|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1-1045 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1877.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 1 MLEKQSIHLPEGLRAAINKAYRMDELSLITELSEQAALDPQQMMAIKTSATKLVQSVRSERKKSTGIDSFLTEYALSSDE 80
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGGIDAFLQEYSLSTEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 81 GIALMCLAEALLRVPDNATIDNLIKDKLAGGDWGAHRGQSESFFVNATTWALMLTGKVLTP-EKAENTLTKALLKLVNRS 159
Cdd:PRK11904 81 GIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLdKKADGTPSGVLKRLVNRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 160 SEAVVRKAVDKAMRIMSKQFVMGRTINEALARAKKKEDRGYRYSYDMLGEAALTSADAARYFEAYKEAIISIGeKADKHS 239
Cdd:PRK11904 161 GEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIG-RAAGGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 240 DVYRRPGISIKLSALHPRYSEFQYERVMAELPPKLLALSRLAKDYGIALTIDAEESERLDLSLDVIEKVFTDESLQGWNG 319
Cdd:PRK11904 240 DLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 320 FGLAVQSYQKRAFYVLDWVAALARSKQRRIMVRLIKGAYWDSEIKKTQMQGFSEYPVFTRKVFTDVSFQACAKKILTMTD 399
Cdd:PRK11904 320 FGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 400 AIYPQFATHNAYSVAMILNLVGGyRDFEFQCLHGMGNELYEQIVPAncYGIPCRIYAPVGSHEDLLPYLVRRLLENGANS 479
Cdd:PRK11904 400 AIYPQFATHNAHTVAAILEMAGH-RGFEFQRLHGMGEALYDALLDA--PGIPCRIYAPVGSHKDLLPYLVRRLLENGANS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 480 SFVNRIVDDKAPISELVEDPVAKSRSLLDKINKNIPLPEDIFLPVRKNSKGFDFTNRLERALLQQELAKIESKEWQASPM 559
Cdd:PRK11904 477 SFVHRLVDPDVPIEELVADPVEKLRSFETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPI 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 560 IAGRKLSRdllqTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTC 639
Cdd:PRK11904 557 INGEGEAR----PVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCV 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 640 REAGKTWSDGIAEVREAIDFCRYYAKKAQELMSSPQRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTG 719
Cdd:PRK11904 633 REAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAG 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 720 NCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIP 799
Cdd:PRK11904 713 NTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVP 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 800 LIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPV 879
Cdd:PRK11904 793 LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPV 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 880 IDKEALSILKNHVENMRKHHEILYQCTVDDEALSGYFMPPTAIAIDSISALEKEVFGPILHVIQFKRKDLDKVINQINQT 959
Cdd:PRK11904 873 IDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAINAT 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 960 GYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPNYLIRLCHERTYTVDTTAAGG 1039
Cdd:PRK11904 953 GYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNTTAAGG 1032
|
....*.
gi 395130835 1040 NASLMS 1045
Cdd:PRK11904 1033 NASLLS 1038
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
13-1032 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1706.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 13 LRAAINKAYRMDELSLITELSEQAALDPQQMMAIKTSATKLVQSVRSERKKsTGIDSFLTEYALSSDEGIALMCLAEALL 92
Cdd:PRK11905 15 LRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKG-TGVEALLQEYSLSSQEGVALMCLAEALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 93 RVPDNATIDNLIKDKLAGGDWGAHRGQSESFFVNATTWALMLTGKVLTPEKaENTLTKALLKLVNRSSEAVVRKAVDKAM 172
Cdd:PRK11905 94 RIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVN-DRGLSAALTRLIARLGEPVIRKAVDMAM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 173 RIMSKQFVMGRTINEALARAKKKEDRGYRYSYDMLGEAALTSADAARYFEAYKEAIISIGeKADKHSDVYRRPGISIKLS 252
Cdd:PRK11905 173 RMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIG-KAATGRGVYDGPGISVKLS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 253 ALHPRYSEFQYERVMAELPPKLLALSRLAKDYGIALTIDAEESERLDLSLDVIEKVFTDESLQGWNGFGLAVQSYQKRAF 332
Cdd:PRK11905 252 ALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIGFVVQAYQKRCP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 333 YVLDWVAALARSKQRRIMVRLIKGAYWDSEIKKTQMQGFSEYPVFTRKVFTDVSFQACAKKILTMTDAIYPQFATHNAYS 412
Cdd:PRK11905 332 FVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVIYPQFATHNAQT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 413 VAMILNLVGGYRDFEFQCLHGMGNELYEQIVPANCYGIPCRIYAPVGSHEDLLPYLVRRLLENGANSSFVNRIVDDKAPI 492
Cdd:PRK11905 412 LAAIYELAGGKGDFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNRIVDENVPV 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 493 SELVEDPVAKSRSLLDKINKNIPLPEDIFLPVRKNSKGFDFTNRLERALLQQELAKIESKEWQASPMIAGRKlSRDLLQT 572
Cdd:PRK11905 492 EELIADPVEKVAAMGVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLAGGD-VDGGTRP 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 573 VMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAE 652
Cdd:PRK11905 571 VLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 653 VREAIDFCRYYAKKAQELMSSPQRfngytgelnelslHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPL 732
Cdd:PRK11905 651 VREAVDFLRYYAAQARRLLNGPGH-------------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPL 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 733 IAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLIAETGGQNAMIV 812
Cdd:PRK11905 718 IAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLIAETGGQNAMIV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 813 DSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHV 892
Cdd:PRK11905 798 DSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHI 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENMRKHHEILYQCTVDDEALSGYFMPPTAIAIDSISALEKEVFGPILHVIQFKRKDLDKVINQINQTGYGLTLGIHSRIN 972
Cdd:PRK11905 878 EAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGLHSRID 957
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 973 ETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPNYLIRLCHERTYTV 1032
Cdd:PRK11905 958 ETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPI 1017
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
13-1049 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1427.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 13 LRAAINKAYRMDELSLitELSEQAALDPQQMMAIKTSATKLVQSVRSERKKSTGIDSFLTEYALSSDEGIALMCLAEALL 92
Cdd:COG4230 16 LRAAIAAAERAEELLA--AAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLSSEALALLLLALLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 93 RVPDNATIDNLIKDKLAGGDWGAHRGQSESFFVNATTWALMLTGKVLTPEKAENTLTKALLKLVNRSSEAVVRKAVDKAM 172
Cdd:COG4230 94 LALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRLGRPGIRRAMRAAM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 173 RIMSKQFVMGRTINEALARAKKKEDRGYRYSYDMLGEAALTSADAARYFEAYKEAIISIGEKADKHSDVYRRPGISIKLS 252
Cdd:COG4230 174 MMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGSGGPGPSISSSLSV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 253 ALHPRYSEFQYERVMAELPPKLLALSRLAKD---YGIALTIDAEESERLDLSLDVIEKVFTDESLQGWNGFGLAVQSYQK 329
Cdd:COG4230 254 LLSARHPRYRRRREERLLLLLLPLLALLALAainINIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVGQAVQAYAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 330 RAFYVLDWVAALARSKQRRIMVRLIKGAYWDSEIKKTQMQGFSEYPVFTRKVFTDVSFQACAKKILTMTDAIYPQFATHN 409
Cdd:COG4230 334 ALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAAQPAFAPQFATHA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 410 AYSVAMILNLvGGYRDFEFQCLHGMGNELYEQIVPANcYGIPCRIYAPVGSHEDLLPYLVRRLLENGANSSFVNRIVDDK 489
Cdd:COG4230 414 AATAAAAAAA-GGGGEFEFQCLHGMGEYLYDQVGRGK-LGRPCRIYAPVGSHEDLLAYLVRRLLENGANSSFVNRIADED 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 490 APISELVEDPVAKSRSLLDKINKNIPLPEDIFLPVRKNSKGFDFTNRLERALLQQELAKIESKEWQASPMIAGRKLSRDL 569
Cdd:COG4230 492 VPVEELIADPVEKARALGGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQAAPLIAGEAASGEA 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 570 lQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDG 649
Cdd:COG4230 572 -RPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDA 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 650 IAEVREAIDFCRYYAKKAQELMSSPQRfngytgelnelsLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQ 729
Cdd:COG4230 651 IAEVREAVDFCRYYAAQARRLFAAPTV------------LRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQ 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 730 TPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLIAETGGQNA 809
Cdd:COG4230 719 TPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLIAETGGQNA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 810 MIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILK 889
Cdd:COG4230 799 MIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLE 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 890 NHVENMRKHHEILYQCTVDDEALSGYFMPPTAIAIDSISALEKEVFGPILHVIQFKRKDLDKVINQINQTGYGLTLGIHS 969
Cdd:COG4230 879 AHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGVHS 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 970 RINETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPNYLIRLCHERTYTVDTTAAGGNASLMSIPEE 1049
Cdd:COG4230 959 RIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTAAGGNASLLALGDW 1038
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
5-1028 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1417.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 5 QSIhLPEG-LRAAINKAYRMDELSLITELSEQAALDPQQMMAIKTSATKLVQSVRsERKKSTG----IDSFLTEYALSSD 79
Cdd:PRK11809 83 EQI-LPQSvLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLR-NQKSAGGragmVQGLLQEFSLSSQ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 80 EGIALMCLAEALLRVPDNATIDNLIKDKLAGGDWGAHRGQSESFFVNATTWALMLTGKvLTPEKAENTLTKALLKLVNRS 159
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGK-LVSTHNEASLSSSLNRIIGKS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 160 SEAVVRKAVDKAMRIMSKQFVMGRTINEALARAKKKEDRGYRYSYDMLGEAALTSADAARYFEAYKEAIISIGeKADKHS 239
Cdd:PRK11809 240 GEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIG-KASNGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 240 DVYRRPGISIKLSALHPRYSEFQYERVMAELPPKLLALSRLAKDYGIALTIDAEESERLDLSLDVIEKVFTDESLQGWNG 319
Cdd:PRK11809 319 GIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNG 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 320 FGLAVQSYQKRAFYVLDWVAALARSKQRRIMVRLIKGAYWDSEIKKTQMQGFSEYPVFTRKVFTDVSFQACAKKILTMTD 399
Cdd:PRK11809 399 IGFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 400 AIYPQFATHNAYSVAMILNLVGG-YR--DFEFQCLHGMGNELYEQIVPANCYGI---PCRIYAPVGSHEDLLPYLVRRLL 473
Cdd:PRK11809 479 LIYPQFATHNAHTLAAIYHLAGQnYYpgQYEFQCLHGMGEPLYEQVVGKVADGKlnrPCRIYAPVGTHETLLAYLVRRLL 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 474 ENGANSSFVNRIVDDKAPISELVEDPVAKSRSLLDKINK------NIPLPEDIFLPVRKNSKGFDFTNRLERALLQQELA 547
Cdd:PRK11809 559 ENGANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQlglphpKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALL 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 548 KIESKEWQASPMIAGrKLSRDLLQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLL 627
Cdd:PRK11809 639 ASAHQKWQAAPMLED-PVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLM 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 628 QANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQelmsspQRFNGYTgelnelslH-PRGTILCISPWNFPLA 706
Cdd:PRK11809 718 EAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVR------DDFDNDT--------HrPLGPVVCISPWNFPLA 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 707 IFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLI 786
Cdd:PRK11809 784 IFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLL 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 787 NRTLATR---GGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAE 863
Cdd:PRK11809 864 QRNLAGRldpQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAE 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 864 LVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEA--LSGYFMPPTAIAIDSISALEKEVFGPILHV 941
Cdd:PRK11809 944 CRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEdwQSGTFVPPTLIELDSFDELKREVFGPVLHV 1023
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 942 IQFKRKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPNYL 1021
Cdd:PRK11809 1024 VRYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1103
|
....*..
gi 395130835 1022 IRLCHER 1028
Cdd:PRK11809 1104 YRLLATR 1110
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
477-1044 |
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: 868.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 477 ANSSFVNRIVDDKAPiselvedpvaksrslldkinkniplpediflpvrknskgfdftnrleRALLQQELAKIESKEWQA 556
Cdd:cd07125 1 ANSSFVNRIFDLEVP-----------------------------------------------LEALADALKAFDEKEWEA 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 557 SPMIAGRKLSRDLLQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMV 636
Cdd:cd07125 34 IPIINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 637 LTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELMSSPQrFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGL 716
Cdd:cd07125 114 LAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPE-LPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAAL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 717 VTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGE 796
Cdd:cd07125 193 AAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 797 IIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDV 876
Cdd:cd07125 273 ILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 877 GPVIDKEALSILKNHVENMRKHHEILYQCTVDDEalSGYFMPPTAIAIDSISALEKEVFGPILHVIQFKRKDLDKVINQI 956
Cdd:cd07125 353 GPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDG--NGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEAIEDI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 957 NQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPNYLIRLCHERTYTVDTTA 1036
Cdd:cd07125 431 NATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLNTTA 510
|
....*...
gi 395130835 1037 AGGNASLM 1044
Cdd:cd07125 511 AGGNPSLL 518
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
36-1041 |
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: 716.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 36 AALDPQQMMAIKTSATKLVQSVRSERkkSTGIDSFLTEYALSSDEGIALMCLAEALLRVPDNATIDNLIKDKLAggdwga 115
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAAP--EGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 116 hrgQSESFFVNATTWALMLTgkvltpekaentltkallkLVNRSSEAVVRKAVDKAMRIMSKQFVMGRTINEALARAKKK 195
Cdd:COG0506 75 ---KSPSFLVNASTWGLMLT-------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 196 EDRGYRYSYDMLGEAALTSADAARYFEAYKEAIISIGEKAdkhsdvYRRPGISIKLSALHPRYSEFQYERVMAELPPKLL 275
Cdd:COG0506 133 RAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG------VDRPGVSVKLSALGPRYSPAQRERVVEELLERLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 276 ALSRLAKDYGIALTIDAEESERLDLSLDVIEKVFTDESLQGWNGFGLAVQSYQKRAFYVLDWVAALARSKQRRIMVRLIK 355
Cdd:COG0506 207 PLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 356 GAYWDSEIKKTQMQGFsEYPVFTRKVFTDVSFQACAKKILTMTDAIYPQFATHNAYSVAMILNLVGGY----RDFEFQCL 431
Cdd:COG0506 287 GAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGERgrppDRFEFQML 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 432 HGMGNELYEQIVPANCYG--IPCRIYAPVGSHEDLLPYLVRRLLENGANSSFVNRIVDDKAPISELVEDPVAKSRSLLDK 509
Cdd:COG0506 366 YGMGEDLQRALAAVDGGRllLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPT 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 510 INKNIPLPEDIFLPVRKNSKGFDFTNRLERALLQQELAKIESKEWQASPMIAGRKLSRDllQTVMSPQQPAYAIGSVQQA 589
Cdd:COG0506 446 PPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAA--AVAVVPAAAAAVVAAAAAA 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 590 TLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQE 669
Cdd:COG0506 524 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAA 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 670 LMSSPQRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEG 749
Cdd:COG0506 604 RAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGG 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 750 VIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSA 829
Cdd:COG0506 684 VLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAAS 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 830 FGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDD 909
Cdd:COG0506 764 ASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLV 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 910 EALSGYFMPPTAIAIDSISALEKEVFGPILHVIQFKRKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYV 989
Cdd:COG0506 844 PGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGG 923
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 395130835 990 NRNMIGAVVGLQPFGGEGLSGTGPKAGGPNYLIRLCHERTYTVDTTAAGGNA 1041
Cdd:COG0506 924 GGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAAA 975
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
519-1024 |
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: 646.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 519 DIFLPVRKNSKGFDFTNRLERALLQQELAKIESKEWQASPMIAGRKLSRDLLQTVMSPQQPAYAIGSVQQATLDDVEVAL 598
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 599 NQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQElmsspqrfn 678
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRD--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 679 gytgELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAG 758
Cdd:TIGR01238 152 ----VLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 759 ETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCS 838
Cdd:TIGR01238 228 ADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 839 ALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEALS--GYF 916
Cdd:TIGR01238 308 ALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACqhGTF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 917 MPPTAIAIDSISALEKEVFGPILHVIQFKRKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGA 996
Cdd:TIGR01238 388 VAPTLFELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGA 467
|
490 500
....*....|....*....|....*...
gi 395130835 997 VVGLQPFGGEGLSGTGPKAGGPNYLIRL 1024
Cdd:TIGR01238 468 VVGVQPFGGQGLSGTGPKAGGPHYLYRL 495
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
539-1031 |
1.74e-176 |
|
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: 524.84 E-value: 1.74e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 539 RALLQQELAKIESKEWQASPMIAGRKL--SRDLlQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEER 616
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEWvdTKER-MVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 617 ASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELMSSPQRFNGYTGELNELSLHPRGTIL 696
Cdd:cd07083 80 ARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 697 CISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLF 776
Cdd:cd07083 160 VISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 777 TGSTDTANLINRTLA---TRGGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRT 853
Cdd:cd07083 240 TGSLETGKKIYEAAArlaPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 854 VELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEalSGYFMPPTAIAIDS--ISALE 931
Cdd:cd07083 320 LERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEG--EGYFVAPTVVEEVPpkARIAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 932 KEVFGPILHVIQFKRKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGT 1011
Cdd:cd07083 398 EEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGT 477
|
490 500
....*....|....*....|
gi 395130835 1012 GPKAGGPNYLIRLCHERTYT 1031
Cdd:cd07083 478 NAKTGGPHYLRRFLEMKAVA 497
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
526-1031 |
5.93e-154 |
|
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: 466.70 E-value: 5.93e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 526 KNSKGFDFTNRLERALLQQELAKIESKEWQASPM-IAGRKLSRDLLQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLA 604
Cdd:cd07124 2 RNEPFTDFADEENRAAFRAALARVREELGREYPLvIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 605 FELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELmsSPQRFNGYTGEL 684
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRL--RGFPVEMVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 685 NELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAA 764
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 765 LVADKRIKAVLFTGSTDTANLINRTLA-TRGGE--IIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALR 841
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYERAAkVQPGQkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 842 VLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEALSGYFMPPTA 921
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 922 IA-IDSISALEK-EVFGPILHVIqfKRKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVG 999
Cdd:cd07124 400 FAdVPPDHRLAQeEIFGPVLAVI--KAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVG 477
|
490 500 510
....*....|....*....|....*....|..
gi 395130835 1000 LQPFGGEGLSGTGPKAGGPNYLIRLCHERTYT 1031
Cdd:cd07124 478 RQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVT 509
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
188-484 |
1.93e-145 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 436.15 E-value: 1.93e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 188 ALARAKKKEDRGYRYSYDMLGEAALTSADAARYFEAYKEAIISIGEKADKHSDVYRrPGISIKLSALHPRYSEFQYERVM 267
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPR-PGISVKLSALHPRYEPLERERVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 268 AELPPKLLALSRLAKDYGIALTIDAEESERLDLSLDVIEKVFTDESLQGWNGFGLAVQSYQKRAFYVLDWVAALARSKQR 347
Cdd:pfam01619 80 AELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 348 RIMVRLIKGAYWDSEIKKTQmQGFSEYPVFTRKVFTDVSFQACAKKILTMTDAIYPQFATHNAYSVAMILNLVGGY---- 423
Cdd:pfam01619 160 PLGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEELgipp 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 395130835 424 RDFEFQCLHGMGNELYEQIVPAncyGIPCRIYAPVGSHEDLLPYLVRRLLENGANSSFVNR 484
Cdd:pfam01619 239 RRFEFQQLYGMGDNLSFALVAA---GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
583-1017 |
9.63e-136 |
|
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: 417.99 E-value: 9.63e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:COG1012 34 LARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSsPQRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMH 742
Cdd:COG1012 114 YAGEARRLYG-ETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 743 QAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLEQVV 822
Cdd:COG1012 193 EAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN---LKRVTLELGGKNPAIVLDDADLDAAV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 823 VDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHH-EI 901
Cdd:COG1012 270 EAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGaEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 902 LYQCTVDDEAlSGYFMPPTAIAI---DSISALEkEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYI 978
Cdd:COG1012 350 LTGGRRPDGE-GGYFVEPTVLADvtpDMRIARE-EIFGPVLSVIPF--DDEEEAIALANDTEYGLAASVFTRDLARARRV 425
|
410 420 430
....*....|....*....|....*....|....*....
gi 395130835 979 RQRVHAGNCYVNRNMIGAVVGlQPFGGEGLSGTGPKAGG 1017
Cdd:COG1012 426 ARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
583-1021 |
4.93e-133 |
|
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: 410.38 E-value: 4.93e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:pfam00171 20 IATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMssPQRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMH 742
Cdd:pfam00171 100 YAGLARRLD--GETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 743 QAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLEQVV 822
Cdd:pfam00171 178 EAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN---LKRVTLELGGKNPLIVLEDADLDAAV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 823 VDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHH-EI 901
Cdd:pfam00171 255 EAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGaKL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 902 LYQCTVDDEalSGYFMPPTAIAI---DSISALEkEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYI 978
Cdd:pfam00171 335 LTGGEAGLD--NGYFVEPTVLANvtpDMRIAQE-EIFGPVLSVIRF--KDEEEAIEIANDTEYGLAAGVFTSDLERALRV 409
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 395130835 979 RQRVHAGNCYVNRNMIGAVVGLqPFGGEGLSGTGpKAGGPNYL 1021
Cdd:pfam00171 410 ARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGL 450
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
595-1032 |
3.00e-128 |
|
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: 396.58 E-value: 3.00e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 595 EVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELMSsP 674
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHG-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 675 QRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLI 754
Cdd:cd07078 80 VIPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 755 PGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLAtrgGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAG 834
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA---ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 835 QRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEALSG 914
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 915 YFMPPTAIAIDSISAL--EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRN 992
Cdd:cd07078 317 YFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 395130835 993 MIGAVVGlQPFGGEGLSGTGpKAGGPNYLIRLCHERTYTV 1032
Cdd:cd07078 395 SVGAEPS-APFGGVKQSGIG-REGGPYGLEEYTEPKTVTI 432
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
526-1022 |
2.41e-127 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 397.38 E-value: 2.41e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 526 KNSKGFDFTNRLERALLQQELAKIESKEWQASPM-IAGRKLSRDLLQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLA 604
Cdd:PRK03137 6 KHEPFTDFSVEENVEAFEEALKKVEKELGQDYPLiIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 605 FELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELmSSPQRFNGYTGEL 684
Cdd:PRK03137 86 FETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKL-ADGKPVESRPGEH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 685 NELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAA 764
Cdd:PRK03137 165 NRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 765 LVADKRIKAVLFTGSTDTANLIN-RTLATRGGE--IIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALR 841
Cdd:PRK03137 245 LVDHPKTRFITFTGSREVGLRIYeRAAKVQPGQiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 842 VLYVQEEVYPRTVELLKGAMAELVVGDPQwLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEalSGYFMPPTA 921
Cdd:PRK03137 325 RAIVHEDVYDEVLEKVVELTKELTVGNPE-DNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDS--KGYFIQPTI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 922 IA-IDSISAL-EKEVFGPILHVIqfKRKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVG 999
Cdd:PRK03137 402 FAdVDPKARImQEEIFGPVVAFI--KAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVG 479
|
490 500
....*....|....*....|...
gi 395130835 1000 LQPFGGEGLSGTGPKAGGPNYLI 1022
Cdd:PRK03137 480 YHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
532-1031 |
1.01e-122 |
|
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: 384.99 E-value: 1.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 532 DFTNRLERALLQQELAKIesKEWQAS---PMIAGRKLSRDLLQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELW 608
Cdd:TIGR01237 8 DFADEENRQAFFKALATV--KEQLGKtypLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 609 SKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELMSSPQRfNGYTGELNELS 688
Cdd:TIGR01237 86 KKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPV-NSREGETNQYV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 689 LHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVAD 768
Cdd:TIGR01237 165 YTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 769 KRIKAVLFTGSTDTANLINRTLA-TRGGE--IIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYV 845
Cdd:TIGR01237 245 PKTSLITFTGSREVGTRIFERAAkVQPGQkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 846 QEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEalSGYFMPPTAIA-I 924
Cdd:TIGR01237 325 HEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDDS--KGYFIGPTIFAdV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 925 DSISAL-EKEVFGPILHVIqfKRKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQPF 1003
Cdd:TIGR01237 403 DRKARLaQEEIFGPVVAFI--RASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPF 480
|
490 500
....*....|....*....|....*...
gi 395130835 1004 GGEGLSGTGPKAGGPNYLIRLCHERTYT 1031
Cdd:TIGR01237 481 GGFKMSGTDSKAGGPDYLALFMQAKTVT 508
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
601-1032 |
6.37e-106 |
|
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: 335.35 E-value: 6.37e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 601 AKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELMSSPQRFNGy 680
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 681 TGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGET 760
Cdd:cd06534 82 PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 761 IGAALVADKRIKAVLFTGSTDTANLINRTLAtrgGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSAL 840
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAA---ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 841 RVLYVQEEVYPRTVELLKGamaelvvgdpqwLSTDVGPvidkealsilknhveNMRKHHEilyqctvddealsgyfmppt 920
Cdd:cd06534 239 SRLLVHESIYDEFVEKLVT------------VLVDVDP---------------DMPIAQE-------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 921 aiaidsisalekEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGl 1000
Cdd:cd06534 272 ------------EIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE- 336
|
410 420 430
....*....|....*....|....*....|..
gi 395130835 1001 QPFGGEGLSGTGpKAGGPNYLIRLCHERTYTV 1032
Cdd:cd06534 337 APFGGVKNSGIG-REGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
583-1016 |
1.49e-99 |
|
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: 322.59 E-value: 1.49e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCrY 662
Cdd:cd07086 26 IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDIC-D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAkkaqelMSSPQRFNGYT--GELNELSL----HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:cd07086 105 YA------VGLSRMLYGLTipSERPGHRLmeqwNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLMHQA----GIPEGVIQLIPGAGEtIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGeiiPLIAETGGQNAMIV 812
Cdd:cd07086 179 VTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG---RVLLELGGNNAIIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 813 DSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHV 892
Cdd:cd07086 255 MDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENMRKHH-EILYQCTVDDEALSGYFMPPTAIAI--DSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHS 969
Cdd:cd07086 335 EIAKSQGgTVLTGGKRIDGGEPGNYVEPTIVTGvtDDARIVQEETFAPILYVIKF--DSLEEAIAINNDVPQGLSSSIFT 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 395130835 970 R-INETVDYIRQR-VHAGNCYVNRNMIGAVVGLqPFGGEGLSGTGPKAG 1016
Cdd:cd07086 413 EdLREAFRWLGPKgSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
583-1018 |
6.70e-92 |
|
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: 301.86 E-value: 6.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07097 28 VGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQelmsspqRFNGYT------GELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:cd07097 108 YAGEAL-------RLSGETlpstrpGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIiplIAETGGQNAMIVDSSA 816
Cdd:cd07097 181 LVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV---QLEMGGKNPLVVLDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 817 LLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMR 896
Cdd:cd07097 258 DLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIAR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 897 KH-HEILYQCTVDDEALSGYFMPPTAIA---IDSISALEkEVFGPILHVIqfKRKDLDKVINQINQTGYGLTLGIHSR-I 971
Cdd:cd07097 338 SEgAKLVYGGERLKRPDEGYYLAPALFAgvtNDMRIARE-EIFGPVAAVI--RVRDYDEALAIANDTEFGLSAGIVTTsL 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 395130835 972 NETVDYIRqRVHAGNCYVNRNMIGavVGLQ-PFGGEGLSGTGPKAGGP 1018
Cdd:cd07097 415 KHATHFKR-RVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGE 459
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
538-1029 |
1.14e-91 |
|
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: 302.58 E-value: 1.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 538 ERALLQQELAKIESKEWQASPMIAGRKLSRDLLQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERA 617
Cdd:cd07123 15 ERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 618 SCLNRFADLLQANM-AELMVLTCREAGKT-WSDGIAEVREAIDFCRYYAKKAQELMSSpQRFNGYTGELNELSLHP-RGT 694
Cdd:cd07123 95 AIFLKAADLLSGKYrYELNAATMLGQGKNvWQAEIDAACELIDFLRFNVKYAEELYAQ-QPLSSPAGVWNRLEYRPlEGF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 695 ILCISPWNFPlAIFTGQVVAGLVTGNCVIAKPAEqTPLIAAYAV-KLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKA 773
Cdd:cd07123 174 VYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 774 VLFTGSTDTANLINRTLATRGGEI--IP-LIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVY 850
Cdd:cd07123 252 LHFTGSTPTFKSLWKQIGENLDRYrtYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLW 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 851 PRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRK--HHEILYQCTVDDEalSGYFMPPTAI-AIDSI 927
Cdd:cd07123 332 PEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSdpEAEIIAGGKCDDS--VGYFVEPTVIeTTDPK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 928 SAL-EKEVFGPILHVIQFKRKDLDKVINQINQTG-YGLTLGIHSR----INETVDYIRQRvhAGNCYVNRNMIGAVVGLQ 1001
Cdd:cd07123 410 HKLmTEEIFGPVLTVYVYPDSDFEETLELVDTTSpYALTGAIFAQdrkaIREATDALRNA--AGNFYINDKPTGAVVGQQ 487
|
490 500
....*....|....*....|....*...
gi 395130835 1002 PFGGEGLSGTGPKAGGPNYLIRLCHERT 1029
Cdd:cd07123 488 PFGGARASGTNDKAGSPLNLLRWVSPRT 515
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
560-1033 |
2.43e-91 |
|
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: 300.42 E-value: 2.43e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 560 IAGRKLSRDLLQTVMSpQQPAY---AIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMV 636
Cdd:cd07131 3 IGGEWVDSASGETFDS-RNPADleeVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 637 LTCREAGKTWSDGIAEVREAIDFCRYYAKKAQelmsspqRFNGYT--GELNE----LSLHPRGTILCISPWNFPLAIFTG 710
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGR-------RLFGETvpSELPNkdamTRRQPIGVVALITPWNFPVAIPSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 711 QVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTL 790
Cdd:cd07131 155 KIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 791 ATRGGeiiPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQ 870
Cdd:cd07131 235 ARPNK---RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 871 WLSTDVGPVIDKEALSILKNHVEnMRKHH--EIL---YQCTVDDEAlSGYFMPPTAIAI--DSISALEKEVFGPILHVIQ 943
Cdd:cd07131 312 DEETDMGPLINEAQLEKVLNYNE-IGKEEgaTLLlggERLTGGGYE-KGYFVEPTVFTDvtPDMRIAQEEIFGPVVALIE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 944 FkrKDLDKVINQINQTGYGLTLGIHSR-INETVdYIRQRVHAGNCYVNRNMIGAVVGLqPFGGEGLSGTGPKAGGPNYLI 1022
Cdd:cd07131 390 V--SSLEEAIEIANDTEYGLSSAIYTEdVNKAF-RARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGTTALD 465
|
490
....*....|.
gi 395130835 1023 RLCHERTYTVD 1033
Cdd:cd07131 466 AFTEWKAVYVD 476
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
583-1012 |
2.13e-87 |
|
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: 288.69 E-value: 2.13e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKT-WSDGIAEVREAIDFCR 661
Cdd:cd07093 10 LAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPiTLARTRDIPRAAANFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 662 YYAKKAQELMSspQRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLM 741
Cdd:cd07093 90 FFADYILQLDG--ESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 742 HQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLEQV 821
Cdd:cd07093 168 NEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN---LKPVSLELGGKNPNIVFADADLDRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 822 VVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKH-HE 900
Cdd:cd07093 245 VDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEgAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 901 ILYQCTVDDEAL--SGYFMPPTAIA-IDSISALEK-EVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVD 976
Cdd:cd07093 325 ILTGGGRPELPDleGGYFVEPTVITgLDNDSRVAQeEIFGPVVTVIPF--DDEEEAIELANDTPYGLAAYVWTRDLGRAH 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 395130835 977 YIRQRVHAGNCYVNRNMigaVVGL-QPFGGEGLSGTG 1012
Cdd:cd07093 403 RVARRLEAGTVWVNCWL---VRDLrTPFGGVKASGIG 436
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
583-1032 |
1.23e-83 |
|
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: 278.72 E-value: 1.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07099 9 LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSSPQRFNG--YTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKL 740
Cdd:cd07099 89 AARNAPRVLAPRKVPTGllMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 741 MHQAGIPEGVIQLIPGAGETiGAALVaDKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLEQ 820
Cdd:cd07099 169 WAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGSVATGRKVMAAAAER---LIPVVLELGGKDPMIVLADADLER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 821 VVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN-MRKHH 899
Cdd:cd07099 244 AAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDaVAKGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 900 EILyqCTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDY 977
Cdd:cd07099 324 KAL--TGGARSNGGGPFYEPTVLTdvPHDMDVMREETFGPVLPVMPV--ADEDEAIALANDSRYGLSASVFSRDLARAEA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 395130835 978 IRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTGpKAGGPNYLIRLCHERTYTV 1032
Cdd:cd07099 400 IARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
583-1012 |
1.62e-83 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 278.16 E-value: 1.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07103 10 IGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQelmsspqRFNGYTGELNE-----LSLH-PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:cd07103 90 FAEEAR-------RIYGRTIPSPApgkriLVIKqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTAnlinRTLATRGGE-IIPLIAETGGqNA-MIVDS 814
Cdd:cd07103 163 LAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVG----KLLMAQAADtVKRVSLELGG-NApFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 815 SALLEQVVVDAVTSAFGSAGQRC-SALRVlYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVE 893
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCvCANRI-YVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 894 NMRKH-HEILyqCTVDDEALSGYFMPPTAIAIDSISAL--EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:cd07103 317 DAVAKgAKVL--TGGKRLGLGGYFYEPTVLTDVTDDMLimNEETFGPVAPIIPF--DTEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 395130835 971 INETVDYIRQRVHAGNCYVNRNMIGAVVglQPFGGEGLSGTG 1012
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLG 432
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
583-1023 |
1.88e-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: 272.55 E-value: 1.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07149 12 IGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSSPQRFNGYTGELNELSLH---PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:cd07149 92 SAEEAKRLAGETIPFDASPGGEGRIGFTirePIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeiiPLIAETGGQNAMIVDSSALLE 819
Cdd:cd07149 172 LLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK-----KVTLELGSNAAVIVDADADLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 820 QVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHV-ENMRKH 898
Cdd:cd07149 247 KAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVeEAVEGG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 899 HEILYQCTVDdealsGYFMPPTAIA-IDSISALEK-EVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVD 976
Cdd:cd07149 327 ARLLTGGKRD-----GAILEPTVLTdVPPDMKVVCeEVFAPVVSLNPF--DTLDEAIAMANDSPYGLQAGVFTNDLQKAL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 395130835 977 YIRQRVHAGNCYVN-----RnmigavVGLQPFGGEGLSGTGPKagGPNYLIR 1023
Cdd:cd07149 400 KAARELEVGGVMINdsstfR------VDHMPYGGVKESGTGRE--GPRYAIE 443
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
583-1016 |
8.26e-79 |
|
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: 265.57 E-value: 8.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFE--LWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFC 660
Cdd:cd07114 10 WARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 661 RYYAKKAQELMSS--PQRFNGYtgeLNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAV 738
Cdd:cd07114 90 RYYAGLADKIEGAviPVDKGDY---LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 739 KLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALL 818
Cdd:cd07114 167 KLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN---LAPVTLELGGKSPNIVFDDADL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 819 EQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKH 898
Cdd:cd07114 244 DAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 899 -HEILY---QCTVDDEAlSGYFMPPTAIAIDSISA--LEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRin 972
Cdd:cd07114 324 gARVLTggeRPSGADLG-AGYFFEPTILADVTNDMriAQEEVFGPVLSVIPF--DDEEEAIALANDSEYGLAAGIWTR-- 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 395130835 973 etvDYIR-----QRVHAGNCYVnrNMIGAVVGLQPFGGEGLSGTGPKAG 1016
Cdd:cd07114 399 ---DLARahrvaRAIEAGTVWV--NTYRALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
560-991 |
5.68e-78 |
|
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: 263.66 E-value: 5.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 560 IAGR-KLSRDLLQTVMSPQQPAyAIGSVQQATLDDVEVALNQAKLAFELWSK-KPVEERASCLNRFADLLQANMAELMVL 637
Cdd:cd07082 6 INGEwKESSGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVANL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 638 TCREAGKTWSDGIAEVREAIDFCRYYAKKAQELMSSPQRFNGYTGELNELSL---HPRGTILCISPWNFPLAIFTGQVVA 714
Cdd:cd07082 85 LMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQvrrEPLGVVLAIGPFNYPLNLTVSKLIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 715 GLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTlatrg 794
Cdd:cd07082 165 ALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ----- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 795 GEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLST 874
Cdd:cd07082 240 HPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 875 DVGPVIDKEALSILKNHVENMRKH-HEILYQctvdDEALSGYFMPPTAIAI--DSISALEKEVFGPILHVIQFkrKDLDK 951
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKgATVLNG----GGREGGNLIYPTLLDPvtPDMRLAWEEPFGPVLPIIRV--NDIEE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 395130835 952 VINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNR 991
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS 433
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
582-991 |
1.11e-76 |
|
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: 259.89 E-value: 1.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCR 661
Cdd:cd07088 25 VVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 662 YYAKKAQElmsspqrfngYTGEL------NE-LSLH--PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPL 732
Cdd:cd07088 105 YMAEWARR----------IEGEIipsdrpNEnIFIFkvPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 733 IAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTAnliNRTLATRGGEIIPLIAETGGQNAMIV 812
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAG---QKIMEAAAENITKVSLELGGKAPAIV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 813 DSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHV 892
Cdd:cd07088 252 MKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENMRKH-HEILYQCTVDDEAlSGYFMPPTAI--AIDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHS 969
Cdd:cd07088 332 ERAVEAgATLLTGGKRPEGE-KGYFYEPTVLtnVRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELANDSEYGLTSYIYT 408
|
410 420
....*....|....*....|..
gi 395130835 970 RINETVDYIRQRVHAGNCYVNR 991
Cdd:cd07088 409 ENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
583-1012 |
2.86e-75 |
|
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: 255.74 E-value: 2.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07145 12 IDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSSPQRFNGYTGELNELSL---HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:cd07145 92 AAEEAKVLRGETIPVDAYEYNERRIAFtvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIiplIAETGGQNAMIVDSSALLE 819
Cdd:cd07145 172 ILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKV---ALELGGSDPMIVLKDADLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 820 QVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN-MRKH 898
Cdd:cd07145 249 RAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDaVEKG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 899 HEILYQCTVDDealsGYFMPPTAIAIDSIS--ALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR-INETV 975
Cdd:cd07145 329 GKILYGGKRDE----GSFFPPTVLENDTPDmiVMKEEVFGPVLPIAKV--KDDEEAVEIANSTEYGLQASVFTNdINRAL 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 395130835 976 dYIRQRVHAGNCYVNR-------NMigavvglqPFGGEGLSGTG 1012
Cdd:cd07145 403 -KVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG 437
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
583-1016 |
4.51e-75 |
|
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: 255.98 E-value: 4.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPV--EERASCLNRFADLLQANMAELMVLTCREAGKT-WSDGIAEVREAIDF 659
Cdd:cd07091 32 ICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIERDRDELAALESLDNGKPlEESAKGDVALSIKC 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKA-----QELMSSPQRFNgYTgelnelSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIA 734
Cdd:cd07091 112 LRYYAGWAdkiqgKTIPIDGNFLA-YT------RREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 735 AYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLiaETGGQNAMIVDS 814
Cdd:cd07091 185 LYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNLKKVTL--ELGGKSPNIVFD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 815 SALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN 894
Cdd:cd07091 263 DADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIES 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 895 MRKHHEILyQCTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRIN 972
Cdd:cd07091 343 GKKEGATL-LTGGERHGSKGYFIQPTVFTdvKDDMKIAKEEIFGPVVTILKF--KTEDEVIERANDTEYGLAAGVFTKDI 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 395130835 973 ETVDYIRQRVHAGNCYVNR-NMIGAVVglqPFGGEGLSGTGPKAG 1016
Cdd:cd07091 420 NKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
583-1016 |
5.98e-75 |
|
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: 255.50 E-value: 5.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFEL--WSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDG-IAEVREAIDF 659
Cdd:cd07142 32 IAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKAQEL----MSSPQRFNGYTgelnelsLH-PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIA 734
Cdd:cd07142 112 FRYYAGWADKIhgmtLPADGPHHVYT-------LHePIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 735 AYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRtLATRgGEIIPLIAETGGQNAMIVDS 814
Cdd:cd07142 185 LLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ-LAAK-SNLKPVTLELGGKSPFIVCE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 815 SALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN 894
Cdd:cd07142 263 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEH 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 895 MRKHHEILyQCTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRIN 972
Cdd:cd07142 343 GKEEGATL-ITGGDRIGSKGYYIQPTIFSdvKDDMKIARDEIFGPVQSILKF--KTVDEVIKRANNSKYGLAAGVFSKNI 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 395130835 973 ETVDYIRQRVHAGNCYVN-RNMIGAVVglqPFGGEGLSGTGPKAG 1016
Cdd:cd07142 420 DTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
593-1010 |
2.31e-74 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 252.19 E-value: 2.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 593 DVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGK-TWsDGIAEVREAIdfcryyAKKAQELM 671
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKpLW-EAQTEVAAMA------GKIDISIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 672 SSPQRfngyTGELNE--------LSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQ 743
Cdd:cd07095 74 AYHER----TGERATpmaqgravLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 744 AGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLiaETGGQNAMIVDSSALLEQVVV 823
Cdd:cd07095 150 AGLPPGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILAL--EMGGNNPLVVWDVADIDAAAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 824 DAVTSAFGSAGQRCSALRVLYV-QEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALS-ILKNHVENMRKHHEI 901
Cdd:cd07095 227 LIVQSAFLTAGQRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAArYLLAQQDLLALGGEP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 902 LYQCTVDDEalSGYFMPPTAIAIDSISAL-EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQ 980
Cdd:cd07095 307 LLAMERLVA--GTAFLSPGIIDVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLA 382
|
410 420 430
....*....|....*....|....*....|
gi 395130835 981 RVHAGNCYVNRNMIGAvVGLQPFGGEGLSG 1010
Cdd:cd07095 383 RIRAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
583-1012 |
3.52e-74 |
|
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: 252.45 E-value: 3.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07106 10 FASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKkaqelMSSPQRfngyTGELNE---LSLH--PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYA 737
Cdd:cd07106 90 TAS-----LDLPDE----VIEDDDtrrVELRrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 738 VKLMHQAgIPEGVIQLIPGAGEtIGAALVADKRIKAVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVDSSAL 817
Cdd:cd07106 161 GELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKV---MASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 818 LEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRK 897
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 898 HH-EILYQCTVDDeaLSGYFMPPTAIA-IDSISAL-EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINET 974
Cdd:cd07106 316 KGaKVLAGGEPLD--GPGYFIPPTIVDdPPEGSRIvDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430
....*....|....*....|....*....|....*...
gi 395130835 975 VDYIRQRVHAGNCYVNRnmIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07106 392 AEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
582-1012 |
4.44e-73 |
|
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: 249.46 E-value: 4.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFELWSKK-PVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFC 660
Cdd:cd07109 9 VFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 661 RYYAKKAQELM--SSPQRfNGYTGelneLSLH-PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYA 737
Cdd:cd07109 89 EYYGGAADKLHgeTIPLG-PGYFV----YTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 738 VKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSAL 817
Cdd:cd07109 164 AELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN---VVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 818 LEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQwLSTDVGPVIDKEALSILKNHVENMRK 897
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVARARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 898 HH-EILYQCTVDDEALS-GYFMPPT---AIAIDSISALEkEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRIN 972
Cdd:cd07109 320 RGaRIVAGGRIAEGAPAgGYFVAPTlldDVPPDSRLAQE-EIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 395130835 973 ETVDYIRQRVHAGNCYVNRNMIGAVVGLqPFGGEGLSGTG 1012
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSGHG 435
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
583-1016 |
8.64e-73 |
|
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: 248.76 E-value: 8.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07101 9 LGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSsPQRFNGYTGEL--NELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKL 740
Cdd:cd07101 89 YARRAERLLK-PRRRRGAIPVLtrTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 741 MHQAGIPEGVIQLIPGAGETIGAALVAdkRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLEQ 820
Cdd:cd07101 168 LIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRR---LIGCSLELGGKNPMIVLEDADLDK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 821 VVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMR-KHH 899
Cdd:cd07101 243 AAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVaKGA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 900 EILYQCTVDDEaLSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDY 977
Cdd:cd07101 323 TVLAGGRARPD-LGPYFYEPTVLTgvTEDMELFAEETFGPVVSIYRV--ADDDEAIELANDTDYGLNASVWTRDGARGRR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 395130835 978 IRQRVHAGNCYVNRNMIGAVVGLQ-PFGGEGLSGTGPKAG 1016
Cdd:cd07101 400 IAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
593-1018 |
2.11e-71 |
|
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: 243.98 E-value: 2.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 593 DVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRyyakkaqELMS 672
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILR-------EAAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 673 SPQRFNG------YTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTP-----LIAayavKLM 741
Cdd:cd07104 74 LPRRPEGeilpsdVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 742 HQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTAnlinRTLATRGGEIIPLIA-ETGGQNAMIVDSSALLEQ 820
Cdd:cd07104 150 EEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIGELAGRHLKKVAlELGGNNPLIVLDDADLDL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 821 VVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMR-KHH 899
Cdd:cd07104 226 AVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVaAGA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 900 EILYQCTVDdealsGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDY 977
Cdd:cd07104 306 RLLTGGTYE-----GLFYQPTVLSdvTPDMPIFREEIFGPVAPVIPF--DDDEEAVELANDTEYGLSAAVFTRDLERAMA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 395130835 978 IRQRVHAGNCYVNRNMI--GAVVglqPFGGEGLSGTGpKAGGP 1018
Cdd:cd07104 379 FAERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
583-1012 |
4.17e-71 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 246.33 E-value: 4.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:PRK09407 45 LATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSsPQRFNGY------TGELNelslHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:PRK09407 125 YARRAPKLLA-PRRRAGAlpvltkTTELR----QPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLMHQAGIPEGVIQLIPGAGETIGAALVAdkRIKAVLFTGSTDTAnlinRTLATRGGE-IIPLIAETGGQNAMIVDSS 815
Cdd:PRK09407 200 AVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATG----RVLAEQAGRrLIGFSLELGGKNPMIVLDD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 816 ALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENM 895
Cdd:PRK09407 274 ADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 896 RKHheilyQCTVddeaLSG---------YFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLT 964
Cdd:PRK09407 354 VAK-----GATV----LAGgkarpdlgpLFYEPTVLTgvTPDMELAREETFGPVVSVYPV--ADVDEAVERANDTPYGLN 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 395130835 965 LGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQ-PFGGEGLSGTG 1012
Cdd:PRK09407 423 ASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
594-1012 |
1.04e-70 |
|
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: 241.98 E-value: 1.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 594 VEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELMsS 673
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFL-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 674 PQRFNGYTGElNELSLHPRGTILCISPWNFPLAiftgQV----VAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEG 749
Cdd:cd07100 80 DEPIETDAGK-AYVRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 750 VIQLIPGAGETIgAALVADKRIKAVLFTGStdtanlinrtlaTRGGEIIPLIA---------ETGGQNAMIVDSSALLEQ 820
Cdd:cd07100 155 VFQNLLIDSDQV-EAIIADPRVRGVTLTGS------------ERAGRAVAAEAgknlkksvlELGGSDPFIVLDDADLDK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 821 VVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKH-H 899
Cdd:cd07100 222 AVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAgA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 900 EILYQCTVDDEAlsGYFMPPTAIA-IDSIS-ALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDY 977
Cdd:cd07100 302 TLLLGGKRPDGP--GAFYPPTVLTdVTPGMpAYDEELFGPVAAVIKV--KDEEEAIALANDSPFGLGGSVFTTDLERAER 377
|
410 420 430
....*....|....*....|....*....|....*
gi 395130835 978 IRQRVHAGNCYVNRnMIGAVVGLqPFGGEGLSGTG 1012
Cdd:cd07100 378 VARRLEAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
587-1010 |
4.45e-70 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 242.17 E-value: 4.45e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 587 QQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIdfcryyAKK 666
Cdd:PRK09457 32 NDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMI------NKI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 667 AqelmSSPQRFNGYTGELNE--------LSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAV 738
Cdd:PRK09457 106 A----ISIQAYHERTGEKRSemadgaavLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 739 KLMHQAGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLiaETGGQNAMIVDSSALL 818
Cdd:PRK09457 182 KLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILAL--EMGGNNPLVIDEVADI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 819 EQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYP-RTVELLKGAMAELVVG----DPQWLstdVGPVID-KEALSILKNHV 892
Cdd:PRK09457 259 DAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVGrwdaEPQPF---MGAVISeQAAQGLVAAQA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENMRKHHEILYQCTVDDEALSgyFMPPTAIAIDSISAL-EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRI 971
Cdd:PRK09457 336 QLLALGGKSLLEMTQLQAGTG--LLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDFDEAIRLANNTRFGLSAGLLSDD 411
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 395130835 972 NETVDYIRQRVHAGncYVNRN--MIGAvVGLQPFGGEGLSG 1010
Cdd:PRK09457 412 REDYDQFLLEIRAG--IVNWNkpLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
582-1016 |
1.05e-69 |
|
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: 240.03 E-value: 1.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDG-IAEVREAIDFC 660
Cdd:cd07115 9 LIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDVPRAADTF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 661 RYYAKKAQELMSS--PQRfngyTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAV 738
Cdd:cd07115 89 RYYAGWADKIEGEviPVR----GPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 739 KLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLAtrgGEIIPLIAETGGQNAMIVDSSALL 818
Cdd:cd07115 165 ELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA---GNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 819 EQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKH 898
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 899 HEILyQCTVDDEALSGYFMPPTAIAI----DSISalEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINET 974
Cdd:cd07115 322 GARL-LTGGKRPGARGFFVEPTIFAAvppeMRIA--QEEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 395130835 975 VDYIRQRVHAGNCYVnrNMIGAVVGLQPFGGEGLSGTGPKAG 1016
Cdd:cd07115 397 AHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
582-1032 |
2.03e-69 |
|
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: 239.18 E-value: 2.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALnqaKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCR 661
Cdd:cd07146 11 VVGTVPAGTEEALREAL---ALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 662 YYAKKAQ----ELMSSP-----QRFNGYTgeLNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPL 732
Cdd:cd07146 88 FAAAEALrddgESFSCDltangKARKIFT--LRE----PLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 733 IAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeiiPLIAETGGQNAMIV 812
Cdd:cd07146 162 SAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK-----RQLLELGGNDPLIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 813 DSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHV 892
Cdd:cd07146 237 MDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENmrkhheilyqcTVDDEA-------LSGYFMPPTaiAIDSIS----ALEKEVFGPILHVIQFkrKDLDKVINQINQTGY 961
Cdd:cd07146 317 EE-----------AIAQGArvllgnqRQGALYAPT--VLDHVPpdaeLVTEETFGPVAPVIRV--KDLDEAIAISNSTAY 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 395130835 962 GLTLGIHSRINETVDYIRQRVHAGNCYVNrNMIGAVVGLQPFGGEGLSGTGPKAGGPNYLIRLCHERTYTV 1032
Cdd:cd07146 382 GLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
583-1017 |
5.53e-69 |
|
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: 238.65 E-value: 5.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07130 25 IARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 yakkAQELmsSPQrFNGYT--GELNELSL----HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:cd07130 105 ----AVGL--SRQ-LYGLTipSERPGHRMmeqwNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLM----HQAGIPEGVIQLIPGAGEtIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIpliAETGGQNAMIV 812
Cdd:cd07130 178 VTKIVarvlEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSL---LELGGNNAIIV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 813 DSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHV 892
Cdd:cd07130 254 MEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENMRKHH-EILYQCTVDDEalSGYFMPPTAIAIDS-ISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:cd07130 334 EEAKSQGgTVLFGGKVIDG--PGNYVEPTIVEGLSdAPIVKEETFAPILYVLKF--DTLEEAIAWNNEVPQGLSSSIFTT 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 395130835 971 -INETVDYIRQRvhAGNC-YVNRNM--IGAVVGlQPFGGEGLSGTGPKAGG 1017
Cdd:cd07130 410 dLRNAFRWLGPK--GSDCgIVNVNIgtSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
583-1012 |
1.73e-68 |
|
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: 236.95 E-value: 1.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07094 12 IGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSSPQRFNGYTGELNELSL---HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:cd07094 92 AAEEAERIRGEEIPLDATQGSDNRLAWtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLatrGGEIIPLiaETGGQNAMIVDSSALLE 819
Cdd:cd07094 172 ILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA---GGKRIAL--ELGGNAPVIVDRDADLD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 820 QVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENmrkhh 899
Cdd:cd07094 247 AAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVEE----- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 900 eilyqcTVDDEA-------LSGYFMPPTAIAIDSISAL--EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:cd07094 322 ------AVEAGArllcggeRDGALFKPTVLEDVPRDTKlsTEETFGPVVPIIRY--DDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 395130835 971 INETVDYIRQRVHAGNCYVNRNMIgAVVGLQPFGGEGLSGTG 1012
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
583-1012 |
6.23e-68 |
|
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: 235.57 E-value: 6.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFEL--WSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIA-EVREAIDF 659
Cdd:cd07112 15 LAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAvDVPSAANT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKAQELM--SSPqrfngyTGElNELSL---HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIA 734
Cdd:cd07112 95 FRWYAEAIDKVYgeVAP------TGP-DALALitrEPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 735 AYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTAnlinRTLATRGGE--IIPLIAETGGQNAMIV 812
Cdd:cd07112 168 LRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVG----RRFLEYSGQsnLKRVWLECGGKSPNIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 813 -DSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNH 891
Cdd:cd07112 244 fADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 892 VENMRKHH-EILYQCTVDDEALSGYFMPPTAIA-IDSISAL-EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIH 968
Cdd:cd07112 324 IESGKAEGaRLVAGGKRVLTETGGFFVEPTVFDgVTPDMRIaREEIFGPVLSVITF--DSEEEAVALANDSVYGLAASVW 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 395130835 969 SRINETVDYIRQRVHAGNCYVnrNMIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07112 402 TSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
583-1012 |
2.21e-67 |
|
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: 233.81 E-value: 2.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07107 10 LARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQEL--MSSPqrfngYTGELNELSLH-PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:cd07107 90 FAGLVTELkgETIP-----VGGRNLHYTLRePYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMHQAgIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLE 819
Cdd:cd07107 165 LAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG---IKHVTLELGGKNALIVFPDADPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 820 QVVVDAVTSA-FGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKH 898
Cdd:cd07107 241 AAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 899 HEILYQCTV--DDEALS-GYFMPPTAIA-IDSISALEK-EVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINE 973
Cdd:cd07107 321 GARLVTGGGrpEGPALEgGFYVEPTVFAdVTPGMRIAReEIFGPVLSVLRW--RDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 395130835 974 TVDYIRQRVHAGNCYVN---RNMIGAvvglqPFGGEGLSGTG 1012
Cdd:cd07107 399 QAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
583-1015 |
2.47e-67 |
|
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: 233.79 E-value: 2.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGK---TWSDGiaEVREAIDF 659
Cdd:cd07108 10 IGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNalrTQARP--EAAVLADL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKAQELmsspqrfNGYTGELNELSLH-----PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIA 734
Cdd:cd07108 88 FRYFGGLAGEL-------KGETLPFGPDVLTytvrePLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 735 AYAVKLMHQAgIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDS 814
Cdd:cd07108 161 LLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR---LIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 815 SALLEQVVVDAVTSA-FGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVE 893
Cdd:cd07108 237 DADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 894 NMRKHHEilyqCTVDDEALS--------GYFMPPTAIA-IDSISAL-EKEVFGPILHVIQFkrKDLDKVINQINQTGYGL 963
Cdd:cd07108 317 LGLSTSG----ATVLRGGPLpgegpladGFFVQPTIFSgVDNEWRLaREEIFGPVLCAIPW--KDEDEVIAMANDSHYGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 395130835 964 TLGIHSRINETVDYIRQRVHAGNCYVNRNMiGAVVGlQPFGGEGLSGTGPKA 1015
Cdd:cd07108 391 AAYVWTRDLGRALRAAHALEAGWVQVNQGG-GQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
586-1035 |
2.15e-66 |
|
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: 230.68 E-value: 2.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 586 VQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAK 665
Cdd:cd07150 15 VAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 666 KAQ----ELMSSpqrfnGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLM 741
Cdd:cd07150 95 ECRrvrgETLPS-----DSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 742 HQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTAnlinRTLATR-GGEIIPLIAETGGQNAMIVDSSALLEQ 820
Cdd:cd07150 170 EEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKaGRHLKKITLELGGKNPLIVLADADLDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 821 VVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMR-KHH 899
Cdd:cd07150 246 AVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVaKGA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 900 EILYQCTVDdealsGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDY 977
Cdd:cd07150 326 KLLTGGKYD-----GNFYQPTVLTdvTPDMRIFREETFGPVTSVIPA--KDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 978 IRQRVHAGNCYVNRNMI--GAVVglqPFGGEGLSGTGpKAGGPNYLirlcHERTYTVDTT 1035
Cdd:cd07150 399 LAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSM----EEFTELKWIT 450
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
583-1012 |
7.51e-65 |
|
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: 227.40 E-value: 7.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVR---EAIDF 659
Cdd:cd07085 29 IARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLrglEVVEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 cryyAKKAQELMSSPQRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:cd07085 109 ----ACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMHQAGIPEGVIQLIPGAGETIGAaLVADKRIKAVLFTGSTDTANLINRTLATRGGEIIpliAETGGQNAMIVDSSALLE 819
Cdd:cd07085 185 LLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQ---ALGGAKNHAVVMPDADLE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 820 QVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVE------ 893
Cdd:cd07085 261 QTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIEsgveeg 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 894 -----NMRKHheilyqcTVDDEAlSGYFMPPTAIA---IDSiSALEKEVFGPILHVIqfKRKDLDKVINQINQTGYGLTL 965
Cdd:cd07085 341 aklvlDGRGV-------KVPGYE-NGNFVGPTILDnvtPDM-KIYKEEIFGPVLSIV--RVDTLDEAIAIINANPYGNGA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 395130835 966 GIHSRINETVDYIRQRVHAGNCYVNrnmIG-AV-VGLQPFGGEGLSGTG 1012
Cdd:cd07085 410 AIFTRSGAAARKFQREVDAGMVGIN---VPiPVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
583-1016 |
8.00e-65 |
|
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: 227.41 E-value: 8.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFEL-WSKK-PVEERASCLNRFADLLQANMAELMVLTCREAGKT--WSDGIaEVREAID 658
Cdd:cd07143 35 ITKIAEATEADVDIAVEVAHAAFETdWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTfgTAKRV-DVQASAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 659 FCRYYAKKA-----QELMSSPQRFNgYTgelnelsLH-PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPL 732
Cdd:cd07143 114 TFRYYGGWAdkihgQVIETDIKKLT-YT-------RHePIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 733 IAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLiaETGGQNAMIV 812
Cdd:cd07143 186 SALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNLKKVTL--ELGGKSPNIV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 813 DSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHV 892
Cdd:cd07143 264 FDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENMRKHHEILyQCTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:cd07143 344 ESGKAEGATV-ETGGKRHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKF--KTEEEAIKRANDSTYGLAAAVFTN 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 395130835 971 INETVDYIRQRVHAGNCYVN-RNMIGAVVglqPFGGEGLSGTGPKAG 1016
Cdd:cd07143 421 NINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
582-1016 |
2.87e-64 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 226.24 E-value: 2.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFE--LWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDG-IAEVREAID 658
Cdd:PLN02766 48 VIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGkAVDIPAAAG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 659 FCRYYAKKAQ----ELMSSPQRFNGYTgeLNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIA 734
Cdd:PLN02766 128 LLRYYAGAADkihgETLKMSRQLQGYT--LKE----PIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 735 AYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLiaETGGQNAMIVDS 814
Cdd:PLN02766 202 LFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKQVSL--ELGGKSPLLIFD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 815 SALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN 894
Cdd:PLN02766 280 DADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEH 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 895 MRKHHEILY---QCTVDdealSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHS 969
Cdd:PLN02766 360 GKREGATLLtggKPCGD----KGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAGIVT 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 395130835 970 RINETVDYIRQRVHAG----NCYVnrnmigAVVGLQPFGGEGLSGTGPKAG 1016
Cdd:PLN02766 434 KDLDVANTVSRSIRAGtiwvNCYF------AFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
583-1016 |
4.18e-64 |
|
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: 225.30 E-value: 4.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFEL---WSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDG-IAEVREAID 658
Cdd:cd07141 35 ICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 659 FCRYYAKKAQELMSS--PQRFNGYTGELNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:cd07141 115 VLRYYAGWADKIHGKtiPMDGDFFTYTRHE----PVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLiaETGGQNAMIVDSSA 816
Cdd:cd07141 191 LASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRVTL--ELGGKSPNIVFADA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 817 LLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVY----PRTVELLKgamaELVVGDPQWLSTDVGPVIDKEALSILKNHV 892
Cdd:cd07141 269 DLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYdefvKRSVERAK----KRVVGNPFDPKTEQGPQIDEEQFKKILELI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENMRKHHEILyQCTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:cd07141 345 ESGKKEGAKL-ECGGKRHGDKGYFIQPTVFSdvTDDMRIAKEEIFGPVQQIFKF--KTIDEVIERANNTTYGLAAAVFTK 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 395130835 971 INETVDYIRQRVHAGNCYVNrnmIGAVVGLQ-PFGGEGLSGTGPKAG 1016
Cdd:cd07141 422 DIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
583-1019 |
9.85e-64 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 222.94 E-value: 9.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRy 662
Cdd:cd07152 4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 yakKAQELMSSPQrfngytGEL-----NELSLH---PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIA 734
Cdd:cd07152 83 ---EAAGLPTQPQ------GEIlpsapGRLSLArrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 735 AYAV-KLMHQAGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLINRtLATRGGEIIPLiaETGGQNAMIVD 813
Cdd:cd07152 154 GVVIaRLFEEAGLPAGVLHVLPGGADA-GEALVEDPNVAMISFTGSTAVGRKVGE-AAGRHLKKVSL--ELGGKNALIVL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 814 SSALLEQVVVDAVTSAFGSAGQRC-SALRVLyVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDkealsilknhv 892
Cdd:cd07152 230 DDADLDLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLIN----------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 893 ENMRKHHEILYQCTVDDEA-------LSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGL 963
Cdd:cd07152 298 ARQLDRVHAIVDDSVAAGArleaggtYDGLFYRPTVLSgvKPGMPAFDEEIFGPVAPVTVF--DSDEEAVALANDTEYGL 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 395130835 964 TLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVgLQPFGGEGLSGTGPKAGGPN 1019
Cdd:cd07152 376 SAGIISRDVGRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGPA 430
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
592-1012 |
1.18e-63 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 224.57 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 592 DDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQ--- 668
Cdd:PLN02278 62 AETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKrvy 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 669 -ELMSSPQRfngyTGELneLSLH-PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGI 746
Cdd:PLN02278 142 gDIIPSPFP----DRRL--LVLKqPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 747 PEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVDAV 826
Cdd:PLN02278 216 PPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKL---MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 827 TSAFGSAGQRC-SALRVLyVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN-MRKHHEILyq 904
Cdd:PLN02278 293 ASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDaVSKGAKVL-- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 905 CTVDDEALSGYFMPPTAIA---IDSISALEkEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQR 981
Cdd:PLN02278 370 LGGKRHSLGGTFYEPTVLGdvtEDMLIFRE-EVFGPVAPLTRF--KTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEA 446
|
410 420 430
....*....|....*....|....*....|.
gi 395130835 982 VHAGNCYVNRNMIGAVVGlqPFGGEGLSGTG 1012
Cdd:PLN02278 447 LEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
583-1016 |
2.28e-63 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 224.69 E-value: 2.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFEL--WSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGI-AEVREAIDF 659
Cdd:PLN02466 86 IAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMFARL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKAQEL--MSSPQRFNGYTGELNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYA 737
Cdd:PLN02466 166 FRYYAGWADKIhgLTVPADGPHHVQTLHE----PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 738 VKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLInRTLATRgGEIIPLIAETGGQNAMIVDSSAL 817
Cdd:PLN02466 242 AKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIV-LELAAK-SNLKPVTLELGGKSPFIVCEDAD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 818 LEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKE----ALSILKNHVE 893
Cdd:PLN02466 320 VDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEqfekILRYIKSGVE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 894 NmrkhhEILYQCTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRI 971
Cdd:PLN02466 400 S-----GATLECGGDRFGSKGYYIQPTVFSnvQDDMLIAQDEIFGPVQSILKF--KDLDEVIRRANNTRYGLAAGVFTQN 472
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 395130835 972 NETVDYIRQRVHAGNCYVN-RNMIGAVVglqPFGGEGLSGTGPKAG 1016
Cdd:PLN02466 473 LDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
583-1012 |
2.83e-63 |
|
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: 221.82 E-value: 2.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIA-EVREAIDFCR 661
Cdd:cd07092 10 IATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdELPGAVDNFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 662 YYAKKAQEL--MSSPQRFNGYTgelNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:cd07092 90 FFAGAARTLegPAAGEYLPGHT---SMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMhQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLAtrgGEIIPLIAETGGQNAMIVDSSALLE 819
Cdd:cd07092 167 LA-AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA---DTLKRVHLELGGKAPVIVFDDADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 820 QVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHH 899
Cdd:cd07092 243 AAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 900 EILYQCTVDDEalSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGI----HSRINE 973
Cdd:cd07092 323 RVLTGGRRAEG--PGYFYEPTVVAgvAQDDEIVQEEIFGPVVTVQPF--DDEDEAIELANDVEYGLASSVwtrdVGRAMR 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 395130835 974 TVdyirQRVHAGNCYVNRNMIgaVVGLQPFGGEGLSGTG 1012
Cdd:cd07092 399 LS----ARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
583-1016 |
6.45e-63 |
|
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: 221.90 E-value: 6.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFE-LWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTW-SDGIAEVREAIDFC 660
Cdd:cd07144 36 IASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 661 RYYAKKA-----QELMSSPQRFnGYTgelnelsLH-PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIA 734
Cdd:cd07144 116 RYYAGWAdkiqgKTIPTSPNKL-AYT-------LHePYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 735 AYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVDS 814
Cdd:cd07144 188 LYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV---MKAAAQNLKAVTLECGGKSPALVFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 815 SALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAE-LVVGDPQWLSTDVGPVIDKEALSILKNHVE 893
Cdd:cd07144 265 DADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQVSKTQYDRVLSYIE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 894 NMRKHHE-ILYQCTVDDEALS-GYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHS 969
Cdd:cd07144 345 KGKKEGAkLVYGGEKAPEGLGkGYFIPPTIFTdvPQDMRIVKEEIFGPVVVISKF--KTYEEAIKKANDTTYGLAAAVFT 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 395130835 970 RINETVDYIRQRVHAGNCYVNR-NM--IGAvvglqPFGGEGLSGTGPKAG 1016
Cdd:cd07144 423 KDIRRAHRVARELEAGMVWINSsNDsdVGV-----PFGGFKMSGIGRELG 467
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
582-1012 |
3.16e-62 |
|
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: 219.88 E-value: 3.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFE--LWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDF 659
Cdd:cd07119 25 VIATVPEGTAEDAKRAIAAARRAFDsgEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYA----KKAQELMSSPQRFNGYTgeLNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAA 735
Cdd:cd07119 105 FRYYAglatKETGEVYDVPPHVISRT--VRE----PVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 736 YAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLAtrgGEIIPLIAETGGQNAMIVDSS 815
Cdd:cd07119 179 ALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA---GNVKKVALELGGKNPNIVFAD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 816 ALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVE-N 894
Cdd:cd07119 256 ADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQlG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 895 MRKHHEILY--QCTVDDEALSGYFMPPTAIA-IDSISALEK-EVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:cd07119 336 KEEGARLVCggKRPTGDELAKGYFVEPTIFDdVDRTMRIVQeEIFGPVLTVERF--DTEEEAIRLANDTPYGLAGAVWTK 413
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 395130835 971 INETVDYIRQRVHAGNCYVNRnmIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07119 414 DIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
588-1016 |
3.98e-62 |
|
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: 218.75 E-value: 3.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 588 QATLDDVEVALNQAKLAFEL--WSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAK 665
Cdd:cd07118 15 EGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAAS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 666 KAQELMSspQRFNGYTGELNELSLH-PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQA 744
Cdd:cd07118 95 LARTLHG--DSYNNLGDDMLGLVLRePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 745 GIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVD 824
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAI---AAAAARNLKKVSLELGGKNPQIVFADADLDAAADA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 825 AVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQ 904
Cdd:cd07118 250 VVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 905 CTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRV 982
Cdd:cd07118 330 GGERLASAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRI 407
|
410 420 430
....*....|....*....|....*....|....
gi 395130835 983 HAGNCYVNRNMIGAVVglQPFGGEGLSGTGPKAG 1016
Cdd:cd07118 408 RAGTVWVNTFLDGSPE--LPFGGFKQSGIGRELG 439
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
583-1012 |
4.12e-62 |
|
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: 219.04 E-value: 4.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWS-KKPVEERASCLNRFADLLQANMAELMVLTCREAGKT-WSDGIAEVREAIDFC 660
Cdd:cd07089 10 IGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPvMTARAMQVDGPIGHL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 661 RYYAKKAQEL-----MSSPQRFNGYTGELneLSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAA 735
Cdd:cd07089 90 RYFADLADSFpwefdLPVPALRGGPGRRV--VRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 736 YAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVDSS 815
Cdd:cd07089 168 LLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRI---MAQAAATLKRVLLELGGKSANIVLDD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 816 ALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENM 895
Cdd:cd07089 245 ADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIARG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 896 RKH-HEILYQCTVDDEALSGYFMPPTAIAI---DSISALEkEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRI 971
Cdd:cd07089 325 RDEgARLVTGGGRPAGLDKGFYVEPTLFADvdnDMRIAQE-EIFGPVLVVIPY--DDDDEAVRIANDSDYGLSGGVWSAD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 395130835 972 NETVDYIRQRVHAGNCYVNrnmigAVVGLQ---PFGGEGLSGTG 1012
Cdd:cd07089 402 VDRAYRVARRIRTGSVGIN-----GGGGYGpdaPFGGYKQSGLG 440
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
583-1012 |
2.83e-61 |
|
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: 216.92 E-value: 2.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFE-LWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKT--WSDGIaEVREAIDF 659
Cdd:cd07113 28 IASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSihLSRAF-EVGQSANF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYA----KKAQELMS----SPQ--RFNGYTgeLNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQ 729
Cdd:cd07113 107 LRYFAgwatKINGETLApsipSMQgeRYTAFT--RRE----PVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 730 TPLIAAYAVKLMHQAGIPEGVIQLIPGAGEtIGAALVADKRIKAVLFTGSTDTANLINRTlATRGGEIIPLiaETGGQNA 809
Cdd:cd07113 181 TPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ-AASDLTRVTL--ELGGKNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 810 MIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILK 889
Cdd:cd07113 257 AAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPHFDKVC 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 890 NHVENMR-KHHEILYqctvDDEALS--GYFMPPTAIAIDSISA--LEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLT 964
Cdd:cd07113 337 SYLDDARaEGDEIVR----GGEALAgeGYFVQPTLVLARSADSrlMREETFGPVVSFVPY--EDEEELIQLINDTPFGLT 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 395130835 965 LGIHSR-INETVDYIrQRVHAGNCYVN-RNMIGAVVglqPFGGEGLSGTG 1012
Cdd:cd07113 411 ASVWTNnLSKALRYI-PRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
583-991 |
4.80e-61 |
|
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: 215.57 E-value: 4.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07102 9 IAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSsPQRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMH 742
Cdd:cd07102 89 MISIAEEALA-DIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 743 QAGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLINRTLAtrgGEIIPLIAETGGQNAMIVDSSALLEQVV 822
Cdd:cd07102 168 EAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAA---GRFIKVGLELGGKDPAYVRPDADLDAAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 823 VDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRK----- 897
Cdd:cd07102 244 ESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAkgara 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 898 ----HHEilyqctvDDEALSGYFMPPTAIA-ID-SISALEKEVFGPILHVIqfKRKDLDKVINQINQTGYGLTLGIHSRI 971
Cdd:cd07102 324 lidgALF-------PEDKAGGAYLAPTVLTnVDhSMRVMREETFGPVVGIM--KVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420
....*....|....*....|
gi 395130835 972 NETVDYIRQRVHAGNCYVNR 991
Cdd:cd07102 395 IARAEALGEQLETGTVFMNR 414
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
582-1018 |
7.67e-61 |
|
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: 216.11 E-value: 7.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTwsdgIAEVRE-----A 656
Cdd:cd07111 49 VLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKP----IRESRDcdiplV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 657 IDFCRYYAKKAQELMSSpqrFNGYtgelnelslHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:cd07111 125 ARHFYHHAGWAQLLDTE---LAGW---------KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLMHQAGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEiipLIAETGGQNAMIVDSSA 816
Cdd:cd07111 193 FAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTGKK---LSLELGGKSPFIVFDDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 817 LLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMR 896
Cdd:cd07111 269 DLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 897 KHHEILYQcTVDDEALSGYFMPPTAIA-IDSISAL-EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHS-RINE 973
Cdd:cd07111 349 AEGADVFQ-PGADLPSKGPFYPPTLFTnVPPASRIaQEEIFGPVLVVLTF--RTAKEAVALANNTPYGLAASVWSeNLSL 425
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 395130835 974 TVDyIRQRVHAGNCYVN-RNMIGAVVglqPFGGEGLSGTGpKAGGP 1018
Cdd:cd07111 426 ALE-VALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGK 466
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
582-1012 |
8.91e-60 |
|
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: 212.16 E-value: 8.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCR 661
Cdd:cd07090 9 VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 662 YYAKKAQELmsspqrfNGYTGELNELSL-----HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:cd07090 89 YYAGLAPTL-------SGEHVPLPGGSFaytrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLMHQAGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVDSSA 816
Cdd:cd07090 162 LAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKV---MSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 817 LLEQVVVDAVTSAFGSAGQRCS-ALRVlYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENM 895
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSnGTRV-FVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 896 RKH-HEILY---QCTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHS 969
Cdd:cd07090 317 KQEgAKVLCggeRVVPEDGLENGFYVSPCVLTdcTDDMTIVREEIFGPVMSILPF--DTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 395130835 970 RINETVDYIRQRVHAGNCYVNRNMIGAVvgLQPFGGEGLSGTG 1012
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPV--EVPFGGYKQSGFG 435
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
582-1012 |
1.19e-59 |
|
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: 211.98 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAG--KTWSDGiAEVREAIDF 659
Cdd:cd07138 26 VIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGapITLARA-AQVGLGIGH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKAQElMSSPQRFNGYTgelneLSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:cd07138 105 LRAAADALKD-FEFEERRGNSL-----VVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTlatrGGEIIPLIA-ETGGQNAMIVDSSALL 818
Cdd:cd07138 179 ILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA----AADTVKRVAlELGGKSANIILDDADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 819 EQVVVDAVTSAFGSAGQRCSAL-RVLyVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALsilkNHVENMrk 897
Cdd:cd07138 255 EKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQF----DRVQGY-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 898 hheIlyQCTVDD------------EALS-GYFMPPTAIA---IDSISALEkEVFGPILHVIQFkrKDLDKVINQINQTGY 961
Cdd:cd07138 328 ---I--QKGIEEgarlvaggpgrpEGLErGYFVKPTVFAdvtPDMTIARE-EIFGPVLSIIPY--DDEDEAIAIANDTPY 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 395130835 962 GLTLGIHSRINETVDYIRQRVHAGNCYVNrnmiGAVVGLQ-PFGGEGLSGTG 1012
Cdd:cd07138 400 GLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
589-1012 |
2.46e-59 |
|
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: 211.82 E-value: 2.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 589 ATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLtcreagKTWSDGIAeVRE--------AIDFC 660
Cdd:cd07559 35 STAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA------ETLDNGKP-IREtlaadiplAIDHF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 661 RYYAK--KAQElmsspqrfnGYTGELNE--LSLH---PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLI 733
Cdd:cd07559 108 RYFAGviRAQE---------GSLSEIDEdtLSYHfhePLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 734 AAYAVKLMHQAgIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVD 813
Cdd:cd07559 179 ILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN---LIPVTLELGGKSPNIFF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 814 SSALLEQV-VVDAVTSAF-GSA---GQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSIL 888
Cdd:cd07559 255 DDAMDADDdFDDKAEEGQlGFAfnqGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 889 KNHVENMRKH-HEILY--QCTVDDEALSGYFMPPTAIAI--DSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGL 963
Cdd:cd07559 335 LSYVDIGKEEgAEVLTggERLTLGGLDKGYFYEPTLIKGgnNDMRIFQEEIFGPVLAVITF--KDEEEAIAIANDTEYGL 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 395130835 964 TLGIHSR-INETVDYIRQrVHAG----NCYvnrNMIGAVVglqPFGGEGLSGTG 1012
Cdd:cd07559 413 GGGVWTRdINRALRVARG-IQTGrvwvNCY---HQYPAHA---PFGGYKKSGIG 459
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
571-1012 |
8.91e-58 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 207.16 E-value: 8.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 571 QTVMSPQQpAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGI 650
Cdd:TIGR03374 18 QPVYNPAT-GEVILEIAEASAEQVDAAVRAADAAFAEWGQTTPKARAECLLKLADVIEENAQVFAELESRNCGKPLHSVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 651 A-EVREAIDFCRYYAKKAQEL--MSSPQRFNGYTGELNElslHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPA 727
Cdd:TIGR03374 97 NdEIPAIVDVFRFFAGAARCLsgLAAGEYLEGHTSMIRR---DPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 728 EQTPLIAAYAVKLMHQAgIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQ 807
Cdd:TIGR03374 174 EITPLTALKLAELAKDI-FPAGVVNILFGRGKTVGDPLTGHEKVRMVSLTGSIATGEHI---LSHTAPSIKRTHMELGGK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 808 NAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSI 887
Cdd:TIGR03374 250 APVIVFDDADIDAVVEGVRTFGFYNAGQDCTAACRIYAQRGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLER 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 888 LKNHVENMRKHHEILYQCTVDDEALSGYFMPPTAIA----IDSIsaLEKEVFGPILHVIQFkrKDLDKVINQINQTGYGL 963
Cdd:TIGR03374 330 VMKAVEEAKALGHIKVITGGEKRKGNGYYFAPTLLAgakqDDAI--VQKEVFGPVVSITSF--DDEEQVVNWANDSQYGL 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 395130835 964 TLGIHSRINETVDYIRQRVHAGNCYVNRNMIgaVVGLQPFGGEGLSGTG 1012
Cdd:TIGR03374 406 ASSVWTKDVGRAHRLSARLQYGCTWVNTHFM--LVSEMPHGGQKLSGYG 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
583-1012 |
1.93e-57 |
|
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: 205.62 E-value: 1.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFcry 662
Cdd:cd07151 23 LAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAI--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 yakkAQELMSSPQRFNG------YTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTP----- 731
Cdd:cd07151 100 ----TREAATFPLRMEGrilpsdVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitggl 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 732 LIAayavKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDtanlINRTLATRGGEIIPLIA-ETGGQNAM 810
Cdd:cd07151 176 LLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTP----VGRHIGELAGRHLKKVAlELGGNNPF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 811 IVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKN 890
Cdd:cd07151 248 VVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 891 HVENmrkhheilyqcTVDDEA-------LSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGY 961
Cdd:cd07151 328 KIEQ-----------AVEEGAtllvggeAEGNVLEPTVLSdvTNDMEIAREEIFGPVAPIIKA--DDEEEALELANDTEY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 395130835 962 GLTLGIHSRINETVDYIRQRVHAGNCYVNR-------NMigavvglqPFGGEGLSGTG 1012
Cdd:cd07151 395 GLSGAVFTSDLERGVQFARRIDAGMTHINDqpvndepHV--------PFGGEKNSGLG 444
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
67-179 |
1.17e-56 |
|
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: 190.79 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 67 IDSFLTEYALSSDEGIALMCLAEALLRVPDNATIDNLIKDKLAGGDWGAHRGQSESFFVNATTWALMLTGKVLTPEkAEN 146
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDE-PEG 79
|
90 100 110
....*....|....*....|....*....|...
gi 395130835 147 TLTKALLKLVNRSSEAVVRKAVDKAMRIMSKQF 179
Cdd:pfam14850 80 TLAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
583-1012 |
2.62e-56 |
|
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: 202.20 E-value: 2.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07110 10 IGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSS-----PQRFNGYTGELNElslHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYA 737
Cdd:cd07110 90 YADLAEQLDAKaeravPLPSEDFKARVRR---EPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 738 VKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATrggEIIPLIAETGGQNAMIVDSSAL 817
Cdd:cd07110 167 AEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ---DIKPVSLELGGKSPIIVFDDAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 818 LEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRK 897
Cdd:cd07110 244 LEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 898 HH-EILYQCTVDDEALSGYFMPPTAIA---IDSISALEkEVFGPILHVIQFKRKdlDKVINQINQTGYGLTLGIHSRINE 973
Cdd:cd07110 324 EGaRLLCGGRRPAHLEKGYFIAPTVFAdvpTDSRIWRE-EIFGPVLCVRSFATE--DEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 395130835 974 TVDYIRQRVHAGNCYVNRNMIgaVVGLQPFGGEGLSGTG 1012
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQP--CFPQAPWGGYKRSGIG 437
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
582-1012 |
7.64e-56 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 201.29 E-value: 7.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGK----TWSDgiaEVREAI 657
Cdd:PRK13473 29 VLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKplhlALND---EIPAIV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 658 DFCRYYAKKAQEL--MSSPQRFNGYTGELNElslHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAA 735
Cdd:PRK13473 106 DVFRFFAGAARCLegKAAGEYLEGHTSMIRR---DPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 736 YAVKLMHQAgIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTlATRGGEIIPLiaETGGQNAMIVDSS 815
Cdd:PRK13473 183 KLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA-AADSVKRTHL--ELGGKAPVIVFDD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 816 ALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENM 895
Cdd:PRK13473 259 ADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 896 RKHHEIlyQCTVDDEALS--GYFMPPTAIA----IDSIsaLEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHS 969
Cdd:PRK13473 339 KALGHI--RVVTGGEAPDgkGYYYEPTLLAgarqDDEI--VQREVFGPVVSVTPF--DDEDQAVRWANDSDYGLASSVWT 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 395130835 970 RinetvDYIR-QRV----HAGNCYVNRN-MIgavVGLQPFGGEGLSGTG 1012
Cdd:PRK13473 413 R-----DVGRaHRVsarlQYGCTWVNTHfML---VSEMPHGGQKQSGYG 453
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
582-1016 |
7.73e-55 |
|
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: 198.87 E-value: 7.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFE--LWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGI-AEVREAID 658
Cdd:cd07140 33 VICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALkTHVGMSIQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 659 FCRYYA---KKAQELM-----SSPQRFNGYTGElnelslHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQT 730
Cdd:cd07140 113 TFRYFAgwcDKIQGKTipinqARPNRNLTLTKR------EPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 731 PLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLiaETGGQNAM 810
Cdd:cd07140 187 PLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLKKVSL--ELGGKSPL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 811 IVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPvidkealsilKN 890
Cdd:cd07140 265 IIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP----------QN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 891 HVENMRKHHEILyQCTVDDEA----------LSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFKRKDLDKVINQINQ 958
Cdd:cd07140 335 HKAHLDKLVEYC-ERGVKEGAtlvyggkqvdRPGFFFEPTVFTdvEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRAND 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 395130835 959 TGYGLTLGIHSR-INETVdYIRQRVHAGNCYVNRNMIGAVVGlqPFGGEGLSGTGPKAG 1016
Cdd:cd07140 414 TEYGLASGVFTKdINKAL-YVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLG 469
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
593-1012 |
1.83e-53 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 193.18 E-value: 1.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 593 DVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKT--WSDGIaeVREAIDFCRYYAKKAqel 670
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATaaWAGFN--VDLAAGMLREAASLI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 671 mssPQRFNGY--TGELNELSL---HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAG 745
Cdd:cd07105 76 ---TQIIGGSipSDKPGTLAMvvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 746 IPEGVIQLIPGAGET---IGAALVADKRIKAVLFTGSTDTANLINRTLATrggEIIPLIAETGGQNAMIVDSSALLEQVV 822
Cdd:cd07105 153 LPKGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK---HLKPVLLELGGKAPAIVLEDADLDAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 823 VDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDpqwlsTDVGPVIDKEALSILKNHVEN-MRKHHEI 901
Cdd:cd07105 230 NAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDaLSKGAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 902 LYQcTVDDEALSGYFMPPTAIA-------IDSIsalekEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRinet 974
Cdd:cd07105 305 VVG-GLADESPSGTSMPPTILDnvtpdmdIYSE-----ESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR---- 372
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 395130835 975 vDYIR-----QRVHAGNCYVNRNMIGAVVGLqPFGGEGLSGTG 1012
Cdd:cd07105 373 -DLARalavaKRIESGAVHINGMTVHDEPTL-PHGGVKSSGYG 413
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
583-1018 |
1.99e-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: 1.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFE--LWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGK-TWSDGIAEVREAIDF 659
Cdd:cd07139 27 VGRVPEATPADVDAAVAAARRAFDngPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMpISWSRRAQGPGPAAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKAQELmSSPQRFNGYTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:cd07139 107 LRYYAALARDF-PFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMHQAGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLE 819
Cdd:cd07139 186 AAEEAGLPPGVVNVVPADREV-GEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER---LARVTLELGGKSAAIVLDDADLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 820 QVVVDAVTSAFGSAGQRCSAL-RVLyVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKH 898
Cdd:cd07139 262 AAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 899 HEILYQCTVDDEALS-GYFMPPTAIA---IDSISALEkEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINET 974
Cdd:cd07139 341 GARLVTGGGRPAGLDrGWFVEPTLFAdvdNDMRIAQE-EIFGPVLSVIPY--DDEDDAVRIANDSDYGLSGSVWTADVER 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 395130835 975 VDYIRQRVHAGNCYVNrnmiGAVVGLQ-PFGGEGLSGTGpKAGGP 1018
Cdd:cd07139 418 GLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGP 457
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
583-1012 |
2.73e-53 |
|
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: 193.33 E-value: 2.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFE--LWSKKPvEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFC 660
Cdd:cd07120 10 IGTYADGGVAEAEAAIAAARRAFDetDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 661 RYYAKKAQEL---MSSPQrfngyTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYA 737
Cdd:cd07120 89 RYYAGLARTEagrMIEPE-----PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 738 VKLMHQA-GIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSA 816
Cdd:cd07120 164 IRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPT---LKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 817 LLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN-M 895
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERaI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 896 RKHHEILYQCTVDDEALS-GYFMPPTAIAIDSISA--LEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRIN 972
Cdd:cd07120 321 AAGAEVVLRGGPVTEGLAkGAFLRPTLLEVDDPDAdiVQEEIFGPVLTLETF--DDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 395130835 973 ETVDYIRQRVHAGNCYVNRNMigAVVGLQPFGGEGLSGTG 1012
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWN--KLFAEAEEGGYRQSGLG 436
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
583-1033 |
1.10e-52 |
|
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: 192.13 E-value: 1.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDG-IAEVREAIDFCR 661
Cdd:cd07098 9 LGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEILVTCEKIR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 662 YYAKKAQELMSSPQRFNG----YTGelNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYA 737
Cdd:cd07098 89 WTLKHGEKALRPESRPGGllmfYKR--ARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 738 VKLMHQA----GIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLINRTLATrggEIIPLIAETGGQNAMIVD 813
Cdd:cd07098 167 LSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAE---SLTPVVLELGGKDPAIVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 814 SSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEAL----SILK 889
Cdd:cd07098 243 DDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFdrleELVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 890 NHVEN--------MRKHHEilyqctvddEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQT 959
Cdd:cd07098 323 DAVEKgarllaggKRYPHP---------EYPQGHYFPPTLLVdvTPDMKIAQEEVFGPVMVVMKA--SDDEEAVEIANST 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 395130835 960 GYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTGpKAGGPNYLIRLCHERTYTVD 1033
Cdd:cd07098 392 EYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTED 464
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
583-1021 |
3.91e-52 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 190.89 E-value: 3.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:PRK11241 39 LGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSSPqrFNGYTGELNELSL-HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLM 741
Cdd:PRK11241 119 FAEEGKRIYGDT--IPGHQADKRLIVIkQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 742 HQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDtanlINRTLATRGGEIIPLIA-ETGGQNAMIVDSSALLEQ 820
Cdd:PRK11241 197 IRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE----IGRQLMEQCAKDIKKVSlELGGNAPFIVFDDADLDK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 821 VVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN-MRKHH 899
Cdd:PRK11241 273 AVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADaLEKGA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 900 EILyqCTVDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDY 977
Cdd:PRK11241 353 RVV--CGGKAHELGGNFFQPTILVdvPANAKVAKEETFGPLAPLFRF--KDEADVIAQANDTEFGLAAYFYARDLSRVFR 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 395130835 978 IRQRVHAGNCYVNRNMIGAVVGlqPFGG---EGLSGTGPKAGGPNYL 1021
Cdd:PRK11241 429 VGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
583-1012 |
2.22e-51 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 188.94 E-value: 2.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGI-AEVREAIDFCR 661
Cdd:PRK13252 35 LATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSvVDIVTGADVLE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 662 YYAKKAQELMSSPQRFNG----YTGElnelslHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYA 737
Cdd:PRK13252 115 YYAGLAPALEGEQIPLRGgsfvYTRR------EPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 738 VKLMHQAGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTAnliNRTLATRGGEIIPLIAETGGQNAMIVDSSAL 817
Cdd:PRK13252 189 AEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTG---KKVMAAAAASLKEVTMELGGKSPLIVFDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 818 LEQVVVDAVTSAFGSAGQRCS-ALRVlYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMR 896
Cdd:PRK13252 265 LDRAADIAMLANFYSSGQVCTnGTRV-FVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 897 KHHEIL----YQCTvDDEALSGYFMPPTAIA--IDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:PRK13252 344 AEGARLlcggERLT-EGGFANGAFVAPTVFTdcTDDMTIVREEIFGPVMSVLTF--DDEDEVIARANDTEYGLAAGVFTA 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 395130835 971 inetvDYIR-QRV----HAGNCYVnrNMIGAVVGLQPFGGEGLSGTG 1012
Cdd:PRK13252 421 -----DLSRaHRVihqlEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
583-970 |
4.84e-51 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 187.07 E-value: 4.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:cd07147 12 VARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKA-------QELMSSPqRFNGYTGELNELslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAA 735
Cdd:cd07147 92 AAEEAtriygevLPLDISA-RGEGRQGLVRRF---PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 736 YAVKLMHQAGIPEGVIQLIPGAGEtIGAALVADKRIKAVLFTGSTDTANLInRTLATRGgeiiPLIAETGGQNAMIVDSS 815
Cdd:cd07147 168 ILGEVLAETGLPKGAFSVLPCSRD-DADLLVTDERIKLLSFTGSPAVGWDL-KARAGKK----KVVLELGGNAAVIVDSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 816 ALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN- 894
Cdd:cd07147 242 ADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEa 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 395130835 895 MRKHHEILYQCTVDdealsGYFMPPTAIAIDSISAL--EKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:cd07147 322 VDAGAKLLTGGKRD-----GALLEPTILEDVPPDMEvnCEEVFGPVVTVEPY--DDFDEALAAVNDSKFGLQAGVFTR 392
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
589-1012 |
5.92e-50 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 183.79 E-value: 5.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 589 ATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQ 668
Cdd:PRK09406 20 LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 669 ELMSSPQRFNGYTGELNELSLH-PRGTILCISPWNFPLaiftGQVV----AGLVTGNCVIAKPAEQTPLIAAYAVKLMHQ 743
Cdd:PRK09406 100 ALLADEPADAAAVGASRAYVRYqPLGVVLAVMPWNFPL----WQVVrfaaPALMAGNVGLLKHASNVPQTALYLADLFRR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 744 AGIPEGVIQ-LIPGAGETigAALVADKRIKAVLFTGSTDTANLINrtlATRGGEIIPLIAETGGQNAMIVDSSALLEQVV 822
Cdd:PRK09406 176 AGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVA---AIAGDEIKKTVLELGGSDPFIVMPSADLDRAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 823 VDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN-MRKHHEI 901
Cdd:PRK09406 251 ETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDaVAAGATI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 902 LyqCTVDDEALSGYFMPPTAIAiDSISALE---KEVFGPILHViqFKRKDLDKVINQINQTGYGLTLGIHSRINETVDYI 978
Cdd:PRK09406 331 L--CGGKRPDGPGWFYPPTVIT-DITPDMRlytEEVFGPVASL--YRVADIDEAIEIANATTFGLGSNAWTRDEAEQERF 405
|
410 420 430
....*....|....*....|....*....|....
gi 395130835 979 RQRVHAGNCYVNrNMIGAVVGLqPFGGEGLSGTG 1012
Cdd:PRK09406 406 IDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSGYG 437
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
589-1012 |
2.21e-49 |
|
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: 182.65 E-value: 2.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 589 ATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTwsdgIAEVRE-----AIDFCRYY 663
Cdd:cd07117 35 ATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKP----IRETRAvdiplAADHFRYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 664 AK--KAQElmsspqrfnGYTGELNE--LSL---HPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAY 736
Cdd:cd07117 111 AGviRAEE---------GSANMIDEdtLSIvlrEPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 AVKLMHQAgIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSA 816
Cdd:cd07117 182 LAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK---LIPATLELGGKSANIIFDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 817 LLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMR 896
Cdd:cd07117 258 NWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 897 KH-HEILY--QCTVDDEALSGYFMPPTAIAI---DSISALEkEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:cd07117 338 EEgAKILTggHRLTENGLDKGFFIEPTLIVNvtnDMRVAQE-EIFGPVATVIKF--KTEDEVIDMANDSEYGLGGGVFTK 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 395130835 971 -INETVDyIRQRVHAGNCYVNR-NMIGAVVglqPFGGEGLSGTG 1012
Cdd:cd07117 415 dINRALR-VARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
586-1012 |
5.42e-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: 181.50 E-value: 5.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 586 VQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVltcreaGKTWSDGIAeVRE--------AI 657
Cdd:cd07116 32 VPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV------AETWDNGKP-VREtlaadiplAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 658 DFCRYYAK--KAQElmsspqrfnGYTGELNE--LSLH---PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQT 730
Cdd:cd07116 105 DHFRYFAGciRAQE---------GSISEIDEntVAYHfhePLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 731 PLIAAYAVKLMHQAgIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRtLATRggEIIPLIAETGGQNAM 810
Cdd:cd07116 176 PASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQ-YASE--NIIPVTLELGGKSPN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 811 IVDSS------ALLEQVVVDAVTSAFGSaGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEA 884
Cdd:cd07116 252 IFFADvmdaddAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 885 LSILKNHVENMRKH-HEILY---QCTVDDEALSGYFMPPTAIAIDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTG 960
Cdd:cd07116 331 LEKILSYIDIGKEEgAEVLTggeRNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTF--KDEEEALEIANDTL 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 395130835 961 YGLTLGIHSRINETVDYIRQRVHAG----NCYvnrnmiGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07116 409 YGLGAGVWTRDGNTAYRMGRGIQAGrvwtNCY------HLYPAHAAFGGYKQSGIG 458
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
582-1016 |
2.42e-48 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 180.42 E-value: 2.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 582 AIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCR 661
Cdd:PLN02315 46 PIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 662 YYAKKAQELMSS---PQRFNGYTGELnelsLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAV 738
Cdd:PLN02315 126 FAVGLSRQLNGSiipSERPNHMMMEV----WNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 739 KL----MHQAGIPEGVIQLIPGAGEtIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIpliAETGGQNAMIVDS 814
Cdd:PLN02315 202 KLvaevLEKNNLPGAIFTSFCGGAE-IGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCL---LELSGNNAIIVMD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 815 SALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVEN 894
Cdd:PLN02315 278 DADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 895 MRKHH-EILYQCTVDDEalSGYFMPPTAIAID-SISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRIN 972
Cdd:PLN02315 358 IKSQGgKILTGGSAIES--EGNFVQPTIVEISpDADVVKEELFGPVLYVMKF--KTLEEAIEINNSVPQGLSSSIFTRNP 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 395130835 973 ETV-DYIRQrvHAGNC-YVNRNMI--GAVVGlQPFGGEGLSGTGPKAG 1016
Cdd:PLN02315 434 ETIfKWIGP--LGSDCgIVNVNIPtnGAEIG-GAFGGEKATGGGREAG 478
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
620-1021 |
2.06e-46 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 172.23 E-value: 2.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 620 LNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQElmsspqrfngYTGEL------NELSL---H 690
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARR----------YEGEIiqsdrpGENILlfkR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 691 PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKR 770
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 771 IKAVLFTGSTDTAnliNRTLATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVY 850
Cdd:PRK10090 151 VAMVSMTGSVSAG---EKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 851 PRTVELLKGAMAELVVGDP-QWLSTDVGPVIDKEALsilkNHVENM-----RKHHEILYQCTVDDEalSGYFMPPTAIaI 924
Cdd:PRK10090 228 DQFVNRLGEAMQAVQFGNPaERNDIAMGPLINAAAL----ERVEQKvaravEEGARVALGGKAVEG--KGYYYPPTLL-L 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 925 D---SISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR-INETVDYIRQrVHAGNCYVNRNMIGAVVGL 1000
Cdd:PRK10090 301 DvrqEMSIMHEETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQnLNVAMKAIKG-LKFGETYINRENFEAMQGF 377
|
410 420
....*....|....*....|..
gi 395130835 1001 QP-FGGEGLSGTGPKAGGPNYL 1021
Cdd:PRK10090 378 HAgWRKSGIGGADGKHGLHEYL 399
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
611-1012 |
4.57e-45 |
|
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: 168.86 E-value: 4.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 611 KPVEERASCLNRFADLLQANMAELMvltcrEA-----GK----TWSDGIAEVREAIDfcrYYAKKAQELM-----SSPQR 676
Cdd:cd07087 17 RSLEWRKAQLKALKRMLTENEEEIA-----AAlyadlGKppaeAYLTEIAVVLGEID---HALKHLKKWMkprrvSVPLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 677 FNGYTGELnelSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAgIPEGVIQLIPG 756
Cdd:cd07087 89 LQPAKAYV---IPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 757 AGETIGAALvaDKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQR 836
Cdd:cd07087 165 GVEVATALL--AEPFDHIFFTGSPAVGKIVMEAAAKH---LTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 837 CSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQwLSTDVGPVIDKEALsilkNHVENMRKHHEILYQCTVDDEALsgyF 916
Cdd:cd07087 240 CIAPDYVLVHESIKDELIEELKKAIKEFYGEDPK-ESPDYGRIINERHF----DRLASLLDDGKVVIGGQVDKEER---Y 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 917 MPPTAIAIDSISA--LEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMI 994
Cdd:cd07087 312 IAPTILDDVSPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLL 389
|
410
....*....|....*...
gi 395130835 995 GAVVGLQPFGGEGLSGTG 1012
Cdd:cd07087 390 HAAIPNLPFGGVGNSGMG 407
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
577-1012 |
6.98e-43 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 163.91 E-value: 6.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 577 QQPayaIGSVQQATLDDVEVALNQAKLAFE--LWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGK----TWSDGI 650
Cdd:PRK09847 45 QAP---LAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKpirhSLRDDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 651 AEVREAIdfcRYYAKKAQELMSSPQRFNGytGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQT 730
Cdd:PRK09847 122 PGAARAI---RWYAEAIDKVYGEVATTSS--HELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 731 PLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTAnlinRTLATRGGE--IIPLIAETGGQN 808
Cdd:PRK09847 197 PLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTG----KQLLKDAGDsnMKRVWLEAGGKS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 809 AMIVDSSAL-LEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSI 887
Cdd:PRK09847 273 ANIVFADCPdLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 888 LKNHVENMRKHHEILyqctVD--DEALSGYFMPPTAIAIDSISALEK-EVFGPILHVIQFKRKdlDKVINQINQTGYGLT 964
Cdd:PRK09847 353 VHSFIREGESKGQLL----LDgrNAGLAAAIGPTIFVDVDPNASLSReEIFGPVLVVTRFTSE--EQALQLANDSQYGLG 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 395130835 965 LGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVglQPFGGEGLSGTG 1012
Cdd:PRK09847 427 AAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSGNG 472
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
583-990 |
1.17e-42 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 163.75 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFEL-----WSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAI 657
Cdd:PLN02467 36 IGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 658 DFCRYYAKKAQEL-------MSSP-QRFNGYTgeLNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQ 729
Cdd:PLN02467 116 GCFEYYADLAEALdakqkapVSLPmETFKGYV--LKE----PLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 730 TPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATrggEIIPLIAETGGQNA 809
Cdd:PLN02467 190 ASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQ---MVKPVSLELGGKSP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 810 MIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILK 889
Cdd:PLN02467 267 IIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 890 NHVENMRKH-HEILYQCTVDDEALSGYFMPPTAIAIDSISA--LEKEVFGPILHVIQFKRKdlDKVINQINQTGYGLTLG 966
Cdd:PLN02467 347 KFISTAKSEgATILCGGKRPEHLKKGFFIEPTIITDVTTSMqiWREEVFGPVLCVKTFSTE--DEAIELANDSHYGLAGA 424
|
410 420
....*....|....*....|....
gi 395130835 967 IHSRINETVDYIRQRVHAGNCYVN 990
Cdd:PLN02467 425 VISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
590-1012 |
1.87e-41 |
|
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: 158.54 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 590 TLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGI-AEVREAIDFCRYYAKKAQ 668
Cdd:cd07135 3 PLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 669 ELMS-SPQRFNGYTGELNELSLH--PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAg 745
Cdd:cd07135 83 KWAKdEKVKDGPLAFMFGKPRIRkePLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 746 IPEGVIQLIPGAGETIGAALvaDKRIKAVLFTGSTDTANLInrtlATRGGE-IIPLIAETGGQNAMIVDSSALLEQVVVD 824
Cdd:cd07135 162 LDPDAFQVVQGGVPETTALL--EQKFDKIFYTGSGRVGRII----AEAAAKhLTPVTLELGGKSPVIVTKNADLELAAKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 825 AVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWlSTDVGPVIDKEALSILKNHVENMRKhhEILYQ 904
Cdd:cd07135 236 ILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTTKG--KVVIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 905 CTVDDEALsgyFMPPTAIAIDSI--SALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRV 982
Cdd:cd07135 313 GEMDEATR---FIPPTIVSDVSWddSLMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRT 387
|
410 420 430
....*....|....*....|....*....|.
gi 395130835 983 HAGNCYVNRNMI-GAVVGLqPFGGEGLSGTG 1012
Cdd:cd07135 388 RSGGVVINDTLIhVGVDNA-PFGGVGDSGYG 417
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
572-1023 |
2.21e-41 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 158.74 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 572 TVMSPQQPAYaIGSVQQATLDDVEVALNQAKLAF-ELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGI 650
Cdd:cd07148 2 EVVNPFDLKP-IGEVPTVDWAAIDKALDTAHALFlDRNNWLPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 651 AEVREAIDFCRYyAKKAQELMSSPQRFNGYT----GELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKP 726
Cdd:cd07148 81 VEVTRAIDGVEL-AADELGQLGGREIPMGLTpasaGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 727 AEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTANLINRTLATrgGEIIPLiaETGG 806
Cdd:cd07148 160 ALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAV-AEKLVTDPRVAFFSFIGSARVGWMLRSKLAP--GTRCAL--EHGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 807 QNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALS 886
Cdd:cd07148 235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 887 ILKNHVENM-----------RKHHEILYQCTVddealsgYFMPPTAIAIDSisaleKEVFGPILHViqFKRKDLDKVINQ 955
Cdd:cd07148 315 RVEEWVNEAvaagarllcggKRLSDTTYAPTV-------LLDPPRDAKVST-----QEIFGPVVCV--YSYDDLDEAIAQ 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 395130835 956 INQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNrNMIGAVVGLQPFGGEGLSGTGpkAGGPNYLIR 1023
Cdd:cd07148 381 ANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVN-DHTAFRVDWMPFAGRRQSGYG--TGGIPYTMH 445
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
585-963 |
1.66e-40 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 156.84 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 585 SVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYA 664
Cdd:PLN00412 46 KVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 665 K-------KAQELMSSPqrFNGytGELNELSLH---PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIA 734
Cdd:PLN00412 126 EegvrilgEGKFLVSDS--FPG--NERNKYCLTskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 735 AYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGStDTANLInrtlaTRGGEIIPLIAETGGQNAMIVDS 814
Cdd:PLN00412 202 LHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAI-----SKKAGMVPLQMELGGKDACIVLE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 815 SALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQwLSTDVGPVIDKEALSILKNHVEN 894
Cdd:PLN00412 276 DADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE-DDCDITPVVSESSANFIEGLVMD 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 895 MRK-----HHE------ILYQCTVDDealsgyFMPPTAIAIDsisalekEVFGPILHVIQFkrKDLDKVINQINQTGYGL 963
Cdd:PLN00412 355 AKEkgatfCQEwkregnLIWPLLLDN------VRPDMRIAWE-------EPFGPVLPVIRI--NSVEEGIHHCNASNFGL 419
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
691-1017 |
1.85e-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: 146.60 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 691 PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGViQLIPGAGETIGAALvaDKR 770
Cdd:cd07134 100 PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEGDAEVAQALL--ELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 771 IKAVLFTGSTDTANLI----NRTLATrggeiIPLiaETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQ 846
Cdd:cd07134 177 FDHIFFTGSPAVGKIVmaaaAKHLAS-----VTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 847 EEVYPRTVELLKGAMAELVVGDPQWL-STDVGPVIDKEALSILKNHVENMRKH-HEILYQCTVDDEALsgyFMPPTAIA- 923
Cdd:cd07134 250 ESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKgAKVEFGGQFDAAQR---YIAPTVLTn 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 924 IDSISA-LEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQP 1002
Cdd:cd07134 327 VTPDMKiMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLP 404
|
330
....*....|....*
gi 395130835 1003 FGGEGLSGTGpKAGG 1017
Cdd:cd07134 405 FGGVNNSGIG-SYHG 418
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
589-990 |
3.94e-34 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 137.30 E-value: 3.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 589 ATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQ 668
Cdd:PRK13968 26 AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 669 ELMSSPQRFngYTGELNELSLHPRGTILCISPWNFPLaiftGQVVAG----LVTGNCVIAKPAEQTPLIAAYAVKLMHQA 744
Cdd:PRK13968 106 AMLKAEPTL--VENQQAVIEYRPLGTILAIMPWNFPL----WQVMRGavpiLLAGNGYLLKHAPNVMGCAQLIAQVFKDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 745 GIPEGVIQLIPGAGETIgAALVADKRIKAVLFTGSTDTANLINrtlATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVD 824
Cdd:PRK13968 180 GIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIG---AQAGAALKKCVLELGGSDPFIVLNDADLELAVKA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 825 AVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVidkeALSILKNHVenmrkHHEIlyQ 904
Cdd:PRK13968 256 AVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPM----ARFDLRDEL-----HHQV--E 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 905 CTVDDEAL----------SGYFMPPTAIA--IDSISALEKEVFGPILHVIQfkRKDLDKVINQINQTGYGLTLGIHSRIN 972
Cdd:PRK13968 325 ATLAEGARlllggekiagAGNYYAPTVLAnvTPEMTAFREELFGPVAAITV--AKDAEHALELANDSEFGLSATIFTTDE 402
|
410
....*....|....*...
gi 395130835 973 ETVDYIRQRVHAGNCYVN 990
Cdd:PRK13968 403 TQARQMAARLECGGVFIN 420
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
583-990 |
4.73e-33 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 136.41 E-value: 4.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 583 IGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRY 662
Cdd:PLN02419 142 VSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 663 YAKKAQELMSS--PQRFNGY-TGELNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVK 739
Cdd:PLN02419 222 ACGMATLQMGEylPNVSNGVdTYSIRE----PLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 740 LMHQAGIPEGVIQLIPGAGETIGaALVADKRIKAVLFTGSTDTANLINRTLATRGGEIiplIAETGGQNAMIVDSSALLE 819
Cdd:PLN02419 298 LAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRI---QSNMGAKNHGLVLPDANID 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 820 QVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVV--GDPqwlSTDVGPVIDKEAlsilknhvenmRK 897
Cdd:PLN02419 374 ATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTcgSEP---DADLGPVISKQA-----------KE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 898 HHEILYQCTVDDEA----------LSGY----FMPPTAIA--IDSISALEKEVFGPILHVIQfkRKDLDKVINQINQTGY 961
Cdd:PLN02419 440 RICRLIQSGVDDGAkllldgrdivVPGYekgnFIGPTILSgvTPDMECYKEEIFGPVLVCMQ--ANSFDEAISIINKNKY 517
|
410 420
....*....|....*....|....*....
gi 395130835 962 GLTLGIHSRINETVDYIRQRVHAGNCYVN 990
Cdd:PLN02419 518 GNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
588-1012 |
2.33e-32 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 132.46 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 588 QATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKT--------WSDGIAEVREAIDF 659
Cdd:PTZ00381 3 PDNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHpfetkmteVLLTVAEIEHLLKH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKAQ---ELMSSPQRfngytgelNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAay 736
Cdd:PTZ00381 83 LDEYLKPEKvdtVGVFGPGK--------SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTS-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 737 avKLMHQ---AGIPEGVIQLIPGAGETIGAALvaDKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVD 813
Cdd:PTZ00381 153 --KLMAKlltKYLDPSYVRVIEGGVEVTTELL--KEPFDHIFFTGSPRVGKLVMQAAAEN---LTPCTLELGGKSPVIVD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 814 SSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQwLSTDVGPVIDKEALSILKNHVE 893
Cdd:PTZ00381 226 KSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPK-KSEDYSRIVNEFHTKRLAELIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 894 NmrKHHEILYQCTVDDEALsgyFMPPTAIA---IDSIsALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSR 970
Cdd:PTZ00381 305 D--HGGKVVYGGEVDIENK---YVAPTIIVnpdLDSP-LMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 395130835 971 INETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTG 1012
Cdd:PTZ00381 377 DKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
594-1018 |
4.95e-30 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 124.66 E-value: 4.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 594 VEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKTWsdgiaevREAIDFC------RYYAKKA 667
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGW-------MFAENICgdqvqlRARAFVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 668 QELmSSPQRFNGYTGELNELSLH----PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQ 743
Cdd:cd07084 74 YSY-RIPHEPGNHLGQGLKQQSHgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 744 AGI-PEGVIQLIPGAGETiGAALVADKRIKAVLFTGSTDTAnlinRTLATRGGEiIPLIAETGGQNAMIVDSSA-----L 817
Cdd:cd07084 153 AGLlPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA----EKLALDAKQ-ARIYLELAGFNWKVLGPDAqavdyV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 818 LEQVVVDAVTsafgSAGQRCSALRVLYVQEEVYPR-TVELLKGAMAELVVGDpqwlsTDVGPVIDKEALSilknHVENMR 896
Cdd:cd07084 227 AWQCVQDMTA----CSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED-----LLLGPVQTFTTLA----MIAHME 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 897 KHHEIL-------YQCTVDDEALSGYFMPPTAIAIDSI----SALEKEVFGPILHVIQFKRKDLDKVINQINQTGYGLTL 965
Cdd:cd07084 294 NLLGSVllfsgkeLKNHSIPSIYGACVASALFVPIDEIlktyELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTA 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 395130835 966 GIHSRINETVD------YIRQRVHAGncyvNRNMIGAVVGLQPFGGEGLSGTGPKAGGP 1018
Cdd:cd07084 374 AIYSNDPIFLQelignlWVAGRTYAI----LRGRTGVAPNQNHGGGPAADPRGAGIGGP 428
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
613-1012 |
1.40e-29 |
|
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: 122.98 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 613 VEERASCLNRFADLLQAN---MAELMVL--TCREAGKTwsdGIAEVREAIDFCRYYAKKAQELMSSPQRFNG--YTGELN 685
Cdd:cd07133 19 LEERRDRLDRLKALLLDNqdaLAEAISAdfGHRSRHET---LLAEILPSIAGIKHARKHLKKWMKPSRRHVGllFLPAKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 686 ELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAgIPEGVIQLIPGAGEtIGAAL 765
Cdd:cd07133 96 EVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVTGGAD-VAAAF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 766 VA---DKrikaVLFTGSTDTANLINRTLATrggEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRV 842
Cdd:cd07133 174 SSlpfDH----LLFTGSTAVGRHVMRAAAE---NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 843 LYVQEEVYPRTVELLKGAMAELVvgdPQWL-STDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEALSG-YFMPPT 920
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKMY---PTLAdNPDYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDFAAtRKLPPT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 921 AI--AIDSISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVV 998
Cdd:cd07133 324 LVlnVTDDMRVMQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQ 401
|
410
....*....|....
gi 395130835 999 GLQPFGGEGLSGTG 1012
Cdd:cd07133 402 DDLPFGGVGASGMG 415
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
597-1012 |
8.80e-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: 120.79 E-value: 8.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 597 ALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGKT-WSDGIAEVREAIDFCRYYAKKAQELMSsPQ 675
Cdd:cd07132 3 AVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPkFEAVLSEILLVKNEIKYAISNLPEWMK-PE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 676 RFN-GYTGELNELSLH--PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEqtplIAAYAVKLMHqagipegviQ 752
Cdd:cd07132 82 PVKkNLATLLDDVYIYkePLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE----VSPATAKLLA---------E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 753 LIP-------------GAGETigaALVADKRIKAVLFTGSTDTANLI----NRTLAtrggeiiPLIAETGGQNAMIVDSS 815
Cdd:cd07132 149 LIPkyldkecypvvlgGVEET---TELLKQRFDYIFYTGSTSVGKIVmqaaAKHLT-------PVTLELGGKSPCYVDKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 816 ALLEQVVVDAVTSAFGSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQwLSTDVGPVIDKEALSILKNHVENM 895
Cdd:cd07132 219 CDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPK-ESPDYGRIINDRHFQRLKKLLSGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 896 RkhheILYQCTVDDEALsgyFMPPTaIAID---SISALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRIN 972
Cdd:cd07132 298 K----VAIGGQTDEKER---YIAPT-VLTDvkpSDPVMQEEIFGPILPIVTV--NNLDEAIEFINSREKPLALYVFSNNK 367
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 395130835 973 ETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07132 368 KVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
691-1012 |
6.89e-27 |
|
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: 114.82 E-value: 6.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 691 PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEgVIQLIPGaGETIGAALVADKR 770
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTK-AIKVIEG-GVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 771 IKaVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGS-AGQRCSALRVLYVQEEV 849
Cdd:cd07137 179 DK-IFFTGSPRVGRII---MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 850 YPRTVELLKGAMAELVVGDPQwLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEALsgyFMPPTAI---AIDS 926
Cdd:cd07137 255 APTLIDALKNTLEKFFGENPK-ESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNL---YIEPTILldpPLDS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 927 iSALEKEVFGPILHVIqfKRKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQPFGGE 1006
Cdd:cd07137 331 -SIMTEEIFGPLLPII--TVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGV 407
|
....*.
gi 395130835 1007 GLSGTG 1012
Cdd:cd07137 408 GESGFG 413
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
611-1012 |
1.36e-26 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 114.52 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 611 KPVEERASCLNRFADLLQANMAELMvltcrEA-----GK----TWSDGIAEVREAIDfcryYAKKAQELMSSPQR----- 676
Cdd:cd07136 17 KDVEFRIEQLKKLKQAIKKYENEIL-----EAlkkdlGKsefeAYMTEIGFVLSEIN----YAIKHLKKWMKPKRvktpl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 677 --FNGYTGELNElslhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAgIPEGVIQLI 754
Cdd:cd07136 88 lnFPSKSYIYYE----PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 755 PGAGETIGAALvaDKRIKAVLFTGSTDTANLINRTLATRggeIIPLIAETGGQNAMIVDSSALLEqvvVDAVTSAFG--- 831
Cdd:cd07136 163 EGGVEENQELL--DQKFDYIFFTGSVRVGKIVMEAAAKH---LTPVTLELGGKSPCIVDEDANLK---LAAKRIVWGkfl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 832 SAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQwLSTDVGPVIDKEALsilkNHVENMRKHHEILYQCTVDDEA 911
Cdd:cd07136 235 NAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPL-ESPDYGRIINEKHF----DRLAGLLDNGKIVFGGNTDRET 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 912 LsgyFMPPTaiAIDSIS----ALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNC 987
Cdd:cd07136 310 L---YIEPT--ILDNVTwddpVMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGG 382
|
410 420
....*....|....*....|....*
gi 395130835 988 YVNRNMIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07136 383 CINDTIMHLANPYLPFGGVGNSGMG 407
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
614-938 |
7.15e-25 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 110.18 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 614 EERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREAIDFCRYYAKKAQELmsSPQRFNgYTGELNELSLHP-- 691
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAAL--GDARLL-RDGEAVQLGKDPaf 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 692 ---------RGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGI-PEGVIQLIPGAGETI 761
Cdd:PRK11903 140 qgqhvlvptRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 762 GAALvadKRIKAVLFTGSTDTANLInRTLATRGGEIIPLIAETGGQNAMI-----VDSSALLEQVVVDAVTSAFGSAGQR 836
Cdd:PRK11903 220 LDHL---QPFDVVSFTGSAETAAVL-RSHPAVVQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 837 CSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILY----QCTVDDEAL 912
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFdgggFALVDADPA 375
|
330 340 350
....*....|....*....|....*....|
gi 395130835 913 SGYFMPPTAI----AIDSISALEKEVFGPI 938
Cdd:PRK11903 376 VAACVGPTLLgasdPDAATAVHDVEVFGPV 405
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
691-1012 |
8.17e-22 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 100.19 E-value: 8.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 691 PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKlmhqaGIPE----GVIQLIPGaGETIGAALV 766
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAA-----NIPKyldsKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 767 ADKRIKaVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVD--SSALLEQVVVDAVTSA-FGS-AGQRCSALRV 842
Cdd:PLN02203 182 QHKWDK-IFFTGSPRVGRII---MTAAAKHLTPVALELGGKCPCIVDslSSSRDTKVAVNRIVGGkWGScAGQACIAIDY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 843 LYVQEEVYPRTVELLKgAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEALsgyFMPPTAI 922
Cdd:PLN02203 258 VLVEERFAPILIELLK-STIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKL---FIEPTIL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 923 ---AIDSiSALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRiNETvdyIRQRV----HAGNCYVNRNMIG 995
Cdd:PLN02203 334 lnpPLDS-DIMTEEIFGPLLPIITV--KKIEDSIAFINSKPKPLAIYAFTN-NEK---LKRRIlsetSSGSVTFNDAIIQ 406
|
330
....*....|....*..
gi 395130835 996 AVVGLQPFGGEGLSGTG 1012
Cdd:PLN02203 407 YACDSLPFGGVGESGFG 423
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
615-938 |
7.79e-21 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 97.34 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 615 ERASCLNRFADLLQANMAELMVLTCReAGKTWSDGIAEVREAIDFCRYYAKKAQELMSSpQRFngYT-GELNELS----- 688
Cdd:cd07128 60 ERAAMLKALAKYLMERKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELPN-AHF--LVeGDVEPLSkdgtf 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 689 -----LHPR-GTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGI-PEGVIQLIPG-AGET 760
Cdd:cd07128 136 vgqhiLTPRrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGsVGDL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 761 IGAALVADkrikAVLFTGSTDTANLInRTLATRGGEIIPLIAETGGQNAMIVDSSA---------LLEQVVVDAVTSAfg 831
Cdd:cd07128 216 LDHLGEQD----VVAFTGSAATAAKL-RAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpefdlFVKEVAREMTVKA-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 832 saGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSILKNHVENMRKHHEILY-----QCT 906
Cdd:cd07128 289 --GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFggpdrFEV 366
|
330 340 350
....*....|....*....|....*....|....*.
gi 395130835 907 VDDEALSGYFMPPTAI----AIDSISALEKEVFGPI 938
Cdd:cd07128 367 VGADAEKGAFFPPTLLlcddPDAATAVHDVEAFGPV 402
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
594-937 |
2.41e-20 |
|
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: 95.30 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 594 VEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAG-----------------KTWSDGIAE---V 653
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpearlqgelgrttgqlRLFADLVREgswL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 654 REAIDfcryyakKAQelmssPQRFNGYTGELnELSLHPRGTILCISPWNFPLAIFT--GQVVAGLVTGNCVIAK--PA-- 727
Cdd:cd07129 81 DARID-------PAD-----PDRQPLPRPDL-RRMLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 728 EQTPLIAAYAVKLMHQAGIPEGVIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRgGEIIPLIAETGGQ 807
Cdd:cd07129 148 GTSELVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAAR-PEPIPFYAELGSV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 808 NAMIVDSSALLEQVVVDA---VTSAFGSAGQRCSALRVLYVqeevyPRTVEL--LKGAMAELVVGDPQwlstdvGPVIDK 882
Cdd:cd07129 227 NPVFILPGALAERGEAIAqgfVGSLTLGAGQFCTNPGLVLV-----PAGPAGdaFIAALAEALAAAPA------QTMLTP 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 883 EALSILKNHVENMRKHHEILyQCTVDDEALSGYFMPPTAIAIDSIS-----ALEKEVFGP 937
Cdd:cd07129 296 GIAEAYRQGVEALAAAPGVR-VLAGGAAAEGGNQAAPTLFKVDAAAfladpALQEEVFGP 354
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
686-1016 |
1.94e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 92.80 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 686 ELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAgIPEGVIQLIPGAGETIGAAL 765
Cdd:PLN02174 107 EIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 766 vaDKRIKAVLFTGSTDTANLInrtLATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFG-SAGQRCSALRVLY 844
Cdd:PLN02174 186 --EQKWDKIFYTGSSKIGRVI---MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYIL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 845 VQEEVYPRTVELLKGAMAELVVGDPQWlSTDVGPVIDKEALSILKNHVENMRKHHEILYQCTVDDEALSgyfMPPTA--- 921
Cdd:PLN02174 261 TTKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRENLK---IAPTIlld 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 922 IAIDSIsALEKEVFGPILHVIQFkrKDLDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHAGNCYVNRNMIGAVVGLQ 1001
Cdd:PLN02174 337 VPLDSL-IMSEEIFGPLLPILTL--NNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTL 413
|
330
....*....|....*
gi 395130835 1002 PFGGEGLSGTGPKAG 1016
Cdd:PLN02174 414 PFGGVGESGMGAYHG 428
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
650-831 |
4.20e-14 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 77.21 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 650 IAEVREAIDFCRYYAKKAQELMSSPQRFNGYTGELNELSLHPRGTILCISPwnfPLAIFTGQVVAGLVTGNCVIakpaeq 729
Cdd:PRK11905 1037 LDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVAD---TEEALLRQLAAALATGNVAV------ 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 730 tplIAAYAVKLMHQAGIPEgviqlIPGAGETIGAALVADKRIKAVLFTGSTDTANLINRTLATRGGEIIPLIAETGGQNa 809
Cdd:PRK11905 1108 ---VAADSGLAAALADLPG-----LVAARIDWTQDWEADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEPTDA- 1178
|
170 180
....*....|....*....|..
gi 395130835 810 miVDSSALLEQVVVDAVTSAFG 831
Cdd:PRK11905 1179 --YDLARLVEERSVSINTTAAG 1198
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
601-969 |
3.26e-13 |
|
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: 73.30 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 601 AKLAFELwsKKP-VEERasclnrFADLLQanmaelmvltcREAGKTWSDGIAEVREAIDFCRYYAKKAQELMSSPQRFNG 679
Cdd:cd07126 69 HRVAHEL--RKPeVEDF------FARLIQ-----------RVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 680 -YTGELNELSLHPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEGVIQLIPGAG 758
Cdd:cd07126 130 dHQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 759 ETIGaALVADKRIKAVLFTGSTDTANLINRTLATRggeiipLIAETGGqnamiVDSSALLEQVV-VDAVT-----SAFGS 832
Cdd:cd07126 210 PTMN-KILLEANPRMTLFTGSSKVAERLALELHGK------VKLEDAG-----FDWKILGPDVSdVDYVAwqcdqDAYAC 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 833 AGQRCSALRVLYVQEE-VYPRTVELLKGAMAELVVGDpqwlsTDVGPVIDKEALSILkNHVEN---------------MR 896
Cdd:cd07126 278 SGQKCSAQSILFAHENwVQAGILDKLKALAEQRKLED-----LTIGPVLTWTTERIL-DHVDKllaipgakvlfggkpLT 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 395130835 897 KHHEILYQCTVDDEALsgyFMPPTAIAIDSISAL-EKEVFGPILHVIQFKRKDLDKVINQINQTGYGLTLGIHS 969
Cdd:cd07126 352 NHSIPSIYGAYEPTAV---FVPLEEIAIEENFELvTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVS 422
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
673-885 |
3.78e-11 |
|
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: 66.48 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 673 SPQRFNGYTGELnELSLHPRGTILCISPWNFPLAIFTgQVVAGLVTGNCVIAKPAEQTPlIAAYAVKLMHQAGIPEG--- 749
Cdd:cd07077 83 IQDVLLPDNGET-YVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpk 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 750 -VIQLIPGAGETIGAALVADKRIKAVLFTGSTDTANLinrtlATRGGEIIPLIAETGGQNAMIVDSSALLEQVVVDAVTS 828
Cdd:cd07077 160 iLVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDA-----AVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 829 AFgSAGQRCSALRVLYVQEEVYPRTVELLKGAMAELVVGDPQ---WLSTDVGPVIDKEAL 885
Cdd:cd07077 235 KF-FDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQetkPLSKETTPSFDDEAL 293
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
679-809 |
2.28e-10 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 64.96 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 679 GYTGELNELSLHPRGTILCISPwnfPLAIFTGQVVAGLVTGNCVIAKPAEQtpliaayavklmhQAGIPEGVIQlipgag 758
Cdd:COG4230 1050 GPTGERNTLTLRPRGRVLCLAD---SLEALLAQLAAALATGNRAVVAADLA-------------LAGLPAVLLP------ 1107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 395130835 759 etigaalvadkRIKAVLFTGstdTANLINRTLATRGGEIIPLIA----------ETGGqNA 809
Cdd:COG4230 1108 -----------PFDAVLFEG---RLRALRQALAARDGAIVPVIDagydlerlleEAGG-NA 1153
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
691-942 |
4.84e-10 |
|
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: 63.27 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 691 PRGTILCIS-----PWNFPLAIFtgqvvAGLVTGNCVIAKPAEQTPLIAAYAVK----LMHQAGI-PEGVIQLIPGAGET 760
Cdd:cd07127 193 PRGVALVIGcstfpTWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVQvareVLAEAGFdPNLVTLAADTPEEP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 761 IGAALVADKRIKAVLFTGSTDTANLINRTlaTRGGEiipLIAETGGQNAMIVDSSALLEQVVVD-AVTSAFGSaGQRCSA 839
Cdd:cd07127 268 IAQTLATRPEVRIIDFTGSNAFGDWLEAN--ARQAQ---VYTEKAGVNTVVVDSTDDLKAMLRNlAFSLSLYS-GQMCTT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 840 LRVLYV--------QEEVYPRTVELLKGAMAELVVGDPQWLSTDVGPVIDKEALSilknHVENMRKHHEILyqctVDDEA 911
Cdd:cd07127 342 PQNIYVprdgiqtdDGRKSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLA----RIAEARQLGEVL----LASEA 413
|
250 260 270
....*....|....*....|....*....|....*....
gi 395130835 912 LSGYFMP------PTAIAIDSI--SALEKEVFGPILHVI 942
Cdd:cd07127 414 VAHPEFPdarvrtPLLLKLDASdeAAYAEERFGPIAFVV 452
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
121-475 |
6.64e-10 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 62.80 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 121 ESFFVNATTWALMLTGKVLTPEKAEnTLTKALLKLVNRSSEAVVRKAVDKAMR-IMSKQFVMGRTINEALARAKKKEDRG 199
Cdd:PLN02681 30 AALFAGLSTSELLRSLLVLQLCAIG-PLVDLGEWLLTSPLMVLGRAIVLALVKaTFYSHFCAGEDAEEAARTVRRLWELG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 200 YRYSYDMLGEAALTSADAARYFEAYKEAI----------------------ISIGEKAdkhSDVYRR---------PGI- 247
Cdd:PLN02681 109 LGGILDYAAEDAGDNAACDRNLEKFLAAIraaatlppssssaavkitalcpPSLLERV---SDLLRWqdrdpngklPWKq 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 248 -SIKLSALH-PRYS--------EFQYERVMAELPPKLLALSRLAKDYGIALTIDAEESeRLDLSLDVIekvfTDESLQGW 317
Cdd:PLN02681 186 wSFPLFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYT-SLQPAIDYI----TYDLAREF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 318 N-GFGLAV-----QSYQKRAFYVLdwVAALARSKQRR--IMVRLIKGAYWDSEIKKTQMQGFsEYPVFTRKVFTDVSFQA 389
Cdd:PLN02681 261 NkGKDRPIvygtyQAYLKDARERL--RLDLERSEREGvpLGAKLVRGAYLSLERRLAASLGV-PSPVHDTIQDTHACYNR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 390 CAKKIL---------TMtdaiypqFATHNAYSV------AMILNLVGGYRDFEFQCLHGMGNELYEQIVPAncyGIPCRI 454
Cdd:PLN02681 338 CAEFLLekasngdgeVM-------LATHNVESGelaaakMNELGLHKGDPRVQFAQLLGMSDNLSFGLGNA---GFRVSK 407
|
410 420
....*....|....*....|.
gi 395130835 455 YAPVGSHEDLLPYLVRRLLEN 475
Cdd:PLN02681 408 YLPYGPVEEVIPYLLRRAEEN 428
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
13-58 |
2.41e-09 |
|
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: 53.62 E-value: 2.41e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 395130835 13 LRAAINKAYRMDELSLITELSEQAALDPQQMMAIKTSATKLVQSVR 58
Cdd:pfam18327 3 LRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
691-1024 |
1.23e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 48.80 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 691 PRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQA----GIPEGVIQLIPGAGETIGAALV 766
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIELAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 767 ADKRIKAVLFTGSTDTANLinrtlATRGGEiiPLIAETGGQNAMIVDSSALLEQVVVDAVTSAFGSAGQRCSALRVLYVQ 846
Cdd:cd07081 175 KFPGIGLLLATGGPAVVKA-----AYSSGK--PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 847 EEVYPRTVELLKGAMAELVVGDPqwlSTDVGPVidkealsILKNHVENmrkhHEILYQCTVDDEALSGYFMPP-TAIAID 925
Cdd:cd07081 248 DSVYDEVMRLFEGQGAYKLTAEE---LQQVQPV-------ILKNGDVN----RDIVGQDAYKIAAAAGLKVPQeTRILIG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 926 SISALEK------EVFGPILHVIQFKRKD--LDKVINQINQTGYGLTLGIHSRINETVDYIRQRVHA------------- 984
Cdd:cd07081 314 EVTSLAEhepfahEKLSPVLAMYRAANFAdaDAKALALKLEGGCGHTSAMYSDNIKAIENMNQFANAmktsrfvkngpcs 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 395130835 985 ----GNCYVNRNMIGAVVGLQPFGGEGLSgtgpKAGGPNYLIRL 1024
Cdd:cd07081 394 qgglGDLYNFRGWPSMTLGCGTWGGNSVS----ENVGPKHLVNL 433
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
660-798 |
3.34e-05 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 48.05 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 660 CRYYAKKAQelmSSPQR-FNGYTGELNELSLHPRGTILCISPWNFPLAIftgQVVAGLVTGN-CVIAKPAEQTPLIAAya 737
Cdd:PRK11809 1158 CDQYAELAQ---AGTTRlLPGPTGERNTYTLLPRERVLCLADTEQDALT---QLAAVLAVGSqALWPDDALHRALVAA-- 1229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 395130835 738 vklmhqagIPEGV---IQLIPgagetigAALVADKRIKAVLFTGSTDTANLINRTLATRGGEII 798
Cdd:PRK11809 1230 --------LPAAVqarIQLAK-------DWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPIV 1278
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
585-959 |
8.85e-04 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 43.03 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 585 SVQQATLDDVEVALNQAKLAfELwskkPVEERASCLNRFADLLQANMAELMVLTCREAGKTWSDGIAEVREA----IDFC 660
Cdd:cd07080 3 SAPDLDALIEELRLNRRALA-AL----PVEEIVDFLDRAGKRLLDPDYPLRQQAERLLPTVTGYSEEMLREGlkrlMALF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 661 RY---YAKKAQELmSSPqrfnGYTGELNELSLH------PRGTILCISPWNFP-LAIFTgqVVAGLVTGNCVIAKPAEQT 730
Cdd:cd07080 78 RRenlERILEREL-GSP----GILDEWVPPGRGgyiraqPRGLVVHIIAGNVPlLPVWS--IVRGLLVKNVNLLKMSSSD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 731 PLIAAYAVKLMhqAGI-PEGVIQL------IPGAGETIGAALV--ADKRIkavlFTGSTDTANLINRTLATrGGEIIPLI 801
Cdd:cd07080 151 PLTATALLRSL--ADVdPNHPLTDsisvvyWPGGDAELEERILasADAVV----AWGGEEAVKAIRSLLPP-GCRLIDFG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 802 AETGGqnAMIVDSSalLEQVVVDAVTSAFgsAG-------QRCSALRVLYVQ---EEVYPRTVELLKGAMAELVvgdpqw 871
Cdd:cd07080 224 PKYSF--AVIDREA--LESEKLAEVADAL--AEdicrydqQACSSPQVVFVEkddDEELREFAEALAAALERLP------ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 872 lstdvgPVIDKEALSI-LKNHVENMRkhheilYQCTVDDEALSGYFMPPTAIAIDSISALEkevFGPILHVIQFK-RKDL 949
Cdd:cd07080 292 ------RRYPALSLSAaESAKIARAR------LEAEFYELKGGVSRDLGWTVIISDEIGLE---ASPLNRTVNVKpVASL 356
|
410
....*....|...
gi 395130835 950 DKVINQIN---QT 959
Cdd:cd07080 357 DDVLRPVTpylQT 369
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
738-870 |
1.07e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 42.75 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 738 VKLMHQA----GIPEGVIQLIPGAG-ETIGAALVADKRIKAVLFTGStdtANLINRTL--ATrggeiIPLIaETG-GQNA 809
Cdd:PRK00197 160 VAVIQEAleeaGLPADAVQLVETTDrAAVGELLKLDGYVDVIIPRGG---AGLIRRVVenAT-----VPVI-EHGdGICH 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 810 MIVDSSALLEQ---VVVDAVTsafgsagQR---CSALRVLYVQEEVYPRTVELLKGAMAELVV---GDPQ 870
Cdd:PRK00197 231 IYVDESADLDKalkIVLNAKT-------QRpsvCNALETLLVHEAIAEEFLPKLAEALAEAGVelrGDEA 293
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
563-778 |
2.15e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 41.81 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 563 RKLSRDLLQTVMSPQQPAYAIGSVQQATLDDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREA 642
Cdd:PRK15398 7 EQVVKAVLAEMLSSQTVSPPAAVGEMGVFASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 643 G-KTWSDGIAEVREAIDfcryYAKKAQELmsSPQRFNGYTG-ELNELSlhPRGTILCISPWNFPLAIFTGQVVAGLVTGN 720
Cdd:PRK15398 87 GmGRVEDKIAKNVAAAE----KTPGVEDL--TTEALTGDNGlTLIEYA--PFGVIGAVTPSTNPTETIINNAISMLAAGN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 395130835 721 CVIAKPAEQTPLIAAYAVKLMHQA----GIPEGVIQLIpgAGETIGAA--LVADKRIKAVLFTG 778
Cdd:PRK15398 159 SVVFSPHPGAKKVSLRAIELLNEAivaaGGPENLVVTV--AEPTIETAqrLMKHPGIALLVVTG 220
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
592-752 |
5.48e-03 |
|
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: 40.30 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 592 DDVEVALNQAKLAFELWSKKPVEERASCLNRFADLLQANMAELMVLTCREAGK-TWSDGIAEVREAIDfcryyaKKAQEL 670
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMgRVEDKIAKNHLAAE------KTPGTE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395130835 671 MSSPQRFNGYTG-ELNELSlhPRGTILCISPWNFPLAIFTGQVVAGLVTGNCVIAKPAEQTPLIAAYAVKLMHQAGIPEG 749
Cdd:cd07121 78 DLTTTAWSGDNGlTLVEYA--PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAG 155
|
...
gi 395130835 750 VIQ 752
Cdd:cd07121 156 GPD 158
|
|
| |
