|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
2-1045 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1763.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 2 LEPKASLQPQPPLREAINSAFRAEEAHYMDMLIKAAQLSTSDVESIRKRAMKLVEQVREGRRKSTGIDSFLTEYALSSDE 81
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGGIDAFLQEYSLSTEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 82 GIALMCLAEAMLRVPDNETIDILIRDKLSGPDWDAHRGQSDSFFVNAATWALMLTGKVLSP-ERIDNDLGRSLFRLANRT 160
Cdd:PRK11904 81 GIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLdKKADGTPSGVLKRLVNRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 161 GEGVIRKAVEKAMRIMSKQFVMGRTIGEALNRARKKEALGYRYSYDMLGEAALTAVDAARYLEAYMDAIDSIGAQvKGKG 240
Cdd:PRK11904 161 GEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRA-AGGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 241 DVYTNPGISIKLSALHPRYQESQYESVMATLPDNLLALCLRAKAANIGLTIDAEESERLEISLDVIEKVFKNPALNGWNG 320
Cdd:PRK11904 240 DLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 321 FGMAVQSYQKRAFYLLDWVAGLARGQNRRMNVRLIKGAYWDSEIKKAQMQGLTEYPVFTRKVFTDVSFQACAKKILTMTD 400
Cdd:PRK11904 320 FGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 401 TIYPQFATHNACSVATILEMCGsYRDFEFQCLHGMGNELYAEIVPAnrLGIPCRIYAPVGTHEDLLPYLVRRLLENGANS 480
Cdd:PRK11904 400 AIYPQFATHNAHTVAAILEMAG-HRGFEFQRLHGMGEALYDALLDA--PGIPCRIYAPVGSHKDLLPYLVRRLLENGANS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 481 SFVNRIVDENAPISELVEDPVSRAKALLESGRRSIPLPRDIFMPERPNSAGLDLNDRTVRRAMAASIEARMPFHFEAAPM 560
Cdd:PRK11904 477 SFVHRLVDPDVPIEELVADPVEKLRSFETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPI 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 561 MDGragSGVEVSVTSPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASL 640
Cdd:PRK11904 557 ING---EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVR 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 641 EAGKTLADGVAEVREAVDFCRYYAARACEMMEKPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGN 720
Cdd:PRK11904 634 EAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGN 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 721 AVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIVPL 800
Cdd:PRK11904 714 TVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPL 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 801 IAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVI 880
Cdd:PRK11904 794 IAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVI 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 881 DKDALAVLQAHVAKMREAHTLIYQCELPSACNNGYFFAPAAFEIPSIRVLEKEVFGPILHVVRFNRKDLDAVIDAINATG 960
Cdd:PRK11904 874 DAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAINATG 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 961 YGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYLHRLCIERTFTVDTTAAGGN 1040
Cdd:PRK11904 954 YGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNTTAAGGN 1033
|
....*
gi 1606703614 1041 ASLMA 1045
Cdd:PRK11904 1034 ASLLS 1038
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
7-1027 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1671.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 7 SLQPQPPLREAINSAFRAEEAHYMDMLIKAAQLSTSDVESIRKRAMKLVEQVREGRRKsTGIDSFLTEYALSSDEGIALM 86
Cdd:PRK11905 8 PFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKG-TGVEALLQEYSLSSQEGVALM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 87 CLAEAMLRVPDNETIDILIRDKLSGPDWDAHRGQSDSFFVNAATWALMLTGKVLSPERiDNDLGRSLFRLANRTGEGVIR 166
Cdd:PRK11905 87 CLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVN-DRGLSAALTRLIARLGEPVIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 167 KAVEKAMRIMSKQFVMGRTIGEALNRARKKEALGYRYSYDMLGEAALTAVDAARYLEAYMDAIDSIGAQVKGKGdVYTNP 246
Cdd:PRK11905 166 KAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRG-VYDGP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 247 GISIKLSALHPRYQESQYESVMATLPDNLLALCLRAKAANIGLTIDAEESERLEISLDVIEKVFKNPALNGWNGFGMAVQ 326
Cdd:PRK11905 245 GISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIGFVVQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 327 SYQKRAFYLLDWVAGLARGQNRRMNVRLIKGAYWDSEIKKAQMQGLTEYPVFTRKVFTDVSFQACAKKILTMTDTIYPQF 406
Cdd:PRK11905 325 AYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVIYPQF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 407 ATHNACSVATILEMCGSYRDFEFQCLHGMGNELYAEIVPANRLGIPCRIYAPVGTHEDLLPYLVRRLLENGANSSFVNRI 486
Cdd:PRK11905 405 ATHNAQTLAAIYELAGGKGDFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNRI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 487 VDENAPISELVEDPVSRAKALLESGRRSIPLPRDIFMPERPNSAGLDLNDRTVRRAMAASIEARMPFHFEAAPMMDGRAG 566
Cdd:PRK11905 485 VDENVPVEELIADPVEKVAAMGVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLAGGDV 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 567 SGVEVSVTSPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTL 646
Cdd:PRK11905 565 DGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTL 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 647 ADGVAEVREAVDFCRYYAARACEMMEKPlalegytgernelSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKP 726
Cdd:PRK11905 645 ANAIAEVREAVDFLRYYAAQARRLLNGP-------------GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKP 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 727 AEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIVPLIAETGG 806
Cdd:PRK11905 712 AEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLIAETGG 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 807 LNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALA 886
Cdd:PRK11905 792 QNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQA 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 887 VLQAHVAKMREAHTLIYQCELPSACNNGYFFAPAAFEIPSIRVLEKEVFGPILHVVRFNRKDLDAVIDAINATGYGLTLG 966
Cdd:PRK11905 872 NIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFG 951
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606703614 967 IHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYLHRLCIE 1027
Cdd:PRK11905 952 LHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
2-1024 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1375.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 2 LEPKASLQPQPPLREAINSAFRAEEAHYMDMLIKAAQLSTSDVESIRKRAMKLVEQVREgRRKSTG----IDSFLTEYAL 77
Cdd:PRK11809 79 LEFAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRN-QKSAGGragmVQGLLQEFSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 78 SSDEGIALMCLAEAMLRVPDNETIDILIRDKLSGPDWDAHRGQSDSFFVNAATWALMLTGKVLSPERIDNdLGRSLFRLA 157
Cdd:PRK11809 158 SSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEAS-LSSSLNRII 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 158 NRTGEGVIRKAVEKAMRIMSKQFVMGRTIGEALNRARKKEALGYRYSYDMLGEAALTAVDAARYLEAYMDAIDSIGAQVK 237
Cdd:PRK11809 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASN 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 238 GKGdVYTNPGISIKLSALHPRYQESQYESVMATLPDNLLALCLRAKAANIGLTIDAEESERLEISLDVIEKVFKNPALNG 317
Cdd:PRK11809 317 GRG-IYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 318 WNGFGMAVQSYQKRAFYLLDWVAGLARGQNRRMNVRLIKGAYWDSEIKKAQMQGLTEYPVFTRKVFTDVSFQACAKKILT 397
Cdd:PRK11809 396 WNGIGFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLA 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 398 MTDTIYPQFATHNACSVATILEMCG-SYR--DFEFQCLHGMGNELYAEIV---PANRLGIPCRIYAPVGTHEDLLPYLVR 471
Cdd:PRK11809 476 VPNLIYPQFATHNAHTLAAIYHLAGqNYYpgQYEFQCLHGMGEPLYEQVVgkvADGKLNRPCRIYAPVGTHETLLAYLVR 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 472 RLLENGANSSFVNRIVDENAPISELVEDPVSRAKALLESGRR------SIPLPRDIFMPERPNSAGLDLNDRTVRRAMAA 545
Cdd:PRK11809 556 RLLENGANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQlglphpKIPLPRDLYGKGRANSAGLDLANEHRLASLSS 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 546 SIEARMPFHFEAAPMMDGRAGSGVEVSVTSPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYAD 625
Cdd:PRK11809 636 ALLASAHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAAD 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 626 LLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARAcemmekplalegytgeRNELS--LH-PRGTVLCISPWN 702
Cdd:PRK11809 716 LMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQV----------------RDDFDndTHrPLGPVVCISPWN 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 703 FPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDT 782
Cdd:PRK11809 780 FPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEV 859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 783 ANRINQTLAAR---SGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKG 859
Cdd:PRK11809 860 ARLLQRNLAGRldpQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRG 939
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 860 AMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPSACN--NGYFFAPAAFEIPSIRVLEKEVFGP 937
Cdd:PRK11809 940 AMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDwqSGTFVPPTLIELDSFDELKREVFGP 1019
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 938 ILHVVRFNRKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGG 1017
Cdd:PRK11809 1020 VLHVVRYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGG 1099
|
....*..
gi 1606703614 1018 PHYLHRL 1024
Cdd:PRK11809 1100 PLYLYRL 1106
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
1-1049 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1358.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 1 MLEPKASLQPQPPLREAINSAFRAEEAHYMDMLikAAQLSTSDVESIRKRAMKLVEQVREGRRKSTGIDSFLTEYALSSD 80
Cdd:COG4230 3 FALFAPLLRPALPLRAAIAAAERAEELLAAAAL--LAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 81 EGIALMCLAEAMLRVPDNETIDILIRDKLSGPDWDAHRGQSDSFFVNAATWALMLTGKVLSPERIDNDLGRSLFRLANRT 160
Cdd:COG4230 81 SEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 161 GEGVIRKAVEKAMRIMSKQFVMGRTIGEALNRARKKEALGYRYSYDMLGEAALTAVDAARYLEAYMDAIDSIGAQVkGKG 240
Cdd:COG4230 161 GRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAA-GGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 241 DVYTNPGISIKLSALHPRYQESQYESVMATLPDNLLALCLRAKAA----NIGLTIDAEESERLEISLDVIEKVFKNPALN 316
Cdd:COG4230 240 SGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAainiNIDEEEDAEELLLLLLLLDLLAALLLDGGLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 317 GWNGFGMAVQSYQKRAFYLLDWVAGLARGQNRRMNVRLIKGAYWDSEIKKAQMQGLTEYPVFTRKVFTDVSFQACAKKIL 396
Cdd:COG4230 320 GGGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 397 TMTDTIYPQFATHNACSVATILEMcGSYRDFEFQCLHGMGnELYAEIVPANRLGIPCRIYAPVGTHEDLLPYLVRRLLEN 476
Cdd:COG4230 400 AAQPAFAPQFATHAAATAAAAAAA-GGGGEFEFQCLHGMG-EYLYDQVGRGKLGRPCRIYAPVGSHEDLLAYLVRRLLEN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 477 GANSSFVNRIVDENAPISELVEDPVSRAKALLESGRRSIPLPRDIFMPERPNSAGLDLNDRTVRRAMAASIEARMPFHFE 556
Cdd:COG4230 478 GANSSFVNRIADEDVPVEELIADPVEKARALGGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQ 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 557 AAPMMDGRAGSGVEVSVTSPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLA 636
Cdd:COG4230 558 AAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMA 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 637 LASLEAGKTLADGVAEVREAVDFCRYYAARACEMMEKPLALegytgernelslHPRGTVLCISPWNFPLAIFTGQAVAAL 716
Cdd:COG4230 638 LLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVL------------RGRGVFVCISPWNFPLAIFTGQVAAAL 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 717 VTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGE 796
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGP 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 797 IVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDV 876
Cdd:COG4230 786 IVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDV 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 877 GPVIDKDALAVLQAHVAKMREAHTLIYQCELPSACNNGYFFAPAAFEIPSIRVLEKEVFGPILHVVRFNRKDLDAVIDAI 956
Cdd:COG4230 866 GPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAI 945
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 957 NATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYLHRLCIERTFTVDTTA 1036
Cdd:COG4230 946 NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTA 1025
|
1050
....*....|...
gi 1606703614 1037 AGGNASLMALPEG 1049
Cdd:COG4230 1026 AGGNASLLALGDW 1038
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
478-1044 |
0e+00 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 793.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 478 ANSSFVNRIVDENAPiselvedpvsrakallesgrrsiplprdifmperpnsagldlndrtvRRAMAASIEARMPFHFEA 557
Cdd:cd07125 1 ANSSFVNRIFDLEVP-----------------------------------------------LEALADALKAFDEKEWEA 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 558 APMMDGRAGSGVEV-SVTSPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLA 636
Cdd:cd07125 34 IPIINGEETETGEGaPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 637 LASLEAGKTLADGVAEVREAVDFCRYYAARACEMMEKPLaLEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAAL 716
Cdd:cd07125 114 LAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPE-LPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAAL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 717 VTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGE 796
Cdd:cd07125 193 AAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 797 IVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDV 876
Cdd:cd07125 273 ILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 877 GPVIDKDALAVLQAHVAKMREAHTLIYQCELPSacNNGYFFAPAAFEIPSIRVLEKEVFGPILHVVRFNRKDLDAVIDAI 956
Cdd:cd07125 353 GPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDD--GNGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEAIEDI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 957 NATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYLHRLCIERTFTVDTTA 1036
Cdd:cd07125 431 NATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLNTTA 510
|
....*...
gi 1606703614 1037 AGGNASLM 1044
Cdd:cd07125 511 AGGNPSLL 518
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
36-1041 |
0e+00 |
|
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440272 [Multi-domain] Cd Length: 975 Bit Score: 661.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 36 AAQLSTSDVESIRKRAMKLVEQVREgrRKSTGIDSFLTEYALSSDEGIALMCLAEAMLRVPDNETIDILIRDKLSgpdwd 115
Cdd:COG0506 2 TAALDEALRARAVALARRLVEAIRA--APEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 116 ahrgQSDSFFVNAATWALMLTgkvlsperidndlgrslfrLANRTGEGVIRKAVEKAMRIMSKQFVMGRTIGEALNRARK 195
Cdd:COG0506 75 ----KSPSFLVNASTWGLMLT-------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 196 KEALGYRYSYDMLGEAALTAVDAARYLEAYMDAIDSIGAQVkgkgdvYTNPGISIKLSALHPRYQESQYESVMATLPDNL 275
Cdd:COG0506 132 LRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG------VDRPGVSVKLSALGPRYSPAQRERVVEELLERL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 276 LALCLRAKAANIGLTIDAEESERLEISLDVIEKVFKNPALNGWNGFGMAVQSYQKRAFYLLDWVAGLARGQNRRMNVRLI 355
Cdd:COG0506 206 RPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 356 KGAYWDSEIKKAQMQGLtEYPVFTRKVFTDVSFQACAKKILTMTDTIYPQFATHNACSVATILEMCGSY----RDFEFQC 431
Cdd:COG0506 286 KGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGERgrppDRFEFQM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 432 LHGMGNELYAEI--VPANRLGIPCRIYAPVGTHEDLLPYLVRRLLENGANSSFVNRIVDENAPISELVEDPVSRAKALLE 509
Cdd:COG0506 365 LYGMGEDLQRALaaVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 510 SGRRSIPLPRDIFMPERPNSAGLDLNDRTVRRAMAASIEARMPFHFEAAPMMDGRAGSGVEVSVTSPQNyRETIGRVIEA 589
Cdd:COG0506 445 TPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAA-AAVVAAAAAA 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 590 SKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARACE 669
Cdd:COG0506 524 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAA 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 670 MMEKPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPS 749
Cdd:COG0506 604 RAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGG 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 750 VMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSA 829
Cdd:COG0506 684 VLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAAS 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 830 FGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPS 909
Cdd:COG0506 764 ASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLV 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 910 ACNNGYFFAPAAFEIPSIRVLEKEVFGPILHVVRFNRKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYV 989
Cdd:COG0506 844 PGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGG 923
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 1606703614 990 NRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYLHRLCIERTFTVDTTAAGGNA 1041
Cdd:COG0506 924 GGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAAA 975
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
520-1024 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 614.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 520 DIFMPERPNSAGLDLNDRTVRRAMAASIEARMPFHFEAAPMMDGRAGSGVEVS-VTSPQNYRETIGRVIEASKEDVEWAL 598
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQpVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 599 SRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARACEMMekplale 678
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVL------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 679 gytgerNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKG 758
Cdd:TIGR01238 154 ------GEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 759 ETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCS 838
Cdd:TIGR01238 228 ADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 839 ALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPS--ACNNGYF 916
Cdd:TIGR01238 308 ALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDsrACQHGTF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 917 FAPAAFEIPSIRVLEKEVFGPILHVVRFNRKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGA 996
Cdd:TIGR01238 388 VAPTLFELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGA 467
|
490 500
....*....|....*....|....*...
gi 1606703614 997 VVGLQPFGGEGLSGTGPKAGGPHYLHRL 1024
Cdd:TIGR01238 468 VVGVQPFGGQGLSGTGPKAGGPHYLYRL 495
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
540-1031 |
7.05e-165 |
|
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: 494.79 E-value: 7.05e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 540 RRAMAASIEARMPFHFEAAPMMDGRA---GSGVEVSVtSPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAER 616
Cdd:cd07083 1 RRAMREALRRVKEEFGRAYPLVIGGEwvdTKERMVSV-SPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 617 AAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARACEMMEKPLALEGYTGERNELSLHPRGTVL 696
Cdd:cd07083 80 ARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 697 CISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMF 776
Cdd:cd07083 160 VISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 777 TGSTDTANRINQTLA---ARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRF 853
Cdd:cd07083 240 TGSLETGKKIYEAAArlaPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 854 MALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPSAcnNGYFFAPAAFEI--PSIRVLE 931
Cdd:cd07083 320 LERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEG--EGYFVAPTVVEEvpPKARIAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 932 KEVFGPILHVVRFNRKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGT 1011
Cdd:cd07083 398 EEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGT 477
|
490 500
....*....|....*....|
gi 1606703614 1012 GPKAGGPHYLHRLCIERTFT 1031
Cdd:cd07083 478 NAKTGGPHYLRRFLEMKAVA 497
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
528-1031 |
7.86e-142 |
|
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: 435.11 E-value: 7.86e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 528 NSAGLDLNDRTVRRAMAASIE-ARMPFHFEAAPMMDGRA-GSGVEVSVTSPQNYRETIGRVIEASKEDVEWALSRAVEGA 605
Cdd:cd07124 3 NEPFTDFADEENRAAFRAALArVREELGREYPLVIGGKEvRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 606 AQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAAracEMME-KPLALEGYTGER 684
Cdd:cd07124 83 PTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAR---EMLRlRGFPVEMVPGED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 685 NELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAA 764
Cdd:cd07124 160 NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 765 LVADPRIKAVMFTGSTDTANRINQtLAARSGE----IVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSAL 840
Cdd:cd07124 240 LVEHPDVRFIAFTGSREVGLRIYE-RAAKVQPgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSAC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 841 RVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPSACNNGYFFAPA 920
Cdd:cd07124 319 SRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 921 AFEI--PSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVV 998
Cdd:cd07124 399 IFADvpPDHRLAQEEIFGPVLAVIKA--KDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALV 476
|
490 500 510
....*....|....*....|....*....|...
gi 1606703614 999 GLQPFGGEGLSGTGPKAGGPHYLHRLCIERTFT 1031
Cdd:cd07124 477 GRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVT 509
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
562-1034 |
4.68e-139 |
|
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: 426.85 E-value: 4.68e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 562 DGR---AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALA 638
Cdd:COG1012 11 GGEwvaAASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 639 SLEAGKTLADGVAEVREAVDFCRYYAARAcEMMEKPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVT 718
Cdd:COG1012 90 TLETGKPLAEARGEVDRAADFLRYYAGEA-RRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 719 GNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIV 798
Cdd:COG1012 169 GNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN---LK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 799 PLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGP 878
Cdd:COG1012 246 RVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 879 VIDKDALAVLQAHVAKMREAH-TLIYQCELPSAcNNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFnrKDLDAVIDA 955
Cdd:COG1012 326 LISEAQLERVLAYIEDAVAEGaELLTGGRRPDG-EGGYFVEPTVLADvtPDMRIAREEIFGPVLSVIPF--DDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1606703614 956 INATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGlQPFGGEGLSGTGPKaGGPHYLHRLCIERTFTVDT 1034
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGRE-GGREGLEEYTETKTVTIRL 479
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
189-485 |
3.18e-138 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 417.28 E-value: 3.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 189 ALNRARKKEALGYRYSYDMLGEAALTAVDAARYLEAYMDAIDSIGAQvKGKGDVYTNPGISIKLSALHPRYQESQYESVM 268
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKA-AGPWPLGPRPGISVKLSALHPRYEPLERERVM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 269 ATLPDNLLALCLRAKAANIGLTIDAEESERLEISLDVIEKVFKNPALNGWNGFGMAVQSYQKRAFYLLDWVAGLARGQNR 348
Cdd:pfam01619 80 AELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 349 RMNVRLIKGAYWDSEIKKAQmQGLTEYPVFTRKVFTDVSFQACAKKILTMTDTIYPQFATHNACSVATILEMCG----SY 424
Cdd:pfam01619 160 PLGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEelgiPP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606703614 425 RDFEFQCLHGMGNELYAEIVpanRLGIPCRIYAPVGTHEDLLPYLVRRLLENGANSSFVNR 485
Cdd:pfam01619 239 RRFEFQQLYGMGDNLSFALV---AAGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
564-1022 |
1.83e-130 |
|
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: 403.45 E-value: 1.83e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAG 643
Cdd:pfam00171 2 VDSESETIEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 644 KTLADGVAEVREAVDFCRYYAArACEMMEkPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVI 723
Cdd:pfam00171 81 KPLAEARGEVDRAIDVLRYYAG-LARRLD-GETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 724 AKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAE 803
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN---LKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 804 TGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKD 883
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 884 ALAVLQAHVAKMREAHtliYQCEL--PSACNNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINAT 959
Cdd:pfam00171 316 QLERVLKYVEDAKEEG---AKLLTggEAGLDNGYFVEPTVLANvtPDMRIAQEEIFGPVLSVIRF--KDEEEAIEIANDT 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1606703614 960 GYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLqPFGGEGLSGTGpKAGGPHYLH 1022
Cdd:pfam00171 391 EYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLE 451
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
597-1032 |
6.64e-125 |
|
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: 388.10 E-value: 6.64e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 597 ALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARAcEMMEKPLA 676
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLA-RRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 677 LEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPG 756
Cdd:cd07078 82 PSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 757 KGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQR 836
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEN---LKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 837 CSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAH-TLIYQCELPSAcNNGY 915
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEG-GKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 916 FFAPAAFEI--PSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNM 993
Cdd:cd07078 318 FVPPTVLTDvdPDMPIAQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 1606703614 994 IGAVVGlQPFGGEGLSGTGpKAGGPHYLHRLCIERTFTV 1032
Cdd:cd07078 396 VGAEPS-APFGGVKQSGIG-REGGPYGLEEYTEPKTVTI 432
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
575-1031 |
5.58e-114 |
|
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: 362.26 E-value: 5.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 575 SPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVR 654
Cdd:TIGR01237 52 NPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 655 EAVDFCRYYAAracEMMEkpLALEGYT----GERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQT 730
Cdd:TIGR01237 132 EAIDFMEYYAR---QMIE--LAKGKPVnsreGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 731 PLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLA-ARSGE--IVPLIAETGGL 807
Cdd:TIGR01237 207 PVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkVQPGQkhLKRVIAEMGGK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 808 NAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAV 887
Cdd:TIGR01237 287 DTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNK 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 888 LQAHVAKMR-EAHTLIYQCELPSacnNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLT 964
Cdd:TIGR01237 367 IMEYIEIGKaEGRLVSGGCGDDS---KGYFIGPTIFAdvDRKARLAQEEIFGPVVAFIRA--SDFDEALEIANNTEYGLT 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1606703614 965 LGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYLHRLCIERTFT 1031
Cdd:TIGR01237 442 GGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVT 508
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
570-1021 |
1.95e-113 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 360.79 E-value: 1.95e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 570 EVSVTSPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADG 649
Cdd:PRK03137 51 KIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 650 VAEVREAVDFCRYYAAracEMME--KPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPA 727
Cdd:PRK03137 131 DADTAEAIDFLEYYAR---QMLKlaDGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 728 EQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQtlaaRSGEIVP-------L 800
Cdd:PRK03137 208 SDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE----RAAKVQPgqiwlkrV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 801 IAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDtDVGPVI 880
Cdd:PRK03137 284 IAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPVI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 881 DKDALAVLQAHVAKMREAHTLIYQCElpSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINA 958
Cdd:PRK03137 363 NQASFDKIMSYIEIGKEEGRLVLGGE--GDDSKGYFIQPTIFAdvDPKARIMQEEIFGPVVAFIKA--KDFDHALEIANN 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1606703614 959 TGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYL 1021
Cdd:PRK03137 439 TEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYL 501
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
600-1032 |
1.72e-98 |
|
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: 315.71 E-value: 1.72e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 600 RAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARACEMMEKPLALEG 679
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 680 yTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGE 759
Cdd:cd06534 82 -PGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 760 TVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSA 839
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAEN---LKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 840 LRVVHVQDEVYPRFMALLKgamaelrvgmperfdtdvgpvidkdalavlqahvakmreahTLIYQCElpsacnngyffap 919
Cdd:cd06534 238 ASRLLVHESIYDEFVEKLV-----------------------------------------TVLVDVD------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 920 aafeiPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVG 999
Cdd:cd06534 264 -----PDMPIAQEEIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE 336
|
410 420 430
....*....|....*....|....*....|...
gi 1606703614 1000 lQPFGGEGLSGTGpKAGGPHYLHRLCIERTFTV 1032
Cdd:cd06534 337 -APFGGVKNSGIG-REGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
564-1033 |
4.70e-97 |
|
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: 315.66 E-value: 4.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAG 643
Cdd:cd07086 8 VGSGGETFTSRNPAN-GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 644 KTLADGVAEVREAVDFCrYYAARACEMmekplaLEGYT--GERNELSL----HPRGTVLCISPWNFPLAIFTGQAVAALV 717
Cdd:cd07086 87 KILPEGLGEVQEMIDIC-DYAVGLSRM------LYGLTipSERPGHRLmeqwNPLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 718 TGNAVIAKPAEQTPLIAAFAVRLMREA----GVLPSVMQLLPGKGEtVGAALVADPRIKAVMFTGSTDTANRINQTLAAR 793
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 794 SGeivPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFD 873
Cdd:cd07086 239 FG---RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 874 TDVGPVIDKDALAVLQAHVAKMREAH-TLIYQCELPSACNNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFnrKDLD 950
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGgTVLTGGKRIDGGEPGNYVEPTIVTGvtDDARIVQEETFAPILYVIKF--DSLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 951 AVIDAINATGYGLTLGIHSRINETVERI--HKRMKVGNCYVNRNMIGAVVGLqPFGGEGLSGTGPKAGG---PHYLHRlc 1025
Cdd:cd07086 394 EAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESGSdawKQYMRR-- 470
|
....*...
gi 1606703614 1026 ieRTFTVD 1033
Cdd:cd07086 471 --STCTIN 476
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
573-1019 |
3.33e-92 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 302.63 E-value: 3.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 573 VTSPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAE 652
Cdd:cd07097 18 NRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 653 VREAVDFCRYYAARAcemmekpLALEGYT------GERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKP 726
Cdd:cd07097 98 VTRAGQIFRYYAGEA-------LRLSGETlpstrpGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 727 AEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIVpliAETGG 806
Cdd:cd07097 171 AELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQ---LEMGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 807 LNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALA 886
Cdd:cd07097 248 KNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 887 VLQAHVAKMR-EAHTLIYQCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGL 963
Cdd:cd07097 328 KDLRYIEIARsEGAKLVYGGERLKRPDEGYYLAPALFAgvTNDMRIAREEIFGPVAAVIRV--RDYDEALAIANDTEFGL 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606703614 964 TLGIHSR----INETVERIhkrmKVGNCYVNRNMIGavVGLQ-PFGGEGLSGTGPKAGGPH 1019
Cdd:cd07097 406 SAGIVTTslkhATHFKRRV----EAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEA 460
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
576-1018 |
8.80e-88 |
|
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: 290.79 E-value: 8.80e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 576 PQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVRE 655
Cdd:cd07131 21 PADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 656 AVDFCRYYAARA---------CEMMEKplalEGYTGERnelslhPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKP 726
Cdd:cd07131 101 AIDMAQYAAGEGrrlfgetvpSELPNK----DAMTRRQ------PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 727 AEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTlAARSGEIVPLiaETGG 806
Cdd:cd07131 171 AEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGET-CARPNKRVAL--EMGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 807 LNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALA 886
Cdd:cd07131 248 KNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 887 VLQAHVA-KMREAHTLIYQCELPSACN--NGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGY 961
Cdd:cd07131 328 KVLNYNEiGKEEGATLLLGGERLTGGGyeKGYFVEPTVFTDvtPDMRIAQEEIFGPVVALIEV--SSLEEAIEIANDTEY 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1606703614 962 GLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLqPFGGEGLSGTGPKAGGP 1018
Cdd:cd07131 406 GLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
581-1032 |
8.24e-85 |
|
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: 281.80 E-value: 8.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:cd07099 7 EVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEMMEKPLALEG--YTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAV 738
Cdd:cd07099 87 DWAARNAPRVLAPRKVPTGllMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 739 RLMREAGVLPSVMQLLPGKGETvGAALVaDPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAETGGLNAMIVDSSALL 818
Cdd:cd07099 167 EAWAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGSVATGRKVMAAAAER---LIPVVLELGGKDPMIVLADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 819 EQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHV--AKMR 896
Cdd:cd07099 242 ERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVddAVAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 897 EAHTLiyqCELPSACNNGYFFAPAAF--EIPSIRVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHSRINET 974
Cdd:cd07099 322 GAKAL---TGGARSNGGGPFYEPTVLtdVPHDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1606703614 975 VERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGpKAGGPHYLHRLCIERTFTV 1032
Cdd:cd07099 397 AEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
581-1022 |
1.19e-84 |
|
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: 281.38 E-value: 1.19e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEV--REAVD 658
Cdd:cd07093 8 EVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDipRAAAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 659 FcRYYA----ARACEMMEKPlalegyTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIA 734
Cdd:cd07093 88 F-RFFAdyilQLDGESYPQD------GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 735 AFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAETGGLNAMIVDS 814
Cdd:cd07093 161 WLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN---LKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 815 SALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAK 894
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 895 MR-EAHTLIYQCELP--SACNNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHS 969
Cdd:cd07093 318 ARaEGATILTGGGRPelPDLEGGYFVEPTVITGldNDSRVAQEEIFGPVVTVIPFD--DEEEAIELANDTPYGLAAYVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1606703614 970 RINETVERIHKRMKVGNCYVNRNMigaVVGL-QPFGGEGLSGTGpKAGGPHYLH 1022
Cdd:cd07093 396 RDLGRAHRVARRLEAGTVWVNCWL---VRDLrTPFGGVKASGIG-REGGDYSLE 445
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
573-1022 |
3.16e-84 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 280.09 E-value: 3.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 573 VTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAE 652
Cdd:cd07103 1 VINPAT-GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 653 VREAVDFCRYYAARAcemmekpLALEGYT------GERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKP 726
Cdd:cd07103 80 VDYAASFLEWFAEEA-------RRIYGRTipspapGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 727 AEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTdtanRINQTLAARSGE-IVPLIAETG 805
Cdd:cd07103 153 AEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGST----AVGKLLMAQAADtVKRVSLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 806 GLNAMIVDSSALLEQVVNDVLVSAFGSAGQRC-SALRvVHVQDEVYPRFMALLKGAMAELRVG--MPErfDTDVGPVIDK 882
Cdd:cd07103 229 GNAPFIVFDDADLDKAVDGAIASKFRNAGQTCvCANR-IYVHESIYDEFVEKLVERVKKLKVGngLDE--GTDMGPLINE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 883 DALAVLQAHVAKMREA-HTLIYQCELPSacNNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINAT 959
Cdd:cd07103 306 RAVEKVEALVEDAVAKgAKVLTGGKRLG--LGGYFYEPTVLTDvtDDMLIMNEETFGPVAPIIPF--DTEDEVIARANDT 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1606703614 960 GYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVglQPFGGEGLSGTGpKAGGPHYLH 1022
Cdd:cd07103 382 PYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLG-REGGKEGLE 441
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
564-991 |
2.67e-82 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 275.60 E-value: 2.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRA-VEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEA 642
Cdd:cd07082 11 KESSGKTIEVYSPID-GEVIGSVPALSALEILEAAETAyDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 643 GKTLADGVAEVREAVDFCRYYAARACEMMEKPLALEGYTGERNELSL---HPRGTVLCISPWNFPLAIFTGQAVAALVTG 719
Cdd:cd07082 90 GKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQvrrEPLGVVLAIGPFNYPLNLTVSKLIPALIMG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 720 NAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInqtlaARSGEIVP 799
Cdd:cd07082 170 NTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL-----KKQHPMKR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 800 LIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPV 879
Cdd:cd07082 245 LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 880 IDKDALAVLQ-------AHVAKM-----REAHTLIYqcelpsacnngyffaPAAFEI--PSIRVLEKEVFGPILHVVRFN 945
Cdd:cd07082 325 IDPKSADFVEgliddavAKGATVlngggREGGNLIY---------------PTLLDPvtPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1606703614 946 rkDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNR 991
Cdd:cd07082 390 --DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS 433
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
575-1030 |
3.65e-82 |
|
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: 276.78 E-value: 3.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 575 SPQNYRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEA-HMPDFLALASLEAGKTL----ADG 649
Cdd:cd07123 52 MPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGkYRYELNAATMLGQGKNVwqaeIDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 650 VAEVreaVDFCRYYAARACEM-MEKPLalEGYTGERNELSLHP-RGTVLCISPWNFPlAIFTGQAVAALVTGNAVIAKPA 727
Cdd:cd07123 132 ACEL---IDFLRFNVKYAEELyAQQPL--SSPAGVWNRLEYRPlEGFVYAVSPFNFT-AIGGNLAGAPALMGNVVLWKPS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 728 EQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIV--P-LIAET 804
Cdd:cd07123 206 DTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRtyPrIVGET 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 805 GGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDA 884
Cdd:cd07123 286 GGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 885 LAVLQAHV--AKMREAHTLIYQCElpsaCNN--GYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFNRKDLDAVIDAINA 958
Cdd:cd07123 366 FDRIKGYIdhAKSDPEAEIIAGGK----CDDsvGYFVEPTVIETtdPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDT 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 959 TG-YGLTLGIHSR----INETVERIhkRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYLHR----LCIERT 1029
Cdd:cd07123 442 TSpYALTGAIFAQdrkaIREATDAL--RNAAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRwvspRTIKET 519
|
.
gi 1606703614 1030 F 1030
Cdd:cd07123 520 F 520
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
562-1022 |
3.66e-81 |
|
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: 272.22 E-value: 3.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 562 DGR---AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALA 638
Cdd:cd07088 3 NGEfvpSSSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 639 SLEAGKTLADGVAEVREAVDFCRYYA--ARACE--MMEKPLAlegytGERNELSLHPRGTVLCISPWNFPLAIFTGQAVA 714
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAewARRIEgeIIPSDRP-----NENIFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 715 ALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInqtLAARS 794
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKI---MEAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 795 GEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDT 874
Cdd:cd07088 234 ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 875 DVGPVIDKDALAVLQAHVAKMREA-HTLIYQCELPSAcNNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFNrkDLDA 951
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAgATLLTGGKRPEG-EKGYFYEPTVLTNvrQDMEIVQEEIFGPVLPVVKFS--SLDE 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606703614 952 VIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQpfGGEGLSGTGpKAGGPHYLH 1022
Cdd:cd07088 391 AIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLG-GADGKHGLE 458
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
573-1012 |
1.15e-77 |
|
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: 262.15 E-value: 1.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 573 VTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAE 652
Cdd:cd07149 3 VISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 653 VREAVDFCRYYAARACEMMEKPLALEGYTGERNELSLH---PRGTVLCISPWNFPL---AIFTGQAVAAlvtGNAVIAKP 726
Cdd:cd07149 82 VDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTirePIGVVAAITPFNFPLnlvAHKVGPAIAA---GNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 727 AEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInqtlaARSGEIVPLIAETGG 806
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI-----ARKAGLKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 807 LNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALA 886
Cdd:cd07149 234 NAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 887 VLQAHVAK-MREAHTLIYQCElpsacNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGL 963
Cdd:cd07149 314 RIEEWVEEaVEGGARLLTGGK-----RDGAILEPTVLTdvPPDMKVVCEEVFAPVVSLNPF--DTLDEAIAMANDSPYGL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1606703614 964 TLGIHSRINETVERIHKRMKVGNCYVN-----RnmigavVGLQPFGGEGLSGTG 1012
Cdd:cd07149 387 QAGVFTNDLQKALKAARELEVGGVMINdsstfR------VDHMPYGGVKESGTG 434
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
581-1016 |
1.82e-77 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 261.72 E-value: 1.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEwalsRAVEGAAQ------WERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVR 654
Cdd:cd07114 8 EPWARVPEASAADVD----RAVAAARAafeggaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 655 EAVDFCRYYAARAcemmekpLALEGYTGERNELSLH------PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAE 728
Cdd:cd07114 84 YLAEWYRYYAGLA-------DKIEGAVIPVDKGDYLnftrrePLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 729 QTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAETGGLN 808
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN---LAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 809 AMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVL 888
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 889 QAHVAKMREA-HTLIYQCELPS--ACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGL 963
Cdd:cd07114 314 ERYVARAREEgARVLTGGERPSgaDLGAGYFFEPTILAdvTNDMRIAQEEVFGPVLSVIPF--DDEEEAIALANDSEYGL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1606703614 964 TLGIHSRINETVERIHKRMKVGNCYVnrNMIGAVVGLQPFGGEGLSGTGPKAG 1016
Cdd:cd07114 392 AAGIWTRDLARAHRVARAIEAGTVWV--NTYRALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
581-1012 |
1.90e-77 |
|
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: 261.31 E-value: 1.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:cd07106 8 EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEmmekPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRL 740
Cdd:cd07106 88 RYTASLDLP----DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 741 MREagVLPS-VMQLLPGKGEtVGAALVADPRIKAVMFTGSTDTANRInqtLAARSGEIVPLIAETGGLNAMIVDSSALLE 819
Cdd:cd07106 164 AQE--VLPPgVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKV---MASAAKTLKRVTLELGGNDAAIVLPDVDID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 820 QVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAH 899
Cdd:cd07106 238 AVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 900 TLIYQCELPsACNNGYFFAPAafeI-----PSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINET 974
Cdd:cd07106 318 AKVLAGGEP-LDGPGYFIPPT---IvddppEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430
....*....|....*....|....*....|....*...
gi 1606703614 975 VERIHKRMKVGNCYVNRnmIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07106 392 AEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
581-1016 |
2.80e-77 |
|
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: 261.09 E-value: 2.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEMME---KPLALEGYTgeRNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFA 737
Cdd:cd07101 87 RYYARRAERLLKprrRRGAIPVLT--RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 738 VRLMREAGVLPSVMQLLPGKGETVGAALVAdpRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAETGGLNAMIVDSSAL 817
Cdd:cd07101 165 VELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRR---LIGCSLELGGKNPMIVLEDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 818 LEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMRE 897
Cdd:cd07101 240 LDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 898 AHTLIYQCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETV 975
Cdd:cd07101 320 KGATVLAGGRARPDLGPYFYEPTVLTgvTEDMELFAEETFGPVVSIYRV--ADDDEAIELANDTDYGLNASVWTRDGARG 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1606703614 976 ERIHKRMKVGNCYVNRNMIGAVVGLQ-PFGGEGLSGTGPKAG 1016
Cdd:cd07101 398 RRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
567-1016 |
3.73e-75 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 255.98 E-value: 3.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 567 SGVEVSVTSPQNyRETIGRVIEASKEDVEwalsRAVEGA------AQWERVPVAERAAVINRYADLLEAHMPDFLALASL 640
Cdd:cd07091 17 SGKTFPTINPAT-EEVICQVAEADEEDVD----AAVKAAraafetGWWRKMDPRERGRLLNKLADLIERDRDELAALESL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 641 EAGKTLADG-VAEVREAVDFCRYYAARACEMMEKPLALEG----YTgeRNElslhPRGTVLCISPWNFPLAIFTGQAVAA 715
Cdd:cd07091 92 DNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIPIDGnflaYT--RRE----PIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 716 LVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSG 795
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 796 EIVPLiaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTD 875
Cdd:cd07091 246 KKVTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 876 VGPVIDKDALAVLQAHVAK-MREAHTLIYQCELPSacNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAV 952
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESgKKEGATLLTGGERHG--SKGYFIQPTVFTdvKDDMKIAKEEIFGPVVTILKF--KTEDEV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1606703614 953 IDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNR-NMIGAVVglqPFGGEGLSGTGPKAG 1016
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
566-1023 |
5.84e-75 |
|
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: 255.59 E-value: 5.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 566 GSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKT 645
Cdd:cd07130 9 GGGGVVTSISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 646 LADGVAEVREAVDFCRYyAARACEMmekplaLEGYT--GERNELSL----HPRGTVLCISPWNFPLAIFTGQAVAALVTG 719
Cdd:cd07130 88 LPEGLGEVQEMIDICDF-AVGLSRQ------LYGLTipSERPGHRMmeqwNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 720 NAVIAKPAEQTPLIAAFAVRLMREA----GVLPSVMQLLPGKGEtVGAALVADPRIKAVMFTGSTDTANRINQTLAARSG 795
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 796 EIvplIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTD 875
Cdd:cd07130 240 RS---LLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 876 VGPVIDKDALAVLQAHVAKMREAH-TLIYQCELPSacNNGYFFAPAAFEIPS-IRVLEKEVFGPILHVVRFnrKDLDAVI 953
Cdd:cd07130 317 VGPLHTKAAVDNYLAAIEEAKSQGgTVLFGGKVID--GPGNYVEPTIVEGLSdAPIVKEETFAPILYVLKF--DTLEEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1606703614 954 DAINATGYGLTLGIHSRINETVERI--HKRMKVGNCYVNRNMIGAVVGlQPFGGEGLSGTGPKAGG---PHYLHR 1023
Cdd:cd07130 393 AWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGSdawKQYMRR 466
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
565-1012 |
3.78e-73 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 252.11 E-value: 3.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 565 AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGK 644
Cdd:PRK09407 28 GAAGPTREVTAPFT-GEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 645 TLADGVAEVREAVDFCRYYAARACEMME---KPLALEGYTgeRNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNA 721
Cdd:PRK09407 107 ARRHAFEEVLDVALTARYYARRAPKLLAprrRAGALPVLT--KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 722 VIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVAdpRIKAVMFTGSTDTANRINQTLAARsgeivpLI 801
Cdd:PRK09407 185 VVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAGRR------LI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 802 ---AETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGP 878
Cdd:PRK09407 257 gfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 879 VIDKDALAVLQAHVAKMREA-HTLIYqcelpsacnnG---------YFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnr 946
Cdd:PRK09407 337 LISEAQLETVSAHVDDAVAKgATVLA----------GgkarpdlgpLFYEPTVLTgvTPDMELAREETFGPVVSVYPV-- 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1606703614 947 KDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQ-PFGGEGLSGTG 1012
Cdd:PRK09407 405 ADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
593-1010 |
3.97e-72 |
|
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: 246.03 E-value: 3.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 593 DVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVreavdfcryyAARACEMME 672
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEV----------AAMAGKIDI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 673 KPLALEGYTGERNE--------LSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREA 744
Cdd:cd07095 71 SIKAYHERTGERATpmaqgravLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 745 GVLPSVMQLLPGKGETvGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIVPLiaETGGLNAMIVDSSALLEQVVND 824
Cdd:cd07095 151 GLPPGVLNLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILAL--EMGGNNPLVVWDVADIDAAAYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 825 VLVSAFGSAGQRCS-ALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALA-VLQAHVAKMREAHTLI 902
Cdd:cd07095 228 IVQSAFLTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAArYLLAQQDLLALGGEPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 903 YQCELPSAcnNGYFFAPAAFEIPSIRVL-EKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHSRINETVERIHKR 981
Cdd:cd07095 308 LAMERLVA--GTAFLSPGIIDVTDAADVpDEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDDEALFERFLAR 383
|
410 420
....*....|....*....|....*....
gi 1606703614 982 MKVGNCYVNRNMIGAvVGLQPFGGEGLSG 1010
Cdd:cd07095 384 IRAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
565-1016 |
4.46e-72 |
|
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: 247.41 E-value: 4.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 565 AGSGVEVSVTSPQNyRETIGRVIEASKEDVEwalsRAVEGAAQ------WERVPVAERAAVINRYADLLEAHMPDFLALA 638
Cdd:cd07142 15 AASGKTFPTIDPRN-GEVIAHVAEGDAEDVD----RAVKAARKafdegpWPRMTGYERSRILLRFADLLEKHADELAALE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 639 SLEAGKTLADG-VAEVREAVDFCRYYAARACEMMEKPLALEG----YTgernelsLH-PRGTVLCISPWNFPLAIFTGQA 712
Cdd:cd07142 90 TWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGphhvYT-------LHePIGVVGQIIPWNFPLLMFAWKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 713 VAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQtLAA 792
Cdd:cd07142 163 GPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ-LAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 793 RSgEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERF 872
Cdd:cd07142 242 KS-NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 873 DTDVGPVIDKDALA-VLQAHVAKMREAHTLIyqCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDL 949
Cdd:cd07142 321 GVEQGPQVDKEQFEkILSYIEHGKEEGATLI--TGGDRIGSKGYYIQPTIFSdvKDDMKIARDEIFGPVQSILKF--KTV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1606703614 950 DAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVN-RNMIGAVVglqPFGGEGLSGTGPKAG 1016
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
580-1016 |
2.21e-71 |
|
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: 244.66 E-value: 2.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 580 RETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGV-AEVREAVD 658
Cdd:cd07115 7 GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLDVPRAAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 659 FCRYYAARACEMMEKPLALEGytGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAV 738
Cdd:cd07115 87 TFRYYAGWADKIEGEVIPVRG--PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 739 RLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQtlaARSGEIVPLIAETGGLNAMIVDSSALL 818
Cdd:cd07115 165 ELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQ---GAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 819 EQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMR-E 897
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGReE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 898 AHTLIYQCELPSAcnNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFnRKDLDAVIDAiNATGYGLTLGIHSRINETV 975
Cdd:cd07115 322 GARLLTGGKRPGA--RGFFVEPTIFAAvpPEMRIAQEEIFGPVVSVMRF-RDEEEALRIA-NGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1606703614 976 ERIHKRMKVGNCYVnrNMIGAVVGLQPFGGEGLSGTGPKAG 1016
Cdd:cd07115 398 HRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
571-1012 |
2.40e-71 |
|
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: 244.95 E-value: 2.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 571 VSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGV 650
Cdd:cd07145 1 IEVRNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 651 AEVREAVDFCRYYAARACEMMEKPLALEGYTGERNELSL---HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPA 727
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFtvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 728 EQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTlAARSGEIVplIAETGGL 807
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASK-AGGTGKKV--ALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 808 NAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAV 887
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 888 LQAHVAK-MREAHTLIYQCELPsacnNGYFFAPAAFEIPSI--RVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLT 964
Cdd:cd07145 317 MENLVNDaVEKGGKILYGGKRD----EGSFFPPTVLENDTPdmIVMKEEVFGPVLPIAKV--KDDEEAVEIANSTEYGLQ 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1606703614 965 LGIHSR-INETVeRIHKRMKVGNCYVNR-------NMigavvglqPFGGEGLSGTG 1012
Cdd:cd07145 391 ASVFTNdINRAL-KVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG 437
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
581-1012 |
7.14e-71 |
|
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: 243.30 E-value: 7.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWE-RVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDF 659
Cdd:cd07109 8 EVFARIARGGAADVDRAVQAARRAFESGWlRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 660 CRYYAARACEMMEKPLALE-GYTGerneLSLH-PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFA 737
Cdd:cd07109 88 FEYYGGAADKLHGETIPLGpGYFV----YTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 738 VRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAETGGLNAMIVDSSAL 817
Cdd:cd07109 164 AELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN---VVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 818 LEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERfDTDVGPVIDKDALAVLQAHV--AKM 895
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVarARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 896 REAHTLIYQCELPSACNNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINE 973
Cdd:cd07109 320 RGARIVAGGRIAEGAPAGGYFVAPTLLDDvpPDSRLAQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 1606703614 974 TVERIHKRMKVGNCYVNRNMIGAVVGLqPFGGEGLSGTG 1012
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAGGGIEL-PFGGVKKSGHG 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
573-1012 |
1.26e-70 |
|
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: 242.72 E-value: 1.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 573 VTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAE 652
Cdd:cd07094 3 VHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 653 VREAVDFCRYYAARACEMMEKPLALEGYTGERNELSL---HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQ 729
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 730 TPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInqtlAARSGeIVPLIAETGGLNA 809
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL----RANAG-GKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 810 MIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQ 889
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 890 AHVAK-MREAHTLIYQCELpsacnNGYFFAPAAFEIPSI--RVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLG 966
Cdd:cd07094 317 RWVEEaVEAGARLLCGGER-----DGALFKPTVLEDVPRdtKLSTEETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1606703614 967 IHSR-INETVErIHKRMKVGNCYVNRNMIgAVVGLQPFGGEGLSGTG 1012
Cdd:cd07094 390 IFTRdLNVAFK-AAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
581-1012 |
1.44e-70 |
|
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: 243.19 E-value: 1.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVR---EAV 657
Cdd:cd07085 27 EVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLrglEVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 658 DFcryyaarACEMmekPLALEGYTGE--RNELSLH----PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTP 731
Cdd:cd07085 107 EF-------ACSI---PHLLKGEYLEnvARGIDTYsyrqPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 732 LIAAFAVRLMREAGVLPSVMQLLPGKGETVGAaLVADPRIKAVMFTGSTDTANRINQTlAARSGEIVplIAETGGLNAMI 811
Cdd:cd07085 177 GAAMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYER-AAANGKRV--QALGGAKNHAV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 812 VDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAH 891
Cdd:cd07085 253 VMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 892 VAK-MREAHTLIyqceL------PSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYG 962
Cdd:cd07085 333 IESgVEEGAKLV----LdgrgvkVPGYENGNFVGPTILDnvTPDMKIYKEEIFGPVLSIVRV--DTLDEAIAIINANPYG 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1606703614 963 LTLGIHSRINETVERIHKRMKVGNCYVNrnmIG-AV-VGLQPFGGEGLSGTG 1012
Cdd:cd07085 407 NGAAIFTRSGAAARKFQREVDAGMVGIN---VPiPVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
581-1016 |
1.39e-69 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 239.57 E-value: 1.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRViEASKEDvewALSRAVEGAA-QWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDF 659
Cdd:cd07146 10 EVVGTV-PAGTEE---ALREALALAAsYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 660 CRYYAARACEMMEKPLALEGYT--GERNELSL-HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAF 736
Cdd:cd07146 86 LRFAAAEALRDDGESFSCDLTAngKARKIFTLrEPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 737 AVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSgeivpLIAETGGLNAMIVDSSA 816
Cdd:cd07146 166 LADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKR-----QLLELGGNDPLIVMDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 817 LLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMR 896
Cdd:cd07146 241 DLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 897 EAHTLIyqceLPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINET 974
Cdd:cd07146 321 AQGARV----LLGNQRQGALYAPTVLDhvPPDAELVTEETFGPVAPVIRV--KDLDEAIAISNSTAYGLSSGVCTNDLDT 394
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1606703614 975 VERIHKRMKVGNCYVNrNMIGAVVGLQPFGGEGLSGTGPKAG 1016
Cdd:cd07146 395 IKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
593-1022 |
5.69e-69 |
|
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: 237.43 E-value: 5.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 593 DVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRyyaaracEMME 672
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILR-------EAAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 673 KPLALEG------YTGERNELSLHPRGTVLCISPWNFPLaIFTGQAVA-ALVTGNAVIAKPAEQTPLIAAFAV-RLMREA 744
Cdd:cd07104 74 LPRRPEGeilpsdVPGKESMVRRVPLGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKPDSRTPVTGGLLIaEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 745 GVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQtLAARSGEIVPLiaETGGLNAMIVDSSALLEQVVND 824
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGE-LAGRHLKKVAL--ELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 825 VLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIyq 904
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARL-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 905 ceLPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRM 982
Cdd:cd07104 308 --LTGGTYEGLFYQPTVLSdvTPDMPIFREEIFGPVAPVIPF--DDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERL 383
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1606703614 983 KVGNCYVNRNMI--GAVVglqPFGGEGLSGTGpKAGGPHYLH 1022
Cdd:cd07104 384 ETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGPASLE 421
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
594-1012 |
1.06e-68 |
|
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: 236.59 E-value: 1.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 594 VEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARACEMME- 672
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 673 KPLALEgytGERNELSLHPRGTVLCISPWNFPL---AIFtgqAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPS 749
Cdd:cd07100 81 EPIETD---AGKAYVRYEPLGVVLGIMPWNFPFwqvFRF---AAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 750 VMQLLPGKGETVgAALVADPRIKAVMFTGSTdtanRINQTLAARSGE-IVPLIAETGGLNAMIVDSSALLEQVVNDVLVS 828
Cdd:cd07100 155 VFQNLLIDSDQV-EAIIADPRVRGVTLTGSE----RAGRAVAAEAGKnLKKSVLELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 829 AFGSAGQRC-SALRVVhVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREA-HTLIYQCE 906
Cdd:cd07100 230 RLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAgATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 907 LPSAcnNGYFFAPA--AFEIPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKV 984
Cdd:cd07100 309 RPDG--PGAFYPPTvlTDVTPGMPAYDEELFGPVAAVIKV--KDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEA 384
|
410 420
....*....|....*....|....*...
gi 1606703614 985 GNCYVNRnMIGAVVGLqPFGGEGLSGTG 1012
Cdd:cd07100 385 GMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
573-1012 |
3.00e-67 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 233.42 E-value: 3.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 573 VTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAE 652
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 653 VREAVDFCRYYAARACEMMEKPLAlegYTGERNELSLH-PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTP 731
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIP---VGGRNLHYTLRePYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 732 LIAAFAVRLMREagVLP-SVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInQTLAARSgeIVPLIAETGGLNAM 810
Cdd:cd07107 157 LSALRLAELARE--VLPpGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAI-MRAAAEG--IKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 811 IVDSSALLEQVVnDVLVSA--FGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALA-V 887
Cdd:cd07107 232 IVFPDADPEAAA-DAAVAGmnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDrV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 888 LQAHVAKMREAHTLIYQCELPS--ACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGL 963
Cdd:cd07107 311 MHYIDSAKREGARLVTGGGRPEgpALEGGFYVEPTVFAdvTPGMRIAREEIFGPVLSVLRW--RDEAEMVAQANGVEYGL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1606703614 964 TLGIHSRINETVERIHKRMKVGNCYVN---RNMIGAvvglqPFGGEGLSGTG 1012
Cdd:cd07107 389 TAAIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
581-1018 |
4.22e-66 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 229.87 E-value: 4.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEMMEKPLAlegytGERNELSLH---PRGTVLCISPWNFPLaIFTGQAVA-ALVTGNAVIAKPAEQTPLIAAF 736
Cdd:cd07152 82 HEAAGLPTQPQGEILP-----SAPGRLSLArrvPLGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKPDPRTPVSGGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 737 AV-RLMREAGVLPSVMQLLPGKGEtVGAALVADPRIKAVMFTGSTDTANRINQtLAARSGEIVPLiaETGGLNAMIVDSS 815
Cdd:cd07152 156 VIaRLFEEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGE-AAGRHLKKVSL--ELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 816 ALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKM 895
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 896 REAHTLIyqceLPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINE 973
Cdd:cd07152 312 VAAGARL----EAGGTYDGLFYRPTVLSgvKPGMPAFDEEIFGPVAPVTVF--DSDEEAVALANDTEYGLSAGIISRDVG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1606703614 974 TVERIHKRMKVGNCYVNRNMIGAVVgLQPFGGEGLSGTGPKAGGP 1018
Cdd:cd07152 386 RAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
565-1022 |
5.07e-66 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 231.12 E-value: 5.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 565 AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGK 644
Cdd:PLN02278 36 AYDGKTFPVYNPAT-GEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 645 TLADGVAEVREAVDFCRYYAARA----CEMMEKPLAlegytgERNELSLH-PRGTVLCISPWNFPLAIFTGQAVAALVTG 719
Cdd:PLN02278 115 PLKEAIGEVAYGASFLEYFAEEAkrvyGDIIPSPFP------DRRLLVLKqPVGVVGAITPWNFPLAMITRKVGPALAAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 720 NAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTdtanRINQTLAARSGEIVP 799
Cdd:PLN02278 189 CTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGST----AVGKKLMAGAAATVK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 800 LIA-ETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRC-SALRVVhVQDEVYPRFMALLKGAMAELRVGMPERFDTDVG 877
Cdd:PLN02278 265 RVSlELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 878 PVIDKDALAVLQAHV-------AKMR---EAHTLiyqcelpsacnNGYFFAPAAF-EIPS-IRVLEKEVFGPILHVVRFN 945
Cdd:PLN02278 344 PLINEAAVQKVESHVqdavskgAKVLlggKRHSL-----------GGTFYEPTVLgDVTEdMLIFREEVFGPVAPLTRFK 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1606703614 946 rKDLDAVIDAiNATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGlqPFGGEGLSGTGpKAGGPHYLH 1022
Cdd:PLN02278 413 -TEEEAIAIA-NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKYGID 484
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
581-1012 |
3.75e-65 |
|
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: 227.62 E-value: 3.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:cd07110 8 ATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEMMEK-----PLALEGYTGERNElslHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAA 735
Cdd:cd07110 88 EYYADLAEQLDAKaeravPLPSEDFKARVRR---EPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 736 FAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAArsgEIVPLIAETGGLNAMIVDSS 815
Cdd:cd07110 165 ELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ---DIKPVSLELGGKSPIIVFDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 816 ALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKM 895
Cdd:cd07110 242 ADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 896 REAH-TLIYQCELPSACNNGYFFAPAAF-EIP-SIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRIN 972
Cdd:cd07110 322 KEEGaRLLCGGRRPAHLEKGYFIAPTVFaDVPtDSRIWREEIFGPVLCVRSF--ATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1606703614 973 ETVERIHKRMKVGNCYVNRNMIgaVVGLQPFGGEGLSGTG 1012
Cdd:cd07110 400 ERCDRVAEALEAGIVWINCSQP--CFPQAPWGGYKRSGIG 437
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
581-1012 |
6.91e-65 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 227.00 E-value: 6.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEwalsRAVEGA----AQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAG--KTLAdGVAEVR 654
Cdd:cd07138 25 EVIGTVPLGTAADVD----RAVAAArrafPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGapITLA-RAAQVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 655 EAVDFCRYYAAracemmekplALEGYTGER---NELSLH-PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQT 730
Cdd:cd07138 100 LGIGHLRAAAD----------ALKDFEFEErrgNSLVVRePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 731 PLIA-AFAvRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTlAARSGEIVPLiaETGGLNA 809
Cdd:cd07138 170 PLSAiILA-EILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA-AADTVKRVAL--ELGGKSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 810 MIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQ 889
Cdd:cd07138 246 NIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 890 AHVAK-MREAHTLIyqC---ELPSACNNGYFFAPAAF--EIPSIRVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGL 963
Cdd:cd07138 326 GYIQKgIEEGARLV--AggpGRPEGLERGYFVKPTVFadVTPDMTIAREEIFGPVLSIIPYD--DEDEAIAIANDTPYGL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1606703614 964 TLGIHSRINETVERIHKRMKVGNCYVNrnmiGAVVGLQ-PFGGEGLSGTG 1012
Cdd:cd07138 402 AGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
564-1012 |
8.91e-65 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 227.19 E-value: 8.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVSVTSPQNyRETIGRVIEASKEDVEWAL--SRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLE 641
Cdd:cd07119 8 EAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIaaARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELARLETLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 642 AGKTLADGVAEVREAVDFCRYYA----ARACEMMEKPLALEGYTgernelsLH-PRGTVLCISPWNFPLAIFTGQAVAAL 716
Cdd:cd07119 87 TGKTLRESEIDIDDVANCFRYYAglatKETGEVYDVPPHVISRT-------VRePVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 717 VTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQtlaARSGE 796
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMR---AAAGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 797 IVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDV 876
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 877 GPVIDKDALAVLQAHV-AKMREAHTLIYQCELPS--ACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDA 951
Cdd:cd07119 317 GPLVSAEHREKVLSYIqLGKEEGARLVCGGKRPTgdELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERF--DTEEE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606703614 952 VIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRnmIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07119 395 AIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
564-1010 |
1.63e-64 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 226.76 E-value: 1.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAG 643
Cdd:PRK09457 10 IAGQGEAFESRNPVS-GEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 644 KTLADGVAEVreavdfcryyAAraceMMEK-PLALEGY---TGERNE--------LSLHPRGTVLCISPWNFPLAIFTGQ 711
Cdd:PRK09457 89 KPLWEAATEV----------TA----MINKiAISIQAYherTGEKRSemadgaavLRHRPHGVVAVFGPYNFPGHLPNGH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 712 AVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETvGAALVADPRIKAVMFTGSTDTANRINQTLA 791
Cdd:PRK09457 155 IVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 792 ARSGEIVPLiaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYP-RFMALLKGAMAELRVGmpe 870
Cdd:PRK09457 234 GQPEKILAL--EMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGdAFLARLVAVAKRLTVG--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 871 RFDTD----VGPVIDKDALAVLQAHVAKMRE--AHTLIyqcELPSACNNGYFFAPAAFEIPSIRVL-EKEVFGPILHVVR 943
Cdd:PRK09457 309 RWDAEpqpfMGAVISEQAAQGLVAAQAQLLAlgGKSLL---EMTQLQAGTGLLTPGIIDVTGVAELpDEEYFGPLLQVVR 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1606703614 944 FNrkDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGncYVNRN--MIGAvVGLQPFGGEGLSG 1010
Cdd:PRK09457 386 YD--DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAG--IVNWNkpLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
581-1022 |
9.76e-64 |
|
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: 223.66 E-value: 9.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWE-RVPVAERAAVINRYADLLEAHMPDFLALASLEAGKT--LADGVAeVREAV 657
Cdd:cd07089 8 EVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmTARAMQ-VDGPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 658 DFCRYYAARAcEMMEKPLALEGyTGERNELSLH-----PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPL 732
Cdd:cd07089 87 GHLRYFADLA-DSFPWEFDLPV-PALRGGPGRRvvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 733 IAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInqtLAARSGEIVPLIAETGGLNAMIV 812
Cdd:cd07089 165 SALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRI---MAQAAATLKRVLLELGGKSANIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 813 DSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHV 892
Cdd:cd07089 242 LDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 893 AKMREA-HTLIYQCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHS 969
Cdd:cd07089 322 ARGRDEgARLVTGGGRPAGLDKGFYVEPTLFAdvDNDMRIAQEEIFGPVLVVIPY--DDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1606703614 970 RINETVERIHKRMKVGNCYVNrnmigAVVGLQ---PFGGEGLSGTGpKAGGPHYLH 1022
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGIN-----GGGGYGpdaPFGGYKQSGLG-RENGIEGLE 449
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
573-1015 |
1.76e-63 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 222.62 E-value: 1.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 573 VTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTL-ADGVA 651
Cdd:cd07108 1 VINPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 652 EVREAVDFCRYYAARACEmmekplaLEGYTGERNELSLH-----PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKP 726
Cdd:cd07108 80 EAAVLADLFRYFGGLAGE-------LKGETLPFGPDVLTytvrePLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 727 AEQTPLiaafAVRLMRE--AGVLPS-VMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAE 803
Cdd:cd07108 153 AEDAPL----AVLLLAEilAQVLPAgVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR---LIPVSLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 804 TGGLNAMIVDSSALLEQVVNDVLVSA-FGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDK 882
Cdd:cd07108 226 LGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 883 DALAVLQAHVAKMREAH--TLIYQCELPSACN--NGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAI 956
Cdd:cd07108 306 KQFAKVCGYIDLGLSTSgaTVLRGGPLPGEGPlaDGFFVQPTIFSgvDNEWRLAREEIFGPVLCAIPW--KDEDEVIAMA 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1606703614 957 NATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMiGAVVGlQPFGGEGLSGTGPKA 1015
Cdd:cd07108 384 NDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGG-GQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
588-1016 |
2.17e-63 |
|
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: 222.60 E-value: 2.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 588 EASKEDVEWALSRAVEG--AAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAA 665
Cdd:cd07118 15 EGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAAS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 666 RAceMMEKPLALEGYTGERNELSLH-PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREA 744
Cdd:cd07118 95 LA--RTLHGDSYNNLGDDMLGLVLRePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 745 GVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInqtLAARSGEIVPLIAETGGLNAMIVDSSALLEQVVND 824
Cdd:cd07118 173 GLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAI---AAAAARNLKKVSLELGGKNPQIVFADADLDAAADA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 825 VLVSAFGSAGQRC-SALRVVhVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIY 903
Cdd:cd07118 250 VVFGVYFNAGECCnSGSRLL-VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 904 QCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKR 981
Cdd:cd07118 329 LGGERLASAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDTALTVARR 406
|
410 420 430
....*....|....*....|....*....|....*
gi 1606703614 982 MKVGNCYVNRNMIGAVVglQPFGGEGLSGTGPKAG 1016
Cdd:cd07118 407 IRAGTVWVNTFLDGSPE--LPFGGFKQSGIGRELG 439
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
581-1032 |
8.02e-63 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 220.66 E-value: 8.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:cd07150 10 SVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYyAARACEMMEKPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRL 740
Cdd:cd07150 90 RA-AAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 741 MREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTlAARSGEIVPLiaETGGLNAMIVDSSALLEQ 820
Cdd:cd07150 169 MEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEK-AGRHLKKITL--ELGGKNPLIVLADADLDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 821 VVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHT 900
Cdd:cd07150 246 AVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 901 LIyqceLPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERI 978
Cdd:cd07150 326 KL----LTGGKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPA--KDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1606703614 979 HKRMKVGNCYVNRNMI--GAVVglqPFGGEGLSGTGpKAGGPHYLHRLCIERTFTV 1032
Cdd:cd07150 400 AERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSMEEFTELKWITV 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
589-991 |
5.00e-62 |
|
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: 218.65 E-value: 5.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 589 ASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARAC 668
Cdd:cd07102 15 ASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 669 EMMeKPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLP 748
Cdd:cd07102 95 EAL-ADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 749 SVMQLLPGKGETvGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeIVPLIAETGGLNAMIVDSSALLEQVVNDVLVS 828
Cdd:cd07102 174 GVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGR---FIKVGLELGGKDPAYVRPDADLDAAAESLVDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 829 AFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHV--AKMREAHTLIYQCE 906
Cdd:cd07102 250 AFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIadAIAKGARALIDGAL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 907 LPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKV 984
Cdd:cd07102 330 FPEDKAGGAYLAPTVLTnvDHSMRVMREETFGPVVGIMKV--KSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLET 407
|
....*..
gi 1606703614 985 GNCYVNR 991
Cdd:cd07102 408 GTVFMNR 414
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
581-1012 |
6.80e-62 |
|
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: 218.24 E-value: 6.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALS--RAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVA-EVREAV 657
Cdd:cd07112 13 RVLAEVAACDAADVDRAVAaaRRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAvDVPSAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 658 DFCRYYAaracEMMEKPLALEGYTGErNELSL---HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIA 734
Cdd:cd07112 93 NTFRWYA----EAIDKVYGEVAPTGP-DALALitrEPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 735 AFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQtLAARSgEIVPLIAETGGLNAMIV-D 813
Cdd:cd07112 168 LRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLE-YSGQS-NLKRVWLECGGKSPNIVfA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 814 SSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVA 893
Cdd:cd07112 246 DAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 894 KMR-EAHTLIYQCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFNRKDlDAVIDAiNATGYGLTLGIHSR 970
Cdd:cd07112 326 SGKaEGARLVAGGKRVLTETGGFFVEPTVFDgvTPDMRIAREEIFGPVLSVITFDSEE-EAVALA-NDSVYGLAASVWTS 403
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1606703614 971 INETVERIHKRMKVGNCYVnrNMIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07112 404 DLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
565-1023 |
6.92e-62 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 219.69 E-value: 6.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 565 AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEG--AAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEA 642
Cdd:PLN02766 32 AASGKTFETRDPRT-GEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 643 GKTLADG-VAEVREAVDFCRYYAARA----CEMMEKPLALEGYTGERnelslhPRGTVLCISPWNFPLAIFTGQAVAALV 717
Cdd:PLN02766 111 GKLFALGkAVDIPAAAGLLRYYAGAAdkihGETLKMSRQLQGYTLKE------PIGVVGHIIPWNFPSTMFFMKVAPALA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 718 TGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTlAARSgEI 797
Cdd:PLN02766 185 AGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQA-AATS-NL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 798 VPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPerFD--TD 875
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP--FDprAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 876 VGPVIDKDAL-AVLQAHVAKMREAHTLIYQCElpSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAV 952
Cdd:PLN02766 341 QGPQVDKQQFeKILSYIEHGKREGATLLTGGK--PCGDKGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1606703614 953 IDAINATGYGLTLGIHSRINETVERIHKRMKVG----NCYVnrnmigAVVGLQPFGGEGLSGTGpKAGGPHYLHR 1023
Cdd:PLN02766 417 IKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGtiwvNCYF------AFDPDCPFGGYKMSGFG-RDQGMDALDK 484
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
561-1016 |
8.04e-62 |
|
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: 218.94 E-value: 8.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 561 MDGRAGSGVE---VSVTSPQNyRETIGRVIEASKEDVEWALS---RAVEGAaqWER-VPVAERAAVINRYADLLEAHMPD 633
Cdd:cd07143 11 INGEFVDSVHggtVKVYNPST-GKLITKIAEATEADVDIAVEvahAAFETD--WGLkVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 634 FLALASLEAGKT-LADGVAEVREAVDFCRYYAARA-------CEMMEKPLAlegYTgeRNElslhPRGTVLCISPWNFPL 705
Cdd:cd07143 88 LASIEALDNGKTfGTAKRVDVQASADTFRYYGGWAdkihgqvIETDIKKLT---YT--RHE----PIGVCGQIIPWNFPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 706 AIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANR 785
Cdd:cd07143 159 LMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 786 INQtlAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELR 865
Cdd:cd07143 239 VME--AAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 866 VGMPERFDTDVGPVIDKDALAVLQAHVAKMR-EAHTLIYQCElpSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVV 942
Cdd:cd07143 317 VGDPFAEDTFQGPQVSQIQYERIMSYIESGKaEGATVETGGK--RHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1606703614 943 RFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVN-RNMIGAVVglqPFGGEGLSGTGPKAG 1016
Cdd:cd07143 395 KF--KTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
581-1012 |
5.51e-61 |
|
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: 215.27 E-value: 5.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVA-EVREAVDF 659
Cdd:cd07092 8 EEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdELPGAVDN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 660 CRYYAArACEMMEKPLA---LEGYTGE-RNElslhPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAA 735
Cdd:cd07092 88 FRFFAG-AARTLEGPAAgeyLPGHTSMiRRE----PIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 736 FAVRLMREagVLPS-VMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTlAARSGEIVPLiaETGGLNAMIVDS 814
Cdd:cd07092 163 LLAELAAE--VLPPgVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADTLKRVHL--ELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 815 SALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAK 894
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 895 MREAHTLIYQCELPSAcnNGYFFAPA-------AFEIpsirvLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGI 967
Cdd:cd07092 318 APAHARVLTGGRRAEG--PGYFYEPTvvagvaqDDEI-----VQEEIFGPVVTVQPF--DDEDEAIELANDVEYGLASSV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1606703614 968 HSRINETVERIHKRMKVGNCYVNRNMIgaVVGLQPFGGEGLSGTG 1012
Cdd:cd07092 389 WTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
565-1016 |
7.81e-61 |
|
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: 216.12 E-value: 7.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 565 AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALsRAVEGAAQ--WERVPVAERAAVINRYADLLEAHMPDFLALASLEA 642
Cdd:cd07144 19 SSDGETIKTVNPST-GEVIASVYAAGEEDVDKAV-KAARKAFEswWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 643 GKTL-ADGVAEVREAVDFCRYYAARACEMMEKPLALegyTGERNELSLH-PRGTVLCISPWNFPLAIFTGQAVAALVTGN 720
Cdd:cd07144 97 GKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPT---SPNKLAYTLHePYGVCGQIIPWNYPLAMAAWKLAPALAAGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 721 AVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTAnRINQTLAARSGEIVPL 800
Cdd:cd07144 174 TVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATG-RLVMKAAAQNLKAVTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 801 iaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAE-LRVGMPERFDTDVGPV 879
Cdd:cd07144 253 --ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDDTVVGPQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 880 IDKDAL-AVLQ-AHVAKMREAHTLIYQCELPSACNNGYFFAPAAF-EIP-SIRVLEKEVFGPILHVVRFnrKDLDAVIDA 955
Cdd:cd07144 331 VSKTQYdRVLSyIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIFtDVPqDMRIVKEEIFGPVVVISKF--KTYEEAIKK 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1606703614 956 INATGYGLTLGIHSRINETVERIHKRMKVGNCYVNR-NM--IGAvvglqPFGGEGLSGTGPKAG 1016
Cdd:cd07144 409 ANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSsNDsdVGV-----PFGGFKMSGIGRELG 467
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
561-1025 |
1.47e-60 |
|
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: 215.00 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 561 MDGRAGSGVE---VSVTSPQNyRETIGRVIEASKEDVEWAL--SRAVEGAAQWERVPvAERAAVINRYADLLEAHMPDFL 635
Cdd:cd07113 4 IDGRPVAGQSekrLDITNPAT-EQVIASVASATEADVDAAVasAWRAFVSAWAKTTP-AERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 636 ALASLEAGKTLA-DGVAEVREAVDFCRYYAARACEMMEKPLA--LEGYTGER-NELSL-HPRGTVLCISPWNFPLAIFTG 710
Cdd:cd07113 82 QLETLCSGKSIHlSRAFEVGQSANFLRYFAGWATKINGETLApsIPSMQGERyTAFTRrEPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 711 QAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGEtVGAALVADPRIKAVMFTGSTDTANRINQTl 790
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 791 AARSGEIVPLiaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPE 870
Cdd:cd07113 240 AASDLTRVTL--ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 871 RFDTDVGPVIDKDAL-AVLQAHVAKMREAHTLIYQCELPSacNNGYFFAPAAFEIPSI--RVLEKEVFGPILHVVRFnrK 947
Cdd:cd07113 318 DESVMFGPLANQPHFdKVCSYLDDARAEGDEIVRGGEALA--GEGYFVQPTLVLARSAdsRLMREETFGPVVSFVPY--E 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1606703614 948 DLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVN-RNMIGAVVglqPFGGEGLSGTGpKAGGPHYLHRLC 1025
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG-REFGSAFIDDYT 468
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
581-1012 |
7.48e-60 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 212.55 E-value: 7.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:cd07090 8 EVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEMMEKPLALEG----YTgeRNElslhPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAF 736
Cdd:cd07090 88 EYYAGLAPTLSGEHVPLPGgsfaYT--RRE----PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 737 AVRLMREAGVLPSVMQLLPGKGETvGAALVADPRIKAVMFTGSTDTANRInqtLAARSGEIVPLIAETGGLNAMIVDSSA 816
Cdd:cd07090 162 LAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKV---MSAAAKGIKHVTLELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 817 LLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMR 896
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 897 -EAHTLIYQCELPS---ACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSR 970
Cdd:cd07090 318 qEGAKVLCGGERVVpedGLENGFYVSPCVLTdcTDDMTIVREEIFGPVMSILPF--DTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1606703614 971 INETVERIHKRMKVGNCYVNRNMIGAVvgLQPFGGEGLSGTG 1012
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPV--EVPFGGYKQSGFG 435
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
560-1016 |
1.37e-59 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 213.90 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 560 MMDGR---AGSGVEVSVTSPQNyRETIGRVIEASKEDVewalSRAVEGAAQ------WERVPVAERAAVINRYADLLEAH 630
Cdd:PLN02466 61 LINGQfvdAASGKTFPTLDPRT-GEVIAHVAEGDAEDV----NRAVAAARKafdegpWPKMTAYERSRILLRFADLLEKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 631 MPDFLALASLEAGKTLADGV-AEVREAVDFCRYYAARAcemmEKplaLEGYT----GERNELSLH-PRGTVLCISPWNFP 704
Cdd:PLN02466 136 NDELAALETWDNGKPYEQSAkAELPMFARLFRYYAGWA----DK---IHGLTvpadGPHHVQTLHePIGVAGQIIPWNFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 705 LAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTAn 784
Cdd:PLN02466 209 LLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTG- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 785 RINQTLAARSgEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAEL 864
Cdd:PLN02466 288 KIVLELAAKS-NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 865 RVGMPERFDTDVGPVIDKDALA-VLQAHVAKMREAHTLiyQCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHV 941
Cdd:PLN02466 367 VVGDPFKKGVEQGPQIDSEQFEkILRYIKSGVESGATL--ECGGDRFGSKGYYIQPTVFSnvQDDMLIAQDEIFGPVQSI 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1606703614 942 VRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVN-RNMIGAVVglqPFGGEGLSGTGPKAG 1016
Cdd:PLN02466 445 LKF--KDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
565-1012 |
2.12e-58 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 208.61 E-value: 2.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 565 AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGK 644
Cdd:PRK13473 13 AGEGEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 645 ----TLADgvaEVREAVDFCRYYAArACEMMEKPLA---LEGYTGE-RNElslhPRGTVLCISPWNFPLAIFTGQAVAAL 716
Cdd:PRK13473 92 plhlALND---EIPAIVDVFRFFAG-AARCLEGKAAgeyLEGHTSMiRRD----PVGVVASIAPWNYPLMMAAWKLAPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 717 VTGNAVIAKPAEQTPLIAAFAVRLMREAgvLPS-VMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTlAARSG 795
Cdd:PRK13473 164 AAGNTVVLKPSEITPLTALKLAELAADI--LPPgVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA-AADSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 796 EIVPLiaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTD 875
Cdd:PRK13473 241 KRTHL--ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 876 VGPVIDKDALAVLQAHVAKMRE-AH-TLIYQCELPSAcnNGYFFAPA--AFEIPSIRVLEKEVFGPILHVVRFnrKDLDA 951
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKAlGHiRVVTGGEAPDG--KGYYYEPTllAGARQDDEIVQREVFGPVVSVTPF--DDEDQ 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1606703614 952 VIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRN-MIgavVGLQPFGGEGLSGTG 1012
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHfML---VSEMPHGGQKQSGYG 453
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
562-1022 |
2.19e-58 |
|
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: 208.58 E-value: 2.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 562 DGR---AGSGVEVSVTSPqNYRETIGRVIEASKEDVEwalsRAVEGAAQ------WERVPVAERAAVINRYADLLEAHMP 632
Cdd:cd07139 4 GGRwvaPSGSETIDVVSP-ATEEVVGRVPEATPADVD----AAVAAARRafdngpWPRLSPAERAAVLRRLADALEARAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 633 DFLALASLEAGKTLA-DGVAEVREAVDFCRYYAARAcEMMEKPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQ 711
Cdd:cd07139 79 ELARLWTAENGMPISwSRRAQGPGPAALLRYYAALA-RDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 712 AVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGkGETVGAALVADPRIKAVMFTGSTDTANRINQTLA 791
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 792 ARsgeIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPER 871
Cdd:cd07139 237 ER---LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 872 FDTDVGPVIDKDALAVLQAHVAK-MREAHTLIYQCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFNRKD 948
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKgRAEGARLVTGGGRPAGLDRGWFVEPTLFAdvDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1606703614 949 lDAVidAI-NATGYGLTLGIHSRINETVERIHKRMKVGNCYVNrnmiGAVVGLQ-PFGGEGLSGTGpKAGGPHYLH 1022
Cdd:cd07139 394 -DAV--RIaNDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGPEGLD 461
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
567-1016 |
2.23e-58 |
|
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: 208.74 E-value: 2.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 567 SGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEG---AAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAG 643
Cdd:cd07141 20 SGKTFPTINPAT-GEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 644 KTLADG-VAEVREAVDFCRYYAARACEMMEKPLALEG----YTgeRNElslhPRGTVLCISPWNFPLAIFTGQAVAALVT 718
Cdd:cd07141 99 KPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDGdfftYT--RHE----PVGVCGQIIPWNFPLLMAAWKLAPALAC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 719 GNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIV 798
Cdd:cd07141 173 GNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 799 PLiaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGP 878
Cdd:cd07141 253 TL--ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 879 VIDKDAL-AVLQAHVAKMREAHTLiyQCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDA 955
Cdd:cd07141 331 QIDEEQFkKILELIESGKKEGAKL--ECGGKRHGDKGYFIQPTVFSdvTDDMRIAKEEIFGPVQQIFKF--KTIDEVIER 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1606703614 956 INATGYGLTLGIHSRINETVERIHKRMKVGNCYVNrnmIGAVVGLQ-PFGGEGLSGTGPKAG 1016
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
583-1033 |
1.61e-57 |
|
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: 206.00 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 583 IGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGV-AEVREAVDFCR 661
Cdd:cd07098 9 LGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEILVTCEKIR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 662 YYAARAcemmEKPLALEGYTG------ERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAA 735
Cdd:cd07098 89 WTLKHG----EKALRPESRPGgllmfyKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 736 FAVRLMREA----GVLPSVMQLLPGKGETvGAALVADPRIKAVMFTGSTDTANRInqtLAARSGEIVPLIAETGGLNAMI 811
Cdd:cd07098 165 FFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKV---MAAAAESLTPVVLELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 812 VDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAH 891
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 892 VA------------KMREAHTliyqcELPSacnnGYFFAPA--AFEIPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAIN 957
Cdd:cd07098 321 VAdavekgarllagGKRYPHP-----EYPQ----GHYFPPTllVDVTPDMKIAQEEVFGPVMVVMKA--SDDEEAVEIAN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1606703614 958 ATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGEGLSGTGpKAGGPHYLHRLCIERTFTVD 1033
Cdd:cd07098 390 STEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTED 464
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
567-1012 |
2.11e-57 |
|
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: 206.04 E-value: 2.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 567 SGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMpDFLALA-SLEAGK- 644
Cdd:cd07559 14 KGEYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENL-ELLAVAeTLDNGKp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 645 ---TLAdgvAEVREAVDFCRYYAARAcemmekpLALEGYTGERNE--LSLH---PRGTVLCISPWNFPLAIFTGQAVAAL 716
Cdd:cd07559 92 ireTLA---ADIPLAIDHFRYFAGVI-------RAQEGSLSEIDEdtLSYHfhePLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 717 VTGNAVIAKPAEQTPLIAAFAVRLMREagVLPS-VMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsg 795
Cdd:cd07559 162 AAGNTVVLKPASQTPLSILVLMELIGD--LLPKgVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAEN-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 796 eIVPLIAETGGLNAMIVDSSALLEQ------VVNDVLVSAFGSaGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMP 869
Cdd:cd07559 238 -LIPVTLELGGKSPNIFFDDAMDADddfddkAEEGQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 870 ERFDTDVGPVIDKDALAVLQAHVAKMRE--AHTLIYQCELPSA-CNNGYFFAPAAFEIP--SIRVLEKEVFGPILHVVRF 944
Cdd:cd07559 316 LDPETMMGAQVSKDQLEKILSYVDIGKEegAEVLTGGERLTLGgLDKGYFYEPTLIKGGnnDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1606703614 945 nrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVG----NCYvnrNMIGAVVglqPFGGEGLSGTG 1012
Cdd:cd07559 396 --KDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGrvwvNCY---HQYPAHA---PFGGYKKSGIG 459
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
555-1026 |
2.63e-56 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 203.21 E-value: 2.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 555 FEAAPMMDGR---AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHM 631
Cdd:PRK11241 9 FRQQALINGEwldANNGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 632 PDFLALASLEAGKTLADGVAEVREAVDFCRYYAARACEMMEKplALEGYTGERNELSL-HPRGTVLCISPWNFPLAIFTG 710
Cdd:PRK11241 88 DDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGD--TIPGHQADKRLIVIkQPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 711 QAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTAnriNQTL 790
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIG---RQLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 791 AARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPE 870
Cdd:PRK11241 243 EQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 871 RFDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPSACnNGYFFAPAAF-EIP-SIRVLEKEVFGPILHVVRFnrKD 948
Cdd:PRK11241 323 EKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHEL-GGNFFQPTILvDVPaNAKVAKEETFGPLAPLFRF--KD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 949 LDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGlqPFGG---EGLSGTGPKAGGPHYLH--R 1023
Cdd:PRK11241 400 EADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYLEikY 477
|
...
gi 1606703614 1024 LCI 1026
Cdd:PRK11241 478 MCI 480
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
580-1022 |
6.41e-55 |
|
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: 198.77 E-value: 6.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 580 RETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTladgVAEVRE---- 655
Cdd:cd07111 47 GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKP----IRESRDcdip 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 656 -AVDFCRYYAARAcEMMEKplALEGYtgernelslHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIA 734
Cdd:cd07111 123 lVARHFYHHAGWA-QLLDT--ELAGW---------KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 735 AFAVRLMREAGVLPSVMQLLPGKGETvGAALVADPRIKAVMFTGSTDTANRINQTLAarsGEIVPLIAETGGLNAMIVDS 814
Cdd:cd07111 191 LLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA---GTGKKLSLELGGKSPFIVFD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 815 SALLEQVVNDVLVSAFGSAGQRCSA-LRVVhVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVA 893
Cdd:cd07111 267 DADLDSAVEGIVDAIWFNQGQVCCAgSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 894 KMREAHTLIYQ--CELPSacnNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnRKDLDAVIDAiNATGYGLTLGIHS 969
Cdd:cd07111 346 EGRAEGADVFQpgADLPS---KGPFYPPTLFTnvPPASRIAQEEIFGPVLVVLTF-RTAKEAVALA-NNTPYGLAASVWS 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1606703614 970 -RINETVErIHKRMKVGNCYVN-RNMIGAVVglqPFGGEGLSGTGpKAGGPHYLH 1022
Cdd:cd07111 421 eNLSLALE-VALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLY 470
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
68-180 |
7.64e-55 |
|
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: 185.79 E-value: 7.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 68 IDSFLTEYALSSDEGIALMCLAEAMLRVPDNETIDILIRDKLSGPDWDAHRGQSDSFFVNAATWALMLTGKVLSPERiDN 147
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEP-EG 79
|
90 100 110
....*....|....*....|....*....|...
gi 1606703614 148 DLGRSLFRLANRTGEGVIRKAVEKAMRIMSKQF 180
Cdd:pfam14850 80 TLAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
564-1012 |
9.71e-55 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 197.91 E-value: 9.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVS-VTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEA 642
Cdd:cd07151 4 RDGTSERTIdVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 643 GKTLADGVAEVREAVDFCRyyaaracEMMEKPLALEG------YTGERNELSLHPRGTVLCISPWNFPLAIfTGQAVA-A 715
Cdd:cd07151 83 GSTRIKANIEWGAAMAITR-------EAATFPLRMEGrilpsdVPGKENRVYREPLGVVGVISPWNFPLHL-SMRSVApA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 716 LVTGNAVIAKPAEQTP-----LIAafavRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQtL 790
Cdd:cd07151 155 LALGNAVVLKPASDTPitgglLLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGE-L 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 791 AARSGEIVPLiaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPE 870
Cdd:cd07151 230 AGRHLKKVAL--ELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 871 RFDTDVGPVIDKDALAVLQAHVAKMREA-HTLIYQCELpsacnNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrK 947
Cdd:cd07151 308 DPDTVVGPLINESQVDGLLDKIEQAVEEgATLLVGGEA-----EGNVLEPTVLSdvTNDMEIAREEIFGPVAPIIKA--D 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1606703614 948 DLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNR-------NMigavvglqPFGGEGLSGTG 1012
Cdd:cd07151 381 DEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDqpvndepHV--------PFGGEKNSGLG 444
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
581-1012 |
7.72e-54 |
|
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: 195.16 E-value: 7.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:cd07147 10 EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEMMEKPLALEGYTGERNELSL---HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFA 737
Cdd:cd07147 90 RIAAEEATRIYGEVLPLDISARGEGRQGLvrrFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 738 VRLMREAGVLPSVMQLLPGKGETvGAALVADPRIKAVMFTGSTDtanrINQTLAARSGEiVPLIAETGGLNAMIVDSSAL 817
Cdd:cd07147 170 GEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPA----VGWDLKARAGK-KKVVLELGGNAAVIVDSDAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 818 LEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMRE 897
Cdd:cd07147 244 LDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 898 AHTLIyqceLPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHSRINETV 975
Cdd:cd07147 324 AGAKL----LTGGKRDGALLEPTILEdvPPDMEVNCEEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQAGVFTRDLEKA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1606703614 976 ERIHKRMKVGNCYVN-----RnmigavVGLQPFGGEGLSGTG 1012
Cdd:cd07147 398 LRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSGIG 433
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
562-1012 |
1.99e-53 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 194.71 E-value: 1.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 562 DGR---AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALA 638
Cdd:PRK13252 12 DGAyveATSGETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 639 SLEAGKTLADG-VAEVREAVDFCRYYAARACemmekplALEG-----------YTgeRNElslhPRGTVLCISPWNFPLA 706
Cdd:PRK13252 91 TLDTGKPIQETsVVDIVTGADVLEYYAGLAP-------ALEGeqiplrggsfvYT--RRE----PLGVCAGIGAWNYPIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 707 IFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGEtVGAALVADPRIKAVMFTGSTDTANRI 786
Cdd:PRK13252 158 IACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 787 nqtLAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRV 866
Cdd:PRK13252 237 ---MAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 867 GMPERFDTDVGPVIDKDALAVLQAHVAK-MREAHTLIYQCE--LPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHV 941
Cdd:PRK13252 314 GDPMDPATNFGPLVSFAHRDKVLGYIEKgKAEGARLLCGGErlTEGGFANGAFVAPTVFTdcTDDMTIVREEIFGPVMSV 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606703614 942 VRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVnrNMIGAVVGLQPFGGEGLSGTG 1012
Cdd:PRK13252 394 LTF--DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
565-1012 |
1.07e-52 |
|
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: 192.28 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 565 AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGK 644
Cdd:cd07117 12 GSSGETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 645 TLADGVA-EVREAVDFCRYYAARAcemmekpLALEGYTGERNE--LSL---HPRGTVLCISPWNFPLAIFTGQAVAALVT 718
Cdd:cd07117 91 PIRETRAvDIPLAADHFRYFAGVI-------RAEEGSANMIDEdtLSIvlrEPIGVVGQIIPWNFPFLMAAWKLAPALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 719 GNAVIAKPAEQTPLIAAFAVRLMREagVLPS-VMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARsgeI 797
Cdd:cd07117 164 GNTVVIKPSSTTSLSLLELAKIIQD--VLPKgVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKK---L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 798 VPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVG 877
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 878 PVIDKDALAVLQAHV--AKMREAHTLIYQCELPSA-CNNGYFFAPAAFEIPS--IRVLEKEVFGPILHVVRFnrKDLDAV 952
Cdd:cd07117 319 AQVNKDQLDKILSYVdiAKEEGAKILTGGHRLTENgLDKGFFIEPTLIVNVTndMRVAQEEIFGPVATVIKF--KTEDEV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1606703614 953 IDAINATGYGLTLGIHSR-INETVeRIHKRMKVGNCYVNR-NMIGAVVglqPFGGEGLSGTG 1012
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKdINRAL-RVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
581-990 |
1.31e-52 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 191.40 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEG--AAQWERVPvAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVD 658
Cdd:cd07120 8 EVIGTYADGGVAEAEAAIAAARRAfdETDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 659 FCRYYAARACEMMEKplALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAV 738
Cdd:cd07120 87 ELRYYAGLARTEAGR--MIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 739 RLMREAGVLPS-VMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInQTLAARSGEIVPLiaETGGLNAMIVDSSAL 817
Cdd:cd07120 165 RILAEIPSLPAgVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAI-MAAAAPTLKRLGL--ELGGKTPCIVFDDAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 818 LEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHV--AKM 895
Cdd:cd07120 242 LDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVerAIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 896 REAHTLIYQCELPSACNNGYFFAPAAFEI--PSIRVLEKEVFGPILHVVRFNRKDlDAVIDAiNATGYGLTLGIHSRINE 973
Cdd:cd07120 322 AGAEVVLRGGPVTEGLAKGAFLRPTLLEVddPDADIVQEEIFGPVLTLETFDDEA-EAVALA-NDTDYGLAASVWTRDLA 399
|
410
....*....|....*..
gi 1606703614 974 TVERIHKRMKVGNCYVN 990
Cdd:cd07120 400 RAMRVARAIRAGTVWIN 416
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
566-1023 |
1.33e-52 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 193.13 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 566 GSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKT 645
Cdd:PLN02315 31 ANGPLVSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 646 LADGVAEVREAVDFCRYYAAracemMEKPLALEGYTGER-NELSL---HPRGTVLCISPWNFPLAIFTGQAVAALVTGNA 721
Cdd:PLN02315 110 LAEGIGEVQEIIDMCDFAVG-----LSRQLNGSIIPSERpNHMMMevwNPLGIVGVITAFNFPCAVLGWNACIALVCGNC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 722 VIAKPAEQTPLIAAFAVRLMreAGVLPSvmQLLPGK-------GETVGAALVADPRIKAVMFTGSTDTANRINQTLAARS 794
Cdd:PLN02315 185 VVWKGAPTTPLITIAMTKLV--AEVLEK--NNLPGAiftsfcgGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 795 GEIvplIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDT 874
Cdd:PLN02315 261 GKC---LLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 875 DVGPVIDKDALAVLQAHVAKMR-EAHTLIYQCELPSAcnNGYFFAPAAFEI-PSIRVLEKEVFGPILHVVRFnrKDLDAV 952
Cdd:PLN02315 338 LLGPLHTPESKKNFEKGIEIIKsQGGKILTGGSAIES--EGNFVQPTIVEIsPDADVVKEELFGPVLYVMKF--KTLEEA 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1606703614 953 IDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMI--GAVVGlQPFGGEGLSGTGPKAGG---PHYLHR 1023
Cdd:PLN02315 414 IEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPtnGAEIG-GAFGGEKATGGGREAGSdswKQYMRR 488
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
581-1012 |
2.00e-51 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 188.02 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:PRK09406 12 ETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEMMEKPLALEGYTGERNELSLH-PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVR 739
Cdd:PRK09406 92 RYYAEHAEALLADEPADAAAVGASRAYVRYqPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 740 LMREAGVLPSVMQ-LLPGKGETvgAALVADPRIKAVMFTGStdtaNRINQTLAARSG-EIVPLIAETGGLNAMIVDSSAL 817
Cdd:PRK09406 172 LFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGS----EPAGRAVAAIAGdEIKKTVLELGGSDPFIVMPSAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 818 LEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMRE 897
Cdd:PRK09406 246 LDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 898 A-HTLIYQCELPSAcnNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHSRINET 974
Cdd:PRK09406 326 AgATILCGGKRPDG--PGWFYPPTVITdiTPDMRLYTEEVFGPVASLYRVA--DIDEAIEIANATTFGLGSNAWTRDEAE 401
|
410 420 430
....*....|....*....|....*....|....*...
gi 1606703614 975 VERIHKRMKVGNCYVNrNMIGAVVGLqPFGGEGLSGTG 1012
Cdd:PRK09406 402 QERFIDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSGYG 437
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
599-1012 |
2.61e-51 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 187.01 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 599 SRAVEGAA----QWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARAcemmekP 674
Cdd:cd07105 3 DQAVEAAAaafpAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLI------T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 675 LALEGY--TGERNELSL---HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPS 749
Cdd:cd07105 77 QIIGGSipSDKPGTLAMvvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 750 VMQLLPGKGETVGA---ALVADPRIKAVMFTGSTDTANRINQTlAARsgEIVPLIAETGGLNAMIVDSSALLEQVVNDVL 826
Cdd:cd07105 157 VLNVVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAET-AAK--HLKPVLLELGGKAPAIVLEDADLDAAANAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 827 VSAFGSAGQRC-SALRVVhVQDEVYPRFMALLKGAMAELRVGmperfDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQC 905
Cdd:cd07105 234 FGAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 906 ELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMK 983
Cdd:cd07105 308 GLADESPSGTSMPPTILDnvTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIE 385
|
410 420
....*....|....*....|....*....
gi 1606703614 984 VGNCYVNRNMIGAVVGLqPFGGEGLSGTG 1012
Cdd:cd07105 386 SGAVHINGMTVHDEPTL-PHGGVKSSGYG 413
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
565-1033 |
4.08e-49 |
|
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: 182.31 E-value: 4.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 565 AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEG--AAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEA 642
Cdd:cd07140 17 AEGGKTYNTINPTD-GSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 643 GK--TLADGvAEVREAVDFCRYYAARACEMMEKPLALEGYTGERNeLSL---HPRGTVLCISPWNFPLAIFTGQAVAALV 717
Cdd:cd07140 96 GAvyTLALK-THVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRN-LTLtkrEPIGVCGIVIPWNYPLMMLAWKMAACLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 718 TGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEI 797
Cdd:cd07140 174 AGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLKK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 798 VPLiaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVG 877
Cdd:cd07140 254 VSL--ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 878 PVIDKDALAVLQAHVAK-MREAHTLIY---QCELPsacnnGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFNRKDLDA 951
Cdd:cd07140 332 PQNHKAHLDKLVEYCERgVKEGATLVYggkQVDRP-----GFFFEPTVFTdvEDHMFIAKEESFGPIMIISKFDDGDVDG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 952 VIDAINATGYGLTLGIHSR-INETVeRIHKRMKVGNCYVNRNMIGAVVGlqPFGGEGLSGTGpKAGGPHYLHRLCIERTF 1030
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKdINKAL-YVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFG-KDLGEEALNEYLKTKTV 482
|
...
gi 1606703614 1031 TVD 1033
Cdd:cd07140 483 TIE 485
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
636-1022 |
9.37e-48 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 176.08 E-value: 9.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 636 ALASLEAGKTLADGVAEVREAVDFCRYYAARAcEMMEKPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAA 715
Cdd:PRK10090 17 ALIVEEGGKIQQLAEVEVAFTADYIDYMAEWA-RRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 716 LVTGNAVIAKPAEQTPLIA-AFAvRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRInqtLAARS 794
Cdd:PRK10090 96 LLTGNTIVIKPSEFTPNNAiAFA-KIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKI---MAAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 795 GEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMP-ERFD 873
Cdd:PRK10090 172 KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPaERND 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 874 TDVGPVIDKDALAVLQAHVAKMREAHTLIyQCELPSACNNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFNrkDLDA 951
Cdd:PRK10090 252 IAMGPLINAAALERVEQKVARAVEEGARV-ALGGKAVEGKGYYYPPTLLLdvRQEMSIMHEETFGPVLPVVAFD--TLEE 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606703614 952 VIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQpfGGEGLSGTGpKAGGPHYLH 1022
Cdd:PRK10090 329 AIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSGIG-GADGKHGLH 396
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
543-990 |
2.71e-47 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 177.23 E-value: 2.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 543 MAASIEARMPF--HFEAAPMMDGRagsgveVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEG-----AAQWERVPVAE 615
Cdd:PLN02467 1 MAIPVPRRQLFigGEWREPVLGKR------IPVVNPAT-EETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 616 RAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYYAARACEMMEK---PLALeGYTGERNELSLHPR 692
Cdd:PLN02467 74 RAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKqkaPVSL-PMETFKGYVLKEPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 693 GTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIK 772
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 773 AVMFTGSTDTANRInqtLAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPR 852
Cdd:PLN02467 233 KIAFTGSTATGRKI---MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 853 FMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAK-MREAHTLIYQCELPSACNNGYFFAPAAFE--IPSIRV 929
Cdd:PLN02467 310 FLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTaKSEGATILCGGKRPEHLKKGFFIEPTIITdvTTSMQI 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1606703614 930 LEKEVFGPILHVVRFNRKdlDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVN 990
Cdd:PLN02467 390 WREEVFGPVLCVKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
541-1012 |
1.47e-45 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 172.00 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 541 RAMAASIEARMpfhfeaapMMDGR---AGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALS--RAVEGAAQWERVPVAE 615
Cdd:PRK09847 12 KALSLAIENRL--------FINGEytaAAENETFETVDPVT-QAPLAKIARGKSVDIDRAVSaaRGVFERGDWSLSSPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 616 RAAVINRYADLLEAHMPDFLALASLEAGK----TLADGVAEVREAVdfcRYYAaracEMMEKPLALEGYTGErNELSL-- 689
Cdd:PRK09847 83 RKAVLNKLADLMEAHAEELALLETLDTGKpirhSLRDDIPGAARAI---RWYA----EAIDKVYGEVATTSS-HELAMiv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 690 -HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVAD 768
Cdd:PRK09847 155 rEPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 769 PRIKAVMFTGSTDTANRINQTLAARSGEIVPLiaETGGLNAMIVDSSAL-LEQVVNDVLVSAFGSAGQRCSALRVVHVQD 847
Cdd:PRK09847 235 NDIDAIAFTGSTRTGKQLLKDAGDSNMKRVWL--EAGGKSANIVFADCPdLQQAASATAAGIFYNQGQVCIAGTRLLLEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 848 EVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDkdalavlQAHVAKMreaHTLIYQCE-----LPSACNNGY--FFAPA 920
Cdd:PRK09847 313 SIADEFLALLKQQAQNWQPGHPLDPATTMGTLID-------CAHADSV---HSFIREGEskgqlLLDGRNAGLaaAIGPT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 921 AFEI--PSIRVLEKEVFGPILHVVRFNRKdlDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVV 998
Cdd:PRK09847 383 IFVDvdPNASLSREEIFGPVLVVTRFTSE--EQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT 460
|
490
....*....|....
gi 1606703614 999 glQPFGGEGLSGTG 1012
Cdd:PRK09847 461 --VPFGGYKQSGNG 472
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
564-990 |
6.81e-44 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 167.24 E-value: 6.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVSVTSPQNyRETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAG 643
Cdd:PLN00412 26 TSSSGKSVAITNPST-RKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 644 KTLADGVAEVREAVDFCRYYAARACEMME--KPLALEGYTG-ERNELSLH---PRGTVLCISPWNFPLAIFTGQAVAALV 717
Cdd:PLN00412 105 KPAKDAVTEVVRSGDLISYTAEEGVRILGegKFLVSDSFPGnERNKYCLTskiPLGVVLAIPPFNYPVNLAVSKIAPALI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 718 TGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGStDTANRInqtlaARSGEI 797
Cdd:PLN00412 185 AGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAI-----SKKAGM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 798 VPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERfDTDVG 877
Cdd:PLN00412 259 VPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDIT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 878 PVIDKDALAVLQAHV--AKMREA--HT-------LIYQCELPSAcnngyffapaafeIPSIRVLEKEVFGPILHVVRFNr 946
Cdd:PLN00412 338 PVVSESSANFIEGLVmdAKEKGAtfCQewkregnLIWPLLLDNV-------------RPDMRIAWEEPFGPVLPVIRIN- 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1606703614 947 kDLDAVIDAINATGYGLTLGIHSR-INETVeRIHKRMKVGNCYVN 990
Cdd:PLN00412 404 -SVEEGIHHCNASNFGLQGCVFTRdINKAI-LISDAMETGTVQIN 446
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
585-1012 |
3.49e-43 |
|
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: 164.55 E-value: 3.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 585 RVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMpDFLALA-SLEAGK----TLAdgvAEVREAVDF 659
Cdd:cd07116 31 EVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANL-EMLAVAeTWDNGKpvreTLA---ADIPLAIDH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 660 CRYYAA--RACEMMEKPLalegytgERNELSLH---PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPlia 734
Cdd:cd07116 107 FRYFAGciRAQEGSISEI-------DENTVAYHfhePLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTP--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 735 AFAVRLMREAGVL--PSVMQLLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTlaaRSGEIVPLIAETGGLNAMIV 812
Cdd:cd07116 177 ASILVLMELIGDLlpPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY---ASENIIPVTLELGGKSPNIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 813 DSS------ALLEQVVNDVLVSAFGSaGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALA 886
Cdd:cd07116 254 FADvmdaddAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 887 VLQAHVAKMRE--AHTLI--YQCELPSACNNGYFFAPAAFEIPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYG 962
Cdd:cd07116 333 KILSYIDIGKEegAEVLTggERNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTF--KDEEEALEIANDTLYG 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1606703614 963 LTLGIHSRINETVERIHKRMKVG----NCYvnrnmiGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07116 411 LGAGVWTRDGNTAYRMGRGIQAGrvwtNCY------HLYPAHAAFGGYKQSGIG 458
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
573-1028 |
2.36e-41 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 158.74 E-value: 2.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 573 VTSPQNyRETIGRVIEASKEDVEWALSRAVE---GAAQWerVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADG 649
Cdd:cd07148 3 VVNPFD-LKPIGEVPTVDWAAIDKALDTAHAlflDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 650 VAEVREAVDFCRYyAARACEMM---EKPLAL-EGYTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAK 725
Cdd:cd07148 80 KVEVTRAIDGVEL-AADELGQLggrEIPMGLtPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 726 PAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGEtVGAALVADPRIKAVMFTGSTDTANRINQTLAArsGEIVPLiaETG 805
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLAP--GTRCAL--EHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 806 GLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDAL 885
Cdd:cd07148 234 GAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 886 AVLQAHV--AKMREAHTLIYQCELPSACnngyfFAPAAFEIP--SIRVLEKEVFGPIlhVVRFNRKDLDAVIDAINATGY 961
Cdd:cd07148 314 DRVEEWVneAVAAGARLLCGGKRLSDTT-----YAPTVLLDPprDAKVSTQEIFGPV--VCVYSYDDLDEAIAQANSLPV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1606703614 962 GLTLGIHSRINETVERIHKRMKVGNCYVNrNMIGAVVGLQPFGGEGLSGTGpkAGG-PHYLHRLCIER 1028
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVN-DHTAFRVDWMPFAGRRQSGYG--TGGiPYTMHDMTQEK 451
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
605-1019 |
6.19e-38 |
|
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: 147.76 E-value: 6.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 605 AAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTladgVAEVREAVDFCRYYAAR-ACEMMEK---------P 674
Cdd:cd07134 11 ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKP----AAEVDLTEILPVLSEINhAIKHLKKwmkpkrvrtP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 675 LALegyTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAgVLPSVMQLL 754
Cdd:cd07134 87 LLL---FGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 755 PGKGEtVGAALVADPrIKAVMFTGSTdTANRINQTLAARSGEIVPLiaETGGLNAMIVDSSALLEQVVNDVLVSAFGSAG 834
Cdd:cd07134 163 EGDAE-VAQALLELP-FDHIFFTGSP-AVGKIVMAAAAKHLASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 835 QRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDT-DVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPSACNN 913
Cdd:cd07134 238 QTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 914 gyFFAPAAFE--IPSIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNR 991
Cdd:cd07134 318 --YIAPTVLTnvTPDMKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVND 393
|
410 420
....*....|....*....|....*...
gi 1606703614 992 NMIGAVVGLQPFGGEGLSGTGpKAGGPH 1019
Cdd:cd07134 394 VVLHFLNPNLPFGGVNNSGIG-SYHGVY 420
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
594-1023 |
8.86e-38 |
|
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: 147.77 E-value: 8.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 594 VEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLadgvaevREAVDFC------RYYAARA 667
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGW-------MFAENICgdqvqlRARAFVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 668 CEMMEKPLALEGYTGERNELSLH---PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREA 744
Cdd:cd07084 74 YSYRIPHEPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 745 GVLP-SVMQLLPGKGETvGAALVADPRIKAVMFTGSTDTAnrinQTLAARSGEIvPLIAETGGLNAMIVDSSA-----LL 818
Cdd:cd07084 154 GLLPpEDVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVA----EKLALDAKQA-RIYLELAGFNWKVLGPDAqavdyVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 819 EQVVNDVLVsafgSAGQRCSALRVVHVQDEvyPRFMALLKGAMAELRVGMPErfDTDVGPVIDKDALAVLQAH------- 891
Cdd:cd07084 228 WQCVQDMTA----CSGQKCTAQSMLFVPEN--WSKTPLVEKLKALLARRKLE--DLLLGPVQTFTTLAMIAHMenllgsv 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 892 VAKMREAHTLIYQCELPSACNNGYFFAPAAFEIPSIRVLEKEVFGPILHVVRFNRKDLDAVIDAINATGYGLTLGIHSRI 971
Cdd:cd07084 300 LLFSGKELKNHSIPSIYGACVASALFVPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSND 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1606703614 972 NETVERIHKRMKV-GNCY-VNRNMIGAVVGLQPFGGEGLSGTGPKAGGPHYLHR 1023
Cdd:cd07084 380 PIFLQELIGNLWVaGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKL 433
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
581-1025 |
4.49e-37 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 146.16 E-value: 4.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 581 ETIGRVIEASKEDVEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFC 660
Cdd:PRK13968 18 EQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLC 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 661 RYYAARACEMME-KPLALEgytGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVR 739
Cdd:PRK13968 98 DWYAEHGPAMLKaEPTLVE---NQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 740 LMREAGVLPSVMQLLPGKGETVgAALVADPRIKAVMFTGSTdtanRINQTLAARSGEIV-PLIAETGGLNAMIVDSSALL 818
Cdd:PRK13968 175 VFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSV----RAGAAIGAQAGAALkKCVLELGGSDPFIVLNDADL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 819 EQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHV-AKMRE 897
Cdd:PRK13968 250 ELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVeATLAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 898 AHTLIYQCELPSACNNGYFFAPAAFEIPSIRVLEKEVFGPILHVVRfnRKDLDAVIDAINATGYGLTLGIHSRINETVER 977
Cdd:PRK13968 330 GARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITV--AKDAEHALELANDSEFGLSATIFTTDETQARQ 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1606703614 978 IHKRMKVGNCYVNRnmIGAVVGLQPFGGEGLSGTGPKAGgpHY-LHRLC 1025
Cdd:PRK13968 408 MAARLECGGVFING--YCASDARVAFGGVKKSGFGRELS--HFgLHEFC 452
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
690-1012 |
1.19e-36 |
|
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: 143.82 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 690 HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAgVLPSVMQLLPGkGETVGAALVADP 769
Cdd:cd07087 99 EPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-GVEVATALLAEP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 770 rIKAVMFTGSTDTANRINQtLAARSgeIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEV 849
Cdd:cd07087 177 -FDHIFFTGSPAVGKIVME-AAAKH--LTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 850 YPRFMALLKGAMAELRVGMPERFDtDVGPVIDKDALAVLqahvAKMREAHTLIY--QCELPSAcnngyFFAPAAFEIPSI 927
Cdd:cd07087 253 KDELIEELKKAIKEFYGEDPKESP-DYGRIINERHFDRL----ASLLDDGKVVIggQVDKEER-----YIAPTILDDVSP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 928 --RVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGG 1005
Cdd:cd07087 323 dsPLMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
....*..
gi 1606703614 1006 EGLSGTG 1012
Cdd:cd07087 401 VGNSGMG 407
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
691-1012 |
1.47e-34 |
|
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: 138.12 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 691 PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAgvL-PSVMQLLPGKGETVGAALvaDP 769
Cdd:cd07135 108 PLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY--LdPDAFQVVQGGVPETTALL--EQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 770 RIKAVMFTGSTdTANRINQTLAARSgeIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEV 849
Cdd:cd07135 184 KFDKIFYTGSG-RVGRIIAEAAAKH--LTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 850 YPRFMALLKGAMAELRVGMPERfDTDVGPVIDKDALAVLQAHVAKMREahTLIYQCELPSACNngyFFAPAA--FEIPSI 927
Cdd:cd07135 261 YDEFVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTTKG--KVVIGGEMDEATR---FIPPTIvsDVSWDD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 928 RVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMI-GAVVGLqPFGGE 1006
Cdd:cd07135 335 SLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhVGVDNA-PFGGV 411
|
....*.
gi 1606703614 1007 GLSGTG 1012
Cdd:cd07135 412 GDSGYG 417
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
524-990 |
9.01e-31 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 129.10 E-value: 9.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 524 PERPNSagLDLNDRTVRRAMAASIEARMPfhfEAAPMMDGraGSGVE------VSVTSPQNyRETIGRVIEASKEDVEWA 597
Cdd:PLN02419 85 PLRPQF--LALRSSWLSTSPEQSTQPQMP---PRVPNLIG--GSFVEsqsssfIDVINPAT-QEVVSKVPLTTNEEFKAA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 598 LSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVAEVREAVDFCRYyaarACEMMEKPLA- 676
Cdd:PLN02419 157 VSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEH----ACGMATLQMGe 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 677 -LEGYTGERNELSL-HPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLL 754
Cdd:PLN02419 233 yLPNVSNGVDTYSIrEPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 755 PGKGETVGaALVADPRIKAVMFTGSTDTANRINQTLAARSGEIVpliAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAG 834
Cdd:PLN02419 313 HGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQ---SNMGAKNHGLVLPDANIDATLNALLAAGFGAAG 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 835 QRCSALRVVHVQDEVYPRFMALLKGAMAeLRVGMPERFDTDVGPVIDKDA----LAVLQAHV---AKM----REAHTLIY 903
Cdd:PLN02419 389 QRCMALSTVVFVGDAKSWEDKLVERAKA-LKVTCGSEPDADLGPVISKQAkeriCRLIQSGVddgAKLlldgRDIVVPGY 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 904 QcelpsacnNGYFFAPAAFE--IPSIRVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHSRINETVERIHKR 981
Cdd:PLN02419 468 E--------KGNFIGPTILSgvTPDMECYKEEIFGPVLVCMQAN--SFDEAISIINKNKYGNGAAIFTSSGAAARKFQMD 537
|
....*....
gi 1606703614 982 MKVGNCYVN 990
Cdd:PLN02419 538 IEAGQIGIN 546
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
691-1012 |
4.81e-27 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 116.28 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 691 PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAgVLPSVMQLLPGkGETVGAALVADPr 770
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 771 IKAVMFTGSTDTANRINQtlaARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVY 850
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQ---AAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 851 PRFMALLKGAMAELRVGMPERfDTDVGPVIDKDALAVLQAhvakMREAH--TLIYQCElpsACNNGYFFAPAAFEIPSI- 927
Cdd:PTZ00381 263 DKFIEALKEAIKEFFGEDPKK-SEDYSRIVNEFHTKRLAE----LIKDHggKVVYGGE---VDIENKYVAPTIIVNPDLd 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 928 -RVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQPFGGE 1006
Cdd:PTZ00381 335 sPLMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
....*.
gi 1606703614 1007 GLSGTG 1012
Cdd:PTZ00381 413 GNSGMG 418
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
594-969 |
7.23e-25 |
|
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: 109.17 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 594 VEWALSRAVEGAAQWERVPVAERAAVINRYADLLEAHMPDFLALASLEAG--KTLADG-----VAEVREAVDFCR---YY 663
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpEARLQGelgrtTGQLRLFADLVRegsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 664 AARacemMEKPLAlEGYTGERNELSLH--PRGTVLCISPWNFPLAIFT--GQAVAALVTGNAVIAK--PA--EQTPLIAA 735
Cdd:cd07129 81 DAR----IDPADP-DRQPLPRPDLRRMlvPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhpGTSELVAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 736 FAVRLMREAGVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTdTANRINQTLAARSGEIVPLIAETGGLNAMIVDSS 815
Cdd:cd07129 156 AIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSR-RGGRALFDAAAARPEPIPFYAELGSVNPVFILPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 816 ALLEQVvnDVLVSAF-----GSAGQRCSA--LrVVHVQDEVYPRFMALLKGAMAE------LRVGMPERFDtdvgpvidk 882
Cdd:cd07129 235 ALAERG--EAIAQGFvgsltLGAGQFCTNpgL-VLVPAGPAGDAFIAALAEALAAapaqtmLTPGIAEAYR--------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 883 DALAVLQAHVAkmreAHTLIyqceLPSACNNGYFFAPAAFEIPSIR-----VLEKEVFGPILHVVRFNrkDLDAVIDAIN 957
Cdd:cd07129 303 QGVEALAAAPG----VRVLA----GGAAAEGGNQAAPTLFKVDAAAfladpALQEEVFGPASLVVRYD--DAAELLAVAE 372
|
410
....*....|..
gi 1606703614 958 ATGYGLTLGIHS 969
Cdd:cd07129 373 ALEGQLTATIHG 384
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
680-1012 |
1.75e-24 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 107.57 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 680 YTGERNELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGvLPSVMQLLPGKGE 759
Cdd:cd07133 90 FLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYF-DEDEVAVVTGGAD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 760 tVGAALVADPrIKAVMFTGSTDTANRInqtLAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSA 839
Cdd:cd07133 169 -VAAAFSSLP-FDHLLFTGSTAVGRHV---MRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 840 LRVVHVQDEVYPRFMALLKGAMAELRVGMPErfDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQC-ELPSACNNGYFFA 918
Cdd:cd07133 244 PDYVLVPEDKLEEFVAAAKAAVAKMYPTLAD--NPDYTSIINERHYARLQGLLEDARAKGARVIELnPAGEDFAATRKLP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 919 P-AAFEIP-SIRVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGA 996
Cdd:cd07133 322 PtLVLNVTdDMRVMQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHV 399
|
330
....*....|....*.
gi 1606703614 997 VVGLQPFGGEGLSGTG 1012
Cdd:cd07133 400 AQDDLPFGGVGASGMG 415
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
564-938 |
1.49e-23 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 105.94 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVSVTSPQNYREtigrVIEASKE--DVEWALSRAVE-GAAQWERVPVAERAAVINRYADLLEAHMPDFLALASL 640
Cdd:PRK11903 14 QAGSGAGTPLFDPVTGEE----LVRVSATglDLAAAFAFAREqGGAALRALTYAQRAALLAAIVKVLQANRDAYYDIATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 641 EAGKTLADGVAEVREAVDFCRYYAARACEMMEKPLALEGytgERNELSLHP-----------RGTVLCISPWNFPLAIFT 709
Cdd:PRK11903 90 NSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDG---EAVQLGKDPafqgqhvlvptRGVALFINAFNFPAWGLW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 710 GQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPS-VMQLLPGKGETVGAALVAdprIKAVMFTGSTDTANRI-- 786
Cdd:PRK11903 167 EKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGILPAgALSVVCGSSAGLLDHLQP---FDVVSFTGSAETAAVLrs 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 787 NQTLAARSgeiVPLIAETGGLNAMIV------DSSA---LLEQVVNDVLVSAfgsaGQRCSALRVVHVQDEVYPRFMALL 857
Cdd:PRK11903 244 HPAVVQRS---VRVNVEADSLNSALLgpdaapGSEAfdlFVKEVVREMTVKS----GQKCTAIRRIFVPEALYDAVAEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 858 KGAMAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIY---QCELPSACNN-GYFFAPAAFEIP----SIRV 929
Cdd:PRK11903 317 AARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFdggGFALVDADPAvAACVGPTLLGASdpdaATAV 396
|
....*....
gi 1606703614 930 LEKEVFGPI 938
Cdd:PRK11903 397 HDVEVFGPV 405
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
564-938 |
1.63e-22 |
|
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: 102.73 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 564 RAGSGVEVSVTSPQNyRETIGRViEASKEDVEWALSRAVE-GAAQWERVPVAERAAVINRYADLLEAHMPDFLALaSLEA 642
Cdd:cd07128 10 HAGTGDGRTLHDAVT-GEVVARV-SSEGLDFAAAVAYAREkGGPALRALTFHERAAMLKALAKYLMERKEDLYAL-SAAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 643 GKTLADGVAEVREAVDFCRYYAARACEMME-KPLALEGytgERNELS----------LHPRGTV-LCISPWNFPLAIFTG 710
Cdd:cd07128 87 GATRRDSWIDIDGGIGTLFAYASLGRRELPnAHFLVEG---DVEPLSkdgtfvgqhiLTPRRGVaVHINAFNFPVWGMLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 711 QAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPS-VMQLLPGKGETVGAALvaDPRiKAVMFTGSTDTAN--RIN 787
Cdd:cd07128 164 KFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLPEgALQLICGSVGDLLDHL--GEQ-DVVAFTGSAATAAklRAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 788 QTLAARSgeiVPLIAETGGLNAMI-----VDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQDEVYPRFMALLKGAMA 862
Cdd:cd07128 241 PNIVARS---IRFNAEADSLNAAIlgpdaTPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 863 ELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIY----QCELPSACNN-GYFFAP----AAFEIPSIRVLEKE 933
Cdd:cd07128 318 KVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFggpdRFEVVGADAEkGAFFPPtlllCDDPDAATAVHDVE 397
|
....*
gi 1606703614 934 VFGPI 938
Cdd:cd07128 398 AFGPV 402
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
691-1012 |
3.48e-22 |
|
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: 100.76 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 691 PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEqtplIAAFAVRLMREagVLPSVMQ------LLPGKGETvgaA 764
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE----VSPATAKLLAE--LIPKYLDkecypvVLGGVEET---T 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 765 LVADPRIKAVMFTGSTDTAnRINQTLAARsgEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVH 844
Cdd:cd07132 171 ELLKQRFDYIFYTGSTSVG-KIVMQAAAK--HLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 845 VQDEVYPRFMALLKGAMAELrVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTliYQCElPSACnngyFFAPAafeI 924
Cdd:cd07132 248 CTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIG--GQTD-EKER----YIAPT---V 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 925 -----PSIRVLEKEVFGPILHVVrfNRKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVG 999
Cdd:cd07132 317 ltdvkPSDPVMQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLD 394
|
330
....*....|...
gi 1606703614 1000 LQPFGGEGLSGTG 1012
Cdd:cd07132 395 SLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
691-1012 |
1.60e-21 |
|
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: 98.64 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 691 PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMrEAGVLPSVMQLLPGkGETVGAALVaDPR 770
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEYLDTKAIKVIEG-GVPETTALL-EQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 771 IKAVMFTGSTDTAnRInqTLAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGS-AGQRCSALRVVHVQDEV 849
Cdd:cd07137 178 WDKIFFTGSPRVG-RI--IMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEESF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 850 YPRFMALLKGAMAELrVGMPERFDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPSacnNGYFFAPAAFEIPSIR- 928
Cdd:cd07137 255 APTLIDALKNTLEKF-FGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDE---KNLYIEPTILLDPPLDs 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 929 -VLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRiNETVE-RIHKRMKVGNCYVNRNMIGAVVGLQPFGGE 1006
Cdd:cd07137 331 sIMTEEIFGPLLPIITV--KKIEESIEIINSRPKPLAAYVFTK-NKELKrRIVAETSSGGVTFNDTVVQYAIDTLPFGGV 407
|
....*.
gi 1606703614 1007 GLSGTG 1012
Cdd:cd07137 408 GESGFG 413
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
691-1012 |
2.08e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 89.79 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 691 PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAvrlmreAGVLPSVMQLLPGK----GETVGAALV 766
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFL------AANIPKYLDSKAVKviegGPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 767 ADPRIKaVMFTGSTDTAnRINQTLAARsgEIVPLIAETGGLNAMIVD---SSALLEQVVNDVLVSAFGS-AGQRCSALRV 842
Cdd:PLN02203 182 QHKWDK-IFFTGSPRVG-RIIMTAAAK--HLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAIDY 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 843 VHVQDEVYPRFMALLKGAMAELRVGMPERFDTdVGPVIDKDALAVLQAHVAKMREAHTLIYqcelpsacnNGYFFAPAAF 922
Cdd:PLN02203 258 VLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRVAASIVH---------GGSIDEKKLF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 923 EIPSI--------RVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRiNETVE-RIHKRMKVGNCYVNRNM 993
Cdd:PLN02203 328 IEPTIllnppldsDIMTEEIFGPLLPIITV--KKIEDSIAFINSKPKPLAIYAFTN-NEKLKrRILSETSSGSVTFNDAI 404
|
330
....*....|....*....
gi 1606703614 994 IGAVVGLQPFGGEGLSGTG 1012
Cdd:PLN02203 405 IQYACDSLPFGGVGESGFG 423
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
691-1012 |
2.92e-18 |
|
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: 88.72 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 691 PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREagVLP----SVMQllpGKGETVGAALv 766
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEE--TFDeeyvAVVE---GGVEENQELL- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 767 aDPRIKAVMFTGSTdtanrinqtlaaRSGEIV---------PLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRC 837
Cdd:cd07136 174 -DQKFDYIFFTGSV------------RVGKIVmeaaakhltPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 838 SALRVVHVQDEVYPRFMALLKGAMAELRVGMPERfDTDVGPVIDkdalavlQAH---VAKMREAHTLIYQCElpsACNNG 914
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIIN-------EKHfdrLAGLLDNGKIVFGGN---TDRET 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 915 YFFAPAAFEIPSI--RVLEKEVFGPILHVVRFnrKDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRN 992
Cdd:cd07136 310 LYIEPTILDNVTWddPVMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDT 387
|
330 340
....*....|....*....|
gi 1606703614 993 MIGAVVGLQPFGGEGLSGTG 1012
Cdd:cd07136 388 IMHLANPYLPFGGVGNSGMG 407
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
644-808 |
7.11e-18 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 89.54 E-value: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 644 KTLADGVAEVREAVDFCRYYAARACEMMEKPLALEGYTGERNELSLHPRGTVLCISPwnfPLAIFTGQAVAALVTGNAVI 723
Cdd:PRK11905 1031 RDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVAD---TEEALLRQLAAALATGNVAV 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 724 AKPAEQTPLIAAFavrlmreagvLPSvmqlLPGKGETVGAALVADPRIKAVMFTGSTDTANRINQTLAARSGEIVPLIAE 803
Cdd:PRK11905 1108 VAADSGLAAALAD----------LPG----LVAARIDWTQDWEADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAA 1173
|
....*
gi 1606703614 804 TGGLN 808
Cdd:PRK11905 1174 EPTDA 1178
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
686-1016 |
1.42e-17 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 87.02 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 686 ELSLHPRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMrEAGVLPSVMQLLPGKGETVGAAL 765
Cdd:PLN02174 107 EIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 766 vaDPRIKAVMFTGSTDTANRInqtLAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFG-SAGQRCSALRVVH 844
Cdd:PLN02174 186 --EQKWDKIFYTGSSKIGRVI---MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYIL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 845 VQDEVYPRFMALLKGAMAELRVGMPERfDTDVGPVIDKDALAVLQAHVAKMREAHTLIYQCELPsacNNGYFFAPAA-FE 923
Cdd:PLN02174 261 TTKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKD---RENLKIAPTIlLD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 924 IP-SIRVLEKEVFGPILHVVRFNrkDLDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVNRNMIGAVVGLQP 1002
Cdd:PLN02174 337 VPlDSLIMSEEIFGPLLPILTLN--NLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLP 414
|
330
....*....|....
gi 1606703614 1003 FGGEGLSGTGPKAG 1016
Cdd:PLN02174 415 FGGVGESGMGAYHG 428
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
633-969 |
1.62e-15 |
|
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: 80.62 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 633 DFLA-LASLEAGKTLADGVAEVREAVDFCRYYAARACEMMEKPLALEG-YTGERNELSLHPRGTVLCISPWNFPLAIFTG 710
Cdd:cd07126 82 DFFArLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPGdHQGQQSSGYRWPYGPVAIITPFNFPLEIPAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 711 QAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGETVGAALV-ADPRIkaVMFTGSTDTANRINQT 789
Cdd:cd07126 162 QLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANPRM--TLFTGSSKVAERLALE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 790 LAARsgeiVPLiaETGGLNAMIvdssaLLEQVVNDVLVS------AFGSAGQRCSALRVVHVQDE-VYPRFMALLKgAMA 862
Cdd:cd07126 240 LHGK----VKL--EDAGFDWKI-----LGPDVSDVDYVAwqcdqdAYACSGQKCSAQSILFAHENwVQAGILDKLK-ALA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 863 ELRvgmpERFDTDVGPVIDKDALAVLqAHVAKM----------------REAHTLIYQCELPSAcnngyFFAPaafeIPS 926
Cdd:cd07126 308 EQR----KLEDLTIGPVLTWTTERIL-DHVDKLlaipgakvlfggkpltNHSIPSIYGAYEPTA-----VFVP----LEE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1606703614 927 IRVLE------KEVFGPILHVVRFNRKDLDAVIDAINATGYGLTLGIHS 969
Cdd:cd07126 374 IAIEEnfelvtTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVS 422
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
545-978 |
6.06e-15 |
|
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: 79.06 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 545 ASIEARMPFHFE-AAPMMDGRAGS-----GVEVSVTSPQNyretigrvieaskeDVEWALSRAVEGAAQWERVPVAERAA 618
Cdd:cd07127 45 AAFEALLGQRFDlDQPGASGWVGGevspyGVELGVTYPQC--------------DPDALLAAARAAMPGWRDAGARARAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 619 VINRYADLLEAHMPDFLALASLEAGKTL-----ADGV-AEVR--EAVDfcryYAARacEMMEKPLALEGYT--GERNELS 688
Cdd:cd07127 111 VCLEILQRLNARSFEMAHAVMHTTGQAFmmafqAGGPhAQDRglEAVA----YAWR--EMSRIPPTAEWEKpqGKHDPLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 689 LH------PRGTVLCIS-----PWNFPLAIFtgqavAALVTGNAVIAKPAEQTPLIAAFAVRLMR----EAGVLPSVMQL 753
Cdd:cd07127 185 MEktftvvPRGVALVIGcstfpTWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVQVARevlaEAGFDPNLVTL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 754 LP-GKGETVGAALVADPRIKAVMFTGSTDTANRINQTlaARSGEivpLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGS 832
Cdd:cd07127 260 AAdTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEAN--ARQAQ---VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 833 AGQRCSALRVVHVQ-------------DEVYPRFMALLKGAMAElrvgmPERFDTDVGPVIDKDALAVlqahVAKMREAH 899
Cdd:cd07127 335 SGQMCTTPQNIYVPrdgiqtddgrksfDEVAADLAAAIDGLLAD-----PARAAALLGAIQSPDTLAR----IAEARQLG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 900 TLIyqceLPSACNNGYFFAPAAFEIPSI--------RVLEKEVFGPILHVVRFNrkDLDAVID---AINATGYGLTLGIH 968
Cdd:cd07127 406 EVL----LASEAVAHPEFPDARVRTPLLlkldasdeAAYAEERFGPIAFVVATD--STDHSIElarESVREHGAMTVGVY 479
|
490
....*....|
gi 1606703614 969 SRINETVERI 978
Cdd:cd07127 480 STDPEVVERV 489
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
125-476 |
1.26e-12 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 71.27 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 125 FVNAATWALMLTGKVLSPERIDN--DLGRSLFRLANRtgeGVIRKAVEKAMR-IMSKQFVMGRTIGEALNRARKKEALGY 201
Cdd:PLN02681 33 FAGLSTSELLRSLLVLQLCAIGPlvDLGEWLLTSPLM---VLGRAIVLALVKaTFYSHFCAGEDAEEAARTVRRLWELGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 202 RYSYDMLGEAALTAVDAARYLEAYMDAIDSIGAQVKGKGDVYT------NPGI------------------------SIK 251
Cdd:PLN02681 110 GGILDYAAEDAGDNAACDRNLEKFLAAIRAAATLPPSSSSAAVkitalcPPSLlervsdllrwqdrdpngklpwkqwSFP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 252 LSALH-PRYQ--------ESQYESVMATLPDNLLALCLRAKAANIGLTIDAEESeRLEISLDVI--------EKVFKNPA 314
Cdd:PLN02681 190 LFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYT-SLQPAIDYItydlarefNKGKDRPI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 315 LNGwngfgmAVQSYQKRAFYLLDWVAGLARGQNRRMNVRLIKGAYWDSEIKKAQMQGlTEYPVFTRKVFTDVSFQACAKK 394
Cdd:PLN02681 269 VYG------TYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLG-VPSPVHDTIQDTHACYNRCAEF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 395 IL---------TMtdtiypqFATHNACSV---ATILEMCGSYRD---FEFQCLHGMGNELyaeivpANRL---GIPCRIY 456
Cdd:PLN02681 342 LLekasngdgeVM-------LATHNVESGelaAAKMNELGLHKGdprVQFAQLLGMSDNL------SFGLgnaGFRVSKY 408
|
410 420
....*....|....*....|
gi 1606703614 457 APVGTHEDLLPYLVRRLLEN 476
Cdd:PLN02681 409 LPYGPVEEVIPYLLRRAEEN 428
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
675-809 |
1.92e-12 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 71.89 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 675 LALEGYTGERNELSLHPRGTVLCISPwnfPLAIFTGQAVAALVTGNAVIAkpaeqtpliaafavrlmreagVLPSVMQLL 754
Cdd:COG4230 1046 LTLPGPTGERNTLTLRPRGRVLCLAD---SLEALLAQLAAALATGNRAVV---------------------AADLALAGL 1101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1606703614 755 PGkgetvgaalVADPRIKAVMFTGstdTANRINQTLAARSGEIVPLIA----------ETGGlNA 809
Cdd:COG4230 1102 PA---------VLLPPFDAVLFEG---RLRALRQALAARDGAIVPVIDagydlerlleEAGG-NA 1153
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
613-870 |
2.56e-10 |
|
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: 63.78 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 613 VAERAAVINRYADLLEAHMPDFLALASLEAGKTLADGVA-----------EVREAVDFCRYYAARACEMMEKPLALEGYT 681
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIAnwiammgcsesKLYKNIDTERGITASVGHIQDVLLPDNGET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 682 GERNElslhPRGTVLCISPWNFPLAIFTgQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREA---GVLPSVMQLLPGKG 758
Cdd:cd07077 95 YVRAF----PIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 759 ETVGAALVADPRIKAVMFTGSTDTANRinqtlAARSGEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFgSAGQRCS 838
Cdd:cd07077 170 DELAEELLSHPKIDLIVATGGRDAVDA-----AVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACA 243
|
250 260 270
....*....|....*....|....*....|..
gi 1606703614 839 ALRVVHVQDEVYPRFMALLKGAMAELRVGMPE 870
Cdd:cd07077 244 SEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQ 275
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
632-798 |
8.24e-09 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 59.99 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 632 PDFLALASLEAGKTLADGVAEVR--EAVDFCRYYAARAceMMEKPLALEGYTGERNELSLHPRGTVLCISPWNFPLAIft 709
Cdd:PRK11809 1128 VDAQLRAALLAPLTALREWAAERepELAALCDQYAELA--QAGTTRLLPGPTGERNTYTLLPRERVLCLADTEQDALT-- 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 710 gQAVAALVTGNAVIakpAEQTPLIAAFAVRLmrEAGVLPSVmQLLPgkgetvgAALVADPRIKAVMFTGSTDTANRINQT 789
Cdd:PRK11809 1204 -QLAAVLAVGSQAL---WPDDALHRALVAAL--PAAVQARI-QLAK-------DWQLADQPFDAVLFHGDSDQLRALCEQ 1269
|
....*....
gi 1606703614 790 LAARSGEIV 798
Cdd:PRK11809 1270 VAQRDGPIV 1278
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
13-59 |
8.45e-09 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 52.08 E-value: 8.45e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1606703614 13 PLREAINSAFRAEEAHYMDMLIKAAQLSTSDVESIRKRAMKLVEQVR 59
Cdd:pfam18327 2 PLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
691-990 |
6.47e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 46.49 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 691 PRGTVLCISPWNFPLAIFTGQAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREAGVLPSVMQLLPGKGET----VGAALV 766
Cdd:cd07081 95 PIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNpsieLAQRLM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 767 ADPRIKAVMFTGSTDTANrinqtlAARSgEIVPLIAETGGLNAMIVDSSALLEQVVNDVLVSAFGSAGQRCSALRVVHVQ 846
Cdd:cd07081 175 KFPGIGLLLATGGPAVVK------AAYS-SGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 847 DEVYPRFMALLKGAMAELRVGmpERFDTdVGPVIDKDAlAVLQAHVAkmREAHTLIyqcelpsacnngyffAPAAFEIP- 925
Cdd:cd07081 248 DSVYDEVMRLFEGQGAYKLTA--EELQQ-VQPVILKNG-DVNRDIVG--QDAYKIA---------------AAAGLKVPq 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 926 SIRVLEKEV-------------FGPILHVVRF-NRKDLDAVIDA-INATGYGLTLGIHSRINETVERIHK---RMKVGNC 987
Cdd:cd07081 307 ETRILIGEVtslaehepfahekLSPVLAMYRAaNFADADAKALAlKLEGGCGHTSAMYSDNIKAIENMNQfanAMKTSRF 386
|
...
gi 1606703614 988 YVN 990
Cdd:cd07081 387 VKN 389
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
706-990 |
2.23e-04 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 44.79 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 706 AIFTgqAVAALVTGNAVIAKPAEQTPLIAAFAVRLMREA----GVLPSVMQLLPGKGETVGAALVADPRIKAVMFTGSTd 781
Cdd:cd07122 112 AIFK--ALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGGP- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 782 tanrINQTLAARSGEivPLIAETGGLNAMIVDSSALLEQVVNDVLVS-AFGSaGQRCSALRVVHVQDEVYPRFMALLK-- 858
Cdd:cd07122 189 ----GMVKAAYSSGK--PAIGVGPGNVPAYIDETADIKRAVKDIILSkTFDN-GTICASEQSVIVDDEIYDEVRAELKrr 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 859 GA--MAELRVGMPERFDTDVGPVIDKDALAVLQAHVAKMreahtliyqcelpsacnngyffapAAFEIPS-IRVL----- 930
Cdd:cd07122 262 GAyfLNEEEKEKLEKALFDDGGTLNPDIVGKSAQKIAEL------------------------AGIEVPEdTKVLvaeet 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1606703614 931 ---EKEVF-----GPILHVVRFNRKD--LDAVIDAINATGYGLTLGIHSRINETVERIHKRMKVGNCYVN 990
Cdd:cd07122 318 gvgPEEPLsreklSPVLAFYRAEDFEeaLEKARELLEYGGAGHTAVIHSNDEEVIEEFALRMPVSRILVN 387
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