE-- 667
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVA---------AMAGKIDis 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 668 LNDWKKLPGPTGEDN-----FIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAG 742
Cdd:cd07095 72 IKAYHERTGERATPMaqgraVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 743 IPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDV 822
Cdd:cd07095 152 LPPGVLNLVQGGR-ETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILAL--EMGGNNPLVVWDVADIDAAAYLI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 823 LISAFRSGGQRCS-ALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKISRDEDTNLL 901
Cdd:cd07095 229 VQSAFLTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 902 skvPMDTNSYNGYFFPPYIYEIQKISQL-KQEVFGPILHIIRFNksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKK 980
Cdd:cd07095 309 ---AMERLVAGTAFLSPGIIDVTDAADVpDEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDDEALFERFLAR 383
|
410 420
....*....|....*....|....*....
gi 1571382267 981 ISVGNVYINRNQIGAAvGTQPFGGRGLSG 1009
Cdd:cd07095 384 IRAGIVNWNRPTTGAS-STAPFGGVGLSG 411
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
571-1011 |
2.03e-67 |
|
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: 233.77 E-value: 2.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 571 VNPAHLEnVIGEVSSATSAQALNALEIAHGAF--TKWQnVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIA 648
Cdd:cd07120 2 IDPATGE-VIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRYYAMIAKNElndwkklPGPTGE---DNF--IFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKP 723
Cdd:cd07120 80 EISGAISELRYYAGLARTE-------AGRMIEpepGSFslVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 724 AEQTPIIAYEAVKILHEA-GIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETG 802
Cdd:cd07120 153 AGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT---LKRLGLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 803 GLNAMIV----DSSALLEQVTKDVLISAfrsgGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIID 878
Cdd:cd07120 230 GKTPCIVfddaDLDAALPKLERALTIFA----GQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLID 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 879 KASIDMLTKHTEKISRDEDTNLLSKVPMDTNSYNGYFFPPYIYEIQKISQ--LKQEVFGPILHIIRFNKSQlnEVISDIN 956
Cdd:cd07120 306 RANVDRVDRMVERAIAAGAEVVLRGGPVTEGLAKGAFLRPTLLEVDDPDAdiVQEEIFGPVLTLETFDDEA--EAVALAN 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1571382267 957 NTGYGLTFSLQSRVQSQIDLISKKISVGNVYINR-NQIGAAVGTqpfGGRGLSGTG 1011
Cdd:cd07120 384 DTDYGLAASVWTRDLARAMRVARAIRAGTVWINDwNKLFAEAEE---GGYRQSGLG 436
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
570-1020 |
4.63e-66 |
|
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: 229.93 E-value: 4.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHlENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAE 649
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 650 VREAIDFLRYYAMIAKnELNDWKKLPGPTGEDNF---IFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQ 726
Cdd:cd07110 80 VDDVAGCFEYYADLAE-QLDAKAERAVPLPSEDFkarVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 727 TPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMlASRDgpIVPLIAETGGLNA 806
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQA-AAQD--IKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 807 MIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLT 886
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 887 KHTEKIsRDEDTNLL--SKVPMDTNSynGYFFPPYIY-EIQKISQL-KQEVFGPILHIIRFNKSQlnEVISDINNTGYGL 962
Cdd:cd07110 316 SFIARG-KEEGARLLcgGRRPAHLEK--GYFIAPTVFaDVPTDSRIwREEIFGPVLCVRSFATED--EAIALANDSEYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1571382267 963 TFSLQSRVQSQIDLISKKISVGNVYINRNQIgaaVGTQ-PFGGRGLSGTGP---KAGGPNYL 1020
Cdd:cd07110 391 AAAVISRDAERCDRVAEALEAGIVWINCSQP---CFPQaPWGGYKRSGIGRelgEWGLDNYL 449
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
570-1032 |
5.06e-66 |
|
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: 229.63 E-value: 5.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDA-IA 648
Cdd:cd07115 1 TLNPATGE-LIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRYYAMIAKnelndwkKLPG---PTGED--NFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKP 723
Cdd:cd07115 80 DVPRAADTFRYYAGWAD-------KIEGeviPVRGPflNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 724 AEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLAsrdGPIVPLIAETGG 803
Cdd:cd07115 153 AELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA---GNLKRVSLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 804 LNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASID 883
Cdd:cd07115 230 KSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 884 MLTKHTEkISRDEDTNLLSKVPMDTNSynGYFFPPYIYEI----QKISQlkQEVFGPILHIIRFNKSQlnEVISDINNTG 959
Cdd:cd07115 310 RVLDYVD-VGREEGARLLTGGKRPGAR--GFFVEPTIFAAvppeMRIAQ--EEIFGPVVSVMRFRDEE--EALRIANGTE 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1571382267 960 YGLTFSLQSRVQSQIDLISKKISVGNVYInrNQIGAAVGTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSVN 1032
Cdd:cd07115 383 YGLAAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEVKSVWVN 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
579-1024 |
5.21e-66 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 229.49 E-value: 5.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 579 VIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLR 658
Cdd:cd07152 3 VLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 659 YYAMIAKNELNDwkKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPI-----IAye 733
Cdd:cd07152 83 EAAGLPTQPQGE--ILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVsggvvIA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 734 avKILHEAGIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQIINRmLASRDGPIVPLiaETGGLNAMIVDSSA 813
Cdd:cd07152 159 --RLFEEAGLPAGVLHVLPGGA-DAGEALVEDPNVAMISFTGSTAVGRKVGE-AAGRHLKKVSL--ELGGKNALIVLDDA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 814 LLEQVTKDVLISAFRSGGQRC-SALRVLfIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDmltkHTEKI 892
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLD----RVHAI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 893 ---SRDEDTNLLSKvpmdtNSYNGYFFPPYIyeiqkISQLK-------QEVFGPILHIIRFnkSQLNEVISDINNTGYGL 962
Cdd:cd07152 308 vddSVAAGARLEAG-----GTYDGLFYRPTV-----LSGVKpgmpafdEEIFGPVAPVTVF--DSDEEAVALANDTEYGL 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1571382267 963 TFSLQSRVQSQIDLISKKISVGNVYINrNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRFS 1024
Cdd:cd07152 376 SAGIISRDVGRAMALADRLRTGMLHIN-DQTVNDEPHNPFGGMGASGNGSRFGGPANWEEFT 436
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
557-1011 |
1.16e-65 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 229.96 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 557 DGKSFldnaeftEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILI 636
Cdd:PLN02278 38 DGKTF-------PVYNPATGE-VIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 637 VEAGKILSDAIAEVREAIDFLRYYAMIAKNELNDWkkLPGPTGEDN-FIFFEGRGVFLCISPWNFPLAIFIGQVSAALAA 715
Cdd:PLN02278 110 LEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDI--IPSPFPDRRlLVLKQPVGVVGAITPWNFPLAMITRKVGPALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 716 GNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQtaqiINRMLASRDGPIV 795
Cdd:PLN02278 188 GCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTA----VGKKLMAGAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 796 PLIA-ETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRC-SALRVLfIQEDIAEKQIKMICNAAQELKIGDPIQLSTDI 873
Cdd:PLN02278 264 KRVSlELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 874 GPIIDKASIDMLTKHT-EKISRDEDTNLLSKvpmdTNSYNGYFFPPYIyeIQKISQ----LKQEVFGPILHIIRFNKSQl 948
Cdd:PLN02278 343 GPLINEAAVQKVESHVqDAVSKGAKVLLGGK----RHSLGGTFYEPTV--LGDVTEdmliFREEVFGPVAPLTRFKTEE- 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1571382267 949 nEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGtqPFGGRGLSGTG 1011
Cdd:PLN02278 416 -EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
569-1011 |
4.33e-65 |
|
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: 227.39 E-value: 4.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 569 EVVNPAHlENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI- 647
Cdd:cd07138 17 DVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 AEVREAIDFLRYYAMIAKNElnDWKKLPGPTgednFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQT 727
Cdd:cd07138 96 AQVGLGIGHLRAAADALKDF--EFEERRGNS----LVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 728 PIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRmLASRDGPIVPLiaETGGLNAM 807
Cdd:cd07138 170 PLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAE-AAADTVKRVAL--ELGGKSAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 808 IVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKAsidmltk 887
Cdd:cd07138 247 IILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAA------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 888 HTEKISR------DEDTNLLSKVP-----MDTnsynGYFFPPYIY-------EIQkisqlKQEVFGPILHIIRFNksQLN 949
Cdd:cd07138 320 QFDRVQGyiqkgiEEGARLVAGGPgrpegLER----GYFVKPTVFadvtpdmTIA-----REEIFGPVLSIIPYD--DED 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1571382267 950 EVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINrnqiGAAVGTQ-PFGGRGLSGTG 1011
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
556-1035 |
6.16e-65 |
|
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: 227.58 E-value: 6.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKsFLDNAEFT--EVVNPAHlENVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKEL 631
Cdd:cd07119 2 IDGE-WVEAASGKtrDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 632 IYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNElnDWKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSA 711
Cdd:cd07119 80 ARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKE--TGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 712 ALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMlASRD 791
Cdd:cd07119 158 ALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRA-AAGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 792 GPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLST 871
Cdd:cd07119 237 VKKVAL--ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 872 DIGPIIDKASIDMLTKHTEkISRDEDTNLLS--KVPMDTNSYNGYFFPPYIY----EIQKISQlkQEVFGPILHIIRFNK 945
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQ-LGKEEGARLVCggKRPTGDELAKGYFVEPTIFddvdRTMRIVQ--EEIFGPVLTVERFDT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 946 SQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYInrNQIGAAVGTQPFGGRGLSGTGpKAGGPNYLQRFSI 1025
Cdd:cd07119 392 EE--EAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWI--NDYHPYFAEAPWGGYKQSGIG-RELGPTGLEEYQE 466
|
490
....*....|
gi 1571382267 1026 EKVVSVNTTA 1035
Cdd:cd07119 467 TKHININLSP 476
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
552-1032 |
1.98e-64 |
|
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: 226.26 E-value: 1.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 552 VGPIIDGKsFLDNAEFT--EVVNPAHlENVIGEVSSATSAQALNALEIAHGAF-TKW-QNVSAEERAKCLEKAADLLEER 627
Cdd:cd07143 7 TGLFINGE-FVDSVHGGtvKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFeTDWgLKVSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 628 MKELIYILIVEAGK-ILSDAIAEVREAIDFLRYYAMIAKnelndwkKLPGPTGEDN-----FIFFEGRGVFLCISPWNFP 701
Cdd:cd07143 85 LDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWAD-------KIHGQVIETDikkltYTRHEPIGVCGQIIPWNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 702 LAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQ 781
Cdd:cd07143 158 LLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 782 IINRMLASRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQEL 861
Cdd:cd07143 238 KVMEAAAKSNLKKVTL--ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 862 KIGDPIQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLlsKVPMDTNSYNGYFFPPYIY----EIQKIsqLKQEVFGPI 937
Cdd:cd07143 316 KVGDPFAEDTFQGPQVSQIQYERIMSYIES-GKAEGATV--ETGGKRHGNEGYFIEPTIFtdvtEDMKI--VKEEIFGPV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 938 LHIIRFNKSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYIN-RNQIGAAVgtqPFGGRGLSGTGPKAGg 1016
Cdd:cd07143 391 VAVIKFKTEE--EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG- 464
|
490
....*....|....*..
gi 1571382267 1017 pNY-LQRFSIEKVVSVN 1032
Cdd:cd07143 465 -EYaLENYTQIKAVHIN 480
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
570-1032 |
2.13e-64 |
|
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: 225.33 E-value: 2.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHlENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAE 649
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 650 VREAIDFLRYYAMIAkNELNDwKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPI 729
Cdd:cd07107 80 VMVAAALLDYFAGLV-TELKG-ETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 730 IAYEAVKILHEAgIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMIV 809
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG---IKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 810 DSSALLEQVTKDVLISA-FRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKH 888
Cdd:cd07107 234 FPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 889 TEKiSRDEDTNLLS--KVPMDTNSYNGYFFPPYIY-EIQKISQL-KQEVFGPILHIIRFnkSQLNEVISDINNTGYGLTF 964
Cdd:cd07107 314 IDS-AKREGARLVTggGRPEGPALEGGFYVEPTVFaDVTPGMRIaREEIFGPVLSVLRW--RDEAEMVAQANGVEYGLTA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571382267 965 SLQSRVQSQIDLISKKISVGNVYIN---RNQIGAavgtqPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSVN 1032
Cdd:cd07107 391 AIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG-REECLEELLSYTQEKNVNVR 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
570-1033 |
6.35e-64 |
|
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: 224.11 E-value: 6.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAE 649
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 650 VREAIDFLRYYAMIAKNELNDWKKLPGptgeDNFIFF--EGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQT 727
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPG----GSFAYTrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 728 PIIAYEAVKILHEAGIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAM 807
Cdd:cd07090 156 PLTALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG---IKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 808 IVDSSALLEQVTKDVLISAFRSGGQRCS-ALRVlFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLT 886
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQVCSnGTRV-FVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 887 KHTEkISRDEDTNLL---SKVPMDTNSYNGYFFPPYIY----EIQKISqlKQEVFGPILHIIRFNKSQlnEVISDINNTG 959
Cdd:cd07090 311 GYIE-SAKQEGAKVLcggERVVPEDGLENGFYVSPCVLtdctDDMTIV--REEIFGPVMSILPFDTEE--EVIRRANDTT 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1571382267 960 YGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAvgTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSVNT 1033
Cdd:cd07090 386 YGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPV--EVPFGGYKQSGFG-RENGTAALEHYTQLKTVYVEM 456
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
573-1015 |
9.39e-64 |
|
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: 223.37 E-value: 9.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 573 PAHlENVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEV 650
Cdd:cd07118 4 PAH-GVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 651 REAIDFLRYYAMIAKNelndwkkLPGPT----GEDNF--IFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPA 724
Cdd:cd07118 83 EGAADLWRYAASLART-------LHGDSynnlGDDMLglVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 725 EQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrmLASRDGPIVPLIAETGGL 804
Cdd:cd07118 156 EFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAI---AAAAARNLKKVSLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 805 NAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDM 884
Cdd:cd07118 233 NPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 885 LTKHTEkISRDEDTNLLSKVPMDtNSYNGYFFPPYIYEIQK--ISQLKQEVFGPILHIIRFNksQLNEVISDINNTGYGL 962
Cdd:cd07118 313 ITDYVD-AGRAEGATLLLGGERL-ASAAGLFYQPTIFTDVTpdMAIAREEIFGPVLSVLTFD--TVDEAIALANDTVYGL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1571382267 963 TFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAvgTQPFGGRGLSGTGPKAG 1015
Cdd:cd07118 389 SAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
553-1031 |
3.19e-63 |
|
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: 222.70 E-value: 3.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 553 GPIIDGKSFLDNAE-FTEVVNPAhLENVIGEVSSATSAQALNALEIAHGAF-TKWQNVSAEERAKCLEKAADLLEERMKE 630
Cdd:cd07113 1 GHFIDGRPVAGQSEkRLDITNPA-TEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 631 LIYILIVEAGKI--LSDAIaEVREAIDFLRYYA----MIAKNELNdwKKLPGPTGED--NFIFFEGRGVFLCISPWNFPL 702
Cdd:cd07113 80 LAQLETLCSGKSihLSRAF-EVGQSANFLRYFAgwatKINGETLA--PSIPSMQGERytAFTRREPVGVVAGIVPWNFSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 703 AIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQI 782
Cdd:cd07113 157 MIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 783 INRmLASRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELK 862
Cdd:cd07113 236 IGR-QAASDLTRVTL--ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 863 IGDPIQLSTDIGPIIDKASIDMLtKHTEKISRDEDTNLL--SKVPmdtnSYNGYFFPPYIYEIQ--KISQLKQEVFGPIL 938
Cdd:cd07113 313 VGSPMDESVMFGPLANQPHFDKV-CSYLDDARAEGDEIVrgGEAL----AGEGYFVQPTLVLARsaDSRLMREETFGPVV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 939 HIIRFNKSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQ-IGAAVgtqPFGGRGLSGTGpKAGGP 1017
Cdd:cd07113 388 SFVPYEDEE--ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTfLDPAV---PFGGMKQSGIG-REFGS 461
|
490
....*....|....
gi 1571382267 1018 NYLQRFSIEKVVSV 1031
Cdd:cd07113 462 AFIDDYTELKSVMI 475
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
593-1011 |
7.44e-63 |
|
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: 220.02 E-value: 7.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 593 NALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELNDwK 672
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 673 KLPGPTGEdNFIFFEGRGVFLCISPWNFPLAifigQV----SAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVL 748
Cdd:cd07100 82 PIETDAGK-AYVRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 749 H--LIPGDGwylGKTLVPDNRISGVAFTGSTQTAQIInrmlASRDGP-IVPLIAETGGLNAMIVDSSALLEQVTKDVLIS 825
Cdd:cd07100 157 QnlLIDSDQ---VEAIIADPRVRGVTLTGSERAGRAV----AAEAGKnLKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 826 AFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKiSRDED-TNLLSKV 904
Cdd:cd07100 230 RLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEE-AVAAGaTLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 905 PMDTnsyNGYFFPPYIYE-IQKISQL-KQEVFGPILHIIRFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKIS 982
Cdd:cd07100 309 RPDG---PGAFYPPTVLTdVTPGMPAyDEELFGPVAAVIKV--KDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
410 420
....*....|....*....|....*....
gi 1571382267 983 VGNVYInrNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:cd07100 384 AGMVFI--NGMVKSDPRLPFGGVKRSGYG 410
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
555-1021 |
2.57e-62 |
|
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: 220.06 E-value: 2.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 555 IIDGKsFLDNA--EFTEVVNPAHlENVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKE 630
Cdd:cd07142 7 FINGQ-FVDAAsgKTFPTIDPRN-GEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 631 LIYILIVEAGKILSDA-IAEVREAIDFLRYYAmiaknelNDWKKLPGPTGEDNFIFF-----EGRGVFLCISPWNFPLAI 704
Cdd:cd07142 85 LAALETWDNGKPYEQArYAEVPLAARLFRYYA-------GWADKIHGMTLPADGPHHvytlhEPIGVVGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 705 FIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIIN 784
Cdd:cd07142 158 FAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 785 RMLASRDgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIG 864
Cdd:cd07142 238 QLAAKSN--LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 865 DPIQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLLskVPMDTNSYNGYFFPPYIY----EIQKISQlkQEVFGPILHI 940
Cdd:cd07142 316 DPFRKGVEQGPQVDKEQFEKILSYIEH-GKEEGATLI--TGGDRIGSKGYYIQPTIFsdvkDDMKIAR--DEIFGPVQSI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 941 IRFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAvgTQPFGGRGLSGTGPKAGG---P 1017
Cdd:cd07142 391 LKF--KTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDA--SIPFGGYKMSGIGREKGIyalN 466
|
....
gi 1571382267 1018 NYLQ 1021
Cdd:cd07142 467 NYLQ 470
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
566-1032 |
3.15e-62 |
|
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: 219.97 E-value: 3.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 566 EFTEVVNPAHlENVIGEVSSATSAQALNALEIAHGAF-TKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKIL- 643
Cdd:cd07144 23 ETIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAFeSWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYh 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 644 SDAIAEVREAIDFLRYYAMIAKnelndwkKLPGPTGEDNFIFF-----EGRGVFLCISPWNFPLAIFIGQVSAALAAGNA 718
Cdd:cd07144 102 SNALGDLDEIIAVIRYYAGWAD-------KIQGKTIPTSPNKLaytlhEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 719 VLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIVpli 798
Cdd:cd07144 175 VVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVT--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 799 AETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQI-KMICNAAQELKIGDPIQLSTDIGPII 877
Cdd:cd07144 252 LECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVeKFVEHVKQNYKVGSPFDDDTVVGPQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 878 DKASIDMLTKHTEKISRDEDTNLLSKVPMDTNSYNGYFFPPYIY-EIQKISQL-KQEVFGPILHIIRFnkSQLNEVISDI 955
Cdd:cd07144 332 SKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIFtDVPQDMRIvKEEIFGPVVVISKF--KTYEEAIKKA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 956 NNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQ---IGAavgtqPFGGRGLSGTGP---KAGGPNYLQrfsiEKVV 1029
Cdd:cd07144 410 NDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNdsdVGV-----PFGGFKMSGIGRelgEYGLETYTQ----TKAV 480
|
...
gi 1571382267 1030 SVN 1032
Cdd:cd07144 481 HIN 483
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
568-1031 |
9.31e-62 |
|
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: 217.94 E-value: 9.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 568 TEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI 647
Cdd:cd07151 12 IDVLNPYTGE-TLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKAN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 AEVREAIDFLRYYAMIAKNElnDWKKLPGPT-GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQ 726
Cdd:cd07151 91 IEWGAAMAITREAATFPLRM--EGRILPSDVpGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 727 TPI-----IAyeavKILHEAGIPKNVLHLIPGDGWYLGKTLVpDNRISGV-AFTGSTQTAQIINRmLASRDGPIVPLiaE 800
Cdd:cd07151 169 TPItggllLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFV-EHPVPRLiSFTGSTPVGRHIGE-LAGRHLKKVAL--E 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 801 TGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKA 880
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 881 SIDMLTKHTEKiSRDEDTNLLSKVPMDtnsynGYFFPPYIYE--IQKISQLKQEVFGPILHIIRFNKSQlnEVISDINNT 958
Cdd:cd07151 321 QVDGLLDKIEQ-AVEEGATLLVGGEAE-----GNVLEPTVLSdvTNDMEIAREEIFGPVAPIIKADDEE--EALELANDT 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1571382267 959 GYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIG--AAVgtqPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd07151 393 EYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdePHV---PFGGEKNSGLG-RFNGEWALEEFTTDKWISV 463
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
556-1011 |
1.54e-61 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 217.77 E-value: 1.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKsFLD--NAEFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIY 633
Cdd:cd07085 5 INGE-WVEskTTEWLDVYNPATGE-VIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 634 ILIVEAGKILSDAIAEVR---EAIDFLRYYAMIAKNE-LNDWKKlpgptGEDNFIFFEGRGVFLCISPWNFPLAIFIGQV 709
Cdd:cd07085 83 LITLEHGKTLADARGDVLrglEVVEFACSIPHLLKGEyLENVAR-----GIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 710 SAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGdgwylGKTLV------PDnrISGVAFTGSTQTAQII 783
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-----GKEAVnalldhPD--IKAVSFVGSTPVGEYI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 784 NRmLASRDGPIVplIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKI 863
Cdd:cd07085 231 YE-RAAANGKRV--QALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 864 GDPIQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLL-----SKVPmdtnSY-NGYFFPPYIYEIQKI--SQLKQEVFG 935
Cdd:cd07085 308 GAGDDPGADMGPVISPAAKERIEGLIES-GVEEGAKLVldgrgVKVP----GYeNGNFVGPTILDNVTPdmKIYKEEIFG 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1571382267 936 PILHIIRFNksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINrnqIGAAV--GTQPFGGRGLSGTG 1011
Cdd:cd07085 383 PVLSIVRVD--TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVplAFFSFGGWKGSFFG 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
570-1029 |
3.76e-61 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 216.34 E-value: 3.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHlENVIGEVSSATSAQALNALEIAHGAF--TKWqNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI 647
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAAARRAFdtGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 A-EVREAIDFLRYYAMIAKNE-----LNDWKKLPGPTGedNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLA 721
Cdd:cd07089 79 AmQVDGPIGHLRYFADLADSFpwefdLPVPALRGGPGR--RVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 722 KPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAqiinRMLASRDGPIV-PLIAE 800
Cdd:cd07089 157 KPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVG----RRIMAQAAATLkRVLLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 801 TGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKA 880
Cdd:cd07089 233 LGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 881 SIDMLTKHTEkISRDEDTNLLSKVPMDTNSYNGYFFPPYIY----EIQKISQlkQEVFGPILHIIRFNksQLNEVISDIN 956
Cdd:cd07089 313 QRDRVEGYIA-RGRDEGARLVTGGGRPAGLDKGFYVEPTLFadvdNDMRIAQ--EEIFGPVLVVIPYD--DDDEAVRIAN 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1571382267 957 NTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRnqiGAAVGTQ-PFGGRGLSGTGpKAGGPNYLQRFSIEKVV 1029
Cdd:cd07089 388 DSDYGLSGGVWSADVDRAYRVARRIRTGSVGING---GGGYGPDaPFGGYKQSGLG-RENGIEGLEEFLETKSI 457
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
579-1015 |
6.72e-61 |
|
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: 215.25 E-value: 6.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 579 VIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLR 658
Cdd:cd07101 8 PLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 659 YYAMIAKNELNDWKKLPG-PTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKI 737
Cdd:cd07101 88 YYARRAERLLKPRRRRGAiPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 738 LHEAGIPKNVLHLIPGDGWYLGKTLVpdNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMIVDSSALLEQ 817
Cdd:cd07101 168 LIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRR---LIGCSLELGGKNPMIVLEDADLDK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 818 VTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKiSRDED 897
Cdd:cd07101 243 AAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD-AVAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 898 TNLL---SKVPmDTNSyngYFFPPYIYE--IQKISQLKQEVFGPILHIIRFnkSQLNEVISDINNTGYGLTFSLQSRVQS 972
Cdd:cd07101 322 ATVLaggRARP-DLGP---YFYEPTVLTgvTEDMELFAEETFGPVVSIYRV--ADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1571382267 973 QIDLISKKISVGNVYINRNQIGA--AVGTqPFGGRGLSGTGPKAG 1015
Cdd:cd07101 396 RGRRIAARLRAGTVNVNEGYAAAwaSIDA-PMGGMKDSGLGRRHG 439
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
553-1017 |
2.09e-59 |
|
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: 211.87 E-value: 2.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 553 GPIIDGKsFL--DNAEFTEVVNPAHLENvIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKE 630
Cdd:cd07111 23 GHFINGK-WVkpENRKSFPTINPATGEV-LASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 631 LIYILIVEAGKilsdAIAEVRE-----AIDFLRYYAMIAK---NELNDWKKLpgptgednfiffegrGVFLCISPWNFPL 702
Cdd:cd07111 101 FAVLESLDNGK----PIRESRDcdiplVARHFYHHAGWAQlldTELAGWKPV---------------GVVGQIVPWNFPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 703 AIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQI 782
Cdd:cd07111 162 LMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 783 INRMLAsrdGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELK 862
Cdd:cd07111 241 LRRATA---GTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 863 IGDPIQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLLSkvPMDTNSYNGYFFPPYIYE-IQKISQLKQ-EVFGPILHI 940
Cdd:cd07111 318 VGDPLDKAIDMGAIVDPAQLKRIRELVEE-GRAEGADVFQ--PGADLPSKGPFYPPTLFTnVPPASRIAQeEIFGPVLVV 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1571382267 941 IRFNKSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYIN-RNQIGAAVgtqPFGGRGLSGTGpKAGGP 1017
Cdd:cd07111 395 LTFRTAK--EAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGK 466
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
556-1009 |
2.83e-59 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 211.74 E-value: 2.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKSFLDNAEFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYIL 635
Cdd:PRK09457 5 INGDWIAGQGEAFESRNPVSGE-VLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 636 IVEAGKILSDAIAEVReaidflryyAMIAK--------NELNDWKKLPGPTGEdNFIFFEGRGVFLCISPWNFPLAIFIG 707
Cdd:PRK09457 84 ARETGKPLWEAATEVT---------AMINKiaisiqayHERTGEKRSEMADGA-AVLRHRPHGVVAVFGPYNFPGHLPNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 708 QVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGdGWYLGKTLVPDNRISGVAFTGSTQTAQIINRML 787
Cdd:PRK09457 154 HIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 788 ASRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDI-AEKQIKMICNAAQELKIGDP 866
Cdd:PRK09457 233 AGQPEKILAL--EMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 867 IQLSTD-IGPIIDKASIDMLTKHTEKI------------SRDEDTNLLSkvpmdtnsyngyffpPYIYEIQKISQL-KQE 932
Cdd:PRK09457 311 DAEPQPfMGAVISEQAAQGLVAAQAQLlalggksllemtQLQAGTGLLT---------------PGIIDVTGVAELpDEE 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1571382267 933 VFGPILHIIRFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRnQIGAAVGTQPFGGRGLSG 1009
Cdd:PRK09457 376 YFGPLLQVVRY--DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNK-PLTGASSAAPFGGVGASG 449
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
569-1022 |
9.20e-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: 209.76 E-value: 9.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 569 EVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIA 648
Cdd:cd07130 15 TSISPANGE-PIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRY--------YAMIAKNE------LNDWKKLpgptgednfiffegrGVFLCISPWNFPLAIFIGQVSAALA 714
Cdd:cd07130 94 EVQEMIDICDFavglsrqlYGLTIPSErpghrmMEQWNPL---------------GVVGVITAFNFPVAVWGWNAAIALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 715 AGNAVLAKPAEQTPIIAYEAVKI----LHEAGIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASR 790
Cdd:cd07130 159 CGNVVVWKPSPTTPLTAIAVTKIvarvLEKNGLPGAIASLVCGGA-DVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 791 DGPIvplIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLS 870
Cdd:cd07130 238 FGRS---LLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 871 TDIGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPMDTnsyNGYFFPPYIYEIQKISQL-KQEVFGPILHIIRFNksQLN 949
Cdd:cd07130 315 TLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDG---PGNYVEPTIVEGLSDAPIvKEETFAPILYVLKFD--TLE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 950 EVISDINNTGYGLTFSLQSRVQSQI-DLISKKIS---VGNVYINRN--QIGAAvgtqpFGGRGLSGTGPKAGG---PNYL 1020
Cdd:cd07130 390 EAIAWNNEVPQGLSSSIFTTDLRNAfRWLGPKGSdcgIVNVNIGTSgaEIGGA-----FGGEKETGGGRESGSdawKQYM 464
|
..
gi 1571382267 1021 QR 1022
Cdd:cd07130 465 RR 466
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
556-1031 |
1.18e-58 |
|
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: 210.04 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKsFLD--NAEFTEVVNPAHlENVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKEL 631
Cdd:cd07140 10 INGE-FVDaeGGKTYNTINPTD-GSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 632 IYILIVEAGKILSDAI-AEVREAIDFLRYYAmiaknelnDW-KKLPGPTGEDN---------FIFFEGRGVFLCISPWNF 700
Cdd:cd07140 88 ATIESLDSGAVYTLALkTHVGMSIQTFRYFA--------GWcDKIQGKTIPINqarpnrnltLTKREPIGVCGIVIPWNY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 701 PLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTA 780
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 781 QIINRMLASRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQE 860
Cdd:cd07140 240 KHIMKSCAVSNLKKVSL--ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 861 LKIGDPIQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLL---SKVPMDtnsynGYFFPPYIYE--IQKISQLKQEVFG 935
Cdd:cd07140 318 MKIGDPLDRSTDHGPQNHKAHLDKLVEYCER-GVKEGATLVyggKQVDRP-----GFFFEPTVFTdvEDHMFIAKEESFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 936 PILHIIRFNKSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINR-NQIGAAvgtQPFGGRGLSGTGpKA 1014
Cdd:cd07140 392 PIMIISKFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTyNKTDVA---APFGGFKQSGFG-KD 467
|
490
....*....|....*..
gi 1571382267 1015 GGPNYLQRFSIEKVVSV 1031
Cdd:cd07140 468 LGEEALNEYLKTKTVTI 484
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
540-1021 |
3.27e-57 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 205.53 E-value: 3.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 540 NDVREFSEKKWQVGPIIDGksflDNAEFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEK 619
Cdd:PRK11241 4 NDSTLFRQQALINGEWLDA----NNGEVIDVTNPANGD-KLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 620 AADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELNDwkKLPGPTGEDNFIFFEGR-GVFLCISPW 698
Cdd:PRK11241 79 WFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGD--TIPGHQADKRLIVIKQPiGVTAAITPW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 699 NFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQ 778
Cdd:PRK11241 157 NFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 779 taqiINRML---ASRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMIC 855
Cdd:PRK11241 237 ----IGRQLmeqCAKDIKKVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 856 NAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPmdtNSYNGYFFPPYIY-EIQKISQL-KQEV 933
Cdd:PRK11241 311 QAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKA---HELGGNFFQPTILvDVPANAKVaKEET 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 934 FGPILHIIRFNKSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGtqPFGG---RGLSGT 1010
Cdd:PRK11241 388 FGPLAPLFRFKDEA--DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGRE 463
|
490
....*....|.
gi 1571382267 1011 GPKAGGPNYLQ 1021
Cdd:PRK11241 464 GSKYGIEDYLE 474
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
556-1025 |
3.58e-57 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 206.21 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKSFldnaeftEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFT--KWQNVSAEERAKCLEKAADLLEERMKELIY 633
Cdd:PLN02766 33 ASGKTF-------ETRDPRTGE-VIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 634 ILIVEAGKILS-DAIAEVREAIDFLRYYAMIAKNELNDWKKLPGPTgeDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAA 712
Cdd:PLN02766 105 LDTIDAGKLFAlGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQL--QGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 713 LAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrMLASRDG 792
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKI--MQAAATS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 793 PIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTD 872
Cdd:PLN02766 261 NLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 873 IGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPMdtnSYNGYFFPPYIY----EIQKISQlkQEVFGPILHIIRFNksQL 948
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTGGKPC---GDKGYYIEPTIFtdvtEDMKIAQ--DEIFGPVMSLMKFK--TV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 949 NEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINrnqIGAAVGTQ-PFGGRGLSGTGPKAGGP---NYLQRFS 1024
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFDPDcPFGGYKMSGFGRDQGMDaldKYLQVKS 490
|
.
gi 1571382267 1025 I 1025
Cdd:PLN02766 491 V 491
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
568-1011 |
5.05e-57 |
|
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: 204.02 E-value: 5.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 568 TEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI 647
Cdd:cd07147 1 LEVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 AEVREAIDFLRYYAMIAKNelNDWKKLPGPTGEDNfiffEGR---------GVFLCISPWNFPLAIFIGQVSAALAAGNA 718
Cdd:cd07147 80 GEVARAIDTFRIAAEEATR--IYGEVLPLDISARG----EGRqglvrrfpiGPVSAITPFNFPLNLVAHKVAPAIAAGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 719 VLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIP--GDGwylGKTLVPDNRISGVAFTGStqtaQIINRMLASRDGPiVP 796
Cdd:cd07147 154 FVLKPASRTPLSALILGEVLAETGLPKGAFSVLPcsRDD---ADLLVTDERIKLLSFTGS----PAVGWDLKARAGK-KK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 797 LIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPI 876
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 877 IDKASIDMLTKHTEKiSRDEDTNLLSKvpmdtNSYNGYFFPPYIYEIQKISQL--KQEVFGPILHIIRFNksQLNEVISD 954
Cdd:cd07147 306 ISESEAERVEGWVNE-AVDAGAKLLTG-----GKRDGALLEPTILEDVPPDMEvnCEEVFGPVVTVEPYD--DFDEALAA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1571382267 955 INNTGYGltfsLQSRVQSQ-IDLI---SKKISVGNVYIN-----RnqigaaVGTQPFGGRGLSGTG 1011
Cdd:cd07147 378 VNDSKFG----LQAGVFTRdLEKAlraWDELEVGGVVINdvptfR------VDHMPYGGVKDSGIG 433
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
571-1011 |
1.42e-56 |
|
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: 202.86 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 571 VNPAhLENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEV 650
Cdd:cd07102 1 ISPI-DGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 651 REAIDFLRYYAMIAKNELNDwKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPII 730
Cdd:cd07102 80 RGMLERARYMISIAEEALAD-IRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 731 AYEAVKILHEAGIPKNVL-HLIPGDGwyLGKTLVPDNRISGVAFTGSTQTAQIINRMLAsrdGPIVPLIAETGGLNAMIV 809
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFqVLHLSHE--TSAALIADPRIDHVSFTGSVAGGRAIQRAAA---GRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 810 DSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKHT 889
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 890 EKISRDEDTNLLSKVPMDTNSYNGYFFPPYIY-------EIqkisqLKQEVFGPILHIIRFnKSQlNEVISDINNTGYGL 962
Cdd:cd07102 314 ADAIAKGARALIDGALFPEDKAGGAYLAPTVLtnvdhsmRV-----MREETFGPVVGIMKV-KSD-AEAIALMNDSEYGL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1571382267 963 TFSLQSRVQSQIDLISKKISVGNVYINR-NQIGAAVgtqPFGGRGLSGTG 1011
Cdd:cd07102 387 TASVWTKDIARAEALGEQLETGTVFMNRcDYLDPAL---AWTGVKDSGRG 433
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
566-1011 |
3.01e-55 |
|
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: 199.88 E-value: 3.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 566 EFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSD 645
Cdd:cd07559 16 EYFDNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 646 AI-AEVREAIDFLRYYAMIAKNELNDWKKLPGPTgeDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPA 724
Cdd:cd07559 95 TLaADIPLAIDHFRYFAGVIRAQEGSLSEIDEDT--LSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 725 EQTPIIAYEAVKILHEAgIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrMLASRDGpIVPLIAETGGL 804
Cdd:cd07559 173 SQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLI--MQYAAEN-LIPVTLELGGK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 805 NAMIVDSSALLEQVTKD------VLISAFRSgGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIID 878
Cdd:cd07559 249 SPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 879 KASIDMLTKHTEkISRDEDTNLLS---KVPMDTNSYNGYFFPPYIYEIQ---KISQlkQEVFGPILHIIRFNKSQlnEVI 952
Cdd:cd07559 328 KDQLEKILSYVD-IGKEEGAEVLTggeRLTLGGLDKGYFYEPTLIKGGNndmRIFQ--EEIFGPVLAVITFKDEE--EAI 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 953 SDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYIN-RNQIGAAVgtqPFGGRGLSGTG 1011
Cdd:cd07559 403 AIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
556-1015 |
4.22e-55 |
|
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: 199.50 E-value: 4.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKSFldnaeftEVVNPAHlENVIGEVSSATSAQALNALEIAHGAF---TKWQNVSAEERAKCLEKAADLLEERMKELI 632
Cdd:cd07141 19 VSGKTF-------PTINPAT-GEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 633 YILIVEAGKILSDA-IAEVREAIDFLRYYAMIAKnelndwkKLPG---PTGEDNFIFFEGRGVFLC--ISPWNFPLAIFI 706
Cdd:cd07141 91 SLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWAD-------KIHGktiPMDGDFFTYTRHEPVGVCgqIIPWNFPLLMAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 707 GQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrM 786
Cdd:cd07141 164 WKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI--Q 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 787 LASRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDP 866
Cdd:cd07141 242 QAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 867 IQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLLS--KVPMDtnsyNGYFFPPYIY----EIQKISqlKQEVFGPILHI 940
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIES-GKKEGAKLECggKRHGD----KGYFIQPTVFsdvtDDMRIA--KEEIFGPVQQI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1571382267 941 IRFNKsqLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINrnqIGAAVGTQ-PFGGRGLSGTGPKAG 1015
Cdd:cd07141 395 FKFKT--IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
570-1011 |
3.62e-54 |
|
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: 196.01 E-value: 3.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIA- 648
Cdd:cd07092 1 VVDPATGE-EIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 649 EVREAIDFLRYYAMIAKNelndwkkLPGPT------GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAK 722
Cdd:cd07092 80 ELPGAVDNFRFFAGAART-------LEGPAageylpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 723 PAEQTPIIAYEAVKILHEaGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMlASRDgpIVPLIAETG 802
Cdd:cd07092 153 PSETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADT--LKRVHLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 803 GLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASI 882
Cdd:cd07092 229 GKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 883 DMLTKHTEKISRDEDTNLLSKVPMDtnsyNGYFFPPYIyeiqkISQLKQ-------EVFGPILHIIRFNKSQlnEVISDI 955
Cdd:cd07092 309 ERVAGFVERAPAHARVLTGGRRAEG----PGYFYEPTV-----VAGVAQddeivqeEIFGPVVTVQPFDDED--EAIELA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1571382267 956 NNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAvgTQPFGGRGLSGTG 1011
Cdd:cd07092 378 NDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAA--EMPHGGFKQSGYG 431
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
563-1025 |
1.74e-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: 194.33 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 563 DNAEFTEVVNPaHLENVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKELIYILIVEAG 640
Cdd:cd07139 11 SGSETIDVVSP-ATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 641 KILS-DAIAEVREAIDFLRYYAMIAKNELNDwKKLPGPTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAV 719
Cdd:cd07139 90 MPISwSRRAQGPGPAALLRYYAALARDFPFE-ERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 720 LAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGD---GWYLgkTLVPDnrISGVAFTGSTQTAQIINRMLASRdgpIVP 796
Cdd:cd07139 169 VLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADrevGEYL--VRHPG--VDKVSFTGSTAAGRRIAAVCGER---LAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 797 LIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSAL-RVLF---IQEDIAEkqikMICNAAQELKIGDPIQLSTD 872
Cdd:cd07139 242 VTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRILVprsRYDEVVE----ALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 873 IGPIIDKASIDMLTKHTEKiSRDEDTNLLS--KVPMDTNsyNGYFFPPYIYE----IQKISQlkQEVFGPILHIIRFnkS 946
Cdd:cd07139 318 IGPLASARQRERVEGYIAK-GRAEGARLVTggGRPAGLD--RGWFVEPTLFAdvdnDMRIAQ--EEIFGPVLSVIPY--D 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 947 QLNEVISDINNTGYGLTFSLQSR-VQSQIDlISKKISVGNVYINrnqiGAAVG-TQPFGGRGLSGTGpKAGGP----NYL 1020
Cdd:cd07139 391 DEDDAVRIANDSDYGLSGSVWTAdVERGLA-VARRIRTGTVGVN----GFRLDfGAPFGGFKQSGIG-REGGPegldAYL 464
|
....*
gi 1571382267 1021 QRFSI 1025
Cdd:cd07139 465 ETKSI 469
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
568-1011 |
1.97e-53 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 195.87 E-value: 1.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 568 TEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAI 647
Cdd:PRK09407 34 REVTAPFTGE-PLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 648 AEVREAIDFLRYYAMIAKNELNDWKK---LPGPTgeDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPA 724
Cdd:PRK09407 113 EEVLDVALTARYYARRAPKLLAPRRRagaLPVLT--KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 725 EQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVpdNRISGVAFTGSTQTAQIINRMLASRdgpivpLI---AET 801
Cdd:PRK09407 191 SQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRR------LIgfsLEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 802 GGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKAS 881
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 882 IDMLTKHTEKiSRDEDTNLLSkvpmdtnsynG---------YFFPPYIYE--IQKISQLKQEVFGPILHIIRFnkSQLNE 950
Cdd:PRK09407 343 LETVSAHVDD-AVAKGATVLA----------GgkarpdlgpLFYEPTVLTgvTPDMELAREETFGPVVSVYPV--ADVDE 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1571382267 951 VISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINrNQIGAAVGT--QPFGGRGLSGTG 1011
Cdd:PRK09407 410 AVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVN-EGYAAAWGSvdAPMGGMKDSGLG 471
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
63-175 |
4.06e-53 |
|
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: 180.78 E-value: 4.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 63 IDSFIQQYSLSNDEGVALMCLAESLLRIPDDYTIDELIKDKIANQEWNKHLGRSSSLFVNASTWSLIIGSSILRNNEEDS 142
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|...
gi 1571382267 143 kFYHIISRLLKNLGEPIIRKAVKQAISILGKHF 175
Cdd:pfam14850 81 -LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
556-1011 |
1.07e-52 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 192.79 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKsFLDNA--EFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIY 633
Cdd:PRK13252 11 IDGA-YVEATsgETFEVINPATGE-VLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 634 ILIVEAGKILSDAI-AEVREAIDFLRYYAMIAKnelndwkKLPG---PTGEDNFIFF--EGRGVFLCISPWNFPLAIFIG 707
Cdd:PRK13252 89 LETLDTGKPIQETSvVDIVTGADVLEYYAGLAP-------ALEGeqiPLRGGSFVYTrrEPLGVCAGIGAWNYPIQIACW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 708 QVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQiinRML 787
Cdd:PRK13252 162 KSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGK---KVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 788 ASRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCS-ALRVlFIQEDIAEKQIKMICNAAQELKIGDP 866
Cdd:PRK13252 238 AAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRV-FVQKSIKAAFEARLLERVERIRIGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 867 IQLSTDIGPIIDKASIDMLTKHTEKiSRDEDTNLLS--KVPMDTNSYNGYFFPPYIYE--IQKISQLKQEVFGPILHIIR 942
Cdd:PRK13252 317 MDPATNFGPLVSFAHRDKVLGYIEK-GKAEGARLLCggERLTEGGFANGAFVAPTVFTdcTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1571382267 943 FNKSQlnEVISDINNTGYGL-----TFSLqSRVQSQIDliskKISVGNVYInrNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:PRK13252 396 FDDED--EVIARANDTEYGLaagvfTADL-SRAHRVIH----QLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
568-1011 |
8.56e-52 |
|
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: 189.17 E-value: 8.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 568 TEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAF---TKWqnVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILS 644
Cdd:cd07148 1 LEVVNPFDLK-PIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 645 DAIAEVREAIDFLRyyamIAKNELNDW--KKLP---GPTGEDN--FIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGN 717
Cdd:cd07148 78 DAKVEVTRAIDGVE----LAADELGQLggREIPmglTPASAGRiaFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 718 AVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQtaqiINRMLASRDGPIVPL 797
Cdd:cd07148 154 PVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCEN-AVAEKLVTDPRVAFFSFIGSAR----VGWMLRSKLAPGTRC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 798 IAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPII 877
Cdd:cd07148 229 ALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 878 DKASIDMLTKHTEKI-----------SRDEDTNLLSKVPMDtnsyngyffPPyiyEIQKISQlkQEVFGPILHIirFNKS 946
Cdd:cd07148 309 RPREVDRVEEWVNEAvaagarllcggKRLSDTTYAPTVLLD---------PP---RDAKVST--QEIFGPVVCV--YSYD 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1571382267 947 QLNEVISDINNtgygLTFSLQSRVQSQ-IDL---ISKKISVGNVYINrNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:cd07148 373 DLDEAIAQANS----LPVAFQAAVFTKdLDValkAVRRLDATAVMVN-DHTAFRVDWMPFAGRRQSGYG 436
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
570-1030 |
2.44e-51 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 189.17 E-value: 2.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 570 VVNPaHLENVIGEVSSATSAQALNALEIAHGAFTK-----WQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILS 644
Cdd:PLN02467 27 VVNP-ATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 645 DAIAEVREAIDFLRYYAMIAKnELNDWKKLPGPTGEDNF---IFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLA 721
Cdd:PLN02467 106 EAAWDMDDVAGCFEYYADLAE-ALDAKQKAPVSLPMETFkgyVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 722 KPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrMLASrdGPIV-PLIAE 800
Cdd:PLN02467 185 KPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI--MTAA--AQMVkPVSLE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 801 TGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKA 880
Cdd:PLN02467 261 LGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 881 SIDMLTKHTEkISRDEDTNLLS--KVPMDTNSynGYFFPPYI-YEIQKISQL-KQEVFGPILHIIRFnkSQLNEVISDIN 956
Cdd:PLN02467 341 QYEKVLKFIS-TAKSEGATILCggKRPEHLKK--GFFIEPTIiTDVTTSMQIwREEVFGPVLCVKTF--STEDEAIELAN 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1571382267 957 NTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQigAAVGTQPFGGRGLSGTGPKAGG---PNYLQRFSIEKVVS 1030
Cdd:PLN02467 416 DSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQ--PCFCQAPWGGIKRSGFGRELGEwglENYLSVKQVTKYIS 490
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
555-1021 |
8.11e-51 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 188.48 E-value: 8.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 555 IIDGKsFLDNA--EFTEVVNPaHLENVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKE 630
Cdd:PLN02466 61 LINGQ-FVDAAsgKTFPTLDP-RTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 631 LIYILIVEAGKILSDAI-AEVREAIDFLRYYAMIAKnelndwkKLPGPTGEDN-----FIFFEGRGVFLCISPWNFPLAI 704
Cdd:PLN02466 139 LAALETWDNGKPYEQSAkAELPMFARLFRYYAGWAD-------KIHGLTVPADgphhvQTLHEPIGVAGQIIPWNFPLLM 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 705 FIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIIN 784
Cdd:PLN02466 212 FAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 785 RmLASRDGpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIG 864
Cdd:PLN02466 292 E-LAAKSN-LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 865 DPIQLSTDIGPIIDKasiDMLTKHTEKISRDEDTNLLSKVPMDTNSYNGYFFPPYIYEIQKISQL--KQEVFGPILHIIR 942
Cdd:PLN02466 370 DPFKKGVEQGPQIDS---EQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLiaQDEIFGPVQSILK 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 943 FnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYIN-RNQIGAAVgtqPFGGRGLSGTGPKAGG---PN 1018
Cdd:PLN02466 447 F--KDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKGIyslNN 521
|
...
gi 1571382267 1019 YLQ 1021
Cdd:PLN02466 522 YLQ 524
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
590-1031 |
9.58e-51 |
|
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: 185.47 E-value: 9.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 590 QALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGkiLSDAIAE--VREAIDFLRYYAMIAKNe 667
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG--ATAAWAGfnVDLAAGMLREAASLITQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 668 lndwkkLPG---PTGEDN---FIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEA 741
Cdd:cd07105 78 ------IIGgsiPSDKPGtlaMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 742 GIPKNVLHLI---PGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRmLASRDgpIVPLIAETGGLNAMIVDSSALLEQV 818
Cdd:cd07105 152 GLPKGVLNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAE-TAAKH--LKPVLLELGGKAPAIVLEDADLDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 819 TKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDpiqlsTDIGPIIDKASIDMLtKHTEKISRDEDT 898
Cdd:cd07105 229 ANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRV-KELVDDALSKGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 899 NLLSKVPMDTNSyNGYFFPPYIYE-IQKISQL-KQEVFGPILHIIRFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDL 976
Cdd:cd07105 303 KLVVGGLADESP-SGTSMPPTILDnVTPDMDIySEESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTRDLARALA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1571382267 977 ISKKISVGNVYINrnqiGAAVG---TQPFGGRGLSGTGpKAGGPNYLQRFSIEKVVSV 1031
Cdd:cd07105 380 VAKRIESGAVHIN----GMTVHdepTLPHGGVKSSGYG-RFNGKWGIDEFTETKWITI 432
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
564-1011 |
7.35e-49 |
|
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: 181.11 E-value: 7.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 564 NAEFTEVVNPAHLEN-------VIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILI 636
Cdd:cd07116 6 GGEWVAPVKGEYFDNitpvtgkVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 637 VEAGKILSDAI-AEVREAIDFLRYYAMIAKNELNDWKKLPGPTgeDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAA 715
Cdd:cd07116 86 WDNGKPVRETLaADIPLAIDHFRYFAGCIRAQEGSISEIDENT--VAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 716 GNAVLAKPAEQTPIIAYEAVKILHEAgIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMlASRDgpIV 795
Cdd:cd07116 164 GNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY-ASEN--II 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 796 PLIAETGGLNAMIVDSS------ALLEQVTKDVLISAFRSgGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQL 869
Cdd:cd07116 240 PVTLELGGKSPNIFFADvmdaddAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 870 STDIGPiidKASIDMLTKHTE--KISRDEDTNLLS---KVPMDTNSYNGYFFPPYIYEIQKISQLKQEVFGPILHIIRFN 944
Cdd:cd07116 319 ETMIGA---QASLEQLEKILSyiDIGKEEGAEVLTggeRNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1571382267 945 KSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAvgTQPFGGRGLSGTG 1011
Cdd:cd07116 396 DEE--EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPA--HAAFGGYKQSGIG 458
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
564-1011 |
1.17e-48 |
|
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: 180.73 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 564 NAEFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGK-I 642
Cdd:cd07117 14 SGETIDSYNPANGE-TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKpI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 643 LSDAIAEVREAIDFLRYYAMIAKNELNDWKKLPGPTGedNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAK 722
Cdd:cd07117 93 RETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTL--SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 723 PAEQTPIIAYEAVKILHEAgIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETG 802
Cdd:cd07117 171 PSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK---LIPATLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 803 GLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASI 882
Cdd:cd07117 247 GKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 883 DMLTKHTEkISRDEDTNLLS--KVPMDTNSYNGYFFPPYIYEI----QKISQlkQEVFGPILHIIRFNKSQlnEVISDIN 956
Cdd:cd07117 327 DKILSYVD-IAKEEGAKILTggHRLTENGLDKGFFIEPTLIVNvtndMRVAQ--EEIFGPVATVIKFKTED--EVIDMAN 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1571382267 957 NTGYGLTFSLQSRVQSQIDLISKKISVGNVYINR-NQIGAAVgtqPFGGRGLSGTG 1011
Cdd:cd07117 402 DSEYGLGGGVFTKDINRALRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
563-1011 |
3.11e-48 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 179.71 E-value: 3.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 563 DNAEFtEVVNPAHlENVIGEVSSATSAQALNALEIAHGAFTK--WQNVSAEERAKCLEKAADLLEERMKELIYILIVEAG 640
Cdd:PRK09847 33 ENETF-ETVDPVT-QAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 641 KILSDAIAE-VREAIDFLRYYAmiaknELNDwkKLPG---PTGEDNF--IFFEGRGVFLCISPWNFPLAIFIGQVSAALA 714
Cdd:PRK09847 111 KPIRHSLRDdIPGAARAIRWYA-----EAID--KVYGevaTTSSHELamIVREPVGVIAAIVPWNFPLLLTCWKLGPALA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 715 AGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIInrMLASRDGPI 794
Cdd:PRK09847 184 AGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQL--LKDAGDSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 795 VPLIAETGGLNAMIVDSSAL-LEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDI 873
Cdd:PRK09847 262 KRVWLEAGGKSANIVFADCPdLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 874 GPIIDKASIDMLTKHTEKISRDEDTNLLSKvpmdTNSYNGYFFPPYIYEIQKISQL-KQEVFGPILHIIRFNKSQlnEVI 952
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKGQLLLDGR----NAGLAAAIGPTIFVDVDPNASLsREEIFGPVLVVTRFTSEE--QAL 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1571382267 953 SDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAvgTQPFGGRGLSGTG 1011
Cdd:PRK09847 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
556-1011 |
9.25e-47 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 175.10 E-value: 9.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 556 IDGKSFLDNAEFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYIL 635
Cdd:PRK13473 7 INGELVAGEGEKQPVYNPATGE-VLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 636 IVEAGKILSDAIA-EVREAIDFLRYYAMIAKNelndwkkLPGP-TGE-----DNFIFFEGRGVFLCISPWNFPLAIFIGQ 708
Cdd:PRK13473 86 SLNCGKPLHLALNdEIPAIVDVFRFFAGAARC-------LEGKaAGEyleghTSMIRRDPVGVVASIAPWNYPLMMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 709 VSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAgIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRmLA 788
Cdd:PRK13473 159 LAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLS-AA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 789 SRDGPIVPLiaETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQ 868
Cdd:PRK13473 237 ADSVKRTHL--ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 869 LSTDIGPIIDKASIDMLTKHTEKISRDEDTNLLS--KVPmdtnSYNGYFFPPYIyeiqkISQLKQ-------EVFGPILH 939
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVERAKALGHIRVVTggEAP----DGKGYYYEPTL-----LAGARQddeivqrEVFGPVVS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1571382267 940 IIRFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNqiGAAVGTQPFGGRGLSGTG 1011
Cdd:PRK13473 386 VTPF--DDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTH--FMLVSEMPHGGQKQSGYG 453
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
617-1021 |
5.00e-46 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 171.07 E-value: 5.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 617 LEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAmiaknelnDW-KKLPGP------TGEDNFIFFEGR 689
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMA--------EWaRRYEGEiiqsdrPGENILLFKRAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 690 GVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRIS 769
Cdd:PRK10090 73 GVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 770 GVAFTGSTQTAQiinRMLASRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEK 849
Cdd:PRK10090 153 MVSMTGSVSAGE---KIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 850 QIKMICNAAQELKIGDPIQLST-DIGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPMDTnsyNGYFFPPYIYE--IQKI 926
Cdd:PRK10090 230 FVNRLGEAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEG---KGYYYPPTLLLdvRQEM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 927 SQLKQEVFGPILHIIRFNksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQP-FGGR 1005
Cdd:PRK10090 307 SIMHEETFGPVLPVVAFD--TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAgWRKS 384
|
410
....*....|....*.
gi 1571382267 1006 GLSGTGPKAGGPNYLQ 1021
Cdd:PRK10090 385 GIGGADGKHGLHEYLQ 400
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
571-1021 |
6.00e-41 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 158.46 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 571 VNPAHlENVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEV 650
Cdd:PLN02315 39 VNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 651 REAIDFLRYYAMIAKnelndwkKLPG---PTGEDNFIFFE---GRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPA 724
Cdd:PLN02315 118 QEIIDMCDFAVGLSR-------QLNGsiiPSERPNHMMMEvwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 725 EQTPIIAYEAVKI----LHEAGIPKNVLHLIPGdGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIvplIAE 800
Cdd:PLN02315 191 PTTPLITIAMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKC---LLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 801 TGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKA 880
Cdd:PLN02315 267 LSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 881 SIDMLTKHTEKIsRDEDTNLLSKvpMDTNSYNGYFFPPYIYEIQ-KISQLKQEVFGPILHIIRFNksQLNEVISDINNTG 959
Cdd:PLN02315 347 SKKNFEKGIEII-KSQGGKILTG--GSAIESEGNFVQPTIVEISpDADVVKEELFGPVLYVMKFK--TLEEAIEINNSVP 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1571382267 960 YGLTFSLQSRvqsQIDLISKKI-----SVGNVYINRNQIGAAVGTqPFGGRGLSGTGPKAGGPNYLQ 1021
Cdd:PLN02315 422 QGLSSSIFTR---NPETIFKWIgplgsDCGIVNVNIPTNGAEIGG-AFGGEKATGGGREAGSDSWKQ 484
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
579-1032 |
1.63e-40 |
|
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: 156.31 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 579 VIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDA-IAEVREAIDFL 657
Cdd:cd07098 8 HLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEILVTCEKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 658 RYyaMIAKNElndwKKL-----PGPTGE---DNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQT-- 727
Cdd:cd07098 88 RW--TLKHGE----KALrpesrPGGLLMfykRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVaw 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 728 PIIAYEAV--KILHEAGIPKNVLHLIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQIInrMLASRDGpIVPLIAETGGLN 805
Cdd:cd07098 162 SSGFFLSIirECLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKV--MAAAAES-LTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 806 AMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDml 885
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFD-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 886 tkHTEKISRD---EDTNLLS-KVPMDTNSY-NGYFFPPYIY----EIQKISQlkQEVFGPILHIIRFnkSQLNEVISDIN 956
Cdd:cd07098 316 --RLEELVADaveKGARLLAgGKRYPHPEYpQGHYFPPTLLvdvtPDMKIAQ--EEVFGPVMVVMKA--SDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1571382267 957 NTGYGLTFSLQSRVQSQIDLISKKISVGNVYInrNQIGAAVGTQ--PFGGRGLSGTGpKAGGPNYLQRFSIEKVVSVN 1032
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAI--NDFGVNYYVQqlPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTED 464
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
571-1011 |
5.14e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 154.51 E-value: 5.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 571 VNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEV 650
Cdd:PRK09406 6 INPATGE-TVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 651 REAIDFLRYYAMIAKNELNDWKKLPGPTGEDN-FIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPI 729
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLADEPADAAAVGASRaYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 730 IAYEAVKILHEAGIPKNVLH--LIPGDGWylgKTLVPDNRISGVAFTGSTQTAQIINRmLASRDgpIVPLIAETGGLNAM 807
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPAGRAVAA-IAGDE--IKKTVLELGGSDPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 808 IVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTK 887
Cdd:PRK09406 239 IVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 888 HTEKISRDEDTNLLSKVPMDTnsyNGYFFPP-YIYEIQKISQL-KQEVFGPILHIIRFnkSQLNEVISDINNTGYGLTFS 965
Cdd:PRK09406 319 QVDDAVAAGATILCGGKRPDG---PGWFYPPtVITDITPDMRLyTEEVFGPVASLYRV--ADIDEAIEIANATTFGLGSN 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1571382267 966 LQSRVQSQIDLISKKISVGNVYInrNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:PRK09406 394 AWTRDEAEQERFIDDLEAGQVFI--NGMTVSYPELPFGGVKRSGYG 437
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
609-1011 |
2.24e-38 |
|
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: 149.21 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 609 SAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDA----IAEVREAIDFlryyamiAKNELNDW---KKLPGP---T 678
Cdd:cd07087 18 SLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteIAVVLGEIDH-------ALKHLKKWmkpRRVSVPlllQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 679 GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAyEAVKILHEAGIPKNVLHLIPGDGWYL 758
Cdd:cd07087 91 PAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATS-ALLAKLIPKYFDPEAVAVVEGGVEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 759 GKTLvpDNRISGVAFTGSTQTAQIINRmLASRDgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALR 838
Cdd:cd07087 170 TALL--AEPFDHIFFTGSPAVGKIVME-AAAKH--LTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 839 VLFIQEDIAEKQIKMICNAAQELkIGDPIQLSTDIGPIIDKasidmltKHTEKI-SRDEDTNLLSKvpMDTNSYNGYFFP 917
Cdd:cd07087 245 YVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINE-------RHFDRLaSLLDDGKVVIG--GQVDKEERYIAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 918 PYIYEIQKISQL-KQEVFGPILHIIRFNksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAA 996
Cdd:cd07087 315 TILDDVSPDSPLmQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAA 392
|
410
....*....|....*
gi 1571382267 997 VGTQPFGGRGLSGTG 1011
Cdd:cd07087 393 IPNLPFGGVGNSGMG 407
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
594-1029 |
2.58e-37 |
|
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: 146.22 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 594 ALEIAHgaFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGK----ILSDAIAEVREAIDFlryyamiAKNELN 669
Cdd:cd07134 5 AAQQAH--ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKpaaeVDLTEILPVLSEINH-------AIKHLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 670 DW---KKLPGPT---GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGI 743
Cdd:cd07134 76 KWmkpKRVRTPLllfGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 744 PKNVLhLIPGDGWYLGKTL-VPDNRIsgvAFTGSTQTAQII----NRMLASrdgpiVPLiaETGGLNAMIVDSSALLEQV 818
Cdd:cd07134 156 EDEVA-VFEGDAEVAQALLeLPFDHI---FFTGSPAVGKIVmaaaAKHLAS-----VTL--ELGGKSPTIVDETADLKKA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 819 TKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIK-MICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTKH-TEKISR-- 894
Cdd:cd07134 225 AKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEhLKAEIEKFYGKDAARKASPDLARIVNDRHFDRLKGLlDDAVAKga 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 895 --------DEDTN-----LLSKVPMDTnsyngyffppyiyeiqKISQlkQEVFGPILHIIRFnkSQLNEVISDINNTGYG 961
Cdd:cd07134 305 kvefggqfDAAQRyiaptVLTNVTPDM----------------KIMQ--EEIFGPVLPIITY--EDLDEVIEYINAKPKP 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1571382267 962 LTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVV 1029
Cdd:cd07134 365 LALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIG-SYHGVYGFKAFSHERAV 431
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
554-1034 |
2.74e-36 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 144.51 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 554 PIIDG---KSFLD-------NAEFTEVVNPAHLeNVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADL 623
Cdd:PLN00412 9 EILDGdvyKYYADgewrtssSGKSVAITNPSTR-KTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 624 LEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELNDWKKL---PGPTGEDNFIFFEGR---GVFLCISP 697
Cdd:PLN00412 88 LKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGKFLvsdSFPGNERNKYCLTSKiplGVVLAIPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 698 WNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGST 777
Cdd:PLN00412 168 FNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 778 QTAQIinrmlaSRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNA 857
Cdd:PLN00412 248 TGIAI------SKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 858 AQELKIGDPiQLSTDIGPIIDKASidmltkhtekisrdedTNLLSKVPMDTNSYNGYFFPPYIYEIQKISQLK------- 930
Cdd:PLN00412 322 VAKLTVGPP-EDDCDITPVVSESS----------------ANFIEGLVMDAKEKGATFCQEWKREGNLIWPLLldnvrpd 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 931 -----QEVFGPILHIIRFNKSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRnqiGAAVGTQ--PFG 1003
Cdd:PLN00412 385 mriawEEPFGPVLPVIRINSVE--EGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINS---APARGPDhfPFQ 459
|
490 500 510
....*....|....*....|....*....|.
gi 1571382267 1004 GRGLSGTGPKaGGPNylqrfSIEKVVSVNTT 1034
Cdd:PLN00412 460 GLKDSGIGSQ-GITN-----SINMMTKVKST 484
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
680-1011 |
2.06e-34 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 138.62 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 680 EDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAyEAVKILHEAGIPKNVLHLIPGDGWYLG 759
Cdd:PTZ00381 101 GKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTS-KLMAKLLTKYLDPSYVRVIEGGVEVTT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 760 KTLvpDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRV 839
Cdd:PTZ00381 180 ELL--KEPFDHIFFTGSPRVGKLVMQAAAEN---LTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDY 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 840 LFIQEDIAEKQIKMICNAAQELkIGDPIQLSTDIGPIIDKASI----DMLTKHTEKISRDEDTNLLSKvpmdtnsyngYF 915
Cdd:PTZ00381 255 VLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTkrlaELIKDHGGKVVYGGEVDIENK----------YV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 916 FPPYIYEIQKISQL-KQEVFGPILHIIRFNksQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIG 994
Cdd:PTZ00381 324 APTIIVNPDLDSPLmQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFH 401
|
330
....*....|....*..
gi 1571382267 995 AAVGTQPFGGRGLSGTG 1011
Cdd:PTZ00381 402 LLNPNLPFGGVGNSGMG 418
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
571-1033 |
1.30e-33 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 135.76 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 571 VNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEV 650
Cdd:PRK13968 12 VNPATGE-QLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 651 REAIDFLRYYAMIAKNELNdwkklPGPTGEDN---FIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQT 727
Cdd:PRK13968 91 AKSANLCDWYAEHGPAMLK-----AEPTLVENqqaVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 728 PIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTlVPDNRISGVAFTGSTQTAQIINrmlASRDGPIVPLIAETGGLNAM 807
Cdd:PRK13968 166 MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQM-INDSRIAAVTVTGSVRAGAAIG---AQAGAALKKCVLELGGSDPF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 808 IVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTDIGPIIDKASIDMLTK 887
Cdd:PRK13968 242 IVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 888 HTEKiSRDEDTNLL---SKVpmdtnSYNGYFFPPYIYE--IQKISQLKQEVFGPILHIIRFNKSQlnEVISDINNTGYGL 962
Cdd:PRK13968 322 QVEA-TLAEGARLLlggEKI-----AGAGNYYAPTVLAnvTPEMTAFREELFGPVAAITVAKDAE--HALELANDSEFGL 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571382267 963 TFSLQSRVQSQIDLISKKISVGNVYInrNQIGAAVGTQPFGGRGLSGTGPKaggpnyLQRFSIEKVVSVNT 1033
Cdd:PRK13968 394 SATIFTTDETQARQMAARLECGGVFI--NGYCASDARVAFGGVKKSGFGRE------LSHFGLHEFCNIQT 456
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
554-983 |
3.89e-33 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 136.41 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 554 PIIDGKSFLDN--AEFTEVVNPAHLEnVIGEVSSATSAQALNALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKEL 631
Cdd:PLN02419 115 PNLIGGSFVESqsSSFIDVINPATQE-VVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 632 IYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELNDWkkLPG-PTGEDNFIFFEGRGVFLCISPWNFPLAIFIGQVS 710
Cdd:PLN02419 194 AMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEY--LPNvSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 711 AALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLgKTLVPDNRISGVAFTGSTQTAQIINRMLASR 790
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 791 DGPIVpliAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMIcNAAQELKIGDPIQLS 870
Cdd:PLN02419 351 GKRIQ---SNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLV-ERAKALKVTCGSEPD 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 871 TDIGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPMDTNSY-NGYFFPPYIYE--IQKISQLKQEVFGPILHIIRFNksQ 947
Cdd:PLN02419 427 ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYeKGNFIGPTILSgvTPDMECYKEEIFGPVLVCMQAN--S 504
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1571382267 948 LNEVISDINNTGYG-----LTFSLQSRVQSQIDLISKKISV 983
Cdd:PLN02419 505 FDEAISIINKNKYGngaaiFTSSGAAARKFQMDIEAGQIGI 545
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
594-1023 |
8.06e-32 |
|
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: 130.05 E-value: 8.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 594 ALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKNELND--- 670
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHepg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 671 WKKLPGPTGEDNFIFFeGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGI-PKNVLH 749
Cdd:cd07084 84 NHLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 750 LIPGDGwYLGKTLVPDNRISGVAFTGSTQTAQiinrMLASrDGPIVPLIAETGGLNAMIVDSSA-LLEQVTKDVLISAFR 828
Cdd:cd07084 163 LINGDG-KTMQALLLHPNPKMVLFTGSSRVAE----KLAL-DAKQARIYLELAGFNWKVLGPDAqAVDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 829 SGGQRCSALRVLFIQEDIA-EKQIKMICNAAQELKIGDpiqlsTDIGPIIDKASIDMLTKHTEKISRDEDTNLLSKVPMD 907
Cdd:cd07084 237 CSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMIAHMENLLGSVLLFSGKELKNHS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 908 TNSYNGYFFPPYIY----EIQKISQL-KQEVFGPILHIIRFNKSQLNEVISDINNTGYGLTFSLQSRVQSQID-LISKKI 981
Cdd:cd07084 312 IPSIYGACVASALFvpidEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQeLIGNLW 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1571382267 982 SVGNVY-INRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYLQRF 1023
Cdd:cd07084 392 VAGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLV 434
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
687-1011 |
2.00e-30 |
|
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: 125.80 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 687 EGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAgIPKNVLHLIPGDGWYLGKTLvpDN 766
Cdd:cd07135 107 EPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL--EQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 767 RISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDI 846
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAKH---LTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 847 AEKQIKMICNAAQELKIGDPIQlSTDIGPIIDKASID----MLTKHTEKIS----RDEDTNllskvpmdtnsyngyFFPP 918
Cdd:cd07135 261 YDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNrlksLLDTTKGKVViggeMDEATR---------------FIPP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 919 YIYEIQKI--SQLKQEVFGPILHIIRFnkSQLNEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVYINRNQIGAA 996
Cdd:cd07135 325 TIVSDVSWddSLMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVG 402
|
330
....*....|....*
gi 1571382267 997 VGTQPFGGRGLSGTG 1011
Cdd:cd07135 403 VDNAPFGGVGDSGYG 417
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
609-1029 |
3.16e-29 |
|
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: 122.13 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 609 SAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIaevREAIDFLRYYAMIAKNELNDW---KKLPGP------TG 679
Cdd:cd07137 19 SAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESF---RDEVSVLVSSCKLAIKELKKWmapEKVKTPlttfpaKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 680 EdnfIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTP---------IIAY---EAVKILhEAGIPKNv 747
Cdd:cd07137 96 E---IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPatsallaklIPEYldtKAIKVI-EGGVPET- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 748 lhlipgdgwylgkTLVPDNRISGVAFTGSTQTAQIInrmLASRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAF 827
Cdd:cd07137 171 -------------TALLEQKWDKIFFTGSPRVGRII---MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 828 RS-GGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQlSTDIGPIIDKASIDMLT------KHTEKI----SRDE 896
Cdd:cd07137 235 GCnNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKE-SKDLSRIVNSHHFQRLSrllddpSVADKIvhggERDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 897 DT-----NLLSKVPMDTnsyngyffppyiyeiqkiSQLKQEVFGPILHIIRFNKSQlnEVISDINNTGYGLT---FSLQS 968
Cdd:cd07137 314 KNlyiepTILLDPPLDS------------------SIMTEEIFGPLLPIITVKKIE--ESIEIINSRPKPLAayvFTKNK 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571382267 969 RVQSQidlISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYlQRFSIEKVV 1029
Cdd:cd07137 374 ELKRR---IVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFGAYHGKFSF-DAFSHKKAV 430
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
594-1011 |
7.01e-29 |
|
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: 121.17 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 594 ALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKEliyilIVEA-GKILSDAIAE-VREAIDFLRYYAMIAKNELNDW 671
Cdd:cd07132 3 AVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDE-----IVEAlAKDLRKPKFEaVLSEILLVKNEIKYAISNLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 672 -KKLPGPTG-----EDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAyeavKILHEAgIPK 745
Cdd:cd07132 78 mKPEPVKKNlatllDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA----KLLAEL-IPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 746 nvlhlipgdgwYLGKTLVP-------------DNRISGVAFTGSTQTAQIInrMLASRDGpIVPLIAETGGLNAMIVDSS 812
Cdd:cd07132 153 -----------YLDKECYPvvlggveettellKQRFDYIFYTGSTSVGKIV--MQAAAKH-LTPVTLELGGKSPCYVDKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 813 ALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELkIGDPIQLSTDIGPIIDKasidmltKHTEKI 892
Cdd:cd07132 219 CDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIIND-------RHFQRL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 893 srdedTNLL--SKVPM--DTNSYNGYFFPPYIYEIQKISQL-KQEVFGPILHIIrfNKSQLNEVISDINNTGYGLTFSLQ 967
Cdd:cd07132 291 -----KKLLsgGKVAIggQTDEKERYIAPTVLTDVKPSDPVmQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVF 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1571382267 968 SRVQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:cd07132 364 SNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
609-1011 |
3.23e-26 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 113.37 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 609 SAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDA----IAEVREAIDFlryyamiAKNELNDW---KKLPGPT--- 678
Cdd:cd07136 18 DVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAymteIGFVLSEINY-------AIKHLKKWmkpKRVKTPLlnf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 679 GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTP----IIAyeavKILHEAgIPKNVLHLIPGD 754
Cdd:cd07136 91 PSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPntskVIA----KIIEET-FDEEYVAVVEGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 755 GWYLGKTLvpDNRISGVAFTGSTQTAQIINRmLASRDgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFRSGGQRC 834
Cdd:cd07136 166 VEENQELL--DQKFDYIFFTGSVRVGKIVME-AAAKH--LTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 835 SALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQlSTDIGPIIDKASIDMLTK--HTEKI----SRDEDTN-----LLSK 903
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGllDNGKIvfggNTDRETLyieptILDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 904 VPMDTNSyngyffppyiyeiqkisqLKQEVFGPILHIIRFNKsqLNEVISDINNTGYGLT---FSLQSRVQSQidlISKK 980
Cdd:cd07136 320 VTWDDPV------------------MQEEIFGPILPVLTYDT--LDEAIEIIKSRPKPLAlylFSEDKKVEKK---VLEN 376
|
410 420 430
....*....|....*....|....*....|.
gi 1571382267 981 ISVGNVYINRNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:cd07136 377 LSFGGGCINDTIMHLANPYLPFGGVGNSGMG 407
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
601-1011 |
2.40e-24 |
|
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: 107.19 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 601 AFTKWQNVSAEERAKCLEKAADLLEERMKELIyilivEAgkILSD---------AIAEVREAIDFLRYyamiAKNELNDW 671
Cdd:cd07133 10 AFLANPPPSLEERRDRLDRLKALLLDNQDALA-----EA--ISADfghrsrhetLLAEILPSIAGIKH----ARKHLKKW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 672 ----KKLPGPT--GEDNFIFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAgIPK 745
Cdd:cd07133 79 mkpsRRHVGLLflPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 746 NVLHLIPGDGwylgktlvpdnrisGVA------------FTGSTQTAQIInrMLASRDGpIVPLIAETGGLNAMIVDSSA 813
Cdd:cd07133 158 DEVAVVTGGA--------------DVAaafsslpfdhllFTGSTAVGRHV--MRAAAEN-LTPVTLELGGKSPAIIAPDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 814 LLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIKMICNAAQELkIGDpIQLSTDIGPIIDKASIDMLTKHTEKiS 893
Cdd:cd07133 221 DLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPT-LADNPDYTSIINERHYARLQGLLED-A 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 894 RDEDTNLLSKVPMDTNSYNGYFFPPYIyeIQKISQ----LKQEVFGPILHIIRFNKsqLNEVISDINNTGYGLTFSLQSR 969
Cdd:cd07133 298 RAKGARVIELNPAGEDFAATRKLPPTL--VLNVTDdmrvMQEEIFGPILPILTYDS--LDEAIDYINARPRPLALYYFGE 373
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1571382267 970 VQSQIDLISKKISVGNVYINRNQIGAAVGTQPFGGRGLSGTG 1011
Cdd:cd07133 374 DKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
579-937 |
2.53e-23 |
|
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: 105.04 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 579 VIGEVSSATS--AQALN-ALEIAHGAFTKWqnvSAEERAKCLEKAADLLEERmKELIYILIVEAGKILSDAIAEVREAID 655
Cdd:cd07128 27 VVARVSSEGLdfAAAVAyAREKGGPALRAL---TFHERAAMLKALAKYLMER-KEDLYALSAATGATRRDSWIDIDGGIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 656 FLRYYAMIAKNELNDWKKLPgptgEDNFI------FFEGR-------GVFLCISPWNFPLAIFIGQVSAALAAGNAVLAK 722
Cdd:cd07128 103 TLFAYASLGRRELPNAHFLV----EGDVEplskdgTFVGQhiltprrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 723 PAEQTPIIAYEAVKILHEAGI-PKNVLHLIPGDGWYLGKTLVPDNRisgVAFTGSTQTAQiinrMLASRDGPI---VPLI 798
Cdd:cd07128 179 PATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDV---VAFTGSAATAA----KLRAHPNIVarsIRFN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 799 AETGGLNAMIVDSSA---------LLEQVTKDVLISAfrsgGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQL 869
Cdd:cd07128 252 AEADSLNAAILGPDAtpgtpefdlFVKEVAREMTVKA----GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLE 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1571382267 870 STDIGPIIDK-------ASIDMLTKHTEKISRDEDTNLLSKVPMDTnsynGYFFPPYIYEIQKISQLKQ----EVFGPI 937
Cdd:cd07128 328 GVRMGPLVSReqredvrAAVATLLAEAEVVFGGPDRFEVVGADAEK----GAFFPPTLLLCDDPDAATAvhdvEAFGPV 402
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
579-937 |
3.70e-20 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 95.54 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 579 VIGEVSSATSAQALnalEIAHG-AFTKWQNVSA------EERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVR 651
Cdd:PRK11903 27 VTGEELVRVSATGL---DLAAAfAFAREQGGAAlraltyAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 652 EAIDFLRYYAMIAKnELNDWKKLPGPTG-----EDNF----IFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAK 722
Cdd:PRK11903 104 GGIFTLGYYAKLGA-ALGDARLLRDGEAvqlgkDPAFqgqhVLVPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 723 PAEQTPIIAYEAVKILHEAGI-PKNVLHLIPGDGWYLGKTLVPDNRisgVAFTGSTQTAQIInRMLASRDGPIVPLIAET 801
Cdd:PRK11903 183 PATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDV---VSFTGSAETAAVL-RSHPAVVQRSVRVNVEA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 802 GGLNAMIV------DSSA---LLEQVTKDVLISAfrsgGQRCSALRVLFIQEDIAEKQIKMICNAAQELKIGDPIQLSTD 872
Cdd:PRK11903 259 DSLNSALLgpdaapGSEAfdlFVKEVVREMTVKS----GQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVR 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1571382267 873 IGPIIDKAS-------IDMLTKHTEkISRDEDTNllskVPMDTNSYNGYFFPPYIYEIQKI--SQL--KQEVFGPI 937
Cdd:PRK11903 335 MGPLVSRAQlaavragLAALRAQAE-VLFDGGGF----ALVDADPAVAACVGPTLLGASDPdaATAvhDVEVFGPV 405
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
594-860 |
9.01e-19 |
|
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: 90.68 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 594 ALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIAEVREAIDFLRYYAMIAKN------- 666
Cdd:cd07129 4 AAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgswldar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 667 ---ELNDWKKLP-----------GPTGednfiffegrgVFlciSPWNFPLAIFI--GQVSAALAAGNAVLAK-----PAe 725
Cdd:cd07129 84 idpADPDRQPLPrpdlrrmlvplGPVA-----------VF---GASNFPLAFSVagGDTASALAAGCPVVVKahpahPG- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 726 qTPIIAYEAV-KILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIvPLIAETGGL 804
Cdd:cd07129 149 -TSELVARAIrAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPI-PFYAELGSV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 805 NAMIVDSSALLEQVTK--DVLISAFRSG-GQRCSALRVLFIQEDIA-EKQIKMICNAAQE 860
Cdd:cd07129 227 NPVFILPGALAERGEAiaQGFVGSLTLGaGQFCTNPGLVLVPAGPAgDAFIAALAEALAA 286
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
609-1029 |
3.49e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 89.02 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 609 SAEERAKCLEKAADLLEERMKELIYILIVEAGKILSDAIaevREAIDFLRYYAMIAKNELNDW---KKLPGPtgednFIF 685
Cdd:PLN02203 26 SLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAY---RDEVGVLTKSANLALSNLKKWmapKKAKLP-----LVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 686 FEGR--------GVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPiiayeAVKILHEAGIPK----NVLHLIPG 753
Cdd:PLN02203 98 FPATaevvpeplGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAP-----ATSAFLAANIPKyldsKAVKVIEG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 754 dGWYLGKTLVpDNRISGVAFTGSTQTAQIInrmLASRDGPIVPLIAETGGLNAMIVD---SSALLEQVTKDVLISAFRS- 829
Cdd:PLN02203 173 -GPAVGEQLL-QHKWDKIFFTGSPRVGRII---MTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSc 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 830 GGQRCSALRVLFIQEDIAEKQIKMICNAAQELkIGDPIQLSTDIGPIIDKasidmltKHTEKISrdedtNLLSKvPMDTN 909
Cdd:PLN02203 248 AGQACIAIDYVLVEERFAPILIELLKSTIKKF-FGENPRESKSMARILNK-------KHFQRLS-----NLLKD-PRVAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 910 S--YNGYF-------------FPPYIYEIqkisqLKQEVFGPILHIIRFNKSQlnEVISDINNTGYGL---TFSLQSRVQ 971
Cdd:PLN02203 314 SivHGGSIdekklfieptillNPPLDSDI-----MTEEIFGPLLPIITVKKIE--DSIAFINSKPKPLaiyAFTNNEKLK 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1571382267 972 SQIdlISKKiSVGNVYINRNQIGAAVGTQPFGGRGLSGTGpKAGGPNYLQRFSIEKVV 1029
Cdd:PLN02203 387 RRI--LSET-SSGSVTFNDAIIQYACDSLPFGGVGESGFG-RYHGKYSFDTFSHEKAV 440
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
645-831 |
1.38e-17 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 88.38 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 645 DAIAEVREAIDFLRYYAMIAKNELNDWKKLPGPTGEDNFIFFEGRGVFLCISPwnfPLAIFIGQVSAALAAGN-AVLAKP 723
Cdd:PRK11905 1035 AWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVAD---TEEALLRQLAAALATGNvAVVAAD 1111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 724 AEqtpiiAYEAVKILHEAgipkNVLHLIPGDGWylgktlVPDNRISGVAFTGSTQTAQIINRMLASRDGPIVPLIAETGG 803
Cdd:PRK11905 1112 SG-----LAAALADLPGL----VAARIDWTQDW------EADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEPT 1176
|
170 180
....*....|....*....|....*...
gi 1571382267 804 LNamiVDSSALLEQVTKDVLISAfrSGG 831
Cdd:PRK11905 1177 DA---YDLARLVEERSVSINTTA--AGG 1199
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
684-1029 |
1.80e-17 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 86.64 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 684 IFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILhEAGIPKNVLHLIpgDGWYLGKTLV 763
Cdd:PLN02174 108 IVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVV--EGAVTETTAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 764 PDNRISGVAFTGSTQTAQIINRMLASRdgpIVPLIAETGGLNAMIVDSSALLEQVTKDVLISAFR-SGGQRCSALRVLFI 842
Cdd:PLN02174 185 LEQKWDKIFYTGSSKIGRVIMAAAAKH---LTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 843 QEDIAEKQIKMICNAAQELKIGDPIQlSTDIGPIIDKASIDMLTKH------TEKI----SRDEDT-----NLLSKVPMD 907
Cdd:PLN02174 262 TKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLldekevSDKIvyggEKDRENlkiapTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 908 TnsyngyffppyiyeiqkiSQLKQEVFGPILHIIRFNKSQlnEVISDINNTGYGLTFSLQSRVQSQIDLISKKISVGNVY 987
Cdd:PLN02174 341 S------------------LIMSEEIFGPLLPILTLNNLE--ESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIV 400
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1571382267 988 INRNQIGAAVGTQPFGGRGLSGTGPKAGGPNYlQRFSIEKVV 1029
Cdd:PLN02174 401 VNDIAVHLALHTLPFGGVGESGMGAYHGKFSF-DAFSHKKAV 441
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
674-806 |
1.79e-14 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 78.44 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 674 LPGPTGEDNFIFFEGRGVFLCISPwnfPLAIFIGQVSAALAAGNAVLAkPAEQTPiiayeavkilheAGIPKNVLHlipg 753
Cdd:COG4230 1048 LPGPTGERNTLTLRPRGRVLCLAD---SLEALLAQLAAALATGNRAVV-AADLAL------------AGLPAVLLP---- 1107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1571382267 754 dgwylgktlvpdnRISGVAFTGstqTAQIINRMLASRDGPIVPLIA----------ETGGlNA 806
Cdd:COG4230 1108 -------------PFDAVLFEG---RLRALRQALAARDGAIVPVIDagydlerlleEAGG-NA 1153
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
263-471 |
3.11e-13 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 73.20 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 263 EELRAKLLELCHEAKKYNISLCIDAEESE-RLEMSLVLFEQLRLDDSLSKWEGLGLAVQAYQKRALSVLDFVEDVAIRSK 341
Cdd:PLN02681 216 ELAHERLQKLCERAAQLGVPLLIDAEYTSlQPAIDYITYDLAREFNKGKDRPIVYGTYQAYLKDARERLRLDLERSEREG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 342 HKIMVRLVKGAYWDSEIKRTQELGLIGyPVFTRKSHTDVCYLACAQKLLSK--ENHFYPCFGTHNAYTfatiIELA---- 415
Cdd:PLN02681 296 VPLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAEFLLEKasNGDGEVMLATHNVES----GELAaakm 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571382267 416 -----DKNHPGFEFQRLHGMGKSLydyAISELATSINCRIYAPVGKHSDLLPYLIRRLLEN 471
Cdd:PLN02681 371 nelglHKGDPRVQFAQLLGMSDNL---SFGLGNAGFRVSKYLPYGPVEEVIPYLLRRAEEN 428
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
695-963 |
1.01e-11 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 68.68 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 695 ISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAGIPKNVLHLIPGDGWYLGKTLVPDNRISgVAFT 774
Cdd:cd07126 149 ITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRM-TLFT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 775 GSTQTAQIINRMLASRdgpiVPLiaETGGLNAMI-------VDSSALleQVTKDvlisAFRSGGQRCSALRVLFIQEDIA 847
Cdd:cd07126 228 GSSKVAERLALELHGK----VKL--EDAGFDWKIlgpdvsdVDYVAW--QCDQD----AYACSGQKCSAQSILFAHENWV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 848 EKQI-KMICNAAQELKIGDpiqlsTDIGPIIDKASIDMLTkHTEKISRDEDTNLLSKVPMDTN----SYNGYFFPPYIY- 921
Cdd:cd07126 296 QAGIlDKLKALAEQRKLED-----LTIGPVLTWTTERILD-HVDKLLAIPGAKVLFGGKPLTNhsipSIYGAYEPTAVFv 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1571382267 922 EIQKISQLK------QEVFGPILHIIRFNKSQLNEVISDINNTGYGLT 963
Cdd:cd07126 370 PLEEIAIEEnfelvtTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLT 417
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
595-845 |
1.99e-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: 61.34 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 595 LEIAHGAFTKWQNVSAEERAK-CLEKAADLlEERMKELIYILIVEAGKILSDAI------AEVR--EAIDFlRYYAMIAK 665
Cdd:cd07127 90 LAAARAAMPGWRDAGARARAGvCLEILQRL-NARSFEMAHAVMHTTGQAFMMAFqaggphAQDRglEAVAY-AWREMSRI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 666 NELNDWKKlpgPTGEDNFIFFE------GRGVFLCIS-----PWNFPLAIFigqvsAALAAGNAVLAKPAEQT----PII 730
Cdd:cd07127 168 PPTAEWEK---PQGKHDPLAMEktftvvPRGVALVIGcstfpTWNGYPGLF-----ASLATGNPVIVKPHPAAilplAIT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 731 AYEAVKILHEAGIPKNVLHLI---PGDGwyLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDgpivpLIAETGGLNAM 807
Cdd:cd07127 240 VQVAREVLAEAGFDPNLVTLAadtPEEP--IAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ-----VYTEKAGVNTV 312
|
250 260 270
....*....|....*....|....*....|....*...
gi 1571382267 808 IVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQED 845
Cdd:cd07127 313 VVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRD 350
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
612-848 |
7.21e-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: 56.08 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 612 ERAKCLEKAADLLEERMKELIYILIVEAG-----KILSDAIAEVREAIDFL--RYYAMI--AKNELND-----------W 671
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALydtrqRLASEAVSERGAYIRSLiaNWIAMMgcSESKLYKnidtergitasV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 672 KKLPGPTGEDNF---IFFEGRGVFLCISPWNFPLAIfIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEA---GIPK 745
Cdd:cd07077 81 GHIQDVLLPDNGetyVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 746 NVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQTAQiinrmLASRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLIS 825
Cdd:cd07077 160 ILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVD-----AAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
250 260
....*....|....*....|...
gi 1571382267 826 AFRSGGQrCSALRVLFIQEDIAE 848
Cdd:cd07077 235 KFFDQNA-CASEQNLYVVDDVLD 256
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
593-862 |
4.69e-06 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 50.31 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 593 NALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGkilsdaiaevreaidFLRYYAMIAKNELNDwK 672
Cdd:cd07121 8 DAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG---------------MGRVEDKIAKNHLAA-E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 673 KLPGP--------TGEDNFIFFEGR--GVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAg 742
Cdd:cd07121 72 KTPGTedltttawSGDNGLTLVEYApfGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 743 ipknvlhlipgdgwyLGKTLVPDNRISGVAfTGSTQTAqiiNRMLASRDgpiVPLIAETGGLN----AM----------- 807
Cdd:cd07121 151 ---------------IAEAGGPDNLVVTVE-EPTIETT---NELMAHPD---INLLVVTGGPAvvkaALssgkkaigaga 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571382267 808 -----IVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQI-KMICNAAQELK 862
Cdd:cd07121 209 gnppvVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIaAMQRNGAYVLN 269
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
9-56 |
8.04e-06 |
|
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: 43.99 E-value: 8.04e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1571382267 9 NALRKRLQAFYRADEKSHVRYLVEKSELSADSKNIIYNIAKQIVEKIR 56
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
674-795 |
1.92e-05 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 48.82 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 674 LPGPTGEDNFIFFEGRGVFLCISPWNFPLAIfigQVSAALAAGNAVLAKPAEQTPIIAyeavkilheAGIPKNVLHLIPg 753
Cdd:PRK11809 1173 LPGPTGERNTYTLLPRERVLCLADTEQDALT---QLAAVLAVGSQALWPDDALHRALV---------AALPAAVQARIQ- 1239
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1571382267 754 dgwYLGKTLVPDNRISGVAFTGSTQTAQIINRMLASRDGPIV 795
Cdd:PRK11809 1240 ---LAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPIV 1278
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
593-862 |
1.38e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 42.58 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 593 NALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGkilsdaiaevreaidFLRYYAMIAKNELNdWK 672
Cdd:PRK15398 40 DAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG---------------MGRVEDKIAKNVAA-AE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 673 KLPGP--------TGEDNFIFFEGR--GVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEAg 742
Cdd:PRK15398 104 KTPGVedlttealTGDNGLTLIEYApfGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEA- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 743 ipknvlhlipgdgwyLGKTLVPDNRISGVAftgsTQTAQIINRMLASRDgpiVPLIAETGGLN----AM----------- 807
Cdd:PRK15398 183 ---------------IVAAGGPENLVVTVA----EPTIETAQRLMKHPG---IALLVVTGGPAvvkaAMksgkkaigaga 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571382267 808 -----IVDSSALLEQVTKDVLISAFRSGGQRCSALRVLFIQEDIAEKQIK-MICNAAQELK 862
Cdd:PRK15398 241 gnppvVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRlMEKNGAVLLT 301
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
594-849 |
1.54e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 42.25 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 594 ALEIAHGAFTKWQNVSAEERAKCLEKAADLLEERMKELIYILIVEAGK-ILSDAIAEVREAIdflRYYAMIAKNElndwk 672
Cdd:cd07081 4 AVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMgRVEDKVIKNHFAA---EYIYNVYKDE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 673 KLPGP-TGEDNF---IFFEGRGVFLCISPWNFPLAIFIGQVSAALAAGNAVLAKPAEQTPIIAYEAVKILHEA----GIP 744
Cdd:cd07081 76 KTCGVlTGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 745 KNVLHLIPGDGWYLGKTLVPDNRISGVAFTGSTQtaqiinrMLASRDGPIVPLIAETGGLNAMIVDSSALLEQVTKDVLI 824
Cdd:cd07081 156 ENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPA-------VVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVK 228
|
250 260
....*....|....*....|....*
gi 1571382267 825 SAFRSGGQRCSALRVLFIQEDIAEK 849
Cdd:cd07081 229 SKTFDNGVICASEQSVIVVDSVYDE 253
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
604-848 |
5.61e-03 |
|
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130164 [Multi-domain] Cd Length: 715 Bit Score: 40.66 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 604 KWQNVSAEERAKCLEKAADLLEERMKE--------------------LIYILIVEAGKILSDA-----IAEVREAIDFLR 658
Cdd:TIGR01092 301 MLQALSSEQRKEILHDIADALEDNEDEilaenkkdvaaaqgagyaasLVARLSMSPSKISSLAislrqLAAMEDPIGRVL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 659 YYAMIAKN-ELndwKKLPGPTGEdNFIFFEGRgvflcispwnfPLAIFigQVSA-ALAAGNAVLAKPAEQtpiiAYEAVK 736
Cdd:TIGR01092 381 KRTRIADNlIL---EKTSVPIGV-LLIVFESR-----------PDALV--QIASlAIRSGNGLLLKGGKE----AARSNA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571382267 737 ILH---EAGIPKNVL-HLIpgdGWYLGKTLVP-----DNRISGVAFTGSTQTAQIINRmlASRdgpiVPLIAETGGLNAM 807
Cdd:TIGR01092 440 ILHkviTEAIPIHVGkKLI---GLVTSREEIPdllklDDVIDLVIPRGSNKLVSQIKK--STK----IPVLGHADGICHV 510
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1571382267 808 IVDSSALLEQVTKDVLISAFRSGGQrCSALRVLFIQEDIAE 848
Cdd:TIGR01092 511 YVDKSASVDMAKRIVRDAKCDYPAA-CNAMETLLVHKDLLR 550
|
|
| |
