|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
3-1041 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1668.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 3 AHVSPPVALSQDWDALDQGKFADETATVRGLLANMPLDGAERAAVLGEAIGLVERARASVKKQGVVESFLQEFSLGTREG 82
Cdd:PRK11904 2 LGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGGIDAFLQEYSLSTEEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 83 LALMCLAEALLRTPDEETRDRLIAEKIGSADWSSHLGQSDSLFVNASTWGLMLTGKLVDVDEEARTDLPGFLKRIVGRLG 162
Cdd:PRK11904 82 IALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADGTPSGVLKRLVNRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 163 EPVIREAVAAAVRIMGEQFVVGRTIEAALKRSN---REGWLCSFDMLGEGARTAHDAERYEKIYADAITAVGKTAKGQGP 239
Cdd:PRK11904 162 EPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARsarNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 240 EAGHGVSVKLSALSPRYEATHEARVWDELYPRILRLARIAAQYDINFTMDAEEADRLALSLKLLDRLAREPELGGWTGLG 319
Cdd:PRK11904 242 PARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 320 LAVQAYQKRCPEVIRRVSELAKSSGRRLMVRLVKGAYWDTEIKRAQVFGRTDYPVFTTKAATDLNYLVCAKAMIEAAPHI 399
Cdd:PRK11904 322 LAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 400 YSQFATHNAHSLAAVYKMASERavKIEFQRLHGMGEALYDAAHDAFGpVTVRAYAPVGGHEDLLPYLVRRLLENGANSSF 479
Cdd:PRK11904 402 YPQFATHNAHTVAAILEMAGHR--GFEFQRLHGMGEALYDALLDAPG-IPCRIYAPVGSHKDLLPYLVRRLLENGANSSF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 480 VHALLDERVPASAVAADPISAVEAHPD-RHAKIPTPKDMY-MDRQNSLGRDYSQAADRERHAVALQKVDSETLTAGPIIG 557
Cdd:PRK11904 479 VHRLVDPDVPIEELVADPVEKLRSFETlPNPKIPLPRDIFgPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPIIN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 558 GklkaGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSRE 637
Cdd:PRK11904 559 G----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVRE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 638 AGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGPVGEINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNA 717
Cdd:PRK11904 635 AGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNT 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 718 VLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIIPFI 797
Cdd:PRK11904 715 VIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLI 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 798 AETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVID 877
Cdd:PRK11904 795 AETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVID 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 878 ADARAMLEAHLKRLEGDAKIIARAELPAGADKGHLFAPTIAEIPTADYLEREVFGPILHVCRYEPSKLKETASKLAARGY 957
Cdd:PRK11904 875 AEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAINATGY 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 958 GLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFASEKAISNNISAQGGDP 1037
Cdd:PRK11904 955 GLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNTTAAGGNA 1034
|
....
gi 2521504918 1038 ALLN 1041
Cdd:PRK11904 1035 SLLS 1038
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
16-1040 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1347.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 16 DALDQGKFADETATVRGLLANMPLDGAERAAVLGEAIGLVERARASVKKQGVvESFLQEFSLGTREGLALMCLAEALLRT 95
Cdd:PRK11905 17 QAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTGV-EALLQEYSLSSQEGVALMCLAEALLRI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 96 PDEETRDRLIAEKIGSADWSSHLGQSDSLFVNASTWGLMLTGKLVDVDEEARtdLPGFLKRIVGRLGEPVIREAVAAAVR 175
Cdd:PRK11905 96 PDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRG--LSAALTRLIARLGEPVIRKAVDMAMR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 176 IMGEQFVVGRTIEAALKRS---NREGWLCSFDMLGEGARTAHDAERYEKIYADAITAVGKTAKGQGPEAGHGVSVKLSAL 252
Cdd:PRK11905 174 MMGEQFVTGETIEEALKRArelEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGVYDGPGISVKLSAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 253 SPRYEATHEARVWDELYPRILRLARIAAQYDINFTMDAEEADRLALSLKLLDRLAREPELGGWTGLGLAVQAYQKRCPEV 332
Cdd:PRK11905 254 HPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIGFVVQAYQKRCPFV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 333 IRRVSELAKSSGRRLMVRLVKGAYWDTEIKRAQVFGRTDYPVFTTKAATDLNYLVCAKAMIEAAPHIYSQFATHNAHSLA 412
Cdd:PRK11905 334 IDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVIYPQFATHNAQTLA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 413 AVYKMASERAvKIEFQRLHGMGEALYD--AAHDAFGpVTVRAYAPVGGHEDLLPYLVRRLLENGANSSFVHALLDERVPA 490
Cdd:PRK11905 414 AIYELAGGKG-DFEFQCLHGMGEPLYDqvVGKEKLG-RPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNRIVDENVPV 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 491 SAVAADPISAVEAHPD-RHAKIPTPKDMYM-DRQNSLGRDYSQAADRERHAVALQKVDSETLTAGPIIGGKlKAGTNAQP 568
Cdd:PRK11905 492 EELIADPVEKVAAMGVaPHPQIPLPRDLYGpERRNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLAGG-DVDGGTRP 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAE 648
Cdd:PRK11905 571 VLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 649 IREAADFCRYYAMLAERDFGGPTELkgpvgeinqlvlhGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPL 728
Cdd:PRK11905 651 VREAVDFLRYYAAQARRLLNGPGHK-------------PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPL 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 729 IAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIIPFIAETGGLNGMFV 808
Cdd:PRK11905 718 IAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLIAETGGQNAMIV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 809 DTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHL 888
Cdd:PRK11905 798 DSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHI 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 889 KRLEGDAKIIARAELPAGADKGHLFAPTIAEIPTADYLEREVFGPILHVCRYEPSKLKETASKLAARGYGLTLGVHSRIE 968
Cdd:PRK11905 878 EAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGLHSRID 957
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2521504918 969 AFAEEVARLVPAGNVYINRSIIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFASEKAISNNISAQGGDPALL 1040
Cdd:PRK11905 958 ETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPIPPAHESVDTDAA 1029
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
1-1042 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1140.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 1 MNAHVSPPVALSQDWDALDQgkfADETATVRGLLANMPLDGAERAAVLGEAIGLVERARAsVKKQGVVESFLQEFSLGTR 80
Cdd:COG4230 6 FAPLLRPALPLRAAIAAAER---AEELLAAAALLAAAALAAAAAAAAAAAALAARERVRA-RRGGGGGLLLLLELSSLSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 81 EGLALMCLAEALLRTPDeeTRDRLIAEKIGSADWSSHLGQSDSLFVNASTWGLMLTGKLVDVDEEARTDLPGFLKRIVGR 160
Cdd:COG4230 82 EALALLLLALLLLALAA--TRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 161 LGEPVIREAVAAAVRIMGEQFVVGRTIEAAL--KRSNREGWLC-----SFDMLGEGARTAHDAERYEKIYADAITAVGKT 233
Cdd:COG4230 160 LGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAeaARKAARKREYyyydmLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 234 AKGQGPEAGHGVSVKLSALSPRYEATHEARVWDELYPRILRLARIAAQYDINFTMDAEEADRLALSLKLLDRLAREPELG 313
Cdd:COG4230 240 SGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 314 GWTGLGLAVQAYQKRCPEVIRRVSELAKSSGRRLMVRLVKGAYWDTEIKRAQVFGRTDYPVFTTKAATDLNYLVCAKAMI 393
Cdd:COG4230 320 GGGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 394 EAAPHIYSQFATHNAHSLAAVYKMASERavKIEFQRLHGMGEALYDAAHDAFGPVTVRAYAPVGGHEDLLPYLVRRLLEN 473
Cdd:COG4230 400 AAQPAFAPQFATHAAATAAAAAAAGGGG--EFEFQCLHGMGEYLYDQVGRGKLGRPCRIYAPVGSHEDLLAYLVRRLLEN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 474 GANSSFVHALLDERVPASAVAADPISAVEAHPD-RHAKIPTPKDMY-MDRQNSLGRDYSQAADRERHAVALQKVDSETLT 551
Cdd:COG4230 478 GANSSFVNRIADEDVPVEELIADPVEKARALGGaPHPRIPLPRDLYgPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQ 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 552 AGPIIGGKLKAGTnAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLV 631
Cdd:COG4230 558 AAPLIAGEAASGE-ARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELM 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 632 ALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTelkgpvgeinqlVLHGRGVFACISPWNFPLAIFTGQIAAA 711
Cdd:COG4230 637 ALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPT------------VLRGRGVFVCISPWNFPLAIFTGQVAAA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 712 LAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPG 791
Cdd:COG4230 705 LAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDG 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 792 AIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATD 871
Cdd:COG4230 785 PIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTD 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 872 IGPVIDADARAMLEAHLKRLEGDAKIIARAELPAGADKGHLFAPTIAEIPTADYLEREVFGPILHVCRYEPSKLKETASK 951
Cdd:COG4230 865 VGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDA 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 952 LAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFASEKAISNNIS 1031
Cdd:COG4230 945 INATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTT 1024
|
1050
....*....|.
gi 2521504918 1032 AQGGDPALLNL 1042
Cdd:COG4230 1025 AAGGNASLLAL 1035
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
26-1039 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1113.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 26 ETATVRGLL--ANMPLDGAERAAVLgeAIGLVERARASVK---KQGVVESFLQEFSLGTREGLALMCLAEALLRTPDEET 100
Cdd:PRK11809 103 ETEAVPMLLeqARLPAPLAEAAHKL--AYQLAEKLRNQKSaggRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKAT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 101 RDRLIAEKIGSADWSSHLGQSDSLFVNASTWGLMLTGKLVDVDEEArtDLPGFLKRIVGRLGEPVIREAVAAAVRIMGEQ 180
Cdd:PRK11809 181 RDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEA--SLSSSLNRIIGKSGEPLIRKGVDMAMRLMGEQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 181 FVVGRTIEAALKRSNR---EGWLCSFDMLGEGARTAHDAERYEKIYADAITAVGKTAKGQGPEAGHGVSVKLSALSPRYE 257
Cdd:PRK11809 259 FVTGETIAEALANARKleeKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGIYEGPGISIKLSALHPRYS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 258 ATHEARVWDELYPRILRLARIAAQYDINFTMDAEEADRLALSLKLLDRLAREPELGGWTGLGLAVQAYQKRCPEVIRRVS 337
Cdd:PRK11809 339 RAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLI 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 338 ELAKSSGRRLMVRLVKGAYWDTEIKRAQVFGRTDYPVFTTKAATDLNYLVCAKAMIEAAPHIYSQFATHNAHSLAAVYKM 417
Cdd:PRK11809 419 DLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLIYPQFATHNAHTLAAIYHL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 418 ASER--AVKIEFQRLHGMGEALYDaahDAFGPVT-------VRAYAPVGGHEDLLPYLVRRLLENGANSSFVHALLDERV 488
Cdd:PRK11809 499 AGQNyyPGQYEFQCLHGMGEPLYE---QVVGKVAdgklnrpCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTSL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 489 PASAVAADPISAVEAHPDR-------HAKIPTPKDMY-MDRQNSLGRDYSQAADRERHAVALQKVDSETLTAGPIIGGKL 560
Cdd:PRK11809 576 PLDELVADPVEAVEKLAQQegqlglpHPKIPLPRDLYgKGRANSAGLDLANEHRLASLSSALLASAHQKWQAAPMLEDPV 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 561 KAGTnAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGK 640
Cdd:PRK11809 656 AAGE-MSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 641 TLNDGVAEIREAADFCRYYAMLAERDFGGPTELK-GPVgeinqlvlhgrgvfACISPWNFPLAIFTGQIAAALAAGNAVL 719
Cdd:PRK11809 735 TFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPlGPV--------------VCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 720 AKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAAR---PGAIIPF 796
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRldpQGRPIPL 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 797 IAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVI 876
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 877 DADARAMLEAHLKRLEGDAKIIARAELPAGAD--KGHLFAPTIAEIPTADYLEREVFGPILHVCRYEPSKLKETASKLAA 954
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSEDwqSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQINA 1040
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 955 RGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFAS---EKAISNNIS 1031
Cdd:PRK11809 1041 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLAtrpEDALAVTLA 1120
|
....*...
gi 2521504918 1032 AQGGDPAL 1039
Cdd:PRK11809 1121 RQDAEYPV 1128
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
475-1040 |
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: 699.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 475 ANSSFVHALLDERVPAsavaadpisaveahpdrhakiptpkdmymdrqnslgrdysqaadrERHAVALQKVDSETLTAGP 554
Cdd:cd07125 1 ANSSFVNRIFDLEVPL---------------------------------------------EALADALKAFDEKEWEAIP 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 555 IIGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALL 634
Cdd:cd07125 36 IINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 635 SREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPtELKGPVGEINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAA 714
Cdd:cd07125 116 AAEAGKTLADADAEVREAIDFCRYYAAQARELFSDP-ELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 715 GNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAII 794
Cdd:cd07125 195 GNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPIL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 795 PFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGP 874
Cdd:cd07125 275 PLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 875 VIDADARAMLEAHLKRLEGDAKIIARAelPAGADKGHLFAPTIAEIPTADYLEREVFGPILHVCRYEPSKLKETASKLAA 954
Cdd:cd07125 355 LIDKPAGKLLRAHTELMRGEAWLIAPA--PLDDGNGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEAIEDINA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 955 RGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFASEKAISNNISAQG 1034
Cdd:cd07125 433 TGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLNTTAAG 512
|
....*.
gi 2521504918 1035 GDPALL 1040
Cdd:cd07125 513 GNPSLL 518
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
38-1036 |
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: 556.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 38 PLDGAERAAVLGEAIGLVERARAsvKKQGVVESFLQEFSLGTREGLALMCLAEALLRTPDEETRDRLIAEKIGsadwssh 117
Cdd:COG0506 4 ALDEALRARAVALARRLVEAIRA--APEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 118 lgQSDSLFVNASTWGLMLTgklvdvdeeartdlpgflkrIVGRLGEPVIREAVAAAVRIMGEQFVVGRTIEAALKRS--- 194
Cdd:COG0506 75 --KSPSFLVNASTWGLMLT--------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAArkl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 195 NREGWLCSFDMLGEGARTAHDAERYEKIYADAITAVGKTAkgqgpEAGHGVSVKLSALSPRYEATHEARVWDELYPRILR 274
Cdd:COG0506 133 RAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERLRP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 275 LARIAAQYDINFTMDAEEADRLALSLKLLDRLAREPELGGWTGLGLAVQAYQKRCPEVIRRVSELAKSSGRRLMVRLVKG 354
Cdd:COG0506 208 LARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 355 AYWDTEIKRAQVFGRtDYPVFTTKAATDLNYLVCAKAMIEAAPHIYSQFATHNAHSLAAVYKMASERAVK---IEFQRLH 431
Cdd:COG0506 288 AYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGERGRPpdrFEFQMLY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 432 GMGEALYDAAHDAFGPVTVRA--YAPVGGHEDLLPYLVRRLLENGANSSFVHALLDERVPASAVAADPISAVEAHPDRHA 509
Cdd:COG0506 367 GMGEDLQRALAAVDGGRLLLYcpVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 510 KIPTPKDMYMDRQ-NSLGRDYSQAADRERHAVALQKVDSETLTAGPIIGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEA 588
Cdd:COG0506 447 PPPPPLRRQRRRRrRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 589 DIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFG 668
Cdd:COG0506 527 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAA 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 669 GPTELKGPVGEINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLA 748
Cdd:COG0506 607 APPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLV 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 749 LVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGS 828
Cdd:COG0506 687 LGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASA 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 829 SGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRLEGDAKIIARAELPAGAD 908
Cdd:COG0506 767 SASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGL 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 909 KGHLFAPTIAEIPTADYLEREVFGPILHVCRYEPSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRS 988
Cdd:COG0506 847 LTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGG 926
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*...
gi 2521504918 989 IIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFASEKAISNNISAQGGD 1036
Cdd:COG0506 927 GGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAA 974
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
521-1022 |
1.85e-161 |
|
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: 485.57 E-value: 1.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 521 RQNSLGRDYSQAADRERHAVALQKVDSETLTAGPIIGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARA 600
Cdd:TIGR01238 7 RKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 601 QIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGgptelkgpvgei 680
Cdd:TIGR01238 87 FPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLG------------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 681 nQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAK 760
Cdd:TIGR01238 155 -EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 761 LVSHPGIDGVAFTGGTDTANLINRSLAARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLY 840
Cdd:TIGR01238 234 LTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 841 VPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRLEGDAKIIARAELPAGAD--KGHLFAPTIA 918
Cdd:TIGR01238 314 VQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRAcqHGTFVAPTLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 919 EIPTADYLEREVFGPILHVCRYEPSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQP 998
Cdd:TIGR01238 394 ELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQP 473
|
490 500
....*....|....*....|....
gi 2521504918 999 FGGEGLSGTGPKAGGPYSLIRFAS 1022
Cdd:TIGR01238 474 FGGQGLSGTGPKAGGPHYLYRLTQ 497
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
535-1030 |
8.96e-149 |
|
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: 452.80 E-value: 8.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 535 RERHAVALQKVDSETLTAGP-IIGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRG 613
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPlVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 614 AVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGPVGEINQLVLHGRGVFAC 693
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 694 ISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFT 773
Cdd:cd07083 161 ISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 774 GGTDTANLINRSLA---ARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALI 850
Cdd:cd07083 241 GSLETGKKIYEAAArlaPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 851 EGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRLEGDAKIIARAELPAGadKGHLFAPTIAEI--PTADYLER 928
Cdd:cd07083 321 ERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEG--EGYFVAPTVVEEvpPKARIAQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 929 EVFGPILHVCRYEPSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPFGGEGLSGTG 1008
Cdd:cd07083 399 EIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTN 478
|
490 500
....*....|....*....|..
gi 2521504918 1009 PKAGGPYSLIRFASEKAISNNI 1030
Cdd:cd07083 479 AKTGGPHYLRRFLEMKAVAERF 500
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
190-482 |
3.53e-133 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 404.18 E-value: 3.53e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 190 ALKRSNR---EGWLCSFDMLGEGARTAHDAERYEKIYADAITAVGKTAKGQGPEAGHGVSVKLSALSPRYEATHEARVWD 266
Cdd:pfam01619 1 ALKTIEKlrkQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 267 ELYPRILRLARIAAQYDINFTMDAEEADRLALSLKLLDRLAREPELGGWTGLGLAVQAYQKRCPEVIRRVSELAKSSGRR 346
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 347 LMVRLVKGAYWDTEIKRAQVFGRtDYPVFTTKAATDLNYLVCAKAMIEAAPHIYSQFATHNAHSLAAVYKMASERAVK-- 424
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQGGW-PYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEELGIPpr 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2521504918 425 -IEFQRLHGMGEALYDAAHDAfgPVTVRAYAPVGGHEDLLPYLVRRLLENGANSSFVHA 482
Cdd:pfam01619 240 rFEFQQLYGMGDNLSFALVAA--GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
522-1030 |
8.79e-113 |
|
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: 358.84 E-value: 8.79e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 522 QNSLGRDYSQAADRERHAVALQKVDSET-LTAGPIIGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARA 600
Cdd:cd07124 2 RNEPFTDFADEENRAAFRAALARVREELgREYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 601 QIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTElkGPVGEI 680
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVE--MVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 681 NQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAK 760
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 761 LVSHPGIDGVAFTGGTDTANLINRSLAAR-PGA--IIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALR 837
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYERAAKVqPGQkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 838 LLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRLEGDAKIIARAELPAGADKGHLFAPTI 917
Cdd:cd07124 320 RVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 918 -AEIPTADYLER-EVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVG 995
Cdd:cd07124 400 fADVPPDHRLAQeEIFGPVLAVIKAK--DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVG 477
|
490 500 510
....*....|....*....|....*....|....*
gi 2521504918 996 VQPFGGEGLSGTGPKAGGPYSLIRFASEKAISNNI 1030
Cdd:cd07124 478 RQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
556-1027 |
8.43e-106 |
|
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: 339.02 E-value: 8.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNAQ--PVTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVAL 633
Cdd:COG1012 10 IGGEWVAAASGEtfDVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 634 LSREAGKTLNDGVAEIREAADFCRYYAMLAERdFGGPTELKGPVGEINQLVLHGRGVFACISPWNFPLAIFTGQIaaala 713
Cdd:COG1012 89 LTLETGKPLAEARGEVDRAADFLRYYAGEARR-LYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLapala 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 714 agnavlaKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpgaI 793
Cdd:COG1012 168 agntvvlKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN---L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 794 IPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIG 873
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 874 PVIDADARAMLEAHLKR-LEGDAKIIARAELPAGaDKGHLFAPTIAEIPTADY--LEREVFGPILHVCRYEPSklkETAS 950
Cdd:COG1012 325 PLISEAQLERVLAYIEDaVAEGAELLTGGRRPDG-EGGYFVEPTVLADVTPDMriAREEIFGPVLSVIPFDDE---EEAI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2521504918 951 KLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGvQPFGGEGLSGTGPKaGGPYSLIRFASEKAIS 1027
Cdd:COG1012 401 ALANDTeYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGRE-GGREGLEEYTETKTVT 476
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
603-1026 |
3.47e-102 |
|
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: 327.63 E-value: 3.47e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERdFGGPTELKGPVGEINQ 682
Cdd:cd07078 13 AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARR-LHGEVIPSPDPGELAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 LVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLV 762
Cdd:cd07078 92 VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 763 SHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVP 842
Cdd:cd07078 172 SHPRVDKISFTGSTAVGKAIMRAAAEN---LKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 843 HDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAELPAGaDKGHLFAPTIAEIP 921
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDaKAEGAKLLCGGKRLEG-GKGYFVPPTVLTDV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 922 TADYL--EREVFGPILHVCRYEPskLKEtASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGvQP 998
Cdd:cd07078 328 DPDMPiaQEEIFGPVLPVIPFKD--EEE-AIELAnDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEPS-AP 403
|
410 420
....*....|....*....|....*...
gi 2521504918 999 FGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07078 404 FGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
561-1026 |
7.96e-95 |
|
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: 309.08 E-value: 7.96e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 561 KAGTNAQPVTNPFDTTrVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGK 640
Cdd:pfam00171 3 DSESETIEVINPATGE-VIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 641 TLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGpvGEINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLA 720
Cdd:pfam00171 82 PLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDP--GRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 721 KPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAET 800
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN---LKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 801 GGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADA 880
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 881 RAMLEAHLKR-LEGDAKIIARAElpAGADKGHLFAPTI-AEIPTADYLER-EVFGPILHVCRYepSKLKEtASKLA-ARG 956
Cdd:pfam00171 317 LERVLKYVEDaKEEGAKLLTGGE--AGLDNGYFVEPTVlANVTPDMRIAQeEIFGPVLSVIRF--KDEEE-AIEIAnDTE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 957 YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVqPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLEEYTEVKTV 459
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
528-1030 |
6.23e-86 |
|
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: 286.76 E-value: 6.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 528 DYSQAADRERHAVALQKVdSETL--TAGPIIGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWD 605
Cdd:TIGR01237 8 DFADEENRQAFFKALATV-KEQLgkTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 606 RKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGPvGEINQLVL 685
Cdd:TIGR01237 87 KTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSRE-GETNQYVY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 686 HGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHP 765
Cdd:TIGR01237 166 TPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 766 GIDGVAFTGGTDTANLIN-RSLAARPGA--IIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVP 842
Cdd:TIGR01237 246 KTSLITFTGSREVGTRIFeRAAKVQPGQkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 843 HDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRLEGDAKIIARAElpAGADKGHLFAPTI-AEI- 920
Cdd:TIGR01237 326 EKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGC--GDDSKGYFIGPTIfADVd 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 921 PTADYLEREVFGPILHVCRyePSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPFG 1000
Cdd:TIGR01237 404 RKARLAQEEIFGPVVAFIR--ASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFG 481
|
490 500 510
....*....|....*....|....*....|
gi 2521504918 1001 GEGLSGTGPKAGGPYSLIRFASEKAISNNI 1030
Cdd:TIGR01237 482 GFKMSGTDSKAGGPDYLALFMQAKTVTEMF 511
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
528-1027 |
6.15e-80 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 270.27 E-value: 6.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 528 DYSQAADRERHAVALQKVDSETLTAGP-IIGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDR 606
Cdd:PRK03137 12 DFSVEENVEAFEEALKKVEKELGQDYPlIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 607 KGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYA--MLAERDfgGPTELKGPvGEINQLV 684
Cdd:PRK03137 92 WSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYArqMLKLAD--GKPVESRP-GEHNRYF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 685 LHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSH 764
Cdd:PRK03137 169 YIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 765 PGIDGVAFTGGTDTANLIN-RSLAARPGA--IIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYV 841
Cdd:PRK03137 249 PKTRFITFTGSREVGLRIYeRAAKVQPGQiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 842 PHDAADALIEGLKGALAAQVVGDPTDPAtDIGPVIDADARAMLEAHLKRLEGDAKIIARAElpAGADKGHLFAPTI-AEI 920
Cdd:PRK03137 329 HEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVINQASFDKIMSYIEIGKEEGRLVLGGE--GDDSKGYFIQPTIfADV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 921 -PTADYLEREVFGPILHVCRyepSKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQP 998
Cdd:PRK03137 406 dPKARIMQEEIFGPVVAFIK---AKDFDHALEIANNTeYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHP 482
|
490 500
....*....|....*....|....*....
gi 2521504918 999 FGGEGLSGTGPKAGGPYSLIRFASEKAIS 1027
Cdd:PRK03137 483 FGGFNMSGTDSKAGGPDYLLLFLQAKTVS 511
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
603-1026 |
2.91e-76 |
|
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: 255.23 E-value: 2.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAeRDFGGPTELKGPVGEINQ 682
Cdd:cd06534 9 AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLA-DKLGGPELPSPDPGGEAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 LVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLV 762
Cdd:cd06534 88 VRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 763 SHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVP 842
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKAAAEN---LKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 843 HDAADALIEGLKGALAAqvvgdptdpatdigpvIDADARAMLEahlkrlegdakiiaraelpagadkghlfaptiaeipt 922
Cdd:cd06534 245 ESIYDEFVEKLVTVLVD----------------VDPDMPIAQE------------------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 923 adylerEVFGPILHVCRYEPsklKETASKLAAR-GYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGvQPFGG 1001
Cdd:cd06534 272 ------EIFGPVLPVIRFKD---EEEAIALANDtEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGG 341
|
410 420
....*....|....*....|....*
gi 2521504918 1002 EGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd06534 342 VKNSGIG-REGGPYGLEEYTRTKTV 365
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
556-1026 |
8.35e-75 |
|
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: 254.87 E-value: 8.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLS 635
Cdd:cd07097 5 IDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 636 REAGKTLNDGVAEIREAADFCRYYAMLAERdFGG---PTELKGPVGEINQLVLhgrGVFACISPWNFPLAIFTGQIAAAL 712
Cdd:cd07097 85 REEGKTLPEARGEVTRAGQIFRYYAGEALR-LSGetlPSTRPGVEVETTREPL---GVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 713 AAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpGA 792
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR-GA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 793 IIPfiAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDI 872
Cdd:cd07097 240 RVQ--LEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 873 GPVIDADARAMLEAHLK--RLEGdAKIIARAELPAGADKGHLFAPTIAEIPTADY--LEREVFGPILHVCRYEpsKLKET 948
Cdd:cd07097 318 GPVVSERQLEKDLRYIEiaRSEG-AKLVYGGERLKRPDEGYYLAPALFAGVTNDMriAREEIFGPVAAVIRVR--DYDEA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2521504918 949 ASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVqPFGGEGLSGTGPKAGGPYSLIRFASEKAI 1026
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
571-1031 |
3.42e-64 |
|
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: 225.30 E-value: 3.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 571 NPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIR 650
Cdd:cd07131 20 NPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 651 EAADFCRYYAMLAERDFGG--PTELKGpvgEINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPL 728
Cdd:cd07131 100 EAIDMAQYAAGEGRRLFGEtvPSELPN---KDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 729 IAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRsLAARPGAIIPfiAETGGLNGMFV 808
Cdd:cd07131 177 CALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE-TCARPNKRVA--LEMGGKNPIIV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 809 DTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDadaRAMLEAHL 888
Cdd:cd07131 254 MDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLIN---EAQLEKVL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 889 K-----RLEGDAKIIARAELPAGA-DKGHLFAPTIAEIPTAD--YLEREVFGPilHVCRYEPSKLKETASKLAARGYGLT 960
Cdd:cd07131 331 NyneigKEEGATLLLGGERLTGGGyEKGYFVEPTVFTDVTPDmrIAQEEIFGP--VVALIEVSSLEEAIEIANDTEYGLS 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2521504918 961 LGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVqPFGGEGLSGTGPKAGGPYSLIRFASEKAISNNIS 1031
Cdd:cd07131 409 SAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGTTALDAFTEWKAVYVDYS 478
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
612-1012 |
7.30e-62 |
|
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: 218.59 E-value: 7.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 612 RGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGG--PTELKGpvgEINQLVLHGRG 689
Cdd:cd07086 59 RGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLtiPSERPG---HRLMEQWNPLG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 690 VFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKA----GLDPNLLALVPGRGEtVGAKLVSHP 765
Cdd:cd07086 136 VVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 766 GIDGVAFTGGTDTANLINRSLAARPGAIIpfiAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDA 845
Cdd:cd07086 215 RVPLVSFTGSTEVGRRVGETVARRFGRVL---LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 846 ADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLK--RLEGdAKIIARAELPAGADKGHLFAPTIAEIPT- 922
Cdd:cd07086 292 YDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEiaKSQG-GTVLTGGKRIDGGEPGNYVEPTIVTGVTd 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 923 -ADYLEREVFGPILHVCRYepSKLKETASKLAARGYGLTLGVHSR--IEAFAEEVARLVPAGNVYINRSIIGAVVGVqPF 999
Cdd:cd07086 371 dARIVQEETFAPILYVIKF--DSLEEAIAINNDVPQGLSSSIFTEdlREAFRWLGPKGSDCGIVNVNIPTSGAEIGG-AF 447
|
410
....*....|...
gi 2521504918 1000 GGEGLSGTGPKAG 1012
Cdd:cd07086 448 GGEKETGGGRESG 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
603-1012 |
7.47e-62 |
|
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: 218.19 E-value: 7.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTelkgPVGEINQ 682
Cdd:cd07114 36 AWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVI----PVDKGDY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 LVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGA 759
Cdd:cd07114 112 LNFTRReplGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 760 KLVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETGGL--NGMFVDttALKEQIIDDVILSAFGSSGQRCSALR 837
Cdd:cd07114 192 ALVEHPLVAKIAFTGGTETGRHIARAAAEN---LAPVTLELGGKspNIVFDD--ADLDAAVNGVVAGIFAAAGQTCVAGS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 838 LLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAELPAGAD--KGHLFA 914
Cdd:cd07114 267 RLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARaREEGARVLTGGERPSGADlgAGYFFE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 915 PTIAEIPTADY--LEREVFGPILHVCRYEPsklKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN--RSI 989
Cdd:cd07114 347 PTILADVTNDMriAQEEVFGPVLSVIPFDD---EEEAIALAnDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNtyRAL 423
|
410 420
....*....|....*....|...
gi 2521504918 990 IGAVvgvqPFGGEGLSGTGPKAG 1012
Cdd:cd07114 424 SPSS----PFGGFKDSGIGRENG 442
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
569-1026 |
5.56e-61 |
|
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: 215.51 E-value: 5.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVA- 647
Cdd:cd07093 1 NFNPA-TGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 648 EIREAADFCRYYAMLAERDFGgpTELKGPVGEINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTP 727
Cdd:cd07093 80 DIPRAAANFRFFADYILQLDG--ESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 728 LIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMF 807
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN---LKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 808 VDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDadaramlEAH 887
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLIS-------KEH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 888 LKRLEG--------DAKIIA---RAELPaGADKGHLFAPTIAEIPTAD--YLEREVFGPILHVcryEPSKLKETASKLA- 953
Cdd:cd07093 308 LEKVLGyvelaraeGATILTgggRPELP-DLEGGYFVEPTVITGLDNDsrVAQEEIFGPVVTV---IPFDDEEEAIELAn 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 954 ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN-------RsiigavvgvQPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07093 384 DTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNcwlvrdlR---------TPFGGVKASGIG-REGGDYSLEFYTELKNV 453
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
68-181 |
5.06e-60 |
|
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: 200.42 E-value: 5.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 68 VESFLQEFSLGTREGLALMCLAEALLRTPDEETRDRLIAEKIGSADWSSHLGQSDSLFVNASTWGLMLTGKLVDVDEEAR 147
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|....
gi 2521504918 148 tdLPGFLKRIVGRLGEPVIREAVAAAVRIMGEQF 181
Cdd:pfam14850 81 --LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
601-1006 |
9.35e-58 |
|
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: 205.58 E-value: 9.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 601 QIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIReaadfcryyAMLAERDFG--------GPTE 672
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVA---------AMAGKIDISikayhertGERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 673 LkgPVGEINQLVLH-GRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVP 751
Cdd:cd07095 84 T--PMAQGRAVLRHrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 752 GRGETvGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIIPFiaETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQ 831
Cdd:cd07095 162 GGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILAL--EMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 832 RCSALRLLYVPHDA-ADALIEGLKGALAAQVVGDPT-DPATDIGPVIDADARAMLEAHLKRLEGDAKIIARAElpAGADK 909
Cdd:cd07095 239 RCTCARRLIVPDGAvGDAFLERLVEAAKRLRIGAPDaEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME--RLVAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 910 GHLFAPTIAEI-PTADYLEREVFGPILHVCRYEPSklkETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINR 987
Cdd:cd07095 317 TAFLSPGIIDVtDAADVPDEEIFGPLLQVYRYDDF---DEAIALAnATRFGLSAGLLSDDEALFERFLARIRAGIVNWNR 393
|
410
....*....|....*....
gi 2521504918 988 SIIGAvVGVQPFGGEGLSG 1006
Cdd:cd07095 394 PTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
533-1029 |
5.21e-57 |
|
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: 205.90 E-value: 5.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 533 ADRERHAVALQKVDSETLTAGPIIGGKLKAGTNAQPVTNPFDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGR 612
Cdd:cd07123 14 PERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 613 GAV-LRAmadaleADM------DRLVALLSREAGKTLndGVAEIR---EAADFCRYYAMLAERDFGGPtELKGPVGEINQ 682
Cdd:cd07123 94 AAIfLKA------ADLlsgkyrYELNAATMLGQGKNV--WQAEIDaacELIDFLRFNVKYAEELYAQQ-PLSSPAGVWNR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 LV---LHGRgVFAcISPWNFPlAIFTGQIAAALAAGNAVLAKPAEqTPLIAAEAV-RLYYKAGLDPNLLALVPGRGETVG 758
Cdd:cd07123 165 LEyrpLEGF-VYA-VSPFNFT-AIGGNLAGAPALMGNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 759 AKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIIPF---IAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSA 835
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYpriVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 836 LRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRlegdAKIIARAELPAGA----DKGH 911
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDH----AKSDPEAEIIAGGkcddSVGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 912 LFAPTI--AEIPTADYLEREVFGPILHVCRYEPSKLKETASKL-AARGYGLTLGVHSRIEAF---AEEVARLVpAGNVYI 985
Cdd:cd07123 397 FVEPTVieTTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVdTTSPYALTGAIFAQDRKAireATDALRNA-AGNFYI 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2521504918 986 NRSIIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFASEKAISNN 1029
Cdd:cd07123 476 NDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKET 519
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
562-1026 |
7.56e-57 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 204.04 E-value: 7.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 562 AGTNAQPVTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKT 641
Cdd:cd07088 10 SSGETIDVLNPA-TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 642 LNDGVAEIREAADFCRYYAMLAERDfggptelkgpVGEINQ-------LVLHGR--GVFACISPWNFPLAIFTGQIAAAL 712
Cdd:cd07088 89 LSLARVEVEFTADYIDYMAEWARRI----------EGEIIPsdrpnenIFIFKVpiGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 713 AAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpga 792
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAEN--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 793 IIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDI 872
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 873 GPVIDADARAMLEAHLKR-LEGDAKIIARAELPAGaDKGHLFAPTIAEI--PTADYLEREVFGPILHVCRYepSKLKETA 949
Cdd:cd07088 316 GPLVNEAALDKVEEMVERaVEAGATLLTGGKRPEG-EKGYFYEPTVLTNvrQDMEIVQEEIFGPVLPVVKF--SSLDEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2521504918 950 SKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQpfGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07088 393 ELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLG-GADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
569-1008 |
4.09e-56 |
|
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: 201.22 E-value: 4.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAE 648
Cdd:cd07106 1 VINP-ATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 649 IREAADFCRYYAMLA------ERDFGGPTELK-GPVgeinqlvlhgrGVFACISPWNFPLAIFTGQIAAALAAGNAVLAK 721
Cdd:cd07106 80 VGGAVAWLRYTASLDlpdeviEDDDTRRVELRrKPL-----------GVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 722 PAEQTPLIAAEAVRLYYKAgLDPNLLALVPGRGEtVGAKLVSHPGIDGVAFTGGTDTANLINRSLAarpGAIIPFIAETG 801
Cdd:cd07106 149 PSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAA---KTLKRVTLELG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 802 GLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPV------ 875
Cdd:cd07106 224 GNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVqnkmqy 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 876 -----IDADARAmleahlkrleGDAKIIARAELPAGadKGHLFAPTIAEIPTAD--YLEREVFGPILHVCRYepSKLKET 948
Cdd:cd07106 304 dkvkeLVEDAKA----------KGAKVLAGGEPLDG--PGYFIPPTIVDDPPEGsrIVDEEQFGPVLPVLKY--SDEDEV 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 949 ASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSiiGAVVGVQPFGGEGLSGTG 1008
Cdd:cd07106 370 IARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
555-1008 |
5.80e-56 |
|
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: 201.65 E-value: 5.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 555 IIGGKLK-AGTNAQPVTNPFDTtRVLGHVSEATEADIDAAVDAAARAQ-IAWDRKGGAGRGAVLRAMADALEADMDRLVA 632
Cdd:cd07082 5 LINGEWKeSSGKTIEVYSPIDG-EVIGSVPALSALEILEAAETAYDAGrGWWPTMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 633 LLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGP------TELKGPVGEINQLVLhgrGVFACISPWNFPL----- 701
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSlpgdwfPGTKGKIAQVRREPL---GVVLAIGPFNYPLnltvs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 702 ----AIFTGQiaaalaagnAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTD 777
Cdd:cd07082 161 klipALIMGN---------TVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 778 TANLInrslaARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGAL 857
Cdd:cd07082 232 VGNRL-----KKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 858 AAQVVGDPTDPATDIGPVIDADARAMLEAHLKrlegDAKII-ARAELPAGADKGHLFAPTIAEIPTAD---YLErEVFGP 933
Cdd:cd07082 307 AKLKVGMPWDNGVDITPLIDPKSADFVEGLID----DAVAKgATVLNGGGREGGNLIYPTLLDPVTPDmrlAWE-EPFGP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 934 ILHVCRYepsKLKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN----RSIigavvGVQPFGGEGLSGTG 1008
Cdd:cd07082 382 VLPIIRV---NDIEEAIELAnKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIG 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
575-1026 |
8.56e-56 |
|
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: 200.53 E-value: 8.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 575 TTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAAD 654
Cdd:cd07099 5 TGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 655 FCRYYAMLAERdFGGPTELKGPVGEINQ---LVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAA 731
Cdd:cd07099 85 AIDWAARNAPR-VLAPRKVPTGLLMPNKkatVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 732 EAVRLYYKAGLDPNLLALVPGRGETvGAKLVSHpGIDGVAFTGGTDTANLINRSLAARPgaiIPFIAETGGLNGMFVDTT 811
Cdd:cd07099 164 LLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDA-GVDKVAFTGSVATGRKVMAAAAERL---IPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 812 ALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR- 890
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 891 LEGDAKIIARAELPAGadKGHLFAPTI-AEIP-TADYLEREVFGPILHVCRYepSKLKETASKLAARGYGLTLGVHSRIE 968
Cdd:cd07099 319 VAKGAKALTGGARSNG--GGPFYEPTVlTDVPhDMDVMREETFGPVLPVMPV--ADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2521504918 969 AFAEEVARLVPAGNVYINRSIIGAVVGVQPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPKAI 451
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
569-1017 |
6.95e-55 |
|
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: 198.04 E-value: 6.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAE 648
Cdd:cd07103 1 VINPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 649 IREAADFCRYYAMLAERDFGgpTELKGPVGEINQLVLHGR-GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTP 727
Cdd:cd07103 80 VDYAASFLEWFAEEARRIYG--RTIPSPAPGKRILVIKQPvGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 728 LIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTAnlinRSLAARPGA-IIPFIAETGGlNGM 806
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVG----KLLMAQAADtVKRVSLELGG-NAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 807 F-VDTTALKEQIIDDVILSAFGSSGQRC-SALRlLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAML 884
Cdd:cd07103 233 FiVFDDADLDKAVDGAIASKFRNAGQTCvCANR-IYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 885 EAHLKR-LEGDAKIIARAElpAGADKGHLFAPTI-AEIPT-ADYLEREVFGPILHVCRYEPSklkETASKLAARG-YGLT 960
Cdd:cd07103 312 EALVEDaVAKGAKVLTGGK--RLGLGGYFYEPTVlTDVTDdMLIMNEETFGPVAPIIPFDTE---DEVIARANDTpYGLA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2521504918 961 LGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVvgVQPFGGEGLSGTGpKAGGPYSL 1017
Cdd:cd07103 387 AYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG-REGGKEGL 440
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
601-1006 |
1.42e-53 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 195.18 E-value: 1.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 601 QIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIReaadfcryyAML--------AERDFGGPTE 672
Cdd:PRK09457 50 FPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVT---------AMInkiaisiqAYHERTGEKR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 673 lkGPVGEINQLVLHG-RGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVP 751
Cdd:PRK09457 121 --SEMADGAAVLRHRpHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 752 GRGETvGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIIPFiaETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQ 831
Cdd:PRK09457 199 GGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILAL--EMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 832 RCSALRLLYVPHDA-ADALIEGLKGALAAQVVGDP-TDPATDIGPVIDAD-ARAMLEAHLKRLEGDAKIIARAELPAgAD 908
Cdd:PRK09457 276 RCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWdAEPQPFMGAVISEQaAQGLVAAQAQLLALGGKSLLEMTQLQ-AG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 909 KGhLFAPTIAEI-PTADYLEREVFGPILHVCRYEPSklkETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN 986
Cdd:PRK09457 355 TG-LLTPGIIDVtGVAELPDEEYFGPLLQVVRYDDF---DEAIRLAnNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWN 430
|
410 420
....*....|....*....|
gi 2521504918 987 RSIIGAvVGVQPFGGEGLSG 1006
Cdd:PRK09457 431 KPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
569-1026 |
1.83e-53 |
|
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: 194.11 E-value: 1.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAE 648
Cdd:cd07110 1 VINPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 649 IREAADFCRYYAMLAER-DFGGPTELKGPVGEINQLVLH-GRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQT 726
Cdd:cd07110 80 VDDVAGCFEYYADLAEQlDAKAERAVPLPSEDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 727 PLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAArpgAIIPFIAETGGLNGM 806
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ---DIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 807 FVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEA 886
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 887 HLKR-LEGDAKIIARAELPAGADKGHLFAPTI-AEIPTADYLER-EVFGPILHVCRYepsKLKETASKLA-ARGYGLTLG 962
Cdd:cd07110 317 FIARgKEEGARLLCGGRRPAHLEKGYFIAPTVfADVPTDSRIWReEIFGPVLCVRSF---ATEDEAIALAnDSEYGLAAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2521504918 963 VHSRIEAFAEEVARLVPAGNVYINRSiigAVVGVQ-PFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWINCS---QPCFPQaPWGGYKRSGIG-RELGEWGLDNYLEVKQI 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
568-1033 |
9.24e-53 |
|
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: 192.53 E-value: 9.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 568 PVTNPFDTTrVLGHVSEAT--EADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDG 645
Cdd:cd07119 16 DIINPANGE-VIATVPEGTaeDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 646 VAEIREAADFCRYYAMLAERDFGGPTELKGPVgeINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQ 725
Cdd:cd07119 95 EIDIDDVANCFRYYAGLATKETGEVYDVPPHV--ISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 726 TPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAarpGAIIPFIAETGGLNG 805
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA---GNVKKVALELGGKNP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 806 MFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLE 885
Cdd:cd07119 250 NIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 886 AHLK--RLEGdAKIIARAELPAGAD--KGHLFAPTIAEIPTADY--LEREVFGPILHVcryEPSKLKETASKLAARG-YG 958
Cdd:cd07119 330 SYIQlgKEEG-ARLVCGGKRPTGDElaKGYFVEPTIFDDVDRTMriVQEEIFGPVLTV---ERFDTEEEAIRLANDTpYG 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2521504918 959 LTLGVHSRIEAFAEEVARLVPAGNVYINRsiIGAVVGVQPFGGEGLSGTGpKAGGPYSLIRFASEKAISNNISAQ 1033
Cdd:cd07119 406 LAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG-RELGPTGLEEYQETKHININLSPQ 477
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
569-1027 |
1.05e-52 |
|
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: 191.80 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPFDTTRVlGHVSEATEADIDAAVdaaaraQIAWDRKGGAG---RGAVLRAMADALEADMDRLVALLSREAGKTLNDG 645
Cdd:cd07146 3 VRNPYTGEVV-GTVPAGTEEALREAL------ALAASYRSTLTryqRSAILNKAAALLEARREEFARLITLESGLCLKDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 646 VAEIREAADFCRYYAMLAERDFGG--PTELKGPVGEinQLVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLA 720
Cdd:cd07146 76 RYEVGRAADVLRFAAAEALRDDGEsfSCDLTANGKA--RKIFTLReplGVVLAITPFNHPLNQVAHKIAPAIAANNRIVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 721 KPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLInrslAARPGaIIPFIAET 800
Cdd:cd07146 154 KPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI----AATAG-YKRQLLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 801 GGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADA 880
Cdd:cd07146 229 GGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 881 RAMLEAHLKRLEGD-AKIiaraeLPAGADKGHLFAPTIAE--IPTADYLEREVFGPILHVCRYEpsKLKETASKLAARGY 957
Cdd:cd07146 309 AIQIENRVEEAIAQgARV-----LLGNQRQGALYAPTVLDhvPPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAY 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 958 GLTLGVHSRIEAFAEEVARLVPAGNVYINrSIIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFASEKAIS 1027
Cdd:cd07146 382 GLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEGVREAMKEMTNVKTYS 450
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
612-1027 |
1.12e-52 |
|
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: 191.79 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 612 RGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGPVGEINQLVLHGR--- 688
Cdd:cd07145 45 RYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFTVRepi 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 689 GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGID 768
Cdd:cd07145 125 GVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 769 GVAFTGGTDTANLINrSLAARPGAIIpfIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADA 848
Cdd:cd07145 205 MISFTGSTAVGLLIA-SKAGGTGKKV--ALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 849 LIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHL-KRLEGDAKIIARAELPAGAdkghLFAPTIAEIPTAD--Y 925
Cdd:cd07145 282 FLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVnDAVEKGGKILYGGKRDEGS----FFPPTVLENDTPDmiV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 926 LEREVFGPILHVCRYEPSklkETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSiiGAV-VGVQPFGGEG 1003
Cdd:cd07145 358 MKEEVFGPVLPIAKVKDD---EEAVEIANSTeYGLQASVFTNDINRALKVARELEAGGVVINDS--TRFrWDNLPFGGFK 432
|
410 420
....*....|....*....|....
gi 2521504918 1004 LSGTGpKAGGPYSLIRFASEKAIS 1027
Cdd:cd07145 433 KSGIG-REGVRYTMLEMTEEKTIV 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
569-1026 |
9.83e-51 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 186.29 E-value: 9.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWD-RKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTL-NDGV 646
Cdd:cd07089 1 VINP-ATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 647 AEIREAADFCRYYAMLA-----ERDFGGPTELKGPVGEInqLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAK 721
Cdd:cd07089 80 MQVDGPIGHLRYFADLAdsfpwEFDLPVPALRGGPGRRV--VRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 722 PAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETG 801
Cdd:cd07089 158 PAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT---LKRVLLELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 802 GLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADAR 881
Cdd:cd07089 235 GKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 882 AMLEAHLK--RLEGdAKIIARAELPAGADKGHLFAPTI-AEIPTADYL-EREVFGPILHVCRYEPSklkETASKLA-ARG 956
Cdd:cd07089 315 DRVEGYIArgRDEG-ARLVTGGGRPAGLDKGFYVEPTLfADVDNDMRIaQEEIFGPVLVVIPYDDD---DEAVRIAnDSD 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2521504918 957 YGLTLGVHSRIEAFAEEVARLVPAGNVYINrsiiGAVVGV--QPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07089 391 YGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG-RENGIEGLEEFLETKSI 457
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
603-1030 |
1.33e-50 |
|
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: 185.72 E-value: 1.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGV-AEIREAADFCRYYAMLAERDFGGPTELKGPVgeIN 681
Cdd:cd07115 34 AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLDVPRAADTFRYYAGWADKIEGEVIPVRGPF--LN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 682 QLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKL 761
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 762 VSHPGIDGVAFTGGTDTANLINRSLAarpGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYV 841
Cdd:cd07115 192 VEHPDVDKITFTGSTAVGRKIMQGAA---GNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 842 PHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDadaramlEAHLKRL--------EGDAKIIARAELPagADKGHLF 913
Cdd:cd07115 269 HESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVS-------QAQFDRVldyvdvgrEEGARLLTGGKRP--GARGFFV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 914 APTI-AEIPTADYLER-EVFGPILHVCRYepsKLKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINrsII 990
Cdd:cd07115 340 EPTIfAAVPPEMRIAQeEIFGPVVSVMRF---RDEEEALRIAnGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TY 414
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2521504918 991 GAVVGVQPFGGEGLSGTGpKAGGPYSLIRFASEKAISNNI 1030
Cdd:cd07115 415 NRFDPGSPFGGYKQSGFG-REMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
556-1026 |
2.15e-50 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 185.40 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGK--LKAGTNAQPVTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVAL 633
Cdd:cd07138 3 IDGAwvAPAGTETIDVINP-ATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 634 LSREAGKTLND--------GVAEIREAADFCRYYAMlaERDFGGPTELKGPVGeinqlvlhgrgVFACISPWNFPLAIFT 705
Cdd:cd07138 82 ITLEMGAPITLaraaqvglGIGHLRAAADALKDFEF--EERRGNSLVVREPIG-----------VCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 706 GQIAAALAAGNAVLAKPAEQTPLIA---AEAVrlyYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLI 782
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAiilAEIL---DEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 783 NRsLAARpgAIIPFIAETGG--LNGMFVDttALKEQIIDDVILSAFGSSGQRCSAL-RLLyVPHDAADALIEGLKGALAA 859
Cdd:cd07138 226 AE-AAAD--TVKRVALELGGksANIILDD--ADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 860 QVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIA-RAELPAGADKGHLFAPTI-AEIPTADYLER-EVFGPIL 935
Cdd:cd07138 300 YVVGDPRDPATTLGPLASAAQFDRVQGYIQKgIEEGARLVAgGPGRPEGLERGYFVKPTVfADVTPDMTIAReEIFGPVL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 936 HVCRYEPsklKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINrsiiGAVVGVQ-PFGGEGLSGTGpKAGG 1013
Cdd:cd07138 380 SIIPYDD---EDEAIAIAnDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG-REWG 451
|
490
....*....|...
gi 2521504918 1014 PYSLIRFASEKAI 1026
Cdd:cd07138 452 RYGLEEFLEVKSI 464
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
601-1008 |
4.26e-50 |
|
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: 183.97 E-value: 4.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 601 QIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELkGPvGEI 680
Cdd:cd07109 33 ESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKLHGETIPL-GP-GYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 681 NQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAK 760
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 761 LVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLY 840
Cdd:cd07109 191 LVAHPGVDHISFTGSVETGIAVMRAAAEN---VVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 841 VPHDAADALIEGLKGALAAQVVGDPTDPAtDIGPVIDADARAMLEAHLKR-LEGDAKIIARAELPAGA-DKGHLFAPTI- 917
Cdd:cd07109 268 VHRSIYDEVLERLVERFRALRVGPGLEDP-DLGPLISAKQLDRVEGFVARaRARGARIVAGGRIAEGApAGGYFVAPTLl 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 918 AEIPTADYLER-EVFGPILHVcryEPSKLKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRsiIGAVVG 995
Cdd:cd07109 347 DDVPPDSRLAQeEIFGPVLAV---MPFDDEAEAIALAnGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGG 421
|
410
....*....|....
gi 2521504918 996 VQ-PFGGEGLSGTG 1008
Cdd:cd07109 422 IElPFGGVKKSGHG 435
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
603-1026 |
4.95e-50 |
|
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: 184.62 E-value: 4.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDG-VAEIREAADFCRYYAMLAERDFGGPTELKGPvgeIN 681
Cdd:cd07142 58 PWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGP---HH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 682 QLVLHGR-GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAK 760
Cdd:cd07142 135 VYTLHEPiGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 761 LVSHPGIDGVAFTGGTDTANLINRsLAARPGaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLY 840
Cdd:cd07142 215 IASHMDVDKVAFTGSTEVGKIIMQ-LAAKSN-LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 841 VPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAElpAGADKGHLFAPTIAE 919
Cdd:cd07142 293 VHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHgKEEGATLITGGD--RIGSKGYYIQPTIFS 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 920 IPTADYL--EREVFGPILHVCRYepSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN-RSIIGAVVgv 996
Cdd:cd07142 371 DVKDDMKiaRDEIFGPVQSILKF--KTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI-- 446
|
410 420 430
....*....|....*....|....*....|
gi 2521504918 997 qPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07142 447 -PFGGYKMSGIG-REKGIYALNNYLQVKAV 474
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
567-1023 |
2.81e-49 |
|
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: 181.64 E-value: 2.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 567 QPVTNPFDTtRVLGHVSEATEADIDAAvdaaaraqIAWDRKGGAG--------RGAVLRAMADALEADMDRLVALLSREA 638
Cdd:cd07149 1 IEVISPYDG-EVIGRVPVASEEDVEKA--------IAAAKEGAKEmkslpayeRAEILERAAQLLEERREEFARTIALEA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 639 GKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGPVGEINQLVLHGR---GVFACISPWNFPL---------AIFTG 706
Cdd:cd07149 72 GKPIKDARKEVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIRepiGVVAAITPFNFPLnlvahkvgpAIAAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 707 QiaaalaagnAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSL 786
Cdd:cd07149 152 N---------AVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 787 AARPGAIipfiaETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPT 866
Cdd:cd07149 223 GLKKVTL-----ELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 867 DPATDIGPVIDADA--RAML---EAhlkrLEGDAKIIAraelpAGADKGHLFAPTIAEIPTAD--YLEREVFGPILHVCR 939
Cdd:cd07149 298 DEDTDVGPMISEAEaeRIEEwveEA----VEGGARLLT-----GGKRDGAILEPTVLTDVPPDmkVVCEEVFAPVVSLNP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 940 YEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIgAVVGVQPFGGEGLSGTGpKAGgpyslIR 1019
Cdd:cd07149 369 FD--TLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSST-FRVDHMPYGGVKESGTG-REG-----PR 439
|
....
gi 2521504918 1020 FASE 1023
Cdd:cd07149 440 YAIE 443
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
569-1011 |
4.40e-49 |
|
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: 181.40 E-value: 4.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTL-NDGVA 647
Cdd:cd07108 1 VINP-ATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 648 EIREAADFCRYYAMLAerdfggpTELKG---PVGEiNQLVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAK 721
Cdd:cd07108 80 EAAVLADLFRYFGGLA-------GELKGetlPFGP-DVLTYTVReplGVVGAILPWNAPLMLAALKIAPALVAGNTVVLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 722 PAEQTPLIAAEAVRLYYKAgLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETG 801
Cdd:cd07108 152 AAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR---LIPVSLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 802 GLNGMFVDTTALKEQIIDDVILSA-FGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADA 880
Cdd:cd07108 228 GKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 881 RAMLEAHLK--RLEGDAKIIARAELPAGAD--KGHLFAPTI-AEIPTADYLER-EVFGPILHVCryePSKLKETASKLAA 954
Cdd:cd07108 308 FAKVCGYIDlgLSTSGATVLRGGPLPGEGPlaDGFFVQPTIfSGVDNEWRLAReEIFGPVLCAI---PWKDEDEVIAMAN 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2521504918 955 RG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSiIGAVVGvQPFGGEGLSGTGPKA 1011
Cdd:cd07108 385 DShYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
612-1027 |
4.78e-49 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 180.99 E-value: 4.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 612 RGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERdFGGPTELKGPVGEINQLVLHGRGVF 691
Cdd:cd07150 45 RERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRR-VRGETLPSDSPGTVSMSVRRPLGVV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 692 ACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVA 771
Cdd:cd07150 124 AGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 772 FTGGTDTAnlinRSLAARPGAIIPFIA-ETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALI 850
Cdd:cd07150 204 FTGSTAVG----REIAEKAGRHLKKITlELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 851 EGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIAraelpAGADKGHLFAPTIAEIPTADY--LE 927
Cdd:cd07150 280 KKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDaVAKGAKLLT-----GGKYDGNFYQPTVLTDVTPDMriFR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 928 REVFGPILHVCryePSKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSII--GAVVgvqPFGGEGL 1004
Cdd:cd07150 355 EETFGPVTSVI---PAKDAEEALELANDTeYGLSAAILTNDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKA 428
|
410 420
....*....|....*....|...
gi 2521504918 1005 SGTGpKAGGPYSLIRFASEKAIS 1027
Cdd:cd07150 429 SGFG-REGGEWSMEEFTELKWIT 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
597-1027 |
5.89e-49 |
|
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: 180.03 E-value: 5.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 597 AARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERdfggptelkgP 676
Cdd:cd07104 9 AAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRR----------P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 677 VGEINQLVLHGR---------GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTP-----LIAaeavRLYYKAGL 742
Cdd:cd07104 79 EGEILPSDVPGKesmvrrvplGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 743 DPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTAnlinRSLAARPGAIIPFIA-ETGGLNGMFVDTTALKEQIIDDV 821
Cdd:cd07104 155 PKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIGELAGRHLKKVAlELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 822 ILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLkrlegDAKIIARA 901
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIV-----EDAVAAGA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 902 ELPAGAD-KGHLFAPTI-----AEIPTADyleREVFGPILHVCRYEPSklkETASKLAARG-YGLTLGVHSRIEAFAEEV 974
Cdd:cd07104 306 RLLTGGTyEGLFYQPTVlsdvtPDMPIFR---EEIFGPVAPVIPFDDD---EEAVELANDTeYGLSAAVFTRDLERAMAF 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2521504918 975 ARLVPAGNVYINRSII--GAVVgvqPFGGEGLSGTGpKAGGPYSLIRFASEKAIS 1027
Cdd:cd07104 380 AERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGPASLEEFTEWQWIT 430
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
556-1008 |
6.04e-49 |
|
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: 181.56 E-value: 6.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNAQ--PVTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVAL 633
Cdd:cd07085 5 INGEWVESKTTEwlDVYNP-ATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 634 LSREAGKTLNDGVAEIR---EAADFCryyamlaerdFGGPTELKGPVGE------INQLVLHGRGVFACISPWNFP---- 700
Cdd:cd07085 84 ITLEHGKTLADARGDVLrglEVVEFA----------CSIPHLLKGEYLEnvargiDTYSYRQPLGVVAGITPFNFPamip 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 701 -----LAIFTGQiaaalaagnAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAkLVSHPGIDGVAFTGG 775
Cdd:cd07085 154 lwmfpMAIACGN---------TFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 776 TDTANLInRSLAARPGAiiPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKG 855
Cdd:cd07085 224 TPVGEYI-YERAAANGK--RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 856 ALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKII--ARAELPAGADKGHLFAPTIAEIPTAD---YLErE 929
Cdd:cd07085 301 RAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESgVEEGAKLVldGRGVKVPGYENGNFVGPTILDNVTPDmkiYKE-E 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 930 VFGPILHVCRYEpsKLKEtASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIigAV-VGVQPFGGEGLSGT 1007
Cdd:cd07085 380 IFGPVLSIVRVD--TLDE-AIAIINANpYGNGAAIFTRSGAAARKFQREVDAGMVGINVPI--PVpLAFFSFGGWKGSFF 454
|
.
gi 2521504918 1008 G 1008
Cdd:cd07085 455 G 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
603-1008 |
8.30e-49 |
|
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: 180.49 E-value: 8.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVA-EIREAADFCRYYAMLAERDFGgptELkGPVGEiN 681
Cdd:cd07112 41 VWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAvDVPSAANTFRWYAEAIDKVYG---EV-APTGP-D 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 682 QLVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVG 758
Cdd:cd07112 116 ALALITReplGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 759 AKLVSHPGIDGVAFTGGTDTANLINRsLAARPGaIIPFIAETGG--LNGMFVDTTALkEQIIDDVILSAFGSSGQRCSAL 836
Cdd:cd07112 196 EALGLHMDVDALAFTGSTEVGRRFLE-YSGQSN-LKRVWLECGGksPNIVFADAPDL-DAAAEAAAAGIFWNQGEVCSAG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 837 RLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDadaramlEAHLKRLEG--DAKIIARAELPAGAD------ 908
Cdd:cd07112 273 SRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVS-------EAHFDKVLGyiESGKAEGARLVAGGKrvltet 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 909 KGHLFAPTI--AEIPTADYLEREVFGPILHVCRYEPsklKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYI 985
Cdd:cd07112 346 GGFFVEPTVfdGVTPDMRIAREEIFGPVLSVITFDS---EEEAVALAnDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV 422
|
410 420
....*....|....*....|...
gi 2521504918 986 NrsIIGAVVGVQPFGGEGLSGTG 1008
Cdd:cd07112 423 N--CFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
569-1026 |
7.35e-48 |
|
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: 177.57 E-value: 7.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAE 648
Cdd:cd07107 1 VINP-ATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 649 IREAADFCRYYAMLAerdfggpTELKG---PVG--EINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPA 723
Cdd:cd07107 80 VMVAAALLDYFAGLV-------TELKGetiPVGgrNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 724 EQTPLIA---AEAVRlyykAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAET 800
Cdd:cd07107 153 EQAPLSAlrlAELAR----EVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG---IKHVTLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 801 GGLNGMFVDTTALKEQIIDDVILSA-FGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDAD 879
Cdd:cd07107 226 GGKNALIVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 880 ARAMLEAHLK--RLEGdAKIIA---RAELPAGAdKGHLFAPTI-AEI-PTADYLEREVFGPILHVCRYepSKLKETASKL 952
Cdd:cd07107 306 QYDRVMHYIDsaKREG-ARLVTgggRPEGPALE-GGFYVEPTVfADVtPGMRIAREEIFGPVLSVLRW--RDEAEMVAQA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2521504918 953 AARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN---RSIIGAvvgvqPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07107 382 NGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG-REECLEELLSYTQEKNV 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
565-1030 |
2.24e-47 |
|
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: 176.95 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 565 NAQPVTNPfDTTRVLGHVSEATEADIDAAVDAAARA-QIAWDRK-GGAGRGAVLRAMADALEADMDRLVALLSREAGKTL 642
Cdd:cd07143 22 GTVKVYNP-STGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 643 NDGVA-EIREAADFCRYYAMLAERDFGGPTE---------LKGPVGEINQLVlhgrgvfacisPWNFPLAIFTGQIAAAL 712
Cdd:cd07143 101 GTAKRvDVQASADTFRYYGGWADKIHGQVIEtdikkltytRHEPIGVCGQII-----------PWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 713 AAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRslAARPGA 792
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME--AAAKSN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 793 IIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDI 872
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 873 GPV---IDADaRAMLEAHLKRLEGdAKIIARAElpAGADKGHLFAPTIAEIPTADY--LEREVFGPILHVCRYEpsKLKE 947
Cdd:cd07143 328 GPQvsqIQYE-RIMSYIESGKAEG-ATVETGGK--RHGNEGYFIEPTIFTDVTEDMkiVKEEIFGPVVAVIKFK--TEEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 948 TASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN-RSIIGAVVgvqPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIG-RELGEYALENYTQIKAV 477
|
....
gi 2521504918 1027 SNNI 1030
Cdd:cd07143 478 HINL 481
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
612-1026 |
4.84e-47 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 175.22 E-value: 4.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 612 RGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKgPvGEINQLVLHGRGVF 691
Cdd:cd07120 44 RARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRMIEPE-P-GSFSLVLREPMGVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 692 ACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKA-GLDPNLLALVPGRGETVGAKLVSHPGIDGV 770
Cdd:cd07120 122 GIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 771 AFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALI 850
Cdd:cd07120 202 SFTGSTATGRAIMAAAAPT---LKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 851 EGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAE-LPAGADKGHLFAPTIAEI--PTADYL 926
Cdd:cd07120 279 DRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERaIAAGAEVVLRGGpVTEGLAKGAFLRPTLLEVddPDADIV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 927 EREVFGPILHVCRYEPSklKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSiiGAVVGVQPFGGEGLSG 1006
Cdd:cd07120 359 QEEIFGPVLTLETFDDE--AEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
410 420
....*....|....*....|
gi 2521504918 1007 TGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07120 435 LG-RLHGVAALEDFIEYKHI 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
569-1026 |
6.81e-47 |
|
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: 174.93 E-value: 6.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPFDTtRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAE 648
Cdd:cd07094 3 VHNPYDG-EVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 649 IREAADFCRYYAMLAERDFGGPTELKGPVGEINQLVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQ 725
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIRepvGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 726 TPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIipfiaETGGLNG 805
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIAL-----ELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 806 MFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLE 885
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 886 AHLKR-LEGDAKIIAraelpAGADKGHLFAPTIAEIPTADYLER--EVFGPILHVCRYepSKLKETASKLAARGYGLTLG 962
Cdd:cd07094 317 RWVEEaVEAGARLLC-----GGERDGALFKPTVLEDVPRDTKLSteETFGPVVPIIRY--DDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2521504918 963 VHSRIEAFAEEVARLVPAGNVYINRSIIgAVVGVQPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG-REGVPYAMEEMTEEKTV 451
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
556-1026 |
1.03e-45 |
|
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: 171.60 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNAQP--VTNPFdTTRVLGHVSEATEADIDAAVDAAARA--QIAWDRKGGAGRGAVLRAMADALEADMDRLV 631
Cdd:cd07139 3 IGGRWVAPSGSETidVVSPA-TEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 632 ALLSREAGKTLN-DGVAEIREAADFCRYYAMLAeRDFGGPTELKGPVGEINQLVLHGRGVFACISPWNFPLAIFTGQIAA 710
Cdd:cd07139 82 RLWTAENGMPISwSRRAQGPGPAALLRYYAALA-RDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 711 ALAAGNAVLAKPAEQTPLIA---AEAVRlyyKAGLDPNLLALVPGrGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLA 787
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAyllAEAAE---EAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 788 ARpgaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTD 867
Cdd:cd07139 237 ER---LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 868 PATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAELPAGADKGHLFAPTI-AEIPTADYLER-EVFGPILHVCRYEPsk 944
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKgRAEGARLVTGGGRPAGLDRGWFVEPTLfADVDNDMRIAQeEIFGPVLSVIPYDD-- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 945 lKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN--RSIIGAvvgvqPFGGEGLSGTGpKAGGPYSLIRFA 1021
Cdd:cd07139 392 -EDDAVRIAnDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNgfRLDFGA-----PFGGFKQSGIG-REGGPEGLDAYL 464
|
....*
gi 2521504918 1022 SEKAI 1026
Cdd:cd07139 465 ETKSI 469
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
568-1026 |
1.59e-45 |
|
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: 171.24 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 568 PVTNPfDTTRVLGHVSEATEADIDAAVDAAARA-QIAWDRK-GGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDG 645
Cdd:cd07091 22 PTINP-ATEEVICQVAEADEEDVDAAVKAARAAfETGWWRKmDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 646 -VAEIREAADFCRYYAMLAERDFGGPTELKGpvgeiNQLVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAK 721
Cdd:cd07091 101 aKGDVALSIKCLRYYAGWADKIQGKTIPIDG-----NFLAYTRRepiGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 722 PAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAArpGAIIPFIAETG 801
Cdd:cd07091 176 PAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK--SNLKKVTLELG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 802 GLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDadar 881
Cdd:cd07091 254 GKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVS---- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 882 amlEAHLKRL---------EGdAKIIARAELPagADKGHLFAPTI-AEI-PTADYLEREVFGPILHVCRYepSKLKETAS 950
Cdd:cd07091 330 ---KAQFDKIlsyiesgkkEG-ATLLTGGERH--GSKGYFIQPTVfTDVkDDMKIAKEEIFGPVVTILKF--KTEDEVIE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2521504918 951 KLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINR-SIIGAVVgvqPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFG-RELGEEGLEEYTQVKAV 474
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
604-1026 |
1.67e-45 |
|
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: 170.60 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGPvgEINQL 683
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLGD--DMLGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 684 VLH-GRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLV 762
Cdd:cd07118 115 VLRePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 763 SHPGIDGVAFTGGTDTANLInrsLAARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVP 842
Cdd:cd07118 195 EHPDVDMVSFTGSTRVGKAI---AAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVH 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 843 HDAADALIEGLKgALAAQV-VGDPTDPATDIGPVIDadaramlEAHLKRLEG--DAKIIARAELPAGAD-----KGHLFA 914
Cdd:cd07118 272 ESIADAFVAAVV-ARSRKVrVGDPLDPETKVGAIIN-------EAQLAKITDyvDAGRAEGATLLLGGErlasaAGLFYQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 915 PTIAEIPTADY--LEREVFGPILHVCRYepsKLKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIG 991
Cdd:cd07118 344 PTIFTDVTPDMaiAREEIFGPVLSVLTF---DTVDEAIALAnDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDG 420
|
410 420 430
....*....|....*....|....*....|....*
gi 2521504918 992 AVvgVQPFGGEGLSGTGPKAgGPYSLIRFASEKAI 1026
Cdd:cd07118 421 SP--ELPFGGFKQSGIGREL-GRYGVEEYTELKTV 452
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
572-1027 |
2.62e-45 |
|
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: 170.18 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 572 PFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIRE 651
Cdd:cd07101 3 PF-TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 652 AADFCRYYAMLAERdFGGPTELKGPVGEINQLVLHGR--GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLI 729
Cdd:cd07101 82 VAIVARYYARRAER-LLKPRRRRGAIPVLTRTTVNRRpkGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 730 AAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHpgIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMFVD 809
Cdd:cd07101 161 ALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRR---LIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 810 TTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLK 889
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 890 R-LEGDAKIIARAElpAGADKGHLF-APTIAEIPTADYLER--EVFGPILHVCRYepSKLKETASKLAARGYGLTLGVHS 965
Cdd:cd07101 316 DaVAKGATVLAGGR--ARPDLGPYFyEPTVLTGVTEDMELFaeETFGPVVSIYRV--ADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2521504918 966 RIEAFAEEVARLVPAGNVYINRSIIGAVVGVQ-PFGGEGLSGTGPKAgGPYSLIRFASEKAIS 1027
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRH-GAEGLLKYTETQTVA 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
541-1008 |
1.78e-44 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 169.29 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 541 ALQKVDSETLTAgpIIGGKLKAGTNAQPVTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMA 620
Cdd:PRK09407 10 APSALTFERLRR--LTARVDGAAGPTREVTAPF-TGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 621 DALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERdFGGPTELKGPVGEINQLVL--HGRGVFACISPWN 698
Cdd:PRK09407 87 DLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPK-LLAPRRRAGALPVLTKTTElrQPKGVVGVISPWN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 699 FPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHpgIDGVAFTGGTDT 778
Cdd:PRK09407 166 YPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 779 AnlinRSLAARPGA-IIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGAL 857
Cdd:PRK09407 244 G----RVLAEQAGRrLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 858 AAQVVGDPTDPATDIGPVIDADARAMLEAHLkrleGDAKiiAR-AELPAG----ADKGHLF-APTIAE--IPTADYLERE 929
Cdd:PRK09407 320 RAMRLGAGYDYSADMGSLISEAQLETVSAHV----DDAV--AKgATVLAGgkarPDLGPLFyEPTVLTgvTPDMELAREE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 930 VFGPILHVCRYEPSklkETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQ-PFGGEGLSGT 1007
Cdd:PRK09407 394 TFGPVVSVYPVADV---DEAVERAnDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGL 470
|
.
gi 2521504918 1008 G 1008
Cdd:PRK09407 471 G 471
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
604-1012 |
2.73e-44 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 168.46 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDG-VAEIREAADFCRYYAMLAERDFGGPTELKGPvgeinq 682
Cdd:PLN02766 76 WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGkAVDIPAAAGLLRYYAGAADKIHGETLKMSRQ------ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 lvLHGR------GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGET 756
Cdd:PLN02766 150 --LQGYtlkepiGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 757 VGAKLVSHPGIDGVAFTGGTDTANLINRSLAArpGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSAL 836
Cdd:PLN02766 228 AGAAIASHMDVDKVSFTGSTEVGRKIMQAAAT--SNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVAS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 837 RLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRLEGDAKIIARAELPAGaDKGHLFAPT 916
Cdd:PLN02766 306 SRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCG-DKGYYIEPT 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 917 IAEIPTADYL--EREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIigAVV 994
Cdd:PLN02766 385 IFTDVTEDMKiaQDEIFGPVMSLMKFK--TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYF--AFD 460
|
410
....*....|....*...
gi 2521504918 995 GVQPFGGEGLSGTGPKAG 1012
Cdd:PLN02766 461 PDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
553-1008 |
4.97e-44 |
|
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: 166.85 E-value: 4.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 553 GPIIGGKLKAG--TNAQPVTNPfDTTRVLGHVSEATEADIDAAVDAAARA-QIAWDRKGGAGRGAVLRAMADALEADMDR 629
Cdd:cd07113 1 GHFIDGRPVAGqsEKRLDITNP-ATEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 630 LVALLSREAGKTLN-DGVAEIREAADFCRYYAMLAERdFGGPT---ELKGPVGEINQLVLHGR--GVFACISPWNFPLAI 703
Cdd:cd07113 80 LAQLETLCSGKSIHlSRAFEVGQSANFLRYFAGWATK-INGETlapSIPSMQGERYTAFTRREpvGVVAGIVPWNFSVMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 704 FTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGEtVGAKLVSHPGIDGVAFTGGTDTANLIN 783
Cdd:cd07113 159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 784 RSLAarpGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVG 863
Cdd:cd07113 238 RQAA---SDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 864 DPTDPATDIGPVID-ADARAMLEA-HLKRLEGDaKIIARAELPAGadKGHLFAPTIAEIPTAD--YLEREVFGPILHVCR 939
Cdd:cd07113 315 SPMDESVMFGPLANqPHFDKVCSYlDDARAEGD-EIVRGGEALAG--EGYFVQPTLVLARSADsrLMREETFGPVVSFVP 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 940 YEPSklKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN-RSIIGAVVgvqPFGGEGLSGTG 1008
Cdd:cd07113 392 YEDE--EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
604-1026 |
3.28e-43 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 166.14 E-value: 3.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGV-AEIREAADFCRYYAMLAERDFGgpteLKGPVGEINQ 682
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMFARLFRYYAGWADKIHG----LTVPADGPHH 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 L-VLHGR-GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAK 760
Cdd:PLN02466 189 VqTLHEPiGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 761 LVSHPGIDGVAFTGGTDTANLInRSLAARPGaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLY 840
Cdd:PLN02466 269 LASHMDVDKLAFTGSTDTGKIV-LELAAKSN-LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 841 VPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKrlegdAKIIARAELPAGAD----KGHLFAPT 916
Cdd:PLN02466 347 VHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIK-----SGVESGATLECGGDrfgsKGYYIQPT 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 917 IAEIPTADYL--EREVFGPILHVCRYepSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN-RSIIGAV 993
Cdd:PLN02466 422 VFSNVQDDMLiaQDEIFGPVQSILKF--KDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAA 499
|
410 420 430
....*....|....*....|....*....|...
gi 2521504918 994 VgvqPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:PLN02466 500 I---PFGGYKMSGIG-REKGIYSLNNYLQVKAV 528
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
604-1030 |
3.35e-43 |
|
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: 164.89 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLN-DGVAEIREAADFCRYYAMLAERDFGG--PTE-------L 673
Cdd:cd07144 62 WSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHsNALGDLDEIIAVIRYYAGWADKIQGKtiPTSpnklaytL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 674 KGPVGEINQLVlhgrgvfacisPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGR 753
Cdd:cd07144 142 HEPYGVCGQII-----------PWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 754 GETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIipfIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRC 833
Cdd:cd07144 211 GAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAV---TLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNC 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 834 SALRLLYVPHDAADALIEGLKGALA-AQVVGDPTDPATDIGPVIDADA--RAMLEAHLKRLEGDAKIIARAELPAGADKG 910
Cdd:cd07144 288 TATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTVVGPQVSKTQydRVLSYIEKGKKEGAKLVYGGEKAPEGLGKG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 911 HLFAPTI-AEIP-TADYLEREVFGPILHVCRYepsKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINR 987
Cdd:cd07144 368 YFIPPTIfTDVPqDMRIVKEEIFGPVVVISKF---KTYEEAIKKANDTtYGLAAAVFTKDIRRAHRVARELEAGMVWINS 444
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2521504918 988 SIIGAvVGVqPFGGEGLSGTGpKAGGPYSLIRFASEKAISNNI 1030
Cdd:cd07144 445 SNDSD-VGV-PFGGFKMSGIG-RELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
562-1027 |
1.04e-42 |
|
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: 162.86 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 562 AGTNAQPVTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKT 641
Cdd:cd07151 7 TSERTIDVLNPY-TGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 642 LNDGVAE-------IREAADFcryyamlaerdfggPTELKGPV------GEINQLVLHGRGVFACISPWNFPLAIFTGQI 708
Cdd:cd07151 86 RIKANIEwgaamaiTREAATF--------------PLRMEGRIlpsdvpGKENRVYREPLGVVGVISPWNFPLHLSMRSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 709 AAALAAGNAVLAKPAEQTP-----LIAaeavRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDtanlIN 783
Cdd:cd07151 152 APALALGNAVVLKPASDTPitgglLLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTP----VG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 784 RSLAARPGAIIPFIA-ETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVV 862
Cdd:cd07151 224 RHIGELAGRHLKKVAlELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 863 GDPTDPATDIGPVIDADARAMLeahLKRLEGDAKIIARAELPAGADkGHLFAPTIAEIPTADY--LEREVFGPILHVCRY 940
Cdd:cd07151 304 GDPSDPDTVVGPLINESQVDGL---LDKIEQAVEEGATLLVGGEAE-GNVLEPTVLSDVTNDMeiAREEIFGPVAPIIKA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 941 EPsklKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVqPFGGEGLSGTGpKAGGPYSLIR 1019
Cdd:cd07151 380 DD---EEEALELAnDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG-RFNGEWALEE 454
|
....*...
gi 2521504918 1020 FASEKAIS 1027
Cdd:cd07151 455 FTTDKWIS 462
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
556-1008 |
1.25e-41 |
|
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: 159.82 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNAQ--PVTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVAL 633
Cdd:cd07559 5 INGEWVAPSKGEyfDNYNPV-NGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 634 LSREAGK----TLNdgvAEIREAADFCRYYAMLAERDFGGPTELKGpvgeiNQLVLHGR---GVFACISPWNFPLAIFTG 706
Cdd:cd07559 84 ETLDNGKpireTLA---ADIPLAIDHFRYFAGVIRAQEGSLSEIDE-----DTLSYHFHeplGVVGQIIPWNFPLLMAAW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 707 QIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSL 786
Cdd:cd07559 156 KLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 787 AARpgaIIPFIAETGGLN-GMFVDTTALKEQIIDDVILSAFG----SSGQRCSALRLLYVPHDAADALIEGLKGALAAQV 861
Cdd:cd07559 235 AEN---LIPVTLELGGKSpNIFFDDAMDADDDFDDKAEEGQLgfafNQGEVCTCPSRALVQESIYDEFIERAVERFEAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 862 VGDPTDPATDIGPVIDADaraMLEAHLKRL----EGDAKIIA---RAELPaGADKGHLFAPTIAEIPTADY--LEREVFG 932
Cdd:cd07559 312 VGNPLDPETMMGAQVSKD---QLEKILSYVdigkEEGAEVLTggeRLTLG-GLDKGYFYEPTLIKGGNNDMriFQEEIFG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 933 PILHVCRYepsKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSII---GAvvgvqPFGGEGLSGTG 1008
Cdd:cd07559 388 PVLAVITF---KDEEEAIAIANDTeYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQypaHA-----PFGGYKKSGIG 459
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
557-941 |
2.11e-41 |
|
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: 159.29 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 557 GGKLKAGTNAQPVTNPFDTtRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSR 636
Cdd:cd07130 4 DGEWGGGGGVVTSISPANG-EPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 637 EAGKTLNDGVAEIREAADFCRYYAMLAeRDFGG---PTELKG--------PVGeinqlvlhgrgVFACISPWNFPLAIFT 705
Cdd:cd07130 83 EMGKILPEGLGEVQEMIDICDFAVGLS-RQLYGltiPSERPGhrmmeqwnPLG-----------VVGVITAFNFPVAVWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 706 GQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKA----GLDPNLLALVPGRGEtVGAKLVSHPGIDGVAFTGGTDTANL 781
Cdd:cd07130 151 WNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 782 INRSLAARPGAIIpfiAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQV 861
Cdd:cd07130 230 VGQAVAARFGRSL---LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 862 VGDPTDPATDIGPVIDADARAMLEAHLKRL-EGDAKIIARAELPAGAdkGHLFAPTIAEIPT-ADYLEREVFGPILHVCR 939
Cdd:cd07130 307 IGDPLDDGTLVGPLHTKAAVDNYLAAIEEAkSQGGTVLFGGKVIDGP--GNYVEPTIVEGLSdAPIVKEETFAPILYVLK 384
|
..
gi 2521504918 940 YE 941
Cdd:cd07130 385 FD 386
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
575-1017 |
4.12e-41 |
|
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: 157.87 E-value: 4.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 575 TTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVA-EIREAA 653
Cdd:cd07092 6 TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdELPGAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 654 DFCRYYAMlAERDFGGP--TE-LKGPVGEINQLVLhgrGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIA 730
Cdd:cd07092 86 DNFRFFAG-AARTLEGPaaGEyLPGHTSMIRREPI---GVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 731 ---AEAVrlyyKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAArpgAIIPFIAETGGLNGMF 807
Cdd:cd07092 162 lllAELA----AEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD---TLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 808 VDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAH 887
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 888 LKRLEGDAKIIARAELPAGadKGHLFAPT-IAEIPTADYL-EREVFGPILHVCRYEPsklKETASKLA-ARGYGLTLGVH 964
Cdd:cd07092 315 VERAPAHARVLTGGRRAEG--PGYFYEPTvVAGVAQDDEIvQEEIFGPVVTVQPFDD---EDEAIELAnDVEYGLASSVW 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2521504918 965 SRIEAFAEEVARLVPAGNVYINRSIIgaVVGVQPFGGEGLSGTGpKAGGPYSL 1017
Cdd:cd07092 390 TRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG-KDLSIYAL 439
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
530-1017 |
5.08e-41 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 158.70 E-value: 5.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 530 SQAADRERHAVALQKVDSETLTAGPIIGGKLKAGTNAQ--PVTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRK 607
Cdd:PLN02278 3 TRASSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKtfPVYNP-ATGEVIANVPCMGRAETNDAIASAHDAFPSWSKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 608 GGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGG--PTelkgPVGEINQLVL 685
Cdd:PLN02278 82 TASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDiiPS----PFPDRRLLVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 686 HGR-GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSH 764
Cdd:PLN02278 158 KQPvGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 765 PGIDGVAFTGGTDtanlINRSLAARPGAIIPFIA-ETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRC-SALRLLyVP 842
Cdd:PLN02278 238 PKVRKITFTGSTA----VGKKLMAGAAATVKRVSlELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 843 HDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKrlegDAkIIARAELPAG----ADKGHLFAPTIA 918
Cdd:PLN02278 313 EGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQ----DA-VSKGAKVLLGgkrhSLGGTFYEPTVL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 919 EIPTADYL--EREVFGPILHVCRYepsKLKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVG 995
Cdd:PLN02278 388 GDVTEDMLifREEVFGPVAPLTRF---KTEEEAIAIAnDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA 464
|
490 500
....*....|....*....|..
gi 2521504918 996 vqPFGGEGLSGTGpKAGGPYSL 1017
Cdd:PLN02278 465 --PFGGVKQSGLG-REGSKYGI 483
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
556-1008 |
5.19e-41 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 158.15 E-value: 5.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGT-NAQPVTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALL 634
Cdd:PRK13473 7 INGELVAGEgEKQPVYNP-ATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 635 SREAGK----TLNDgvaEIREAADFCRYYAMlAERDFGGPTE---LKG--------PVGeinqlvlhgrgVFACISPWNF 699
Cdd:PRK13473 86 SLNCGKplhlALND---EIPAIVDVFRFFAG-AARCLEGKAAgeyLEGhtsmirrdPVG-----------VVASIAPWNY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 700 PLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTA 779
Cdd:PRK13473 151 PLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 780 NLINRSLAARP-------GAIIPFIAetgglngmFVDttALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEG 852
Cdd:PRK13473 230 KHVLSAAADSVkrthlelGGKAPVIV--------FDD--ADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 853 LKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRL--EGDAKIIARAELPAGadKGHLFAPT-IAEIPTADYL-ER 928
Cdd:PRK13473 300 LAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAkaLGHIRVVTGGEAPDG--KGYYYEPTlLAGARQDDEIvQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 929 EVFGPILHVCRYEPsklKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIgaVVGVQPFGGEGLSGT 1007
Cdd:PRK13473 378 EVFGPVVSVTPFDD---EDQAVRWAnDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGY 452
|
.
gi 2521504918 1008 G 1008
Cdd:PRK13473 453 G 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
577-1020 |
6.60e-41 |
|
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: 157.07 E-value: 6.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 577 RVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFC 656
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 657 RYYAMLaerdfggPTElkgPVGEI-----NQLVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTP- 727
Cdd:cd07152 82 HEAAGL-------PTQ---PQGEIlpsapGRLSLARRvplGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 728 ----LIAaeavRLYYKAGLDPNLLALVPGRGEtVGAKLVSHPGIDGVAFTGGTDTAnlinRSLAARPGAIIPFIA-ETGG 802
Cdd:cd07152 152 sggvVIA----RLFEEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVG----RKVGEAAGRHLKKVSlELGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 803 LNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARA 882
Cdd:cd07152 223 KNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 883 MLEAHLkrlegDAKIIARAELPAGAD-KGHLFAPT-IAEI-PTADYLEREVFGPILHVCryePSKLKETASKLAARG-YG 958
Cdd:cd07152 303 RVHAIV-----DDSVAAGARLEAGGTyDGLFYRPTvLSGVkPGMPAFDEEIFGPVAPVT---VFDSDEEAVALANDTeYG 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2521504918 959 LTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVgVQPFGGEGLSGTGPKAGGPYSLIRF 1020
Cdd:cd07152 375 LSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGPANWEEF 435
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
603-1008 |
1.58e-40 |
|
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: 155.31 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAErDFGGPTELKGPVGEiNQ 682
Cdd:cd07100 14 AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAE-AFLADEPIETDAGK-AY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 LVLHGRGVFACISPWNFPL---------AIFTGQIaaalaagnaVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGR 753
Cdd:cd07100 92 VRYEPLGVVLGIMPWNFPFwqvfrfaapNLMAGNT---------VLLKHASNVPGCALAIEELFREAGFPEGVFQNLLID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 754 GETVgAKLVSHPGIDGVAFTGGTDTAnlinRSLAARPG-AIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQR 832
Cdd:cd07100 163 SDQV-EAIIADPRVRGVTLTGSERAG----RAVAAEAGkNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 833 C-SALRLLyVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAELPAGadKG 910
Cdd:cd07100 238 CiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEaVAAGATLLLGGKRPDG--PG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 911 HLFAPTIAEIPTAD---YLErEVFGPILHVCRYepsKLKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN 986
Cdd:cd07100 315 AFYPPTVLTDVTPGmpaYDE-ELFGPVAAVIKV---KDEEEAIALAnDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420
....*....|....*....|....*
gi 2521504918 987 rsiigAVVGVQ---PFGGEGLSGTG 1008
Cdd:cd07100 391 -----GMVKSDprlPFGGVKRSGYG 410
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
601-987 |
2.67e-40 |
|
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: 155.48 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 601 QIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGgPTELKGPVGEI 680
Cdd:cd07102 31 QKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALA-DIRVPEKDGFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 681 NQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETvGAK 760
Cdd:cd07102 110 RYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 761 LVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMFV------DTTAlkEQIIDdvilSAFGSSGQRCS 834
Cdd:cd07102 189 LIADPRIDHVSFTGSVAGGRAIQRAAAGR---FIKVGLELGGKDPAYVrpdadlDAAA--ESLVD----GAFFNSGQSCC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 835 ALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLK--RLEGDAKIIARAELPAGADKGHL 912
Cdd:cd07102 260 SIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAdaIAKGARALIDGALFPEDKAGGAY 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2521504918 913 FAPTI-AEI-PTADYLEREVFGPILHVcryEPSKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINR 987
Cdd:cd07102 340 LAPTVlTNVdHSMRVMREETFGPVVGI---MKVKSDAEAIALMNDSeYGLTASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
556-1008 |
1.61e-39 |
|
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: 153.76 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNAQ--PVTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVAL 633
Cdd:cd07117 5 INGEWVKGSSGEtiDSYNPA-NGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 634 LSREAGKTLNDGVA-EIREAADFCRYYAMLAERDfggptelKGPVGEINQ----LVLHGR-GVFACISPWNFPLAIFTGQ 707
Cdd:cd07117 84 ETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAE-------EGSANMIDEdtlsIVLREPiGVVGQIIPWNFPFLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 708 IAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLA 787
Cdd:cd07117 157 LAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 788 ARpgaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTD 867
Cdd:cd07117 236 KK---LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 868 PATDIGPVIDADARAMLEAHLK-RLEGDAKIIARAE--LPAGADKGHLFAPTIAEIPTADY--LEREVFGPILHVCRYep 942
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDiAKEEGAKILTGGHrlTENGLDKGFFIEPTLIVNVTNDMrvAQEEIFGPVATVIKF-- 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2521504918 943 sKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINR-SIIGAVVgvqPFGGEGLSGTG 1008
Cdd:cd07117 391 -KTEDEVIDMANDSeYGLGGGVFTKDINRALRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
536-1017 |
2.46e-39 |
|
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: 153.32 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 536 ERHAVALQKVDSETLTAGPIIGGKLKAGTNAQ--PVTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRG 613
Cdd:cd07111 6 ESAACALAWLDAHDRSFGHFINGKWVKPENRKsfPTINPA-TGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 614 AVLRAMADALEADMDRLVALLSREAGKTlndgvaeIREAAD---------FCRY--YAMLAERDFGGPtelkGPVGEINQ 682
Cdd:cd07111 85 RHLYRIARHIQKHQRLFAVLESLDNGKP-------IRESRDcdiplvarhFYHHagWAQLLDTELAGW----KPVGVVGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 LVlhgrgvfacisPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETvGAKLV 762
Cdd:cd07111 154 IV-----------PWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 763 SHPGIDGVAFTGGTDTANLINRSLAarpGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSA-LRLLyV 841
Cdd:cd07111 222 NHPGVDKVAFTGSTEVGRALRRATA---GTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAgSRLL-V 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 842 PHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDAD----ARAMLEAhlKRLEGDAKIIARAELPagaDKGHLFAPTI 917
Cdd:cd07111 298 QESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAqlkrIRELVEE--GRAEGADVFQPGADLP---SKGPFYPPTL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 918 AE-IPTADYLER-EVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN-RSIIGAVV 994
Cdd:cd07111 373 FTnVPPASRIAQeEIFGPVLVVLTFR--TAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA 450
|
490 500
....*....|....*....|...
gi 2521504918 995 gvqPFGGEGLSGTGpKAGGPYSL 1017
Cdd:cd07111 451 ---GFGGYRESGFG-REGGKEGL 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
542-1017 |
2.46e-38 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 150.06 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 542 LQKVDSETLTAGPIIGGKLKAGTNAQ--PVTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAM 619
Cdd:PRK11241 1 MQLNDSTLFRQQALINGEWLDANNGEviDVTNP-ANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 620 ADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGgpTELKGPVGEINQLVLHGR-GVFACISPWN 698
Cdd:PRK11241 80 FNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG--DTIPGHQADKRLIVIKQPiGVTAAITPWN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 699 FPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDt 778
Cdd:PRK11241 158 FPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 779 anlINRSLAARPGAIIPFIA-ETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGAL 857
Cdd:PRK11241 237 ---IGRQLMEQCAKDIKKVSlELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 858 AAQVVGDPTDPATDIGPVIDADARAMLEAHLK-RLEGDAKIIARAElpAGADKGHLFAPTI-AEIP-TADYLEREVFGPI 934
Cdd:PRK11241 314 SKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIAdALEKGARVVCGGK--AHELGGNFFQPTIlVDVPaNAKVAKEETFGPL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 935 LHVCRYepsklKETASKLAARG---YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGvqPFGGEGLSGTGpKA 1011
Cdd:PRK11241 392 APLFRF-----KDEADVIAQANdteFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASGLG-RE 463
|
....*.
gi 2521504918 1012 GGPYSL 1017
Cdd:PRK11241 464 GSKYGI 469
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
575-1027 |
7.23e-38 |
|
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: 148.60 E-value: 7.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 575 TTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGV-AEIREAA 653
Cdd:cd07098 5 TGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEILVTC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 654 DFCRYyaMLAErdfgGPTELKGPVGEINQLVLHGR--------GVFACISPWNFPL---------AIFTGQiaaalaagn 716
Cdd:cd07098 85 EKIRW--TLKH----GEKALRPESRPGGLLMFYKRarveyeplGVVGAIVSWNYPFhnllgpiiaALFAGN--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 717 AVLAKPAEQTPLIAAEAVRLYYKA----GLDPNLLALVPGRGETvGAKLVSHPGIDGVAFTGGTDTANLINRSlAARpgA 792
Cdd:cd07098 150 AIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAA-AAE--S 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 793 IIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDI 872
Cdd:cd07098 226 LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 873 GPVIdADARAmleAHLKRLEGDAkIIARAELPAGAD--------KGHLFAPTI-AEI-PTADYLEREVFGPILHVCRYEP 942
Cdd:cd07098 306 GAMI-SPARF---DRLEELVADA-VEKGARLLAGGKryphpeypQGHYFPPTLlVDVtPDMKIAQEEVFGPVMVVMKASD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 943 SklkETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRsiIGAVVGVQ--PFGGEGLSGTGpKAGGPYSLIR 1019
Cdd:cd07098 381 D---EEAVEIAnSTEYGLGASVFGKDIKRARRIASQLETGMVAIND--FGVNYYVQqlPFGGVKGSGFG-RFAGEEGLRG 454
|
....*...
gi 2521504918 1020 FASEKAIS 1027
Cdd:cd07098 455 LCNPKSVT 462
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
604-1031 |
2.82e-37 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 147.57 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAER-DFGGPTELKGPVGEINQ 682
Cdd:PLN02467 66 WARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEAlDAKQKAPVSLPMETFKG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 LVL-HGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKL 761
Cdd:PLN02467 146 YVLkEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 762 VSHPGIDGVAFTGGTDTANLINRSLAArpgAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYV 841
Cdd:PLN02467 226 ASHPGVDKIAFTGSTATGRKIMTAAAQ---MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 842 PHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLK--RLEGdAKIIARAELPAGADKGHLFAPTI-A 918
Cdd:PLN02467 303 HERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFIStaKSEG-ATILCGGKRPEHLKKGFFIEPTIiT 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 919 EIPTADYLER-EVFGPILHVCRYepsKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSiigavvgv 996
Cdd:PLN02467 382 DVTTSMQIWReEVFGPVLCVKTF---STEDEAIELANDShYGLAGAVISNDLERCERVSEAFQAGIVWINCS-------- 450
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2521504918 997 Q------PFGGEGLSGTGpKAGGPYSLIRFASEKAISNNIS 1031
Cdd:PLN02467 451 QpcfcqaPWGGIKRSGFG-RELGEWGLENYLSVKQVTKYIS 490
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
604-1026 |
4.19e-36 |
|
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: 143.64 E-value: 4.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDG-VAEIREAADFCRYYAMLAERDFGGPTELKG------- 675
Cdd:cd07141 63 WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDGdfftytr 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 676 --PVGEINQlvlhgrgvfacISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGR 753
Cdd:cd07141 143 hePVGVCGQ-----------IIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 754 GETVGAKLVSHPGIDGVAFTGGTDTANLINRslAARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRC 833
Cdd:cd07141 212 GPTAGAAISSHPDIDKVAFTGSTEVGKLIQQ--AAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 834 SALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADA----RAMLEAHLKrlEGdakiiarAELPAG--- 906
Cdd:cd07141 290 CAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQfkkiLELIESGKK--EG-------AKLECGgkr 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 907 -ADKGHLFAPTIAEIPTAD--YLEREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNV 983
Cdd:cd07141 361 hGDKGYFIQPTVFSDVTDDmrIAKEEIFGPVQQIFKFK--TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTV 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2521504918 984 YINrsiIGAVVGVQ-PFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07141 439 WVN---CYNVVSPQaPFGGYKMSGNG-RELGEYGLQEYTEVKTV 478
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
603-1026 |
7.78e-36 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 141.99 E-value: 7.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFcRYYAMLAE--RDFGGPTELKGPVGEI 680
Cdd:cd07084 14 AARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQL-RARAFVIYsyRIPHEPGNHLGQGLKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 681 N-QLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAG-LDPNLLALVPGRGETvG 758
Cdd:cd07084 93 QsHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGKT-M 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 759 AKLVSHPGIDGVAFTGGTDTAnlinRSLAARPgAIIPFIAETGGLNGMFVDTTA-LKEQIIDDVILSAFGSSGQRCSALR 837
Cdd:cd07084 172 QALLLHPNPKMVLFTGSSRVA----EKLALDA-KQARIYLELAGFNWKVLGPDAqAVDYVAWQCVQDMTACSGQKCTAQS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 838 LLYVPHD-AADALIEGLKGALAAQVVGDPTdpatdIGPVIDADARAMLeAHLKRLEG--------DAKIIARAELPAGAD 908
Cdd:cd07084 247 MLFVPENwSKTPLVEKLKALLARRKLEDLL-----LGPVQTFTTLAMI-AHMENLLGsvllfsgkELKNHSIPSIYGACV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 909 KGHLFAPTIAEIPTADYLEREVFGPILHVCRYEPSKLKeTASKLAARGYG-LTLGVHSRIEAFAEEVA-RLVPAGNVY-I 985
Cdd:cd07084 321 ASALFVPIDEILKTYELVTEEIFGPFAIVVEYKKDQLA-LVLELLERMHGsLTAAIYSNDPIFLQELIgNLWVAGRTYaI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2521504918 986 NRSIIGAVVGVQPFGGEGLSGTGPKAGGPYSLIRFASEKAI 1026
Cdd:cd07084 400 LRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
569-1008 |
1.38e-34 |
|
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: 138.59 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 569 VTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAE 648
Cdd:cd07090 1 VIEP-ATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 649 IREAADFCRYYAMLAERDFGGPTELK-GPVGEINQLVLhgrGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTP 727
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPgGSFAYTRREPL---GVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 728 LIAAEAVRLYYKAGLDPNLLALVPGRGETvGAKLVSHPGIDGVAFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMF 807
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKG---IKHVTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 808 VDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAH 887
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 888 LK--RLEGdAKIIA---RAELPAGADKGHLFAPTIAEIPTADY--LEREVFGPILHVCRYepsklkETASKLAARG---- 956
Cdd:cd07090 313 IEsaKQEG-AKVLCggeRVVPEDGLENGFYVSPCVLTDCTDDMtiVREEIFGPVMSILPF------DTEEEVIRRAndtt 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2521504918 957 YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVvgVQPFGGEGLSGTG 1008
Cdd:cd07090 386 YGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPV--EVPFGGYKQSGFG 435
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
604-1008 |
5.78e-34 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 137.33 E-value: 5.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAE-IREAADFCRYYAMLAERDFG--GPTelkGPvGEI 680
Cdd:PRK09847 75 WSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDdIPGAARAIRWYAEAIDKVYGevATT---SS-HEL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 681 NQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAK 760
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 761 LVSHPGIDGVAFTGGTDTANLINRSlaARPGAIIPFIAETGG--LNGMFVDTTALkEQIIDDVILSAFGSSGQRCSALRL 838
Cdd:PRK09847 231 LSRHNDIDAIAFTGSTRTGKQLLKD--AGDSNMKRVWLEAGGksANIVFADCPDL-QQAASATAAGIFYNQGQVCIAGTR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 839 LYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKrlEGDAKiiaRAELPAGADKGHLFA--PT 916
Cdd:PRK09847 308 LLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIR--EGESK---GQLLLDGRNAGLAAAigPT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 917 I-AEIPTADYLER-EVFGPILHVCRYepsKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAV 993
Cdd:PRK09847 383 IfVDVDPNASLSReEIFGPVLVVTRF---TSEEQALQLANDSqYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM 459
|
410
....*....|....*
gi 2521504918 994 vgVQPFGGEGLSGTG 1008
Cdd:PRK09847 460 --TVPFGGYKQSGNG 472
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
556-1008 |
5.23e-33 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 134.24 E-value: 5.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNAQ--PVTNPFdTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVAL 633
Cdd:PRK13252 11 IDGAYVEATSGEtfEVINPA-TGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 634 LSREAGKTLNDG-VAEIREAADFCRYYAMLAerdfggptelkgPVGEINQLVLHGR----------GVFACISPWNFPLA 702
Cdd:PRK13252 90 ETLDTGKPIQETsVVDIVTGADVLEYYAGLA------------PALEGEQIPLRGGsfvytrreplGVCAGIGAWNYPIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 703 IFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGEtVGAKLVSHPGIDGVAFTGGTDTAnli 782
Cdd:PRK13252 158 IACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTG--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 783 NRSLAARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVV 862
Cdd:PRK13252 234 KKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 863 GDPTDPATDIGPVIDADARAMLEAHLK--RLEGdAKIIA--RAELPAGADKGHLFAPTIAEIPTAD--YLEREVFGPILH 936
Cdd:PRK13252 314 GDPMDPATNFGPLVSFAHRDKVLGYIEkgKAEG-ARLLCggERLTEGGFANGAFVAPTVFTDCTDDmtIVREEIFGPVMS 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2521504918 937 VCRYEPSklKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRsiIGAVVGVQPFGGEGLSGTG 1008
Cdd:PRK13252 393 VLTFDDE--DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINT--WGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
612-1008 |
7.25e-33 |
|
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: 133.14 E-value: 7.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 612 RGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTEL------KGPVGEINQLvl 685
Cdd:cd07147 45 RAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIYGEVLPLdisargEGRQGLVRRF-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 686 hGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETvGAKLVSHP 765
Cdd:cd07147 123 -PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 766 GIDGVAFTGGTDTANLInRSLAARPGAIIpfiaETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDA 845
Cdd:cd07147 201 RIKLLSFTGSPAVGWDL-KARAGKKKVVL----ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 846 ADALIEGLKGALAAQVVGDPTDPATDIGPVIDadaramlEAHLKRLEG--DAKIIARAELPAGAD-KGHLFAPTI-AEIP 921
Cdd:cd07147 276 YDEFKSRLVARVKALKTGDPKDDATDVGPMIS-------ESEAERVEGwvNEAVDAGAKLLTGGKrDGALLEPTIlEDVP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 922 TADYLER-EVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINrSIIGAVVGVQPFG 1000
Cdd:cd07147 349 PDMEVNCeEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIN-DVPTFRVDHMPYG 425
|
....*...
gi 2521504918 1001 GEGLSGTG 1008
Cdd:cd07147 426 GVKDSGIG 433
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
616-987 |
8.15e-31 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 126.39 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 616 LRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGPvGEINQLVLHGRGVFACIS 695
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRP-GENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 696 PWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGG 775
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 776 TDTANLInrsLAARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKG 855
Cdd:PRK10090 160 VSAGEKI---MAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 856 ALAAQVVGDPTD-PATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAElpAGADKGHLFAPT-IAEIPTA-DYLEREVF 931
Cdd:PRK10090 237 AMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARaVEEGARVALGGK--AVEGKGYYYPPTlLLDVRQEmSIMHEETF 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2521504918 932 GPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINR 987
Cdd:PRK10090 315 GPVLPVVAFD--TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINR 368
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
603-1026 |
1.39e-30 |
|
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: 126.15 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTelkgPVGEINQ 682
Cdd:cd07105 15 AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSI----PSDKPGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 LVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALV---PGRGET 756
Cdd:cd07105 91 LAMVVKepvGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 757 VGAKLVSHPGIDGVAFTGGTDTANLINrSLAARpgAIIPFIAETGGLNGMFVdttaLKEQIIDD----VILSAFGSSGQR 832
Cdd:cd07105 171 VVEALIAHPAVRKVNFTGSTRVGRIIA-ETAAK--HLKPVLLELGGKAPAIV----LEDADLDAaanaALFGAFLNSGQI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 833 CSALRLLYVPHDAADALIEGLKgALAAQVVGDPTDPatdiGPVIDADARamleAHLKRLEGDA-----KIIArAELPAGA 907
Cdd:cd07105 244 CMSTERIIVHESIADEFVEKLK-AAAEKLFAGPVVL----GSLVSAAAA----DRVKELVDDAlskgaKLVV-GGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 908 DKGHLFAPTIAEIPTAD---YLErEVFGPILHVCRYEPSklkETASKLAAR-GYGLTLGVHSRIEAFAEEVARLVPAGNV 983
Cdd:cd07105 314 PSGTSMPPTILDNVTPDmdiYSE-ESFGPVVSIIRVKDE---EEAVRIANDsEYGLSAAVFTRDLARALAVAKRIESGAV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2521504918 984 YINRSIIG--AVVgvqPFGGEGLSGTGpkaggpysliRFASEKAI 1026
Cdd:cd07105 390 HINGMTVHdePTL---PHGGVKSSGYG----------RFNGKWGI 421
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
612-1026 |
2.40e-29 |
|
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: 122.91 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 612 RGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYyAMLAERDFGG---PTEL-KGPVGEINQLVLHG 687
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVEL-AADELGQLGGreiPMGLtPASAGRIAFTTREP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 688 RGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGEtVGAKLVSHPGI 767
Cdd:cd07148 125 IGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 768 DGVAFTGGTDTANLINRSLAarPGAIIPFiaETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAAD 847
Cdd:cd07148 204 AFFSFIGSARVGWMLRSKLA--PGTRCAL--EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIAD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 848 ALIEGLKGALAAQVVGDPTDPATDIGPVIDAdaramleAHLKRLEG--DAKIIARAELPAGADK--GHLFAPTIAEIPTA 923
Cdd:cd07148 280 DFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP-------REVDRVEEwvNEAVAAGARLLCGGKRlsDTTYAPTVLLDPPR 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 924 DYL--EREVFGPIlhVCRYEPSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN-----RsiigavVGV 996
Cdd:cd07148 353 DAKvsTQEIFGPV--VCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNdhtafR------VDW 424
|
410 420 430
....*....|....*....|....*....|.
gi 2521504918 997 QPFGGEGLSGTGpkAGG-PYSLIRFASEKAI 1026
Cdd:cd07148 425 MPFAGRRQSGYG--TGGiPYTMHDMTQEKMA 453
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
689-1026 |
7.54e-29 |
|
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: 120.71 E-value: 7.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 689 GVFACISPWNFPL---------AIFTGQiaaalaagnAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLALVPGrGETVGA 759
Cdd:cd07087 102 GVVLIIGPWNYPLqlalapligAIAAGN---------TVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GVEVAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 760 KLVSHPgIDGVAFTGGTDTANLINRSlAARpgAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLL 839
Cdd:cd07087 171 ALLAEP-FDHIFFTGSPAVGKIVMEA-AAK--HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 840 YVPHDAADALIEGLKGALAAQvVGDPTDPATDIGPVIDadaramlEAHLKRLEG---DAKIIARAElpagADKGHLF-AP 915
Cdd:cd07087 247 LVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIIN-------ERHFDRLASlldDGKVVIGGQ----VDKEERYiAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 916 TIAEIPTADY--LEREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAV 993
Cdd:cd07087 315 TILDDVSPDSplMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAA 392
|
330 340 350
....*....|....*....|....*....|...
gi 2521504918 994 VGVQPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07087 393 IPNLPFGGVGNSGMG-AYHGKAGFDTFSHLKSV 424
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
556-1008 |
5.37e-27 |
|
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: 116.01 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNAQPVTNPFDTT-RVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVALL 634
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTgKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 635 SREAGKTLNDGV-AEIREAADFCRYYAMLAERDFGGPTELKGPVgeINQLVLHGRGVFACISPWNFPLAIFTGQIAAALA 713
Cdd:cd07116 85 TWDNGKPVRETLaADIPLAIDHFRYFAGCIRAQEGSISEIDENT--VAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 714 AGNAVLAKPAEQTP---LIAAEAVrlyyKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARp 790
Cdd:cd07116 163 AGNCVVLKPAEQTPasiLVLMELI----GDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 791 gaIIPFIAETGGL--NGMFVDTTALKEQIIDDVI----LSAFgSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGD 864
Cdd:cd07116 238 --IIPVTLELGGKspNIFFADVMDADDAFFDKALegfvMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 865 PTDPATDIGPVIDADARAMLEAHLK--RLEGdAKIIA---RAELPAGADKGHLFAPTIAEIPTADYLEREVFGPILHVCR 939
Cdd:cd07116 315 PLDTETMIGAQASLEQLEKILSYIDigKEEG-AEVLTggeRNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTT 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 940 YepsKLKETASKLAARG-YGLTLGVHSRIEAFAEEVARLVPAGNVYINrsIIGAVVGVQPFGGEGLSGTG 1008
Cdd:cd07116 394 F---KDEEEALEIANDTlYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
553-1012 |
2.78e-26 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 114.16 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 553 GPIIGGKLKAGTNAQPVTNPFDTtRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVA 632
Cdd:PLN02315 22 GCYVGGEWRANGPLVSSVNPANN-QPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 633 LLSREAGKTLNDGVAEIREAADFCRYYAMLAeRDFGG---PTElkgpvgEINQLVL---HGRGVFACISPWNFPLAIFTG 706
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLS-RQLNGsiiPSE------RPNHMMMevwNPLGIVGVITAFNFPCAVLGW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 707 QIAAALAAGNAVLAKPAEQTPLIAAEAVRLYY----KAGLDPNLLALVPGrGETVGAKLVSHPGIDGVAFTGGTDTANLI 782
Cdd:PLN02315 174 NACIALVCGNCVVWKGAPTTPLITIAMTKLVAevleKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 783 NRSLAARPGAIipfIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVV 862
Cdd:PLN02315 253 QQTVNARFGKC---LLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 863 GDPTDPATDIGPVIDADARAMLEAHLKRLEGDA-KIIARAElpAGADKGHLFAPTIAEI-PTADYLEREVFGPILHVCRY 940
Cdd:PLN02315 330 GDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGgKILTGGS--AIESEGNFVQPTIVEIsPDADVVKEELFGPVLYVMKF 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2521504918 941 EpsKLKETASKLAARGYGLTLGVHSRieaFAEEVARLV-PAGN----VYINRSIIGAVVGvQPFGGEGLSGTGPKAG 1012
Cdd:PLN02315 408 K--TLEEAIEINNSVPQGLSSSIFTR---NPETIFKWIgPLGSdcgiVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
604-1027 |
1.00e-25 |
|
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: 112.20 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGV-AEIREAADFCRYYAmlaerdfGGPTELKGPVGEINQ 682
Cdd:cd07140 61 WGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALkTHVGMSIQTFRYFA-------GWCDKIQGKTIPINQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 683 ------LVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGR 753
Cdd:cd07140 134 arpnrnLTLTKRepiGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 754 GETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAArpGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRC 833
Cdd:cd07140 214 GSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAV--SNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENC 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 834 SALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPvidadarAMLEAHLKRL--------EGDAKII---ARAE 902
Cdd:cd07140 292 IAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP-------QNHKAHLDKLveycergvKEGATLVyggKQVD 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 903 LPagadkGHLFAPTI-AEIPTADYL-EREVFGPILHVCRYEPSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPA 980
Cdd:cd07140 365 RP-----GFFFEPTVfTDVEDHMFIaKEESFGPIMIISKFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEA 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2521504918 981 GNVYIN---RSIIGAvvgvqPFGGEGLSGTGpKAGGPYSLIRFASEKAIS 1027
Cdd:cd07140 440 GTVFVNtynKTDVAA-----PFGGFKQSGFG-KDLGEEALNEYLKTKTVT 483
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
601-939 |
1.43e-25 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 111.77 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 601 QIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYA-----MLAERDFGGPTELKG 675
Cdd:PLN00412 66 QKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAeegvrILGEGKFLVSDSFPG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 676 pvGEINQLVLHGR---GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPG 752
Cdd:PLN00412 146 --NERNKYCLTSKiplGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 753 RGETVGAKLVSHPGIDGVAFTGGtDTANLInrslaARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQR 832
Cdd:PLN00412 224 KGSEIGDFLTMHPGVNCISFTGG-DTGIAI-----SKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 833 CSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPAtDIGPVIDADARAMLEAhlkrLEGDAKIIARAELPAGADKGHL 912
Cdd:PLN00412 298 CTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDC-DITPVVSESSANFIEG----LVMDAKEKGATFCQEWKREGNL 372
|
330 340
....*....|....*....|....*....
gi 2521504918 913 FAPTIAEIPTADY--LEREVFGPILHVCR 939
Cdd:PLN00412 373 IWPLLLDNVRPDMriAWEEPFGPVLPVIR 401
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
610-1008 |
6.88e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 109.44 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 610 AGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGGPTELKGPVGEINQLVLHGR- 688
Cdd:PRK09406 45 AQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALLADEPADAAAVGASRAYVRYQPl 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 689 GVFACISPWNFPL---------AIFTGQIaaalaagnaVLAKPAEQTPLIAAEAVRLYYKAGL-DPNLLALVPGRGETvg 758
Cdd:PRK09406 125 GVVLAVMPWNFPLwqvvrfaapALMAGNV---------GLLKHASNVPQTALYLADLFRRAGFpDGCFQTLLVGSGAV-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 759 AKLVSHPGIDGVAFTGgtdtANLINRSLAARPG-AIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALR 837
Cdd:PRK09406 194 EAILRDPRVAAATLTG----SEPAGRAVAAIAGdEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 838 LLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAELPAGadKGHLFAPT 916
Cdd:PRK09406 270 RFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDaVAAGATILCGGKRPDG--PGWFYPPT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 917 -IAEIPTADYLER-EVFGPILHVcrYEPSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINrsiiGAVV 994
Cdd:PRK09406 348 vITDITPDMRLYTeEVFGPVASL--YRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN----GMTV 421
|
410
....*....|....*.
gi 2521504918 995 GVQ--PFGGEGLSGTG 1008
Cdd:PRK09406 422 SYPelPFGGVKRSGYG 437
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
601-1026 |
1.69e-24 |
|
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: 107.70 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 601 QIAWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTlndgVAEIR---------EAADFCRYYamlaeRDFGGPT 671
Cdd:cd07134 11 ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP----AAEVDlteilpvlsEINHAIKHL-----KKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 672 ELKGPV---GEINQLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLA 748
Cdd:cd07134 82 RVRTPLllfGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 749 LVPGRGETVGAkLVSHPgIDGVAFTGGTDTANLINRSlAARPGAIIPFiaETGGLNGMFVDTTALKEQIIDDVILSAFGS 828
Cdd:cd07134 161 VFEGDAEVAQA-LLELP-FDHIFFTGSPAVGKIVMAA-AAKHLASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 829 SGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPAT-DIGPVIDadaramlEAHLKRLEG---DAkiIAR-AEL 903
Cdd:cd07134 236 AGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVN-------DRHFDRLKGlldDA--VAKgAKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 904 PAGA---DKGHLFAPTIAE--IPTADYLEREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLV 978
Cdd:cd07134 307 EFGGqfdAAQRYIAPTVLTnvTPDMKIMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2521504918 979 PAGNVYINRSIIGAVVGVQPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07134 385 SSGGVVVNDVVLHFLNPNLPFGGVNNSGIG-SYHGVYGFKAFSHERAV 431
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
556-1040 |
2.54e-24 |
|
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: 108.13 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 556 IGGKLKAGTNA-QPVTNPFdTTRVLGHVSEATeadidaavdAAARAQIAWDR-KGGAG--------RGAVLRAMADALEA 625
Cdd:cd07128 5 VAGQWHAGTGDgRTLHDAV-TGEVVARVSSEG---------LDFAAAVAYAReKGGPAlraltfheRAAMLKALAKYLME 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 626 DMDRLVALlSREAGKTLNDGVAEIREAADFCRYYAMLAERDfgGPTELKGPVGEINQLVLHG-----------RGVFACI 694
Cdd:cd07128 75 RKEDLYAL-SAATGATRRDSWIDIDGGIGTLFAYASLGRRE--LPNAHFLVEGDVEPLSKDGtfvgqhiltprRGVAVHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 695 SPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPN-LLALVPGrgeTVGAKLVSHPGIDGVAFT 773
Cdd:cd07128 152 NAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLPEgALQLICG---SVGDLLDHLGEQDVVAFT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 774 GGTDTANLInRSLAARPGAIIPFIAETGGLNGMFVDTTALKEQ-----IIDDVILSAFGSSGQRCSALRLLYVPHDAADA 848
Cdd:cd07128 229 GSAATAAKL-RAHPNIVARSIRFNAEADSLNAAILGPDATPGTpefdlFVKEVAREMTVKAGQKCTAIRRAFVPEARVDA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 849 LIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRLEGDAKIIAR-----AELPAGADKGHLFAPTI--AEIP 921
Cdd:cd07128 308 VIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGgpdrfEVVGADAEKGAFFPPTLllCDDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 922 -TADYL-EREVFGPilhVCRYEPSKLKETASKLAARGYG-LTLGVHSRIEAFAEEVARLVPA--GNVYI-NRSIIGAVVG 995
Cdd:cd07128 388 dAATAVhDVEAFGP---VATLMPYDSLAEAIELAARGRGsLVASVVTNDPAFARELVLGAAPyhGRLLVlNRDSAKESTG 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2521504918 996 ---VQP---FGGEGLSGTGPKAGGPYSLIRFASEKAISnnisaqgGDPALL 1040
Cdd:cd07128 465 hgsPLPqlvHGGPGRAGGGEELGGLRGVKHYMQRTAVQ-------GSPTML 508
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
610-1013 |
6.53e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 104.02 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 610 AGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYYA----MLAERDF---GGPTEL-KGPVGEIN 681
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaALGDARLlrdGEAVQLgKDPAFQGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 682 QLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAG-LDPNLLALVPGRGetvgAK 760
Cdd:PRK11903 143 HVLVPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS----AG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 761 LVSH-PGIDGVAFTGGTDTANLInRSLAARPGAIIPFIAETGGLNGMF-----VDTTALKEQIIDDVILSAFGSSGQRCS 834
Cdd:PRK11903 219 LLDHlQPFDVVSFTGSAETAAVL-RSHPAVVQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQKCT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 835 ALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKRLEGDAKII----ARAELPAGADKG 910
Cdd:PRK11903 298 AIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLfdggGFALVDADPAVA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 911 HLFAPTIAEIPTADYL----EREVFGPILHVCRYEPSklkETASKLAARGYG-LTLGVHSRIEAFAEEVA-RLVPA-GNV 983
Cdd:PRK11903 378 ACVGPTLLGASDPDAAtavhDVEVFGPVATLLPYRDA---AHALALARRGQGsLVASVYSDDAAFLAAAAlELADShGRV 454
|
410 420 430
....*....|....*....|....*....|....*..
gi 2521504918 984 Y-INRSIIGAVVG---VQP---FGGEGLSGTGPKAGG 1013
Cdd:PRK11903 455 HvISPDVAALHTGhgnVMPqslHGGPGRAGGGEELGG 491
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
604-1008 |
2.55e-22 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 101.48 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 604 WDRKGGAGRGAVLRAMADALEADMDRLVALLSREAGKTLNDGVAEIREAADFCRYY-----AMLAERdfggPTELkgpvg 678
Cdd:PRK13968 45 WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYaehgpAMLKAE----PTLV----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 679 EINQLVLHGR--GVFACISPWNFPL-AIFTGQIaAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGE 755
Cdd:PRK13968 116 ENQQAVIEYRplGTILAIMPWNFPLwQVMRGAV-PILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADND 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 756 TVgAKLVSHPGIDGVAFTGGTDTANLINRSLAArpgAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSA 835
Cdd:PRK13968 195 GV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGA---ALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 836 LRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLEAHLKR-LEGDAKIIARAELPAGAdkGHLFA 914
Cdd:PRK13968 271 AKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEAtLAEGARLLLGGEKIAGA--GNYYA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 915 PTIAE--IPTADYLEREVFGPilhVCRYEPSKLKETASKLA-ARGYGLTLGVHSRIEAFAEEVARLVPAGNVYIN-RSII 990
Cdd:PRK13968 349 PTVLAnvTPEMTAFREELFGP---VAAITVAKDAEHALELAnDSEFGLSATIFTTDETQARQMAARLECGGVFINgYCAS 425
|
410
....*....|....*...
gi 2521504918 991 GAVVGvqpFGGEGLSGTG 1008
Cdd:PRK13968 426 DARVA---FGGVKKSGFG 440
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
555-989 |
4.33e-21 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 99.05 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 555 IIGGKLKAGTNAQ--PVTNPfDTTRVLGHVSEATEADIDAAVDAAARAQIAWDRKGGAGRGAVLRAMADALEADMDRLVA 632
Cdd:PLN02419 117 LIGGSFVESQSSSfiDVINP-ATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 633 LLSREAGKTLNDGVAEIREAADFCRYYAMLAERDFGgptELKGPV--GEINQLVLHGRGVFACISPWNFPLAIFTGQIAA 710
Cdd:PLN02419 196 NITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMG---EYLPNVsnGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 711 ALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGAkLVSHPGIDGVAFTgGTDTANLINRSLAARP 790
Cdd:PLN02419 273 AVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFV-GSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 791 GAIIPfiAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAA---DALIEGLKgalaAQVVGDPTD 867
Cdd:PLN02419 351 GKRIQ--SNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVERAK----ALKVTCGSE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 868 PATDIGPVIDADARAMLEAHLKR-LEGDAKII--ARAELPAGADKGHLFAPTIAE--IPTADYLEREVFGPILhVCrYEP 942
Cdd:PLN02419 425 PDADLGPVISKQAKERICRLIQSgVDDGAKLLldGRDIVVPGYEKGNFIGPTILSgvTPDMECYKEEIFGPVL-VC-MQA 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2521504918 943 SKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSI 989
Cdd:PLN02419 503 NSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI 549
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
689-1008 |
7.98e-21 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 97.41 E-value: 7.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 689 GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLALVPGrGETVGAKLVSHPgID 768
Cdd:PTZ00381 111 GVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP-FD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 769 GVAFTGGTDTANLINRSLAARpgaIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAADA 848
Cdd:PTZ00381 188 HIFFTGSPRVGKLVMQAAAEN---LTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 849 LIEGLKGALAAQVVGDPTDpATDIGPVIDadaramlEAHLKRLEG-----DAKIIARAElpagADKGHLF-APTIAEIPT 922
Cdd:PTZ00381 265 FIEALKEAIKEFFGEDPKK-SEDYSRIVN-------EFHTKRLAElikdhGGKVVYGGE----VDIENKYvAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 923 ADY--LEREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPFG 1000
Cdd:PTZ00381 333 LDSplMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFG 410
|
....*...
gi 2521504918 1001 GEGLSGTG 1008
Cdd:PTZ00381 411 GVGNSGMG 418
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
603-980 |
5.13e-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: 94.53 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 603 AWDRKGGAGRGAVLRAMADALEADMDRLVALLSREAG--KTLNDG-----VAEIREAADFCRYYAMLAER-DFGGPTELK 674
Cdd:cd07129 14 SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpEARLQGelgrtTGQLRLFADLVREGSWLDARiDPADPDRQP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 675 GPVGEINQLvLHGRGVFACISPWNFPLA------------------IFTGQiaaalaagnavlakPA-----EQTPLIAA 731
Cdd:cd07129 94 LPRPDLRRM-LVPLGPVAVFGASNFPLAfsvaggdtasalaagcpvVVKAH--------------PAhpgtsELVARAIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 732 EAVRlyyKAGLDPNLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPgAIIPFIAETGGLNGMFVDTT 811
Cdd:cd07129 159 AALR---ATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARP-EPIPFYAELGSVNPVFILPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 812 ALKE---QIIDDVILSAFGSSGQRCSALRLLYVPHDAA-DALIEGLKGALAAQVvgdptdPATDIGPVIdadaRAMLEAH 887
Cdd:cd07129 235 ALAErgeAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAP------AQTMLTPGI----AEAYRQG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 888 LKRLEGDAKIIARAElPAGADKGHLFAPTIAEIPTADYLER-----EVFGPILHVCRYE-PSKLKETASKLAARgygLTL 961
Cdd:cd07129 305 VEALAAAPGVRVLAG-GAAAEGGNQAAPTLFKVDAAAFLADpalqeEVFGPASLVVRYDdAAELLAVAEALEGQ---LTA 380
|
410
....*....|....*....
gi 2521504918 962 GVHSRIEAFAeEVARLVPA 980
Cdd:cd07129 381 TIHGEEDDLA-LARELLPV 398
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
688-1028 |
1.45e-18 |
|
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: 89.59 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 688 RGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLALVPGRGETVGAKLVSHpgI 767
Cdd:cd07135 109 LGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQK--F 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 768 DGVAFTGGTDTANLINRSlAARpgAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDAAD 847
Cdd:cd07135 186 DKIFYTGSGRVGRIIAEA-AAK--HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 848 ALIEGLKGALAAQVVGDPTDPaTDIGPVIDadaramlEAHLKRLEG-----DAKIIARAElpagADKGHLF-APTIAEIP 921
Cdd:cd07135 263 EFVEELKKVLDEFYPGGANAS-PDYTRIVN-------PRHFNRLKSlldttKGKVVIGGE----MDEATRFiPPTIVSDV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 922 TAD--YLEREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPF 999
Cdd:cd07135 331 SWDdsLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPF 408
|
330 340
....*....|....*....|....*....
gi 2521504918 1000 GGEGLSGTGpKAGGPYSLIRFASEKAISN 1028
Cdd:cd07135 409 GGVGDSGYG-AYHGKYGFDTFTHERTVVK 436
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
689-1008 |
3.94e-18 |
|
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: 88.31 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 689 GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIA---AEAVRLYYkaglDPNLLALVPGRGEtVGAKLVSHP 765
Cdd:cd07133 103 GVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSallAELLAEYF----DEDEVAVVTGGAD-VAAAFSSLP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 766 gIDGVAFTGGTDTANLINRSlAARpgAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHDA 845
Cdd:cd07133 178 -FDHLLFTGSTAVGRHVMRA-AAE--NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 846 ADALIEGLKGALAAQVVGDPTDPatDIGPVIDadaramlEAHLKRLEG---DAK-----IIARAELPAGADKGHLFAPTI 917
Cdd:cd07133 254 LEEFVAAAKAAVAKMYPTLADNP--DYTSIIN-------ERHYARLQGlleDARakgarVIELNPAGEDFAATRKLPPTL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 918 AEIPTAD--YLEREVFGPILHVCRYepSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVG 995
Cdd:cd07133 325 VLNVTDDmrVMQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQD 402
|
330
....*....|...
gi 2521504918 996 VQPFGGEGLSGTG 1008
Cdd:cd07133 403 DLPFGGVGASGMG 415
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
689-1026 |
7.18e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 87.86 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 689 GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIA---AEAVRLYykagLDPNLLALVPGrGETVGAKLVSHP 765
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSaflAANIPKY----LDSKAVKVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 766 GiDGVAFTGGTDTANLInrsLAARPGAIIPFIAETGGLNGMFVDTTALK---EQIIDDVILSAFGS-SGQRCSALRLLYV 841
Cdd:PLN02203 185 W-DKIFFTGSPRVGRII---MTAAAKHLTPVALELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQACIAIDYVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 842 PHDAADALIEGLKGALAAQVVGDPTDPatdigpviDADARAMLEAHLKRLEG---DAKIIARAELPAGADKGHLF-APTI 917
Cdd:PLN02203 261 EERFAPILIELLKSTIKKFFGENPRES--------KSMARILNKKHFQRLSNllkDPRVAASIVHGGSIDEKKLFiEPTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 918 AEIP--TADYLEREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVG 995
Cdd:PLN02203 333 LLNPplDSDIMTEEIFGPLLPIITVK--KIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACD 410
|
330 340 350
....*....|....*....|....*....|.
gi 2521504918 996 VQPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:PLN02203 411 SLPFGGVGESGFG-RYHGKYSFDTFSHEKAV 440
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
612-1026 |
8.39e-18 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 87.47 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 612 RGAVLRAMADALEADMDRLVALLSREAGK-TLNDGVAEIREAADFCRYyAMLAERDFGGPTELKGPVGEI---NQLVLHG 687
Cdd:cd07137 23 RKSQLKGLLRLVDENEDDIFAALRQDLGKpSAESFRDEVSVLVSSCKL-AIKELKKWMAPEKVKTPLTTFpakAEIVSEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 688 RGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLALVPGrGETVGAKLVSHPGi 767
Cdd:cd07137 102 LGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-GVPETTALLEQKW- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 768 DGVAFTGGTDTANLInrsLAARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGS-SGQRCSALRLLYVPHDAA 846
Cdd:cd07137 179 DKIFFTGSPRVGRII---MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESFA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 847 DALIEGLKGALaAQVVGDptDPATDigpviDADARAMLEAHLKRLEG--DAKIIARAELPAGA-DKGHLF-APTIAEIPT 922
Cdd:cd07137 256 PTLIDALKNTL-EKFFGE--NPKES-----KDLSRIVNSHHFQRLSRllDDPSVADKIVHGGErDEKNLYiEPTILLDPP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 923 AD--YLEREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQPFG 1000
Cdd:cd07137 328 LDssIMTEEIFGPLLPIITVK--KIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFG 405
|
410 420
....*....|....*....|....*.
gi 2521504918 1001 GEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07137 406 GVGESGFG-AYHGKFSFDAFSHKKAV 430
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
249-484 |
5.44e-16 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 82.06 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 249 LSALSPRYEAT--------HEARVWDELYPRILRLARIAAQYDINFTMDAEEA------DRLALSLKL-LDRLAREPELG 313
Cdd:PLN02681 191 FADSSPLYHATsepepltaEEERLLELAHERLQKLCERAAQLGVPLLIDAEYTslqpaiDYITYDLAReFNKGKDRPIVY 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 314 GwtglglAVQAYQKRCPEVIRRVSELAKSSGRRLMVRLVKGAYWDTEIKRAQVFGrTDYPVFTTKAATDLNYLVCAKAMI 393
Cdd:PLN02681 271 G------TYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLG-VPSPVHDTIQDTHACYNRCAEFLL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 394 EAAPHIYSQ--FATHNAHSL-AAVYKMA----SERAVKIEFQRLHGMGEAL-YDAAHDAFgpvTVRAYAPVGGHEDLLPY 465
Cdd:PLN02681 344 EKASNGDGEvmLATHNVESGeLAAAKMNelglHKGDPRVQFAQLLGMSDNLsFGLGNAGF---RVSKYLPYGPVEEVIPY 420
|
250 260
....*....|....*....|..
gi 2521504918 466 LVRRLLENG---ANSSFVHALL 484
Cdd:PLN02681 421 LLRRAEENRgllSGSAIDRQLL 442
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
689-1026 |
1.54e-14 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 77.16 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 689 GVFACISPWNFPL---------AIFTGQiaaalaagnAVLAKPAEQTP---LIAAEAVRLYYkaglDPNLLALVPGrGET 756
Cdd:cd07136 102 GVVLIIAPWNYPFqlalapligAIAAGN---------TAVLKPSELTPntsKVIAKIIEETF----DEEYVAVVEG-GVE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 757 VGAKLVSHPgIDGVAFTGGTDTANLINRSlAARpgAIIPFIAETGGLNGMFVDTTAlkeqiidDVILSA----FG---SS 829
Cdd:cd07136 168 ENQELLDQK-FDYIFFTGSVRVGKIVMEA-AAK--HLTPVTLELGGKSPCIVDEDA-------NLKLAAkrivWGkflNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 830 GQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDpATDIGPVIDadaramlEAHLKRLEG---DAKIIARAElpag 906
Cdd:cd07136 237 GQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIIN-------EKHFDRLAGlldNGKIVFGGN---- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 907 ADKGHLF-APTIAEIPTAD--YLEREVFGPILHVCRYEpsKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNV 983
Cdd:cd07136 305 TDRETLYiEPTILDNVTWDdpVMQEEIFGPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGG 382
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2521504918 984 YINRSIIGAVVGVQPFGGEGLSGTGpKAGGPYSLIRFASEKAI 1026
Cdd:cd07136 383 CINDTIMHLANPYLPFGGVGNSGMG-SYHGKYSFDTFSHKKSI 424
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
682-1026 |
3.37e-14 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 76.62 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 682 QLVLHGRGVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAgLDPNLLALVPGRGETVGAKL 761
Cdd:PLN02174 107 EIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 762 vsHPGIDGVAFTGGTDTANLInrsLAARPGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFG-SSGQRCSALRLLY 840
Cdd:PLN02174 186 --EQKWDKIFYTGSSKIGRVI---MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYIL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 841 VPHDAADALIEGLKGALAAQVVGDPTDpATDIGPVIDADARAMLEAHLKRLEGDAKIIARAElpagADKGHL-FAPTI-A 918
Cdd:PLN02174 261 TTKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGE----KDRENLkIAPTIlL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 919 EIPTADY-LEREVFGPILHVcrYEPSKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVVGVQ 997
Cdd:PLN02174 336 DVPLDSLiMSEEIFGPLLPI--LTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTL 413
|
330 340
....*....|....*....|....*....
gi 2521504918 998 PFGGEGLSGTGPKAgGPYSLIRFASEKAI 1026
Cdd:PLN02174 414 PFGGVGESGMGAYH-GKFSFDAFSHKKAV 441
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
647-804 |
2.26e-11 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 68.35 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 647 AEIREAADFCRYYAMLAERDFGGPTELKGPVGEINQLVLHGRGVFACISPwnfPLAIFTGQIAAALAagnavlakpAEQT 726
Cdd:PRK11905 1038 DKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVAD---TEEALLRQLAAALA---------TGNV 1105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2521504918 727 PLIAAEAVRLYYKAGLDPNLLAlvpgrGETVGAKLVSHPGIDGVAFTGGTDTANLINRSLAARPGAIIPFIAETGGLN 804
Cdd:PRK11905 1106 AVVAADSGLAAALADLPGLVAA-----RIDWTQDWEADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEPTDA 1178
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
718-988 |
8.10e-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: 62.50 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 718 VLAKPAEQTPLIAAEAVR----LYYKAGLDPNLLALVP-GRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSlaARPGA 792
Cdd:cd07127 224 VIVKPHPAAILPLAITVQvareVLAEAGFDPNLVTLAAdTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEAN--ARQAQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 793 IipfIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRLLYVPHD---------AADALIEGLKGALAAqVVG 863
Cdd:cd07127 302 V---YTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDG-LLA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 864 DPTDPATDIGPVIDADARAMLE--AHLKRLEGDAKIIARAELPAGADKGHLFAPTIAEipTADYLEREVFGPILHVCRYE 941
Cdd:cd07127 378 DPARAAALLGAIQSPDTLARIAeaRQLGEVLLASEAVAHPEFPDARVRTPLLLKLDAS--DEAAYAEERFGPIAFVVATD 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2521504918 942 PSKLKETASKLAARGYG-LTLGVHSRIEAFAE---EVARLVPA-------GNVYINRS 988
Cdd:cd07127 456 STDHSIELARESVREHGaMTVGVYSTDPEVVErvqEAALDAGValsinltGGVFVNQS 513
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
628-974 |
8.72e-09 |
|
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: 59.05 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 628 DRLVALLSREAGKTLNDGVAEIRE--------AADFCRYYAmlaeRDFGGPTELKGPVGeinqlvlHGR----GVFACIS 695
Cdd:cd07126 82 DFFARLIQRVAPKSDAQALGEVVVtrkflenfAGDQVRFLA----RSFNVPGDHQGQQS-------SGYrwpyGPVAIIT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 696 PWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIAAEAVRLYYKAGLDPNLLALVPGRGETVGaKLVSHPGIDGVAFTGG 775
Cdd:cd07126 151 PFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPRMTLFTGS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 776 TDTANLINRSLAARpgaiiPFIAETGglngmfVDTTALKEQIID-DVIL-----SAFGSSGQRCSALRLLYVPHDAADAL 849
Cdd:cd07126 230 SKVAERLALELHGK-----VKLEDAG------FDWKILGPDVSDvDYVAwqcdqDAYACSGQKCSAQSILFAHENWVQAG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 850 IEGLKGALAAQ-VVGDPTdpatdIGPVIDADARAMLEaHLKRL--------EGDAKIIARAELPA--GA-DKGHLFAP-- 915
Cdd:cd07126 299 ILDKLKALAEQrKLEDLT-----IGPVLTWTTERILD-HVDKLlaipgakvLFGGKPLTNHSIPSiyGAyEPTAVFVPle 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2521504918 916 TIAEIPTADYLEREVFGPILHVCRYEPSKLKETASKLAARGYGLTLGVHSRIEAFAEEV 974
Cdd:cd07126 373 EIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
689-1008 |
1.36e-06 |
|
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: 52.22 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 689 GVFACISPWNFPLAIFTGQIAAALAAGNAVLAKPAEQTPLIA---AEAVRLYykagLDPNLLALVPGrGETVGAKLVSHP 765
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAkllAELIPKY----LDKECYPVVLG-GVEETTELLKQR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 766 gIDGVAFTGGTDTANLInRSLAARpgAIIPFIAETGGLNGMFVDTTALKEQIIDDVILSAFGSSGQRCSALRllYVPHDA 845
Cdd:cd07132 177 -FDYIFYTGSTSVGKIV-MQAAAK--HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPD--YVLCTP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 846 A--DALIEGLKGALAAQVVGDPTDPAtDIGPVIDadaramlEAHLKRLEgdaKIIARAELPAGA--DKGHLF-APTI-AE 919
Cdd:cd07132 251 EvqEKFVEALKKTLKEFYGEDPKESP-DYGRIIN-------DRHFQRLK---KLLSGGKVAIGGqtDEKERYiAPTVlTD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 920 IPTAD-YLEREVFGPILhvcryeP----SKLKETASKLAARGYGLTLGVHSRIEAFAEEVARLVPAGNVYINRSIIGAVV 994
Cdd:cd07132 320 VKPSDpVMQEEIFGPIL------PivtvNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTL 393
|
330
....*....|....
gi 2521504918 995 GVQPFGGEGLSGTG 1008
Cdd:cd07132 394 DSLPFGGVGNSGMG 407
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
745-885 |
4.80e-05 |
|
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: 46.83 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 745 NLLALVPGRGETVGAKLVSHPGIDGVAFTGGTDTANLINRSlaarpGAIIPFIAETGGLNGMFVDTTALKEQIIDDVILS 824
Cdd:cd07077 160 ILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKH-----SPHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2521504918 825 AFgSSGQRCSALRLLYVPHDAADALIEGLKGALAAQVVGDPTDPATDIGPVIDADARAMLE 885
Cdd:cd07077 235 KF-FDQNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFDDEALE 294
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
669-802 |
7.42e-04 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 43.77 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2521504918 669 GPTELKGPVGEINQLVLHGRGVFACISpwnfplaiftgqiaaalaagnavlakPAEQTPLIAAEAVrlyYKAGLDpnllA 748
Cdd:COG4230 1044 GALTLPGPTGERNTLTLRPRGRVLCLA--------------------------DSLEALLAQLAAA---LATGNR----A 1090
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2521504918 749 LVPGRGETVGAKLVSHPGIDGVAFTGgtdTANLINRSLAARPGAIIPFIA----------ETGG 802
Cdd:COG4230 1091 VVAADLALAGLPAVLLPPFDAVLFEG---RLRALRQALAARDGAIVPVIDagydlerlleEAGG 1151
|
|
| |
