|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
8-1037 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1869.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 8 LSPSFIDRPLDELWQLISPLYMVDESKWLAELLPMARPSAEEKSQITTNATVLIERVRADKQAIQMIDALLLEYSLDTKE 87
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGGIDAFLQEYSLSTEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 88 GILLMCLAEALMRIPDAATADALIRDKLSVADWKSHLKNSDSTFVNASTWGLLLTGKVVSMDRKDTKSASSTISRLVNKV 167
Cdd:PRK11904 81 GIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADGTPSGVLKRLVNRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 168 SEPIIRQAMNQAMKIMGHQFVLGRNIAEAQKNGRPSRDKGFTYSFDMLGESALTTADAKKYFNDYIKAVESVGSNKYGND 247
Cdd:PRK11904 161 GEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 248 KTAAPTVSIKLSALHPRYEVANEARVMTEMHDTVLELLLRARDLDVGITIDAEEADRLELSLALFEKLYRHPRLQGWGKF 327
Cdd:PRK11904 241 LPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 328 GIVVQAYSKRALPTLIWLAALAKEQGDVIPLRLVKGAYWDTELKLSQQNGYDAYPVYTRKEATDVAYLACARFLLSEqiR 407
Cdd:PRK11904 321 GLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA--R 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 408 GCIYPQFASHNAHTVSAIATMAEHQEYEFQRLHGMGDALYNHALEIYGVDVRIYAPVGSHKDLLPYLVRRLLENGANSSF 487
Cdd:PRK11904 399 GAIYPQFATHNAHTVAAILEMAGHRGFEFQRLHGMGEALYDALLDAPGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 488 VHRLVDADCPIAELTEHPVDTLDSRPTLHNSLIPLPSKIF-AGRKNSCNINVDIISEVTPFNTELSLQMQKTWQAAPVVN 566
Cdd:PRK11904 479 VHRLVDPDVPIEELVADPVEKLRSFETLPNPKIPLPRDIFgPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPIIN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 567 GQvittelDNAKPVSAPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCH 646
Cdd:PRK11904 559 GE------GEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCV 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 647 KEAGKTIHDSLDEVREAVDFCRYYAMQAIENFSVAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAG 726
Cdd:PRK11904 633 REAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAG 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 727 NTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVAT 806
Cdd:PRK11904 713 NTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVP 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 807 LIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPV 886
Cdd:PRK11904 793 LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPV 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 887 IDLLAKNKLQAHIDKMRATSKLVGEVSLTDECNFGDFIAPIAFEINSINQLENEQFGPILHIVRYKAADLNNVIAEINAT 966
Cdd:PRK11904 873 IDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAINAT 952
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030906275 967 GFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRF-TKQVVS 1037
Cdd:PRK11904 953 GYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFaTEKTVT 1024
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
6-1033 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1482.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 6 DALSPSFidRPLDELWQLISPLYMVDESKWLAELLPMARPSAEEKSQITTNATVLIERVRADKQAiQMIDALLLEYSLDT 85
Cdd:PRK11905 3 QMFAPPF--RPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKG-TGVEALLQEYSLSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 86 KEGILLMCLAEALMRIPDAATADALIRDKLSVADWKSHLKNSDSTFVNASTWGLLLTGKVVSMDrkDTKSASSTISRLVN 165
Cdd:PRK11905 80 QEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTV--NDRGLSAALTRLIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 166 KVSEPIIRQAMNQAMKIMGHQFVLGRNIAEAQKNGRPSRDKGFTYSFDMLGESALTTADAKKYFNDYIKAVESVGSNKYG 245
Cdd:PRK11905 158 RLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 246 NDKTAAPTVSIKLSALHPRYEVANEARVMTEMHDTVLELLLRARDLDVGITIDAEEADRLELSLALFEKLYRHPRLQGWG 325
Cdd:PRK11905 238 RGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 326 KFGIVVQAYSKRALPTLIWLAALAKEQGDVIPLRLVKGAYWDTELKLSQQNGYDAYPVYTRKEATDVAYLACARFLLSEq 405
Cdd:PRK11905 318 GIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAA- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 406 iRGCIYPQFASHNAHTVSAIATMAE-HQEYEFQRLHGMGDALYNhalEIYGVD-----VRIYAPVGSHKDLLPYLVRRLL 479
Cdd:PRK11905 397 -RDVIYPQFATHNAQTLAAIYELAGgKGDFEFQCLHGMGEPLYD---QVVGKEklgrpCRIYAPVGTHETLLAYLVRRLL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 480 ENGANSSFVHRLVDADCPIAELTEHPVDTLDSRPTLHNSLIPLPSKIFA-GRKNSCNINVDIISEVTPFNTELSLQMQKT 558
Cdd:PRK11905 473 ENGANSSFVNRIVDENVPVEELIADPVEKVAAMGVAPHPQIPLPRDLYGpERRNSKGLDLSDEATLAALDEALNAFAAKT 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 559 WQAAPVVNGQVITtelDNAKPVSAPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANL 638
Cdd:PRK11905 553 WHAAPLLAGGDVD---GGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHM 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 639 AELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFsvaknqvrfdgiaQQVTRQGQGVFVCISPWNFPLAIFLGQ 718
Cdd:PRK11905 630 PELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLL-------------NGPGHKPLGPVVCISPWNFPLAIFTGQ 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 719 VAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALA 798
Cdd:PRK11905 697 IAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLA 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 799 KRDTNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQH 878
Cdd:PRK11905 777 KRSGPPVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWR 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 879 HHTDVGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTDECNFGDFIAPIAFEINSINQLENEQFGPILHIVRYKAADLNN 958
Cdd:PRK11905 857 LSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDR 936
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030906275 959 VIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRFTK 1033
Cdd:PRK11905 937 VIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVR 1011
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
6-1034 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1310.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 6 DALSPSFIDRPLDELWQLISPLYMVDEskwLAELLPMARPSAEEKSQITTNATVLIERVRADKQAIQMIDALLLEYSLDT 85
Cdd:COG4230 2 PFALFAPLLRPALPLRAAIAAAERAEE---LLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 86 KEGILLMCLAEALMRIPDAATADALIRDKLSVADWKSHLKNSDSTFVNASTWGLLLTGKVVSMDRKDTKSASSTISRLVN 165
Cdd:COG4230 79 LSSEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 166 KVSEPIIRQAMNQAMKIMGHQFVLGRNIAEAQKNGRPSRDKGFTYSFDMLGESALTTADAKKYFNDYIKAVESVGSNKYG 245
Cdd:COG4230 159 RLGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 246 NDKTAAPTVSIKLSALHPRYEVANEARVMTEMHDTVLELLLRARDLDVGITIDAEEADRLELSLALFEKLYRHPRLQGWG 325
Cdd:COG4230 239 GSGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 326 KFGIVVQAYSKRALPTLIWLAALAKEQGDVIPLRLVKGAYWDTELKLSQQNGYDAYPVYTRKEATDVAYLACARFLLSEQ 405
Cdd:COG4230 319 GGGGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 406 IR--GCIYPQFASHNAHTVSAIATMAEHQEYEFQRLHGMGDALYNHAL-EIYGVDVRIYAPVGSHKDLLPYLVRRLLENG 482
Cdd:COG4230 399 LAaqPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVGrGKLGRPCRIYAPVGSHEDLLAYLVRRLLENG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 483 ANSSFVHRLVDADCPIAELTEHPVDTLDSRPTLHNSLIPLPSKIF-AGRKNSCNINVDIISEVTPFNTELSLQMQKTWQA 561
Cdd:COG4230 479 ANSSFVNRIADEDVPVEELIADPVEKARALGGAPHPRIPLPRDLYgPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 562 APVVNGQVITTEldnAKPVSAPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAEL 641
Cdd:COG4230 559 APLIAGEAASGE---ARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAEL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 642 VALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFsvaknqvrfdgiAQQVTRQGQGVFVCISPWNFPLAIFLGQVAA 721
Cdd:COG4230 636 MALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLF------------AAPTVLRGRGVFVCISPWNFPLAIFTGQVAA 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 722 ALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRD 801
Cdd:COG4230 704 ALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARD 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 802 TNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHT 881
Cdd:COG4230 784 GPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLST 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 882 DVGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTDECNFGDFIAPIAFEINSINQLENEQFGPILHIVRYKAADLNNVIA 961
Cdd:COG4230 864 DVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVID 943
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030906275 962 EINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRFTKQ 1034
Cdd:COG4230 944 AINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATE 1016
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
39-1030 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1183.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 39 LLPMARPSAEEKSQITTNATVLIERVRADKQA---IQMIDALLLEYSLDTKEGILLMCLAEALMRIPDAATADALIRDKL 115
Cdd:PRK11809 110 LLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAggrAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 116 SVADWKSHLKNSDSTFVNASTWGLLLTGKVVSmdRKDTKSASSTISRLVNKVSEPIIRQAMNQAMKIMGHQFVLGRNIAE 195
Cdd:PRK11809 190 SNGNWQSHLGRSPSLFVNAATWGLLFTGKLVS--THNEASLSSSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 196 AQKNGRPSRDKGFTYSFDMLGESALTTADAKKYFNDYIKAVESVGSNKYGNDKTAAPTVSIKLSALHPRYEVANEARVMT 275
Cdd:PRK11809 268 ALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVME 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 276 EMHDTVLELLLRARDLDVGITIDAEEADRLELSLALFEKLYRHPRLQGWGKFGIVVQAYSKRAlPTLI-WLAALAKEQGD 354
Cdd:PRK11809 348 ELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRC-PFVIdYLIDLARRSRR 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 355 VIPLRLVKGAYWDTELKLSQQNGYDAYPVYTRKEATDVAYLACARFLLSEQirGCIYPQFASHNAHTVSAIATMAEHQ-- 432
Cdd:PRK11809 427 RLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVP--NLIYPQFATHNAHTLAAIYHLAGQNyy 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 433 --EYEFQRLHGMGDALYNhalEIYGVDV--------RIYAPVGSHKDLLPYLVRRLLENGANSSFVHRLVDADCPIAELT 502
Cdd:PRK11809 505 pgQYEFQCLHGMGEPLYE---QVVGKVAdgklnrpcRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELV 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 503 EHPVDTLDSRPTLHNSL------IPLPSKIFA-GRKNSCNINVDIISEVTPFNTELSLQMQKTWQAAPVVNGQVITTEld 575
Cdd:PRK11809 582 ADPVEAVEKLAQQEGQLglphpkIPLPRDLYGkGRANSAGLDLANEHRLASLSSALLASAHQKWQAAPMLEDPVAAGE-- 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 576 nAKPVSAPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHD 655
Cdd:PRK11809 660 -MSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSN 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 656 SLDEVREAVDFCRYYAMQAIENFSvakNQvrfdgiaqqvTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAE 735
Cdd:PRK11809 739 AIAEVREAVDFLRYYAGQVRDDFD---ND----------THRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAE 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 736 QTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKR-DTNVAT--LIAETG 812
Cdd:PRK11809 806 QTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRlDPQGRPipLIAETG 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 813 GQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAK 892
Cdd:PRK11809 886 GQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAK 965
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 893 NKLQAHIDKMRATSKLVGEVSLTDECN--FGDFIAPIAFEINSINQLENEQFGPILHIVRYKAADLNNVIAEINATGFGL 970
Cdd:PRK11809 966 ANIERHIQAMRAKGRPVFQAARENSEDwqSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQINASGYGL 1045
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 971 TMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYR 1030
Cdd:PRK11809 1046 TLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
483-1031 |
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: 727.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 483 ANSSFVHRLVDADCPIAeltehpvdtldsrptlhnsliplpskifagrknscninvdiisevtPFNTELSLQMQKTWQAA 562
Cdd:cd07125 1 ANSSFVNRIFDLEVPLE----------------------------------------------ALADALKAFDEKEWEAI 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 563 PVVNGQVITTelDNAKPVSAPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELV 642
Cdd:cd07125 35 PIINGEETET--GEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 643 ALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFSVAKNQVRFDGIaQQVTRQGQGVFVCISPWNFPLAIFLGQVAAA 722
Cdd:cd07125 113 ALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGEL-NGLELHGRGVFVCISPWNFPLAIFTGQIAAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 723 LVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDT 802
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 803 NVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTD 882
Cdd:cd07125 272 PILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 883 VGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTDecNFGDFIAPIAFEINSINQLENEQFGPILHIVRYKAADLNNVIAE 962
Cdd:cd07125 352 VGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDD--GNGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEAIED 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 963 INATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRF 1031
Cdd:cd07125 430 INATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRF 498
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
529-1033 |
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: 700.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 529 GRKNSCNINVDIISEVTPFNTELSLQMQKTWQAAPVVNGQVITTelDNAKPVSAPYDRRIHVGQVLWSTPAEVTTALDTA 608
Cdd:TIGR01238 6 GRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKAD--GEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 609 ADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFSvaknqvrfd 688
Cdd:TIGR01238 84 QQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLG--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 689 giaqQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAV 768
Cdd:TIGR01238 155 ----EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 769 GSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALR 848
Cdd:TIGR01238 231 GAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 849 VLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTD--ECNFGDFIAP 926
Cdd:TIGR01238 311 VLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDsrACQHGTFVAP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 927 IAFEINSINQLENEQFGPILHIVRYKAADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVG 1006
Cdd:TIGR01238 391 TLFELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVG 470
|
490 500
....*....|....*....|....*..
gi 2030906275 1007 VQPFGGQGLSGTGPKAGGPHYLYRFTK 1033
Cdd:TIGR01238 471 VQPFGGQGLSGTGPKAGGPHYLYRLTQ 497
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
43-1035 |
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: 647.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 43 ARPSAEEKSQITTNATVLIERVRAdkQAIQMIDALLLEYSLDTKEGILLMCLAEALMRIPDAATADALIRDKLSvadwks 122
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRA--APEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 123 hlkNSDSTFVNASTWGLLLTgkvvsmdrkdtksasstisrLVNKVSEPIIRQAMNQAMKIMGHQFVLGRNIAEAQKNGRP 202
Cdd:COG0506 75 ---KSPSFLVNASTWGLMLT--------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 203 SRDKGFTYSFDMLGESALTTADAKKYFNDYIKAVESVGSNKYGNdktaaPTVSIKLSALHPRYEVANEARVMTEMHDTVL 282
Cdd:COG0506 132 LRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAGVDR-----PGVSVKLSALGPRYSPAQRERVVEELLERLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 283 ELLLRARDLDVGITIDAEEADRLELSLALFEKLYRHPRLQGWGKFGIVVQAYSKRALPTLIWLAALAKEQGDVIPLRLVK 362
Cdd:COG0506 207 PLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 363 GAYWDTELKLSQQNGYDaYPVYTRKEATDVAYLACARFLLSEqiRGCIYPQFASHNAHTVSAIATMAEHQ-----EYEFQ 437
Cdd:COG0506 287 GAYWDPEIVRAQVHGWP-YPVFTRKADTDANYLRCARKLLEA--GDAIYPQFATHNARTIAAALALAGERgrppdRFEFQ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 438 RLHGMGDALYNHALEIYGVDVRIYAPVGSHKDLLPYLVRRLLENGANSSFVHRLVDADCPIAELTEHPVDTLDSRPTLHN 517
Cdd:COG0506 364 MLYGMGEDLQRALAAVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 518 SLIPLPSKIFAGRKNSCNINVDIISEVTPFNTELSLQMQKTWQAAPVVNGQVITTE-LDNAKPVSAPYDRRIHVGQVLWS 596
Cdd:COG0506 444 PTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAaAAAAAVAVVPAAAAAVVAAAAAA 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 597 TPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAiE 676
Cdd:COG0506 524 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAA-A 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 677 NFSVAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKE 756
Cdd:COG0506 603 ARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGG 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 757 AVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSA 836
Cdd:COG0506 683 GVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAA 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 837 FASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTD 916
Cdd:COG0506 763 SASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPL 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 917 ECNFGDFIAPIAFEINSINQLENEQFGPILHIVRYKAADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQI-RVGNCY 995
Cdd:COG0506 843 VPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGgGGGGGG 922
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 2030906275 996 INRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRFTKQV 1035
Cdd:COG0506 923 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAA 962
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
559-1032 |
1.42e-167 |
|
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: 501.34 E-value: 1.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 559 WQAAPVVNGQVITTELDNAKPVSaPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANL 638
Cdd:cd07083 16 GRAYPLVIGGEWVDTKERMVSVS-PFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 639 AELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFSVAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQ 718
Cdd:cd07083 95 RELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 719 VAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALA 798
Cdd:cd07083 175 IVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 799 KRDTNVAT---LIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGL 875
Cdd:cd07083 255 RLAPGQTWfkrLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 876 PQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTDecNFGDFIAPIAFEINS--INQLENEQFGPILHIVRYKA 953
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLE--GEGYFVAPTVVEEVPpkARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 954 ADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRFT 1032
Cdd:cd07083 413 DDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFL 491
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
196-490 |
3.64e-145 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 435.00 E-value: 3.64e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 196 AQKNGRPSRDKGFTYSFDMLGESALTTADAKKYFNDYIKAVESVGSNKYGNDKTAAPTVSIKLSALHPRYEVANEARVMT 275
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 276 EMHDTVLELLLRARDLDVGITIDAEEADRLELSLALFEKLYRHPRLQGWGKFGIVVQAYSKRALPTLIWLAALAKEQGDV 355
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 356 IPLRLVKGAYWDTELKLSQQNGYDaYPVYTRKEATDVAYLACARFLLSEqiRGCIYPQFASHNAHTVSAIATMAEHQ--- 432
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQGGWP-YPVFTRKEATDANYEACARFLLEN--HDRIYPQFATHNARSVAAALALAEELgip 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 433 --EYEFQRLHGMGDALYNHALEIyGVDVRIYAPVGSHKDLLPYLVRRLLENGANSSFVHR 490
Cdd:pfam01619 238 prRFEFQQLYGMGDNLSFALVAA-GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
565-1032 |
4.06e-127 |
|
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: 395.26 E-value: 4.06e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVAL 644
Cdd:COG1012 10 IGGEWVAAASGETFDVINPATGEV-LARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 645 CHKEAGKTIHDSLDEVREAVDFCRYYAmQAIENFSVAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALV 724
Cdd:COG1012 89 LTLETGKPLAEARGEVDRAADFLRYYA-GEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 725 AGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNV 804
Cdd:COG1012 168 AGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE---NL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 805 ATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVG 884
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 885 PVIDLLAKNKLQAHIDKMRATS-KLV--GEVSLTDEcnfGDFIAPIAFEI----NSINQleNEQFGPILHIVRYKaaDLN 957
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGaELLtgGRRPDGEG---GYFVEPTVLADvtpdMRIAR--EEIFGPVLSVIPFD--DEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030906275 958 NVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINrDQVGAVVGVQPFGGQGLSGTGPKaGGPHYLYRFT 1032
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWIN-DGTTGAVPQAPFGGVKQSGIGRE-GGREGLEEYT 470
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
563-1037 |
3.77e-125 |
|
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: 391.20 E-value: 3.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 563 PVVNGQVITTEldnAK-PVSAPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAEL 641
Cdd:cd07124 35 LVIGGKEVRTE---EKiESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 642 VALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFSVAKNQVRfdGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAA 721
Cdd:cd07124 112 AAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVP--GEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 722 ALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRD 801
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 802 ---TNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQH 878
Cdd:cd07124 270 pgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 879 HHTDVGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTDECNFGDFIAPIAFE-INSINQLENEQ-FGPILHIVRYKaaDL 956
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFAdVPPDHRLAQEEiFGPVLAVIKAK--DF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 957 NNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRFTK-QV 1035
Cdd:cd07124 428 DEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQpKT 507
|
..
gi 2030906275 1036 VS 1037
Cdd:cd07124 508 VT 509
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
604-1032 |
2.36e-117 |
|
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: 367.69 E-value: 2.36e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 604 ALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFSVAKN 683
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 684 QVRFDGIAQqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPG 763
Cdd:cd07078 83 SPDPGELAI-VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 764 GGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVAtliAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQR 843
Cdd:cd07078 162 DGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVT---LELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 844 CSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRAT-SKLV--GEVSLTDEcnf 920
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEgAKLLcgGKRLEGGK--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 921 GDFIAPIAFEINSINQL--ENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINR 998
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....
gi 2030906275 999 DQVGAVVGvQPFGGQGLSGTGpKAGGPHYLYRFT 1032
Cdd:cd07078 394 YSVGAEPS-APFGGVKQSGIG-REGGPYGLEEYT 425
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
579-1032 |
3.32e-116 |
|
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: 365.70 E-value: 3.32e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 579 PVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD 658
Cdd:pfam00171 10 EVINPATGEV-IATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 659 EVREAVDFCRYYAMQAI----ENFSVAKNQVRFdgiaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPA 734
Cdd:pfam00171 89 EVDRAIDVLRYYAGLARrldgETLPSDPGRLAY------TRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 735 EQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQ 814
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ---NLKRVTLELGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 815 NTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNK 894
Cdd:pfam00171 240 NPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLER 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 895 LQAHIDkmRATSK----LVGEVSLTDEcnfGDFIAPIAFEiNSINQLE---NEQFGPILHIVRYKaaDLNNVIAEINATG 967
Cdd:pfam00171 320 VLKYVE--DAKEEgaklLTGGEAGLDN---GYFVEPTVLA-NVTPDMRiaqEEIFGPVLSVIRFK--DEEEAIEIANDTE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030906275 968 FGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVqPFGGQGLSGTGpKAGGPHYLYRFT 1032
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLEEYT 454
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
563-1031 |
5.86e-104 |
|
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: 335.30 E-value: 5.86e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 563 PVVNGQVITTEldnAKPVSA-PYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAEL 641
Cdd:TIGR01237 35 LVINGERVETE---NKIVSInPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 642 VALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIEnFSVAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAA 721
Cdd:TIGR01237 112 SALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIE-LAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 722 ALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAK-- 799
Cdd:TIGR01237 191 PIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKvq 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 800 -RDTNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQH 878
Cdd:TIGR01237 271 pGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 879 HHTDVGPVIDLLAKNKLQAHIDKMRATSKLVgeVSLTDECNFGDFIAPIAF-EINSINQLENEQ-FGPILHIVRykAADL 956
Cdd:TIGR01237 351 ADVYVGPVIDQKSFNKIMEYIEIGKAEGRLV--SGGCGDDSKGYFIGPTIFaDVDRKARLAQEEiFGPVVAFIR--ASDF 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030906275 957 NNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRF 1031
Cdd:TIGR01237 427 DEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALF 501
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
564-1034 |
1.59e-99 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 323.42 E-value: 1.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 564 VVNGQVITTEldnAKPVSA-PYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELV 642
Cdd:PRK03137 40 IIGGERITTE---DKIVSInPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 643 ALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIEnFSVAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAA 722
Cdd:PRK03137 117 AWLVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 723 LVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKR-- 800
Cdd:PRK03137 196 IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVqp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 801 -DTNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQhH 879
Cdd:PRK03137 276 gQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPE-D 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 880 HTDVGPVIDLLAKNKLQAHIDKMRATSKLV--GEvslTDEcNFGDFIAPIAF-EINSINQLENEQ-FGPILHIVryKAAD 955
Cdd:PRK03137 355 NAYMGPVINQASFDKIMSYIEIGKEEGRLVlgGE---GDD-SKGYFIQPTIFaDVDPKARIMQEEiFGPVVAFI--KAKD 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 956 LNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRFTKQ 1034
Cdd:PRK03137 429 FDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQA 507
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
606-1032 |
1.54e-95 |
|
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: 307.62 E-value: 1.54e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 606 DTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFSVAKNQV 685
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 686 RFDGIAQqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGG 765
Cdd:cd06534 81 DPGGEAY-VRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 766 AAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVAtliAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCS 845
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVT---LELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 846 ALRVLFVQEDIADRITSLIQGAMqelhiglpqhhhTDVGPvidllaknklqahidKMRAtsklvgevsltdecnfgdfia 925
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVTVL------------VDVDP---------------DMPI--------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 926 piafeinsinqLENEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVV 1005
Cdd:cd06534 269 -----------AQEEIFGPVLPVIRFKDEE--EAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP 335
|
410 420
....*....|....*....|....*..
gi 2030906275 1006 GvQPFGGQGLSGTGpKAGGPHYLYRFT 1032
Cdd:cd06534 336 E-APFGGVKNSGIG-REGGPYGLEEYT 360
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
577-1033 |
4.58e-81 |
|
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: 272.20 E-value: 4.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 577 AKPVSAPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS 656
Cdd:cd07097 15 GEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 657 LDEVREAVDFCRYYAMQAIENFSVAKNQVRfDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQ 736
Cdd:cd07097 95 RGEVTRAGQIFRYYAGEALRLSGETLPSTR-PGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 737 TSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVAtliAETGGQNT 816
Cdd:cd07097 174 TPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQ---LEMGGKNP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 817 MIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQ 896
Cdd:cd07097 251 LVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 897 AHIDKMRAT-SKLV-GEVSLTDECNfGDFIAPIAFEiNSINQL---ENEQFGPILHIVRYKaaDLNNVIAEINATGFGLT 971
Cdd:cd07097 331 RYIEIARSEgAKLVyGGERLKRPDE-GYYLAPALFA-GVTNDMriaREEIFGPVAAVIRVR--DYDEALAIANDTEFGLS 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030906275 972 MGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVqPFGGQGLSGTGPKAGGPHYLYRFTK 1033
Cdd:cd07097 407 AGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGEAALEFYTT 467
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
583-1032 |
4.37e-79 |
|
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: 266.91 E-value: 4.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 583 PYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVRE 662
Cdd:cd07131 21 PADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 663 AVDFCRYYAMQAIENF-----SVAKNQVRFdgiaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQT 737
Cdd:cd07131 101 AIDMAQYAAGEGRRLFgetvpSELPNKDAM------TRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 738 SLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVAtliAETGGQNTM 817
Cdd:cd07131 175 PACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVA---LEMGGKNPI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 818 IVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQA 897
Cdd:cd07131 252 IVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 898 HIDKMR---ATSKLVGEVSLTDECNFGDFIAPIAFEI--NSINQLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTM 972
Cdd:cd07131 332 YNEIGKeegATLLLGGERLTGGGYEKGYFVEPTVFTDvtPDMRIAQEEIFGPVVALIEVS--SLEEAIEIANDTEYGLSS 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 973 GIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVqPFGGQGLSGTGPKAGGPHYLYRFT 1032
Cdd:cd07131 410 AIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGTTALDAFT 468
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
564-1032 |
4.13e-77 |
|
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: 262.91 E-value: 4.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 564 VVNGQVITTelDNAKPVSAPYDRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANL-AELV 642
Cdd:cd07123 36 VIGGKEVRT--GNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 643 ALCHKEAGKTIHDS-LDEVREAVDFCRY--------YAMQAIENFSVAKNQVRFDGIaqqvtrqgQGVFVCISPWNFPlA 713
Cdd:cd07123 114 AATMLGQGKNVWQAeIDAACELIDFLRFnvkyaeelYAQQPLSSPAGVWNRLEYRPL--------EGFVYAVSPFNFT-A 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 714 IFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVI 793
Cdd:cd07123 185 IGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 794 NRALAkrdTNVAT------LIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGA 867
Cdd:cd07123 265 WKQIG---ENLDRyrtyprIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 868 MQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLvgEVSLTDECN--FGDFIAPIAFEINSINQ--LENEQFG 943
Cdd:cd07123 342 LKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEA--EIIAGGKCDdsVGYFVEPTVIETTDPKHklMTEEIFG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 944 PILHIVRYKAADLNNVIAEINATG-FGLTMGIHSRNERTYTDIERQIR--VGNCYINRDQVGAVVGVQPFGGQGLSGTGP 1020
Cdd:cd07123 420 PVLTVYVYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARASGTND 499
|
490
....*....|..
gi 2030906275 1021 KAGGPHYLYRFT 1032
Cdd:cd07123 500 KAGSPLNLLRWV 511
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
589-1031 |
3.51e-76 |
|
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: 257.88 E-value: 3.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 589 HVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHD--SLDEVREAVDF 666
Cdd:cd07093 9 VLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLarTRDIPRAAANF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 667 cRYYA----MQAIENFSVAKNQVRFdgiaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAA 742
Cdd:cd07093 89 -RFFAdyilQLDGESYPQDGGALNY------VLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 743 RTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVAtliAETGGQNTMIVDST 822
Cdd:cd07093 162 LLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVS---LELGGKNPNIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 823 ALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDllaknklQAHIDKM 902
Cdd:cd07093 239 ADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLIS-------KEHLEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 903 R----------ATSKLVGEVSLTDECNFGDFIAPIAFE-INS---INQleNEQFGPILHIVRYKAADlnNVIAEINATGF 968
Cdd:cd07093 312 LgyvelaraegATILTGGGRPELPDLEGGYFVEPTVITgLDNdsrVAQ--EEIFGPVVTVIPFDDEE--EAIELANDTPY 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030906275 969 GLTMGIHSRNERTYTDIERQIRVG----NCYINRDQvgavvgVQPFGGQGLSGTGPKagGPHYLYRF 1031
Cdd:cd07093 388 GLAAYVWTRDLGRAHRVARRLEAGtvwvNCWLVRDL------RTPFGGVKASGIGRE--GGDYSLEF 446
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
589-1032 |
6.43e-76 |
|
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: 256.98 E-value: 6.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 589 HVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCR 668
Cdd:cd07103 9 VIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 669 YYAMQA-------IENfsvaknqvRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIA 741
Cdd:cd07103 89 WFAEEArriygrtIPS--------PAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 742 ARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDS 821
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAAD---TVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 822 TALPEQVVRDVMRSAFASAGQRC-SALRVlFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHID 900
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCvCANRI-YVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 901 kmRATSK----LVGEVSLTDEcnfGDFIAP-----------IAFEinsinqlenEQFGPILHIVRYKaaDLNNVIAEINA 965
Cdd:cd07103 317 --DAVAKgakvLTGGKRLGLG---GYFYEPtvltdvtddmlIMNE---------ETFGPVAPIIPFD--TEDEVIARAND 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2030906275 966 TGFGLTMGIHSRNERTYTDIERQIRVGNCYINRdqvGAVVGVQ-PFGGQGLSGTGpKAGGPHYLYRFT 1032
Cdd:cd07103 381 TPYGLAAYVFTRDLARAWRVAEALEAGMVGINT---GLISDAEaPFGGVKESGLG-REGGKEGLEEYL 444
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
597-1023 |
2.89e-75 |
|
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: 256.34 E-value: 2.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 597 TPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQA-- 674
Cdd:cd07086 33 SPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICDYAVGLSrm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 675 IENFSVAKNQVRFDGIAQqvtRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEA--- 751
Cdd:cd07086 113 LYGLTIPSERPGHRLMEQ---WNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVlek 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 752 -GLPKEAVHLLPGGGAaVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVatlIAETGGQNTMIVDSTALPEQVVR 830
Cdd:cd07086 190 nGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRV---LLELGGNNAIIVMDDADLDLAVR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 831 DVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRA-TSKLV 909
Cdd:cd07086 266 AVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSqGGTVL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 910 GEVSLTDECNFGDFIAPIAFEINSiNQLE---NEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTytdIE 986
Cdd:cd07086 346 TGGKRIDGGEPGNYVEPTIVTGVT-DDARivqEETFAPILYVIKFD--SLEEAIAINNDVPQGLSSSIFTEDLRE---AF 419
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2030906275 987 RQIRVGNC-----YINRDQVGAVVGVqPFGGQGLSGTGPKAG 1023
Cdd:cd07086 420 RWLGPKGSdcgivNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
565-1019 |
3.44e-75 |
|
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: 255.96 E-value: 3.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTElDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSA-VPVAERAACLNKIADLLEANLAELVA 643
Cdd:cd07082 6 INGEWKESS-GKTIEVYSPIDGEV-IGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 644 LCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIEnfsVAKNQVRFD------GIAQQVTRQGQGVFVCISPWNFPLAIFLG 717
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKR---LDGDSLPGDwfpgtkGKIAQVRREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 718 QVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRAL 797
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 798 AKRDtnvatLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQ 877
Cdd:cd07082 241 PMKR-----LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 878 HHHTDVGPVIDLLAKNKLQAHIDKmrATSKlVGEVSLTDECNFGDFIAPIAFEINSIN-QLEN-EQFGPILHIVRYKaaD 955
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDD--AVAK-GATVLNGGGREGGNLIYPTLLDPVTPDmRLAWeEPFGPVLPIIRVN--D 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2030906275 956 LNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRD-QVGavVGVQPFGGQGLSGTG 1019
Cdd:cd07082 391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcQRG--PDHFPFLGRKDSGIG 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
565-1036 |
8.22e-72 |
|
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: 246.41 E-value: 8.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVAL 644
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEV-VATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 645 CHKEAGKTIHDSLDEVREAVDFCRYYAMQA-------IENFSVAKNQvrfdgiaqQVTRQGQGVFVCISPWNFPLAIFLG 717
Cdd:cd07088 81 IVEEQGKTLSLARVEVEFTADYIDYMAEWArriegeiIPSDRPNENI--------FIFKVPIGVVAGILPWNFPFFLIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 718 QVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRAL 797
Cdd:cd07088 153 KLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 798 AKrdtNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQ 877
Cdd:cd07088 233 AE---NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 878 HHHTDVGPVIdllakNKLQ-AHIDKMRATSKLVGEVSLT----DECNFGDFIAPIAFEI--NSINQLENEQFGPILHIVR 950
Cdd:cd07088 310 DAATDMGPLV-----NEAAlDKVEEMVERAVEAGATLLTggkrPEGEKGYFYEPTVLTNvrQDMEIVQEEIFGPVLPVVK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 951 YKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQpfGGQGLSGTGpKAGGPHYLYR 1030
Cdd:cd07088 385 FS--SLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLG-GADGKHGLEE 459
|
....*..
gi 2030906275 1031 FT-KQVV 1036
Cdd:cd07088 460 YLqTKVV 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
596-1023 |
9.05e-72 |
|
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: 245.92 E-value: 9.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 596 STPAEVTTALDTAADYF--PTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQ 673
Cdd:cd07114 16 ASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 674 A--IENFSVAknqVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEA 751
Cdd:cd07114 96 AdkIEGAVIP---VDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 752 GLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALPEQVVRD 831
Cdd:cd07114 173 GFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE---NLAPVTLELGGKSPNIVFDDADLDAAVNG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 832 VMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMR---ATSKL 908
Cdd:cd07114 250 VVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAReegARVLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 909 VGEVSLTDECNFGDFIAPIAFEINSINQ--LENEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNERTYTDIE 986
Cdd:cd07114 330 GGERPSGADLGAGYFFEPTILADVTNDMriAQEEVFGPVLSVIPFDDEE--EAIALANDSEYGLAAGIWTRDLARAHRVA 407
|
410 420 430
....*....|....*....|....*....|....*....
gi 2030906275 987 RQIRVGNCYIN--RdqvgAVVGVQPFGGQGLSGTGPKAG 1023
Cdd:cd07114 408 RAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
612-1017 |
9.25e-71 |
|
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: 242.18 E-value: 9.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 612 FPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVReavdfcryyAMQAIENFSVAKNQVRF---- 687
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVA---------AMAGKIDISIKAYHERTgera 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 688 --DGIAQQVTRQ-GQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGG 764
Cdd:cd07095 84 tpMAQGRAVLRHrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 765 GaAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATLiaETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRC 844
Cdd:cd07095 164 R-ETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILAL--EMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 845 SALRVLFVQED-IADRITSLIQGAMQELHIGLPQHHHTDVGP-VIDLLAKNKLQAHIDKMRATSKLVGEVSLTDEcnFGD 922
Cdd:cd07095 241 TCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPlIIAAAAARYLLAQQDLLALGGEPLLAMERLVA--GTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 923 FIAPIAFEINSINQLENEQ-FGPILHIVRYkaADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQV 1001
Cdd:cd07095 319 FLSPGIIDVTDAADVPDEEiFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT 396
|
410
....*....|....*.
gi 2030906275 1002 GAvVGVQPFGGQGLSG 1017
Cdd:cd07095 397 GA-SSTAPFGGVGLSG 411
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
590-1037 |
1.06e-70 |
|
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: 242.43 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRY 669
Cdd:cd07106 10 FASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 670 YAMQAIEnfsvakNQVRFDGIAQQV--TRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMEL 747
Cdd:cd07106 90 TASLDLP------DEVIEDDDTRRVelRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 748 MLEAgLPKEAVHLLPGGGaAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALPEQ 827
Cdd:cd07106 164 AQEV-LPPGVLNVVSGGD-ELGPALTSHPDIRKISFTGSTATGKKVMASAAK---TLKRVTLELGGNDAAIVLPDVDIDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 828 VVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVidllaKNKLQ--------AHI 899
Cdd:cd07106 239 VAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPV-----QNKMQydkvkelvEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 900 DKMRATSKLVGEVsltdECNFGDFIAP-IAFEINSINQL-ENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSR 977
Cdd:cd07106 314 KAKGAKVLAGGEP----LDGPGYFIPPtIVDDPPEGSRIvDEEQFGPVLPVLKYS--DEDEVIARANDSEYGLGASVWSS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2030906275 978 NERTYTDIERQIRVGNCYINrdQVGAVVGVQPFGGQGLSGTGpKAGGPHYLYRFTK-QVVS 1037
Cdd:cd07106 388 DLERAEAVARRLEAGTVWIN--THGALDPDAPFGGHKQSGIG-VEFGIEGLKEYTQtQVIN 445
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
579-1019 |
1.20e-70 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 242.50 E-value: 1.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 579 PVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD 658
Cdd:cd07149 2 EVISPYDGEV-IGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 659 EVREAVDFCRYYAMQAIEnfsVAKNQVRFDGIAQQVTRQG------QGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAK 732
Cdd:cd07149 81 EVDRAIETLRLSAEEAKR---LAGETIPFDASPGGEGRIGftirepIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 733 PAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTnvaTLiaETG 812
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKV---TL--ELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 813 GQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAK 892
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 893 NKLQAHIDK-MRATSKLV--GEVSltdecnfGDFIAP-IAFEINSINQLENEQ-FGPILHIVRYKaaDLNNVIAEINATG 967
Cdd:cd07149 313 ERIEEWVEEaVEGGARLLtgGKRD-------GAILEPtVLTDVPPDMKVVCEEvFAPVVSLNPFD--TLDEAIAMANDSP 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2030906275 968 FGLTMGIHSRNERTYTDIERQIRVGNCYINrDQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07149 384 YGLQAGVFTNDLQKALKAARELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
565-1019 |
2.04e-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: 242.81 E-value: 2.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVAL 644
Cdd:cd07085 5 INGEWVESKTTEWLDVYNPATGEV-IARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 645 CHKEAGKTIHDSLDEVR---EAVDFC--RYYAMQAIENFSVAKnqvrfdGIAQQVTRQGQGVFVCISPWNFPLAIFLGQV 719
Cdd:cd07085 84 ITLEHGKTLADARGDVLrglEVVEFAcsIPHLLKGEYLENVAR------GIDTYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 720 AAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTsDERIAGVVFTGSTETAQVI-NRALA 798
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIyERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 799 --KRdtnVATLiaeTGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLP 876
Cdd:cd07085 237 ngKR---VQAL---GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 877 QHHHTDVGPVIDLLAKNKLQAHIDK-MRATSKLV--GEVSLTDECNFGDFIAPIAFEINSINQ--LENEQFGPILHIVRy 951
Cdd:cd07085 311 DDPGADMGPVISPAAKERIEGLIESgVEEGAKLVldGRGVKVPGYENGNFVGPTILDNVTPDMkiYKEEIFGPVLSIVR- 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 952 kAADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINrdqVG-AV-VGVQPFGGQGLSGTG 1019
Cdd:cd07085 390 -VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPiPVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
580-1019 |
1.61e-68 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 236.56 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 580 VSAPYDRRiHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDE 659
Cdd:cd07094 3 VHNPYDGE-VIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 660 VREAVDFCRYYAMQAIENFSVaknQVRFDGIAQQVTRQGQ------GVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKP 733
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGE---EIPLDATQGSDNRLAWtirepvGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 734 AEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRdtnvaTLIAETGG 813
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGK-----RIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 814 QNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKN 893
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 894 KLQAHIDK-MRATSKLVGEVSLTdecnfGDFIAPIAFEINSINQL--ENEQFGPILHIVRYKaaDLNNVIAEINATGFGL 970
Cdd:cd07094 314 RVERWVEEaVEAGARLLCGGERD-----GALFKPTVLEDVPRDTKlsTEETFGPVVPIIRYD--DFEEAIRIANSTDYGL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2030906275 971 TMGIHSRNERTYTDIERQIRVGNCYINrDQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07094 387 QAGIFTRDLNVAFKAAEKLEVGGVMVN-DSSAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
590-1034 |
6.74e-68 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 234.81 E-value: 6.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRY 669
Cdd:cd07099 9 LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 670 YAMQAIEnfsVAKNQVR-----FDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAART 744
Cdd:cd07099 89 AARNAPR---VLAPRKVptgllMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 745 MELMLEAGLPKEAVHLLPGGGaAVGSLLTsDERIAGVVFTGSTETAQVINRALAKRDTNVatlIAETGGQNTMIVDSTAL 824
Cdd:cd07099 166 AEAWAAAGPPQGVLQVVTGDG-ATGAALI-DAGVDKVAFTGSVATGRKVMAAAAERLIPV---VLELGGKDPMIVLADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 825 PEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHID---K 901
Cdd:cd07099 241 LERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDdavA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 902 MRATSKLVGEVSLTDecnfGDFIAPIAF-EIN-SINQLENEQFGPILHIVRYkaADLNNVIAEINATGFGLTMGIHSRNE 979
Cdd:cd07099 321 KGAKALTGGARSNGG----GPFYEPTVLtDVPhDMDVMREETFGPVLPVMPV--ADEDEAIALANDSRYGLSASVFSRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2030906275 980 RTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGpKAGGPHYLYRFTKQ 1034
Cdd:cd07099 395 ARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRP 448
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
587-1035 |
1.06e-67 |
|
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: 234.53 E-value: 1.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 587 RIHVGqvlwsTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKT-------IHDSLDE 659
Cdd:cd07150 14 RVAVG-----SRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTygkawfeTTFTPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 660 VREAVDFCRYYAMQAIenfsvaknQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSL 739
Cdd:cd07150 89 LRAAAGECRRVRGETL--------PSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 740 IAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINrALAKRDTNVATLiaETGGQNTMIV 819
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIA-EKAGRHLKKITL--ELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 820 DSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHI 899
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 900 DkmRATSKlvGEVSLTDECNFGDFIAPIAF----EINSInqLENEQFGPILHIVRykAADLNNVIAEINATGFGLTMGIH 975
Cdd:cd07150 318 E--DAVAK--GAKLLTGGKYDGNFYQPTVLtdvtPDMRI--FREETFGPVTSVIP--AKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2030906275 976 SRNERTYTDIERQIRVGNCYIN----RDQVGAvvgvqPFGGQGLSGTGpKAGGPHYLYRFTKQV 1035
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINdptiLDEAHV-----PFGGVKASGFG-REGGEWSMEEFTELK 447
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
579-1019 |
9.30e-66 |
|
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: 229.16 E-value: 9.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 579 PVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD 658
Cdd:cd07145 2 EVRNPANGEV-IDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 659 EVREAVDFCRYYAMQA---------IENFSVAKNQVRFdgiaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTV 729
Cdd:cd07145 81 EVERTIRLFKLAAEEAkvlrgetipVDAYEYNERRIAF------TVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 730 IAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVI-NRA--LAKRdtnvat 806
Cdd:cd07145 155 VVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIaSKAggTGKK------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 807 LIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPV 886
Cdd:cd07145 229 VALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 887 IDLLAKNKLQAHIDKmrATSKlVGEVSLTDECNFGDFIAPIAFEINSINQ--LENEQFGPILHIVRYKAADLNNVIAeiN 964
Cdd:cd07145 309 ISPEAVERMENLVND--AVEK-GGKILYGGKRDEGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDDEEAVEIA--N 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2030906275 965 ATGFGLTMGIHSRNERTYTDIERQIRVGNCYINrDQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07145 384 STEYGLQASVFTNDINRALKVARELEAGGVVIN-DSTRFRWDNLPFGGFKKSGIG 437
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
589-1019 |
1.55e-65 |
|
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: 228.27 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 589 HVGQVLWSTPAEVTTALDTAADYFPT-WSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFC 667
Cdd:cd07109 9 VFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 668 RYYAMQA--IENFSVAKNqvrfDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTM 745
Cdd:cd07109 89 EYYGGAAdkLHGETIPLG----PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 746 ELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALP 825
Cdd:cd07109 165 ELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE---NVVPVTLELGGKSPQIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 826 EQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHtDVGPVIDLLAKNKLQAHIDKMRAT 905
Cdd:cd07109 242 EAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDP-DLGPLISAKQLDRVEGFVARARAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 906 SK--LVGEVSLTDECNFGDFIAPIAFEINSINQL--ENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERT 981
Cdd:cd07109 321 GAriVAGGRIAEGAPAGGYFVAPTLLDDVPPDSRlaQEEIFGPVLAVMPFD--DEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 2030906275 982 YTDIERQIRVGNCYINrdQVGAVVGVQ-PFGGQGLSGTG 1019
Cdd:cd07109 399 ALRVARRLRAGQVFVN--NYGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
596-1032 |
2.53e-65 |
|
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: 227.96 E-value: 2.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 596 STPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAI 675
Cdd:cd07101 15 STPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 676 ENFSVAKNQVRFDGIAQ-QVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLP 754
Cdd:cd07101 95 RLLKPRRRRGAIPVLTRtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 755 KEAVHLLPGGGAAVGSLLTsdERIAGVVFTGSTETAQVINRALAKRdtnvatLI---AETGGQNTMIVDSTALPEQVVRD 831
Cdd:cd07101 175 RDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRR------LIgcsLELGGKNPMIVLEDADLDKAAAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 832 VMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSK--LV 909
Cdd:cd07101 247 AVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGAtvLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 910 GEVSLTDecnfgdfIAPIAFEINSINQLE-------NEQFGPILHIvrYKAADLNNVIAEINATGFGLTMGIHSRNERTY 982
Cdd:cd07101 327 GGRARPD-------LGPYFYEPTVLTGVTedmelfaEETFGPVVSI--YRVADDDEAIELANDTDYGLNASVWTRDGARG 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2030906275 983 TDIERQIRVGNCYINRDQVGAVVGVQ-PFGGQGLSGTGPKAgGPHYLYRFT 1032
Cdd:cd07101 398 RRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRH-GAEGLLKYT 447
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
590-1023 |
9.28e-65 |
|
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: 226.71 E-value: 9.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWS--AVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD-EVREAVDF 666
Cdd:cd07091 32 ICQVAEADEEDVDAAVKAARAAFETGWwrKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAKgDVALSIKC 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 667 CRYYAMQA--IENFSVAKNQVRFdgiaqQVTRQgQGVFVC--ISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAA 742
Cdd:cd07091 112 LRYYAGWAdkIQGKTIPIDGNFL-----AYTRR-EPIGVCgqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 743 RTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdTNVATLIAETGGQNTMIVDST 822
Cdd:cd07091 186 YLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK--SNLKKVTLELGGKSPNIVFDD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 823 ALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDK- 901
Cdd:cd07091 264 ADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESg 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 902 MRATSKLV--GEVSLTDecnfGDFIAPIAFeinsINQLEN------EQFGPILHIVRYKaaDLNNVIAEINATGFGLTMG 973
Cdd:cd07091 344 KKEGATLLtgGERHGSK----GYFIQPTVF----TDVKDDmkiakeEIFGPVVTILKFK--TEDEVIERANDTEYGLAAG 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2030906275 974 IHSRNERTYTDIERQIRVGNCYINrdqVGAVVGVQ-PFGGQGLSGTGPKAG 1023
Cdd:cd07091 414 VFTKDINKALRVSRALKAGTVWVN---TYNVFDAAvPFGGFKQSGFGRELG 461
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
591-1017 |
9.80e-65 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 227.15 E-value: 9.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 591 GQVLWS----TPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVReavdf 666
Cdd:PRK09457 25 GEVLWQgndaTAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVT----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 667 cryyAMQAIENFSVAKNQVRfDGIAQQVTRQGQ--------GVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTS 738
Cdd:PRK09457 100 ----AMINKIAISIQAYHER-TGEKRSEMADGAavlrhrphGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 739 LIAARTMELMLEAGLPKEAVHLLPgGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATLiaETGGQNTMI 818
Cdd:PRK09457 175 WVAELTVKLWQQAGLPAGVLNLVQ-GGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILAL--EMGGNNPLV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 819 VDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDI-ADRITSLIQGAMQELHIGLP-QHHHTDVGPVIDLLAKNKL- 895
Cdd:PRK09457 252 IDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWdAEPQPFMGAVISEQAAQGLv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 896 --QAHIDKMRATSKLvgEVSLTDEcNFGdFIAPIAFEINSINQLENEQ-FGPILHIVRYkaADLNNVIAEINATGFGLTM 972
Cdd:PRK09457 332 aaQAQLLALGGKSLL--EMTQLQA-GTG-LLTPGIIDVTGVAELPDEEyFGPLLQVVRY--DDFDEAIRLANNTRFGLSA 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2030906275 973 GIHSRNERTYTDIERQIRVGNCYINRDQVGAvVGVQPFGGQGLSG 1017
Cdd:PRK09457 406 GLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
600-1032 |
3.40e-64 |
|
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: 223.95 E-value: 3.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 600 EVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRyyamQAIENFS 679
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILR----EAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 680 VAKNQV---RFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQT----SLIAARTMElmlEAG 752
Cdd:cd07104 77 RPEGEIlpsDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTpvtgGLLIAEIFE---EAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 753 LPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATliaETGGQNTMIVDSTALPEQVVRDV 832
Cdd:cd07104 154 LPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVAL---ELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 833 MRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRAT-SKLV-- 909
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAgARLLtg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 910 GEVSltdecnfGDFIAPIAF----EINSInqLENEQFGPILHIVryKAADLNNVIAEINATGFGLTMGIHSRNERTYTDI 985
Cdd:cd07104 311 GTYE-------GLFYQPTVLsdvtPDMPI--FREEIFGPVAPVI--PFDDDEEAVELANDTEYGLSAAVFTRDLERAMAF 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2030906275 986 ERQIRVGNCYINrDQV---GAVVgvqPFGGQGLSGTGpKAGGPHYLYRFT 1032
Cdd:cd07104 380 AERLETGMVHIN-DQTvndEPHV---PFGGVKASGGG-RFGGPASLEEFT 424
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
579-1019 |
3.41e-64 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 226.68 E-value: 3.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 579 PVSAPYDRRiHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD 658
Cdd:PRK09407 35 EVTAPFTGE-PLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 659 EVREAVDFCRYYAMQAIENFSVAKNQVRFDGIAQ-QVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQT 737
Cdd:PRK09407 114 EVLDVALTARYYARRAPKLLAPRRRAGALPVLTKtTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 738 SLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTsdERIAGVVFTGSTETAQVINRALAKRdtnvatLI---AETGGQ 814
Cdd:PRK09407 194 PLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRR------LIgfsLELGGK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 815 NTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNK 894
Cdd:PRK09407 266 NPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 895 LQAHIDKmrATSK----LVGEVSLTDecnfgdfIAPIAFEINSINQLE-------NEQFGPILHIvrYKAADLNNVIAEI 963
Cdd:PRK09407 346 VSAHVDD--AVAKgatvLAGGKARPD-------LGPLFYEPTVLTGVTpdmelarEETFGPVVSV--YPVADVDEAVERA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2030906275 964 NATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQ-PFGGQGLSGTG 1019
Cdd:PRK09407 415 NDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
580-1023 |
4.49e-64 |
|
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: 224.16 E-value: 4.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 580 VSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAvpvAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDE 659
Cdd:cd07146 3 VRNPYTGEV-VGTVPAGTEEALREALALAASYRSTLTR---YQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 660 VREAVDFCRYYAMQAI----ENFS--VAKNQVRFDGIaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKP 733
Cdd:cd07146 79 VGRAADVLRFAAAEALrddgESFScdLTANGKARKIF---TLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 734 AEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRdtnvaTLIAETGG 813
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK-----RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 814 QNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKN 893
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 894 KLQAHIDkmRATSKlvGEVSLTDECNFGDFIAPIAFE--INSINQLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLT 971
Cdd:cd07146 311 QIENRVE--EAIAQ--GARVLLGNQRQGALYAPTVLDhvPPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGLS 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2030906275 972 MGIHSRNERTYTDIERQIRVGNCYINrDQVGAVVGVQPFGGQGLSGTGPKAG 1023
Cdd:cd07146 385 SGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
565-1035 |
1.24e-62 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 221.03 E-value: 1.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYF--PTWSAVPVAERAACLNKIADLLEANLAELV 642
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEV-IATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 643 ALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIenfSVAKNQVRFDGIAQQVT-RQGQGVFVCISPWNFPLAIFLGQVAA 721
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLAT---KETGEVYDVPPHVISRTvREPVGVCGLITPWNYPLLQAAWKLAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 722 ALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRD 801
Cdd:cd07119 158 ALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 802 TNVATliaETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHT 881
Cdd:cd07119 238 KKVAL---ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 882 DVGPVIDLLAKNKLQAHIDKMRAT-SKLV--GEVSLTDECNFGDFIAPIAFE--INSINQLENEQFGPILHIVRYKAADl 956
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEgARLVcgGKRPTGDELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERFDTEE- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 957 nNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGvqPFGGQGLSGTGpKAGGPHYL--YRFTKQ 1034
Cdd:cd07119 394 -EAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEA--PWGGYKQSGIG-RELGPTGLeeYQETKH 469
|
.
gi 2030906275 1035 V 1035
Cdd:cd07119 470 I 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
598-1019 |
1.13e-61 |
|
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: 217.86 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 598 PAEVTTALDTAADYFP--TWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSL-DEVREAVDFCRYYAmQA 674
Cdd:cd07112 23 AADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALaVDVPSAANTFRWYA-EA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 675 IENfsvaknqvRFDGIAQQ-------VTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMEL 747
Cdd:cd07112 102 IDK--------VYGEVAPTgpdalalITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 748 MLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAkrDTNVATLIAETGGQNTMIV-DSTALPE 826
Cdd:cd07112 174 ALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSG--QSNLKRVWLECGGKSPNIVfADAPDLD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 827 QVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATS 906
Cdd:cd07112 252 AAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESGKAEG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 907 KLV---GEVSLTDECnfGDFIAPIAFEiNSINQLE---NEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNER 980
Cdd:cd07112 332 ARLvagGKRVLTETG--GFFVEPTVFD-GVTPDMRiarEEIFGPVLSVITFDSEE--EAVALANDSVYGLAASVWTSDLS 406
|
410 420 430
....*....|....*....|....*....|....*....
gi 2030906275 981 TYTDIERQIRVGNCYINrdQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07112 407 RAHRVARRLRAGTVWVN--CFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
590-1023 |
7.62e-61 |
|
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: 215.00 E-value: 7.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD-EVREAVDFCR 668
Cdd:cd07115 10 IARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPRAADTFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 669 YYAMQAiENFSVAKNQVRfDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELM 748
Cdd:cd07115 90 YYAGWA-DKIEGEVIPVR-GPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 749 LEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAkrdTNVATLIAETGGQNTMIVDSTALPEQV 828
Cdd:cd07115 168 AEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA---GNLKRVSLELGGKSANIVFADADLDAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 829 VRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRA--TS 906
Cdd:cd07115 245 VRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREegAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 907 KLVGEVSLTDEcnfGDFIAPIAFEI----NSINQleNEQFGPILHIVRYKAADLNNVIAeiNATGFGLTMGIHSRNERTY 982
Cdd:cd07115 325 LLTGGKRPGAR---GFFVEPTIFAAvppeMRIAQ--EEIFGPVVSVMRFRDEEEALRIA--NGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2030906275 983 TDIERQIRVGNCYINrdQVGAVVGVQPFGGQGLSGTGPKAG 1023
Cdd:cd07115 398 HRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
74-187 |
7.70e-60 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 199.65 E-value: 7.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 74 IDALLLEYSLDTKEGILLMCLAEALMRIPDAATADALIRDKLSVADWKSHLKNSDSTFVNASTWGLLLTGKVVSMDRKDT 153
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|....
gi 2030906275 154 ksASSTISRLVNKVSEPIIRQAMNQAMKIMGHQF 187
Cdd:pfam14850 81 --LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
590-1019 |
8.38e-60 |
|
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: 212.36 E-value: 8.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS--------LDEVR 661
Cdd:cd07138 27 IGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLAraaqvglgIGHLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 662 EAVDFCRYYAMQAIENFSVaknqvrfdgiaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIA 741
Cdd:cd07138 107 AAADALKDFEFEERRGNSL-------------VVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 742 ARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALA---KRdtnvATLiaETGGQNTMI 818
Cdd:cd07138 174 IILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAdtvKR----VAL--ELGGKSANI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 819 VDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAH 898
Cdd:cd07138 248 ILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 899 IDK-MRATSKLV-GEVSLTDECNFGDFIAP-----------IAFEinsinqlenEQFGPILHIVRYKaaDLNNVIAEINA 965
Cdd:cd07138 328 IQKgIEEGARLVaGGPGRPEGLERGYFVKPtvfadvtpdmtIARE---------EIFGPVLSIIPYD--DEDEAIAIAND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2030906275 966 TGFGLTMGIHSRNERTYTDIERQIRVGNCYINrdqvGAVVGVQ-PFGGQGLSGTG 1019
Cdd:cd07138 397 TPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
590-1034 |
3.16e-59 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 210.56 E-value: 3.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWS-AVPVAERAACLNKIADLLEANLAELVALCHKEAGKTI---HDSLDEVreAVD 665
Cdd:cd07089 10 IGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmtaRAMQVDG--PIG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 666 FCRYYAmQAIENFS----VAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIA 741
Cdd:cd07089 88 HLRYFA-DLADSFPwefdLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 742 ARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDS 821
Cdd:cd07089 167 LLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA---TLKRVLLELGGKSANIVLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 822 TALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDK 901
Cdd:cd07089 244 DADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIAR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 902 MRAT-SKLVGEVSLTDECNFGDFIAPIAFE--INSINQLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRN 978
Cdd:cd07089 324 GRDEgARLVTGGGRPAGLDKGFYVEPTLFAdvDNDMRIAQEEIFGPVLVVIPYD--DDDEAVRIANDSDYGLSGGVWSAD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2030906275 979 ERTYTDIERQIRVGNCYINrdqvGAVVGV--QPFGGQGLSGTGpKAGGPHYLYRFTKQ 1034
Cdd:cd07089 402 VDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG-RENGIEGLEEFLET 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
585-1036 |
5.48e-59 |
|
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: 209.91 E-value: 5.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 585 DRRIHVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIH-DSLDEVREA 663
Cdd:cd07108 5 ATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQARPEAAVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 664 VDFCRYYAMQAIEnfsVAKNQVRF-DGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAA 742
Cdd:cd07108 85 ADLFRYFGGLAGE---LKGETLPFgPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 743 RTMELMLEAgLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDST 822
Cdd:cd07108 162 LLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPV-SL--ELGGKSPMIVFPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 823 ALPEQVVRDV---MRsaFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHI 899
Cdd:cd07108 238 ADLDDAVDGAiagMR--FTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 900 DKMRATS--------KLVGEVSLTDecnfGDFIAPIAF-EINSINQLENEQ-FGPILHIVRYKaaDLNNVIAEINATGFG 969
Cdd:cd07108 316 DLGLSTSgatvlrggPLPGEGPLAD----GFFVQPTIFsGVDNEWRLAREEiFGPVLCAIPWK--DEDEVIAMANDSHYG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 970 LTMGIHSRNERTYTDIERQIRVGNCYINRDqVGAVVGvQPFGGQGLSGTGPKAGGPHYLYRFT--KQVV 1036
Cdd:cd07108 390 LAAYVWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREASLEGMLEHFTqkKTVN 456
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
590-1019 |
6.12e-59 |
|
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: 209.92 E-value: 6.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRY 669
Cdd:cd07107 10 LARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 670 YAMQAIE----NFSVAKNQVRFdgiaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTM 745
Cdd:cd07107 90 FAGLVTElkgeTIPVGGRNLHY------TLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 746 ELMLEAgLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRdtnVATLIAETGGQNTMIVDSTALP 825
Cdd:cd07107 164 ELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG---IKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 826 EQVVRDVMRSA-FASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRA 904
Cdd:cd07107 240 EAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 905 T-SKLV--GEVSLTDECNFGDFIAPIAF-EINSINQLENEQ-FGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNE 979
Cdd:cd07107 320 EgARLVtgGGRPEGPALEGGFYVEPTVFaDVTPGMRIAREEiFGPVLSVLRWR--DEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2030906275 980 RTYTDIERQIRVGNCYIN---RDQVGAvvgvqPFGGQGLSGTG 1019
Cdd:cd07107 398 SQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
583-1019 |
2.91e-58 |
|
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: 207.97 E-value: 2.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 583 PYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVRE 662
Cdd:cd07110 4 PATEAT-IGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 663 AVDFCRYYAMQA--IENF---SVAKNQVRFDGIaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQT 737
Cdd:cd07110 83 VAGCFEYYADLAeqLDAKaerAVPLPSEDFKAR---VRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 738 SLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRAlAKRDTNVATLiaETGGQNTM 817
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQA-AAQDIKPVSL--ELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 818 IVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQA 897
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 898 HIDKMRAT-SKLVGEVSLTDECNFGDFIAPIAF-EINSINQLENEQ-FGPILHIVRYKAADlnNVIAEINATGFGLTMGI 974
Cdd:cd07110 317 FIARGKEEgARLLCGGRRPAHLEKGYFIAPTVFaDVPTDSRIWREEiFGPVLCVRSFATED--EAIALANDSEYGLAAAV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2030906275 975 HSRNERTYTDIERQIRVGNCYINRDQvgaVVGVQ-PFGGQGLSGTG 1019
Cdd:cd07110 395 ISRDAERCDRVAEALEAGIVWINCSQ---PCFPQaPWGGYKRSGIG 437
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
591-1032 |
3.95e-58 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 207.15 E-value: 3.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 591 GQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRyy 670
Cdd:cd07152 5 GEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELH-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 671 amQAIENFSVAKNQV--RFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTS----LIAART 744
Cdd:cd07152 83 --EAAGLPTQPQGEIlpSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 745 MElmlEAGLPKEAVHLLPgGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATliaETGGQNTMIVDSTAL 824
Cdd:cd07152 161 FE---EAGLPAGVLHVLP-GGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL---ELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 825 PEQVVRDVMRSAFASAGQRC-SALRVLfVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDllakNKLQAHIDKMR 903
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLIN----ARQLDRVHAIV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 904 ATSKLVGEVSLTDECNFGDFIAPI----------AFeinsinqlENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMG 973
Cdd:cd07152 309 DDSVAAGARLEAGGTYDGLFYRPTvlsgvkpgmpAF--------DEEIFGPVAPVTVFD--SDEEAVALANDTEYGLSAG 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 974 IHSRNERTYTDIERQIRVGNCYINrDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRFT 1032
Cdd:cd07152 379 IISRDVGRAMALADRLRTGMLHIN-DQTVNDEPHNPFGGMGASGNGSRFGGPANWEEFT 436
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
596-1019 |
5.09e-58 |
|
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: 206.79 E-value: 5.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 596 STPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSL-DEVREAVDFCRYY--AM 672
Cdd:cd07092 16 ASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPGAVDNFRFFagAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 673 QAIENFSVAKNQvrfDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEaG 752
Cdd:cd07092 96 RTLEGPAAGEYL---PGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-V 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 753 LPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALPEQVVRDV 832
Cdd:cd07092 172 LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD---TLKRVHLELGGKAPVIVFDDADLDAAVAGI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 833 MRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLVGEV 912
Cdd:cd07092 249 ATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHARVLTGG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 913 SLTDECNFgdFIAP--IAFEINSINQLENEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNERTYTDIERQIR 990
Cdd:cd07092 329 RRAEGPGY--FYEPtvVAGVAQDDEIVQEEIFGPVVTVQPFDDED--EAIELANDVEYGLASSVWTRDVGRAMRLSARLD 404
|
410 420
....*....|....*....|....*....
gi 2030906275 991 VGNCYINRDQVgaVVGVQPFGGQGLSGTG 1019
Cdd:cd07092 405 FGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
597-1023 |
7.81e-58 |
|
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: 206.42 E-value: 7.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 597 TPAEVTTALDTAADYFPT--WSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQA 674
Cdd:cd07118 17 TVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 675 IENFSVAKNQVRfDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLP 754
Cdd:cd07118 97 RTLHGDSYNNLG-DDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 755 KEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALPEQVVRDVMR 834
Cdd:cd07118 176 AGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR---NLKKVSLELGGKNPQIVFADADLDAAADAVVF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 835 SAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMR---ATSKLVGE 911
Cdd:cd07118 253 GVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRaegATLLLGGE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 912 VsltDECNFGDFIAPIAF----EINSINQleNEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNERTYTDIER 987
Cdd:cd07118 333 R---LASAAGLFYQPTIFtdvtPDMAIAR--EEIFGPVLSVLTFDTVD--EAIALANDTVYGLSAGVWSKDIDTALTVAR 405
|
410 420 430
....*....|....*....|....*....|....*.
gi 2030906275 988 QIRVGNCYINRDQVGAVvgVQPFGGQGLSGTGPKAG 1023
Cdd:cd07118 406 RIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
604-1019 |
7.24e-57 |
|
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: 203.08 E-value: 7.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 604 ALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAiENFsVAKN 683
Cdd:cd07100 4 ALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENA-EAF-LADE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 684 QVRFDGIAQQVTRQGQGVFVCISPWNFPLAiflgQV----AAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVH 759
Cdd:cd07100 82 PIETDAGKAYVRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 760 LLPGGGAAVGSLLtSDERIAGVVFTGST----ETAQVINRALAKrdtnvATLiaETGGQNTMIVDSTALPEQVVRDVMRS 835
Cdd:cd07100 158 NLLIDSDQVEAII-ADPRVRGVTLTGSEragrAVAAEAGKNLKK-----SVL--ELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 836 AFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMR---ATSKLVGEV 912
Cdd:cd07100 230 RLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVaagATLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 913 S-----------LTDecnfgdfIAP--IAFeinsinqlENEQFGPILHIvrYKAADLNNVIAEINATGFGLTMGIHSRNE 979
Cdd:cd07100 310 PdgpgafypptvLTD-------VTPgmPAY--------DEELFGPVAAV--IKVKDEEEAIALANDSPFGLGGSVFTTDL 372
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2030906275 980 RTYTDIERQIRVGNCYINrdqvgAVVGVQ---PFGGQGLSGTG 1019
Cdd:cd07100 373 ERAERVARRLEAGMVFIN-----GMVKSDprlPFGGVKRSGYG 410
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
590-1019 |
8.81e-57 |
|
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: 203.69 E-value: 8.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRY 669
Cdd:cd07090 10 LATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 670 YAMQAIenfSVAKNQVRFDGIAQQVT-RQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELM 748
Cdd:cd07090 90 YAGLAP---TLSGEHVPLPGGSFAYTrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 749 LEAGLPKEAVHLLPGGGaAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPEQV 828
Cdd:cd07090 167 TEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHV-TL--ELGGKSPLIIFDDADLENA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 829 VRDVMRSAFASAGQRCS-ALRVlFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRA--T 905
Cdd:cd07090 243 VNGAMMANFLSQGQVCSnGTRV-FVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQegA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 906 SKLVG--EVSLTDECNFGDFIAPIAFEINS--INQLENEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRnert 981
Cdd:cd07090 322 KVLCGgeRVVPEDGLENGFYVSPCVLTDCTddMTIVREEIFGPVMSILPFDTEE--EVIRRANDTTYGLAAGVFTR---- 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2030906275 982 ytDIERQIRV------GNCYINRDQVgAVVGVqPFGGQGLSGTG 1019
Cdd:cd07090 396 --DLQRAHRViaqlqaGTCWINTYNI-SPVEV-PFGGYKQSGFG 435
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
565-1019 |
3.64e-56 |
|
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: 202.29 E-value: 3.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPT-WSAVPVAERAACLNKIADLLEANLAELVA 643
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQV-IASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 644 LCHKEAGKTIHDS-LDEVREAVDFCRYYAMQAIE------NFSV-AKNQVRFDGIAQqvtRQGQGVFVCISPWNFPLAIF 715
Cdd:cd07113 83 LETLCSGKSIHLSrAFEVGQSANFLRYFAGWATKingetlAPSIpSMQGERYTAFTR---REPVGVVAGIVPWNFSVMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 716 LGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGaAVGSLLTSDERIAGVVFTGSTETAQVINR 795
Cdd:cd07113 160 VWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 796 ALAKRDTNVaTLiaETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGL 875
Cdd:cd07113 239 QAASDLTRV-TL--ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 876 PQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLV--GEVSLTDEcnfGDFIAPIAFEINSINQ--LENEQFGPILHIVRY 951
Cdd:cd07113 316 PMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIvrGGEALAGE---GYFVQPTLVLARSADSrlMREETFGPVVSFVPY 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030906275 952 kaADLNNVIAEINATGFGLTMGIHSRNertytdIERQIRvgncYINRDQVGAV-VGVQ-------PFGGQGLSGTG 1019
Cdd:cd07113 393 --EDEEELIQLINDTPFGLTASVWTNN------LSKALR----YIPRIEAGTVwVNMHtfldpavPFGGMKQSGIG 456
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
591-1026 |
6.77e-55 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 199.15 E-value: 6.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 591 GQVLWSTP----AEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDF 666
Cdd:PLN02278 50 GEVIANVPcmgrAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 667 CRYYAMQAIENF------SVAKNQVrfdgiaqQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLI 740
Cdd:PLN02278 130 LEYFAEEAKRVYgdiipsPFPDRRL-------LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 741 AARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVD 820
Cdd:PLN02278 203 ALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA---TVKRVSLELGGNAPFIVF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 821 STALPEQVVRDVMRSAFASAGQRC-SALRVLfVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHI 899
Cdd:PLN02278 280 DDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 900 DKmrATSK----LVGEVSLTDEcnfGDFIAPIAFEINSINQL--ENEQFGPILHIVRYKAADlnNVIAEINATGFGLTMG 973
Cdd:PLN02278 359 QD--AVSKgakvLLGGKRHSLG---GTFYEPTVLGDVTEDMLifREEVFGPVAPLTRFKTEE--EAIAIANDTEAGLAAY 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 974 IHSRnertytDIERQIRV------GNCYINRDQVGAVVGvqPFGGQGLSGTGpKAGGPH 1026
Cdd:PLN02278 432 IFTR------DLQRAWRVsealeyGIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKY 481
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
604-1023 |
1.22e-54 |
|
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: 198.10 E-value: 1.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 604 ALDTAADYFPtWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS-LDEVREAVDFCRYYAMQAIENFSVAk 682
Cdd:cd07142 49 AARKAFDEGP-WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMT- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 683 nqVRFDGIAQ-QVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLL 761
Cdd:cd07142 127 --LPADGPHHvYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 762 PGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATLiaETGGQNTMIVDSTALPEQVVRDVMRSAFASAG 841
Cdd:cd07142 205 TGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 842 QRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDK-MRATSKLVgevslTDECNF 920
Cdd:cd07142 283 QCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHgKEEGATLI-----TGGDRI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 921 GD---FIAPIAFEINSINQL--ENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVG--- 992
Cdd:cd07142 358 GSkgyYIQPTIFSDVKDDMKiaRDEIFGPVQSILKFK--TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGtvw 435
|
410 420 430
....*....|....*....|....*....|..
gi 2030906275 993 -NCYinrDQVGAVVgvqPFGGQGLSGTGPKAG 1023
Cdd:cd07142 436 vNCY---DVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
558-980 |
1.25e-54 |
|
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: 197.81 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 558 TWQAapvvNGQVITteldnakpVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEAN 637
Cdd:cd07130 6 EWGG----GGGVVT--------SISPANGEP-IARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 638 LAELVALCHKEAGKTIHDSLDEVREAVDFCRYyamqaienfsvAKNQVR-FDGIAQQVTRQGQ---------GVFVCISP 707
Cdd:cd07130 73 KEALGKLVSLEMGKILPEGLGEVQEMIDICDF-----------AVGLSRqLYGLTIPSERPGHrmmeqwnplGVVGVITA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 708 WNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEA----GLPKEAVHLLPGGgAAVGSLLTSDERIAGVVF 783
Cdd:cd07130 142 FNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCGG-ADVGEALVKDPRVPLVSF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 784 TGSTETAQVINRALAKRdtnVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSL 863
Cdd:cd07130 221 TGSTAVGRQVGQAVAAR---FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLER 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 864 IQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRAT--SKLVGEVSLTDEcnfGDFIAPIAFEINSINQL-ENE 940
Cdd:cd07130 298 LKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQggTVLFGGKVIDGP---GNYVEPTIVEGLSDAPIvKEE 374
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2030906275 941 QFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNER 980
Cdd:cd07130 375 TFAPILYVLKFD--TLEEAIAWNNEVPQGLSSSIFTTDLR 412
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
565-1019 |
2.11e-54 |
|
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: 197.57 E-value: 2.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTE----LDNAKPVSapydrrihvGQVLW----STPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEA 636
Cdd:cd07559 5 INGEWVAPSkgeyFDNYNPVN---------GKVLCeiprSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 637 NLAELVALCHKEAGKTIHDSLD-EVREAVDFCRYYAmQAIENFSVAKNQVRFDGIAqQVTRQGQGVFVCISPWNFPLAIF 715
Cdd:cd07559 76 NLELLAVAETLDNGKPIRETLAaDIPLAIDHFRYFA-GVIRAQEGSLSEIDEDTLS-YHFHEPLGVVGQIIPWNFPLLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 716 LGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAgLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINR 795
Cdd:cd07559 154 AWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 796 ALAKRDTNVaTLiaETGGQNTMIVDSTALPEQ------VVRDVMRSAFaSAGQRCSALRVLFVQEDIADRITSLIQGAMQ 869
Cdd:cd07559 233 YAAENLIPV-TL--ELGGKSPNIFFDDAMDADddfddkAEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 870 ELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLV---GEVSLTDECNFGDFIAP--IAFEINSINQLENEQFGP 944
Cdd:cd07559 309 AIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVltgGERLTLGGLDKGYFYEPtlIKGGNNDMRIFQEEIFGP 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 945 ILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVG----NCYiNRDQVGAvvgvqPFGGQGLSGTG 1019
Cdd:cd07559 389 VLAVITFKDEE--EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGrvwvNCY-HQYPAHA-----PFGGYKKSGIG 459
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
583-1019 |
3.32e-54 |
|
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: 195.93 E-value: 3.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 583 PYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVRE 662
Cdd:cd07102 3 PIDGSV-IAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 663 AVDFCRYyaMQAIENFSVAKNQVR-FDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIA 741
Cdd:cd07102 82 MLERARY--MISIAEEALADIRVPeKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 742 ARTMELMLEAGLPKEAVHLLPGGGAAVGSLLtSDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDS 821
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHETSAALI-ADPRIDHVSFTGSVAGGRAIQRAAAGRFIKV-GL--ELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 822 TALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDK 901
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 902 mrATSK----LVGEVSLTDECNFGDFIAPIAF-EIN-SINQLENEQFGPILHIvrYKAADLNNVIAEINATGFGLTMGIH 975
Cdd:cd07102 316 --AIAKgaraLIDGALFPEDKAGGAYLAPTVLtNVDhSMRVMREETFGPVVGI--MKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2030906275 976 SRNERTYTDIERQIRVGNCYINR-DQVGAVVgvqPFGGQGLSGTG 1019
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNRcDYLDPAL---AWTGVKDSGRG 433
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
579-1019 |
3.80e-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: 195.93 E-value: 3.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 579 PVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD 658
Cdd:cd07147 2 EVTNPYTGEV-VARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 659 EVREAVDFCRYYAMQAIENFSvakNQVRFDGIAQQVTRQG------QGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAK 732
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYG---EVLPLDISARGEGRQGlvrrfpIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 733 PAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAvGSLLTSDERIAGVVFTGSTETAQVI-NRALAKRdtnvatLIAET 811
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLkARAGKKK------VVLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 812 GGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLA 891
Cdd:cd07147 231 GGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 892 KNKLQAHIDK-MRATSKLV--GEVSltdecnfGDFIAPIAFEINSINQLEN--EQFGPILHIVRYKaaDLNNVIAEINAT 966
Cdd:cd07147 311 AERVEGWVNEaVDAGAKLLtgGKRD-------GALLEPTILEDVPPDMEVNceEVFGPVVTVEPYD--DFDEALAAVNDS 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2030906275 967 GFGLTMGIHSRNERTYTDIERQIRVGNCYINrdQVGAV-VGVQPFGGQGLSGTG 1019
Cdd:cd07147 382 KFGLQAGVFTRDLEKALRAWDELEVGGVVIN--DVPTFrVDHMPYGGVKDSGIG 433
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
590-1023 |
4.61e-54 |
|
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: 196.47 E-value: 4.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPT-WSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIH-DSLDEVREAVDFC 667
Cdd:cd07144 36 IASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHsNALGDLDEIIAVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 668 RYYAMQAI----ENFSVAKNQVRFdgiaqqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAAR 743
Cdd:cd07144 116 RYYAGWADkiqgKTIPTSPNKLAY------TLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 744 TMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAkrdTNVATLIAETGGQNTMIVDSTA 823
Cdd:cd07144 190 FANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA---QNLKAVTLECGGKSPALVFEDA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 824 LPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADR-ITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKM 902
Cdd:cd07144 267 DLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKfVEKFVEHVKQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 903 RAT-SKLV--GEVSLTDECNfGDFIAPIAFeiNSINQ----LENEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIH 975
Cdd:cd07144 347 KKEgAKLVygGEKAPEGLGK-GYFIPPTIF--TDVPQdmriVKEEIFGPVVVISKFKTYE--EAIKKANDTTYGLAAAVF 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2030906275 976 SRNERTYTDIERQIRVGNCYINRDQVGAvVGVqPFGGQGLSGTGPKAG 1023
Cdd:cd07144 422 TKDIRRAHRVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
565-1023 |
5.93e-54 |
|
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: 196.21 E-value: 5.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPT-WS-AVPVAERAACLNKIADLLEANLAELV 642
Cdd:cd07143 11 INGEFVDSVHGGTVKVYNPSTGKL-ITKIAEATEADVDIAVEVAHAAFETdWGlKVSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 643 ALCHKEAGKTIHDSLD-EVREAVDFCRYYAMQAIENF--SVAKNQVRFdgiaqQVTRQgQGVFVC--ISPWNFPLAIFLG 717
Cdd:cd07143 90 SIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHgqVIETDIKKL-----TYTRH-EPIGVCgqIIPWNFPLLMCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 718 QVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRAL 797
Cdd:cd07143 164 KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 798 AKRDTNVATLiaETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQ 877
Cdd:cd07143 244 AKSNLKKVTL--ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 878 HHHTDVGPVIDLLAKNKLQAHIDKMRATSKLVgEVSLTDECNFGDFIAPIAFEINSINQ--LENEQFGPILHIVRYKaaD 955
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATV-ETGGKRHGNEGYFIEPTIFTDVTEDMkiVKEEIFGPVVAVIKFK--T 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 956 LNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYIN-RDQVGAVVgvqPFGGQGLSGTGPKAG 1023
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
596-1019 |
1.46e-53 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 194.10 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 596 STPAEVTTALDTAADYF--PTWSAVPvAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQ 673
Cdd:cd07120 16 GGVAEAEAAIAAARRAFdeTDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 674 AIENFSVAKnQVRFDGIAQqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEA-G 752
Cdd:cd07120 95 ARTEAGRMI-EPEPGSFSL-VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 753 LPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATliaETGGQNTMIVDSTALPEQVVRDV 832
Cdd:cd07120 173 LPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGL---ELGGKTPCIVFDDADLDAALPKL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 833 MRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLV--- 909
Cdd:cd07120 250 ERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVvlr 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 910 GEvSLTDECNFGDFIAPIAFEI--NSINQLENEQFGPILHIVRYkaADLNNVIAEINATGFGLTMGIHSRNERTYTDIER 987
Cdd:cd07120 330 GG-PVTEGLAKGAFLRPTLLEVddPDADIVQEEIFGPVLTLETF--DDEAEAVALANDTDYGLAASVWTRDLARAMRVAR 406
|
410 420 430
....*....|....*....|....*....|..
gi 2030906275 988 QIRVGNCYINrdQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07120 407 AIRAGTVWIN--DWNKLFAEAEEGGYRQSGLG 436
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
590-1032 |
6.29e-51 |
|
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: 187.01 E-value: 6.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYF--PTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD-EVREAVDF 666
Cdd:cd07139 27 VGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRaQGPGPAAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 667 CRYYAmQAIENFSVAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTME 746
Cdd:cd07139 107 LRYYA-ALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 747 LMLEAGLPKEAVHLLPgGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPE 826
Cdd:cd07139 186 AAEEAGLPPGVVNVVP-ADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARV-TL--ELGGKSAAIVLDDADLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 827 QVVRDVMRSAFASAGQRCSAL-RVLfVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRA- 904
Cdd:cd07139 262 AAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIAKGRAe 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 905 TSKLV--GEVSltDECNFGDFIAPIAFE--INSINQLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNER 980
Cdd:cd07139 341 GARLVtgGGRP--AGLDRGWFVEPTLFAdvDNDMRIAQEEIFGPVLSVIPYD--DEDDAVRIANDSDYGLSGSVWTADVE 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2030906275 981 TYTDIERQIRVGNCYINrdqvGAVVGVQ-PFGGQGLSGTGpKAGGPHYLYRFT 1032
Cdd:cd07139 417 RGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG-REGGPEGLDAYL 464
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
600-1019 |
1.01e-50 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 185.47 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 600 EVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIENFS 679
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 680 VAKNQVRFDGIAqQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVH 759
Cdd:cd07105 81 GSIPSDKPGTLA-MVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 760 LL---PGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSA 836
Cdd:cd07105 160 VVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK---HLKPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 837 FASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGlpqhhHTDVGPVIDLLAKNKLQAHIDKmrATSK----LVGev 912
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDD--ALSKgaklVVG-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 913 SLTDECNFGDFIAPIAFE-------INSInqlenEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDI 985
Cdd:cd07105 308 GLADESPSGTSMPPTILDnvtpdmdIYSE-----ESFGPVVSIIRVK--DEEEAVRIANDSEYGLSAAVFTRDLARALAV 380
|
410 420 430
....*....|....*....|....*....|....*..
gi 2030906275 986 ERQIRVGNCYINrdqvGAVVGVQ---PFGGQGLSGTG 1019
Cdd:cd07105 381 AKRIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
599-1023 |
5.32e-50 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 184.47 E-value: 5.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 599 AEVTTALDTAADYF---PTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS-LDEVREAVDFCRYYAMQA 674
Cdd:cd07141 44 ADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 675 IENFSvakNQVRFDGIAQQVTRQgQGVFVC--ISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAG 752
Cdd:cd07141 124 DKIHG---KTIPMDGDFFTYTRH-EPVGVCgqIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 753 LPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdTNVATLIAETGGQNTMIVDSTALPEQVVRDV 832
Cdd:cd07141 200 FPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGK--SNLKRVTLELGGKSPNIVFADADLDYAVEQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 833 MRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHID-------KMRAT 905
Cdd:cd07141 278 HEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIEsgkkegaKLECG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 906 SKLVGEVsltdecnfGDFIAPIAFE--INSINQLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYT 983
Cdd:cd07141 358 GKRHGDK--------GYFIQPTVFSdvTDDMRIAKEEIFGPVQQIFKFK--TIDEVIERANNTTYGLAAAVFTKDIDKAI 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2030906275 984 DIERQIRVG----NCYinrdqvgAVVGVQ-PFGGQGLSGTGPKAG 1023
Cdd:cd07141 428 TFSNALRAGtvwvNCY-------NVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
565-1019 |
1.16e-49 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 183.42 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANlAELVAL 644
Cdd:cd07117 5 INGEWVKGSSGETIDSYNPANGET-LSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDEN-KELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 645 CHK-EAGKTIHDSLD-EVREAVDFCRYYAmQAIENFSVAKNQVRFDGIAqQVTRQGQGVFVCISPWNFPLAIFLGQVAAA 722
Cdd:cd07117 83 VETlDNGKPIRETRAvDIPLAADHFRYFA-GVIRAEEGSANMIDEDTLS-IVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 723 LVAGNTVIAKPAEQTSLIAARTMELMLEAgLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDT 802
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 803 NvATLiaETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTD 882
Cdd:cd07117 240 P-ATL--ELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 883 VGPVIDLLAKNKLQAHID--KMRATSKLVGEVSLT-DECNFGDFIAP--IAFEINSINQLENEQFGPILHIVRYKAADln 957
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDiaKEEGAKILTGGHRLTeNGLDKGFFIEPtlIVNVTNDMRVAQEEIFGPVATVIKFKTED-- 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030906275 958 NVIAEINATGFGLTMGIHSRNERTYTDIERQIRVG----NCYiNRDQVGAvvgvqPFGGQGLSGTG 1019
Cdd:cd07117 395 EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGrvwvNTY-NQIPAGA-----PFGGYKKSGIG 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
599-1038 |
3.03e-49 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 183.10 E-value: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 599 AEVTTALDTAADYFP--TWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGK--TIHDSLDeVREAVDFCRYYAMQA 674
Cdd:PLN02766 58 EDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKlfALGKAVD-IPAAAGLLRYYAGAA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 675 IE-NFSVAKNQVRFDGIAqqvTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGL 753
Cdd:PLN02766 137 DKiHGETLKMSRQLQGYT---LKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 754 PKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdTNVATLIAETGGQNTMIVDSTALPEQVVRDVM 833
Cdd:PLN02766 214 PDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAT--SNLKQVSLELGGKSPLLIFDDADVDMAVDLAL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 834 RSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHID--KMRATSKLVGE 911
Cdd:PLN02766 292 LGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEhgKREGATLLTGG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 912 VSLTDEcnfGDFIAPIAF----EINSINQleNEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNERTYTDIER 987
Cdd:PLN02766 372 KPCGDK---GYYIEPTIFtdvtEDMKIAQ--DEIFGPVMSLMKFKTVE--EAIKKANNTKYGLAAGIVTKDLDVANTVSR 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2030906275 988 QIRVG----NCYINRDQVGavvgvqPFGGQGLSGTGpKAGGPHYLYRF--TKQVVSA 1038
Cdd:PLN02766 445 SIRAGtiwvNCYFAFDPDC------PFGGYKMSGFG-RDQGMDALDKYlqVKSVVTP 494
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
562-1031 |
1.59e-48 |
|
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: 180.28 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 562 APVVNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAEL 641
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEV-LASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 642 VALCHKEAGKTIHDSLD-EVREAVDFCRYYAMQAienfsvAKNQVRFDGiaqqvtRQGQGVFVCISPWNFPLAIFLGQVA 720
Cdd:cd07111 102 AVLESLDNGKPIRESRDcDIPLVARHFYHHAGWA------QLLDTELAG------WKPVGVVGQIVPWNFPLLMLAWKIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 721 AALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGaAVGSLLTSDERIAGVVFTGSTETAQVINRALAKr 800
Cdd:cd07111 170 PALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALRRATAG- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 801 dtNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHH 880
Cdd:cd07111 248 --TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 881 TDVGPVIDLLAKNKlqahIDKMRATSKLVGEVSLTDECNF---GDFIAPIAFE-INSINQLENEQ-FGPILHIVRYKAAD 955
Cdd:cd07111 326 IDMGAIVDPAQLKR----IRELVEEGRAEGADVFQPGADLpskGPFYPPTLFTnVPPASRIAQEEiFGPVLVVLTFRTAK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 956 lnNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYIN----RDqvGAVvgvqPFGGQGLSGTGpKAGGPHYLYRF 1031
Cdd:cd07111 402 --EAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlFD--AAA----GFGGYRESGFG-REGGKEGLYEY 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
604-1023 |
2.87e-48 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 180.77 E-value: 2.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 604 ALDTAADYFPtWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLD-EVREAVDFCRYYAMQAIENFSVAk 682
Cdd:PLN02466 103 AARKAFDEGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLT- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 683 nqVRFDGIAQ-QVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLL 761
Cdd:PLN02466 181 --VPADGPHHvQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 762 PGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVATLiaETGGQNTMIVDSTALPEQVVRDVMRSAFASAG 841
Cdd:PLN02466 259 SGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 842 QRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIdkmratsKLVGEVSLTDEC--- 918
Cdd:PLN02466 337 QCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYI-------KSGVESGATLECggd 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 919 NFGD---FIAPIAFEINSINQL--ENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGN 993
Cdd:PLN02466 410 RFGSkgyYIQPTVFSNVQDDMLiaQDEIFGPVQSILKFK--DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGT 487
|
410 420 430
....*....|....*....|....*....|.
gi 2030906275 994 CYIN-RDQVGAVVgvqPFGGQGLSGTGPKAG 1023
Cdd:PLN02466 488 VWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
565-1023 |
5.15e-48 |
|
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: 178.84 E-value: 5.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 565 VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPT--WSAVPVAERAACLNKIADLLEANLAELV 642
Cdd:cd07140 10 INGEFVDAEGGKTYNTINPTDGSV-ICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 643 ALCHKEAGKTIHDSLD-EVREAVDFCRYYA--MQAIENFSVAKNQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQV 719
Cdd:cd07140 89 TIESLDSGAVYTLALKtHVGMSIQTFRYFAgwCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 720 AAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAk 799
Cdd:cd07140 169 AACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 800 rDTNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHH 879
Cdd:cd07140 248 -VSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 880 HTDVGPvidllaKNKlQAHIDKM--------RATSKLVGEVSLTDECNFgdFIAPIAF----EINSINQleNEQFGPILH 947
Cdd:cd07140 327 STDHGP------QNH-KAHLDKLveycergvKEGATLVYGGKQVDRPGF--FFEPTVFtdveDHMFIAK--EESFGPIMI 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030906275 948 IVRYKAADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGvqPFGGQGLSGTGPKAG 1023
Cdd:cd07140 396 ISKFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFGKDLG 469
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
559-1028 |
6.10e-48 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 178.56 E-value: 6.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 559 WQAAPvvNGQVItteldnakPVSAPYDrrihvGQVLWSTP----AEVTTALDTAADYFPTWSAVPVAERAACLNKIADLL 634
Cdd:PRK11241 19 WLDAN--NGEVI--------DVTNPAN-----GDKLGSVPkmgaDETRAAIDAANRALPAWRALTAKERANILRRWFNLM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 635 EANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQA--IENFSVAKNQVRFDGIaqqVTRQGQGVFVCISPWNFPL 712
Cdd:PRK11241 84 MEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGkrIYGDTIPGHQADKRLI---VIKQPIGVTAAITPWNFPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 713 AIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQV 792
Cdd:PRK11241 161 AMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 793 INRALAKrdtNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELH 872
Cdd:PRK11241 241 LMEQCAK---DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 873 IGLPQHHHTDVGPVIDLLAKNKLQAHI-DKMRATSKLV-GEVSLTDECNFgdFIAPIAFEI-NSINQLENEQFGPILHIV 949
Cdd:PRK11241 318 IGDGLEKGVTIGPLIDEKAVAKVEEHIaDALEKGARVVcGGKAHELGGNF--FQPTILVDVpANAKVAKEETFGPLAPLF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 950 RYKaaDLNNVIAEINATGFGLTMGIHSRnertytDIERQIRVGNCyINRDQVGAVVG-----VQPFGG---QGLSGTGPK 1021
Cdd:PRK11241 396 RFK--DEADVIAQANDTEFGLAAYFYAR------DLSRVFRVGEA-LEYGIVGINTGiisneVAPFGGikaSGLGREGSK 466
|
....*..
gi 2030906275 1022 AGGPHYL 1028
Cdd:PRK11241 467 YGIEDYL 473
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
591-1019 |
1.20e-46 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 175.07 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 591 GQVLWS----TPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSL--DEVREAv 664
Cdd:PRK13252 32 GEVLATvqaaTPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETSvvDIVTGA- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 665 DFCRYYA--MQAIENfsvakNQVRFDGIAQQVTRQGQ-GVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIA 741
Cdd:PRK13252 111 DVLEYYAglAPALEG-----EQIPLRGGSFVYTRREPlGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 742 ARTMELMLEAGLPKEAVHLLPGGGaAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDS 821
Cdd:PRK13252 186 LKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEV-TM--ELGGKSPLIVFD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 822 TALPEQVVRDVMRSAFASAGQRCS-ALRVlFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHID 900
Cdd:PRK13252 262 DADLDRAADIAMLANFYSSGQVCTnGTRV-FVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 901 KMRAT-SKLV--GEVSLTDECNFGDFIAPIAFE--INSINQLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIH 975
Cdd:PRK13252 341 KGKAEgARLLcgGERLTEGGFANGAFVAPTVFTdcTDDMTIVREEIFGPVMSVLTFD--DEDEVIARANDTEYGLAAGVF 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2030906275 976 SRnertytDIER------QIRVGNCYINrdQVGAVVGVQPFGGQGLSGTG 1019
Cdd:PRK13252 419 TA------DLSRahrvihQLEAGICWIN--TWGESPAEMPVGGYKQSGIG 460
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
590-1019 |
1.34e-46 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 174.33 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 590 VGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSL-DEVREAVDFCR 668
Cdd:PRK13473 30 LAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALnDEIPAIVDVFR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 669 YYAMQA--IENFSVAKNQvrfDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTME 746
Cdd:PRK13473 110 FFAGAArcLEGKAAGEYL---EGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 747 LMLEAgLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALPE 826
Cdd:PRK13473 187 LAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAAD---SVKRTHLELGGKAPVIVFDDADLD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 827 QVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATS 906
Cdd:PRK13473 263 AVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 907 --KLV--GEVSLTDecnfGDFIAP--IA-----FEInsinqLENEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIH 975
Cdd:PRK13473 343 hiRVVtgGEAPDGK----GYYYEPtlLAgarqdDEI-----VQREVFGPVVSVTPFDDED--QAVRWANDSDYGLASSVW 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2030906275 976 SRnertytDIERQIRVGncyiNRDQVGAV--------VGVQPFGGQGLSGTG 1019
Cdd:PRK13473 412 TR------DVGRAHRVS----ARLQYGCTwvnthfmlVSEMPHGGQKQSGYG 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
579-1032 |
7.15e-46 |
|
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: 172.10 E-value: 7.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 579 PVSAPYDrrihvGQVLWSTPA----EVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKT-- 652
Cdd:cd07151 13 DVLNPYT-----GETLAEIPAaskeDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTri 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 653 -----IHDSLDEVREAVDFCryYAMQAIENFSVAknqvrfDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGN 727
Cdd:cd07151 88 kanieWGAAMAITREAATFP--LRMEGRILPSDV------PGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 728 TVIAKPAEQT----SLIAARTMElmlEAGLPKEAVHLLPGGGAAVGSLLTsDERIAGVV-FTGSTETAQVINRaLAKRdt 802
Cdd:cd07151 160 AVVLKPASDTpitgGLLLAKIFE---EAGLPKGVLNVVVGAGSEIGDAFV-EHPVPRLIsFTGSTPVGRHIGE-LAGR-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 803 NVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTD 882
Cdd:cd07151 233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 883 VGPVIDLLAKNKLQAHIDKMR---ATSKLVGEVSltdecnfGDFIAPIAFE--INSINQLENEQFGPILHIVryKAADLN 957
Cdd:cd07151 313 VGPLINESQVDGLLDKIEQAVeegATLLVGGEAE-------GNVLEPTVLSdvTNDMEIAREEIFGPVAPII--KADDEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 958 NVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINrDQvgavvGVQ-----PFGGQGLSGTGpKAGGPHYLYRFT 1032
Cdd:cd07151 384 EALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQ-----PVNdephvPFGGEKNSGLG-RFNGEWALEEFT 456
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
575-1019 |
4.63e-44 |
|
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: 167.24 E-value: 4.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 575 DNAKPVSapydrrihvGQVLW----STPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAG 650
Cdd:cd07116 19 DNITPVT---------GKVFCevprSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 651 KTIHDSLD-EVREAVDFCRYYAmQAIENFSVAKNQVRFDGIAQQVtRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTV 729
Cdd:cd07116 90 KPVRETLAaDIPLAIDHFRYFA-GCIRAQEGSISEIDENTVAYHF-HEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 730 IAKPAEQTSLIAARTMELMLEAgLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtNVATLIA 809
Cdd:cd07116 168 VLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE---NIIPVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 810 ETGGQ-------NTMIVDSTALPEQVVRDVMrsaFA-SAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHT 881
Cdd:cd07116 244 ELGGKspniffaDVMDADDAFFDKALEGFVM---FAlNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 882 DVGPVIDLLAKNKLQAHID--KMRATSKLVG--EVSLTDECNFGDFIAPIAFEINSINQLENEQFGPILHIVRYKaaDLN 957
Cdd:cd07116 321 MIGAQASLEQLEKILSYIDigKEEGAEVLTGgeRNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFK--DEE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2030906275 958 NVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINrdQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07116 399 EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
627-1036 |
2.37e-43 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 163.37 E-value: 2.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 627 LNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAienfsvaknqVRFDGIAQQVTRQGQGVFVC-- 704
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWA----------RRYEGEIIQSDRPGENILLFkr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 705 -------ISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDER 777
Cdd:PRK10090 71 algvttgILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 778 IAGVVFTGSTETAQVINRALAKRDTNVATliaETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIA 857
Cdd:PRK10090 151 VAMVSMTGSVSAGEKIMAAAAKNITKVCL---ELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 858 DRITSLIQGAMQELHIGLP-QHHHTDVGPVIDLLAKNKLQAHIDKMR---ATSKLVGEVSLTDecnfGDFIAP--IAFEI 931
Cdd:PRK10090 228 DQFVNRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVeegARVALGGKAVEGK----GYYYPPtlLLDVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 932 NSINQLENEQFGPILHIVRYKAadLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQpfG 1011
Cdd:PRK10090 304 QEMSIMHEETFGPVLPVVAFDT--LEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--A 379
|
410 420
....*....|....*....|....*.
gi 2030906275 1012 GQGLSGTGpKAGGPHYLYRFTK-QVV 1036
Cdd:PRK10090 380 GWRKSGIG-GADGKHGLHEYLQtQVV 404
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
580-1019 |
1.67e-42 |
|
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: 161.82 E-value: 1.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 580 VSAPYDRRiHVGQVLWSTPAEVTTALDTAADYFPT---WsaVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS 656
Cdd:cd07148 3 VVNPFDLK-PIGEVPTVDWAAIDKALDTAHALFLDrnnW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 657 LDEVREAVDFCRYyAMQAIENFsvAKNQVRFD------GIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVI 730
Cdd:cd07148 80 KVEVTRAIDGVEL-AADELGQL--GGREIPMGltpasaGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 731 AKPAEQTSLIAARTMELMLEAGLPKEAVHLLPgGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKrdtnvATLIA- 809
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAP-----GTRCAl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 810 ETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDL 889
Cdd:cd07148 231 EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 890 LAKNKLQAHIDKMRA--TSKLVGEVSLTDECnfgdfIAP-IAFE-INSINQLENEQFGPILHIVRYKaaDLNNVIAEINA 965
Cdd:cd07148 311 REVDRVEEWVNEAVAagARLLCGGKRLSDTT-----YAPtVLLDpPRDAKVSTQEIFGPVVCVYSYD--DLDEAIAQANS 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2030906275 966 TGFGLTMGIHSRNERTYTDIERQIRVGNCYINrDQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07148 384 LPVAFQAAVFTKDLDVALKAVRRLDATAVMVN-DHTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
610-1019 |
1.55e-41 |
|
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: 158.46 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 610 DYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS-LDE---VREAVDFcryyamqAIENFS--VAKN 683
Cdd:cd07087 9 ETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAyLTEiavVLGEIDH-------ALKHLKkwMKPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 684 QVRFDGIAQ----QVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEqtslIAARTMELM---LEAGLPKE 756
Cdd:cd07087 82 RVSVPLLLQpakaYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSE----LAPATSALLaklIPKYFDPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 757 AVHLLPGGGAAVGSLLtsDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPEQVVRDVMRSA 836
Cdd:cd07087 158 AVAVVEGGVEVATALL--AEPFDHIFFTGSPAVGKIVMEAAAKHLTPV-TL--ELGGKSPCIVDKDANLEVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 837 FASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHiGLPQHHHTDVGPVIDllaknklQAHIDKMRA---TSKLV--GE 911
Cdd:cd07087 233 FLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFY-GEDPKESPDYGRIIN-------ERHFDRLASlldDGKVVigGQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 912 VSLTDecnfgDFIAPIAFEINSINQ--LENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQI 989
Cdd:cd07087 305 VDKEE-----RYIAPTILDDVSPDSplMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAET 377
|
410 420 430
....*....|....*....|....*....|
gi 2030906275 990 RVGNCYINRDQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07087 378 SSGGVCVNDVLLHAAIPNLPFGGVGNSGMG 407
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
592-1033 |
2.05e-40 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 156.59 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 592 QVLWSTPAEVTTALDTAADYFPT--WSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSL-DEVREAVDFCR 668
Cdd:PRK09847 50 KIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLrDDIPGAARAIR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 669 YYAmQAIENFSVAKNQVRFDGIAQqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELM 748
Cdd:PRK09847 130 WYA-EAIDKVYGEVATTSSHELAM-IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 749 LEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETA-QVINRAlakRDTNVATLIAETGGQNTMIV--DSTALp 825
Cdd:PRK09847 208 KEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGkQLLKDA---GDSNMKRVWLEAGGKSANIVfaDCPDL- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 826 EQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRAT 905
Cdd:PRK09847 284 QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 906 SKLvgevsLTD--ECNFGDFIAPIAF-EINSINQLENEQ-FGPILHIVRYKAADLNNVIAeiNATGFGLTMGIHSRNERT 981
Cdd:PRK09847 364 GQL-----LLDgrNAGLAAAIGPTIFvDVDPNASLSREEiFGPVLVVTRFTSEEQALQLA--NDSQYGLGAAVWTRDLSR 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2030906275 982 YTDIERQIRVGNCYINRDQVGAVvgVQPFGGQGLSGTGpKAGGPHYLYRFTK 1033
Cdd:PRK09847 437 AHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG-RDKSLHALEKFTE 485
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
589-1023 |
5.28e-40 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 154.77 E-value: 5.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 589 HVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHD-SLDEVREAVDFC 667
Cdd:cd07098 8 HLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDaSLGEILVTCEKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 668 RY---YAMQAIENFSVAKNQVRFDGIAQqVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAART 744
Cdd:cd07098 88 RWtlkHGEKALRPESRPGGLLMFYKRAR-VEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 745 MELMLEA----GLPKEAVHLLPGGGAAvGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNVatlIAETGGQNTMIV- 819
Cdd:cd07098 167 LSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPV---VLELGGKDPAIVl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 820 DSTALpEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHI 899
Cdd:cd07098 243 DDADL-DQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 900 -DKMRATSKLV--GEVSLTDECNFGDFIAP--IAFEINSINQLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGI 974
Cdd:cd07098 322 aDAVEKGARLLagGKRYPHPEYPQGHYFPPtlLVDVTPDMKIAQEEVFGPVMVVMKAS--DDEEAVEIANSTEYGLGASV 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2030906275 975 HSRNERTYTDIERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTGPKAG 1023
Cdd:cd07098 400 FGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
596-1019 |
5.80e-39 |
|
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: 150.83 E-value: 5.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 596 STPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS-LDEVREAVDFCryyaMQA 674
Cdd:cd07135 2 TPLDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETlLTEVSGVKNDI----LHM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 675 IENFS--VAKNQVRFDGIAQQ-----VTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLiAARTMEL 747
Cdd:cd07135 78 LKNLKkwAKDEKVKDGPLAFMfgkprIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPH-TAALLAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 748 MLEAGLPKEAVHLLPGGGAAVGSLLtsDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPEQ 827
Cdd:cd07135 157 LVPKYLDPDAFQVVQGGVPETTALL--EQKFDKIFYTGSGRVGRIIAEAAAKHLTPV-TL--ELGGKSPVIVTKNADLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 828 VVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPqHHHTDVGPVIDLLAKNKLQAHIDKMRatsk 907
Cdd:cd07135 232 AAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDTTK---- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 908 lvGEVSLTDECNFGD-FIAPIAFEINSINQ--LENEQFGPILHIVryKAADLNNVIAEINATGFGLTMGIHSRNERTYTD 984
Cdd:cd07135 307 --GKVVIGGEMDEATrFIPPTIVSDVSWDDslMSEELFGPVLPII--KVDDLDEAIKVINSRDTPLALYIFTDDKSEIDH 382
|
410 420 430
....*....|....*....|....*....|....*..
gi 2030906275 985 IERQIRVGNCYINrdQVGAVVGVQ--PFGGQGLSGTG 1019
Cdd:cd07135 383 ILTRTRSGGVVIN--DTLIHVGVDnaPFGGVGDSGYG 417
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
597-1019 |
3.26e-38 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 149.12 E-value: 3.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 597 TPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIE 676
Cdd:PRK09406 21 TDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 677 NFSVAKNQVRFDGIAQQVTR-QGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAE---QTSLIAArtmELMLEAG 752
Cdd:PRK09406 101 LLADEPADAAAVGASRAYVRyQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASnvpQTALYLA---DLFRRAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 753 LPKEAVHLLPGGGAAVGSLLtSDERIAGVVFTGSTETAQVINrALAKRDTNVATLiaETGGQNTMIVDSTALPEQVVRDV 832
Cdd:PRK09406 178 FPDGCFQTLLVGSGAVEAIL-RDPRVAAATLTGSEPAGRAVA-AIAGDEIKKTVL--ELGGSDPFIVMPSADLDRAAETA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 833 MRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRA--TSKLVG 910
Cdd:PRK09406 254 VTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAagATILCG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 911 EVSLTDEcnfGDFIAP--IAFEINSINQLENEQFGPILHIvrYKAADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQ 988
Cdd:PRK09406 334 GKRPDGP---GWFYPPtvITDITPDMRLYTEEVFGPVASL--YRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDD 408
|
410 420 430
....*....|....*....|....*....|...
gi 2030906275 989 IRVGNCYINrdqvGAVVGVQ--PFGGQGLSGTG 1019
Cdd:PRK09406 409 LEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
611-1026 |
8.60e-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: 147.37 E-value: 8.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 611 YFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKT--------IHDSLDEVREAVDFCRYYaMQAIEnfsvAK 682
Cdd:cd07134 10 HALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPaaevdlteILPVLSEINHAIKHLKKW-MKPKR----VR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 683 NQVRFDGIAQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAArTMELMLEAGLPKEAVHLLP 762
Cdd:cd07134 85 TPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSA-VIAKIIREAFDEDEVAVFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 763 GGGAAVGSLLtsDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQ 842
Cdd:cd07134 164 GDAEVAQALL--ELPFDHIFFTGSPAVGKIVMAAAAKHLASV-TL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 843 RCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHT-DVGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTDECnfG 921
Cdd:cd07134 239 TCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAA--Q 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 922 DFIAPIAFEINSINQ--LENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINrD 999
Cdd:cd07134 317 RYIAPTVLTNVTPDMkiMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-D 393
|
410 420
....*....|....*....|....*...
gi 2030906275 1000 QVGAVVGVQ-PFGGQGLSGTGpKAGGPH 1026
Cdd:cd07134 394 VVLHFLNPNlPFGGVNNSGIG-SYHGVY 420
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
561-1036 |
2.61e-36 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 144.49 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 561 AAPV------VNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPT-----WSAVPVAERAACLNK 629
Cdd:PLN02467 2 AIPVprrqlfIGGEWREPVLGKRIPVVNPATEET-IGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 630 IADLLEANLAELVALCHKEAGKTIHDS---LDEVREAVDfcrYYAMQAIENFSVAKNQVRF--DGIAQQVTRQGQGVFVC 704
Cdd:PLN02467 81 IAAKITERKSELAKLETLDCGKPLDEAawdMDDVAGCFE---YYADLAEALDAKQKAPVSLpmETFKGYVLKEPLGVVGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 705 ISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFT 784
Cdd:PLN02467 158 ITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 785 GSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLI 864
Cdd:PLN02467 238 GSTATGRKIMTAAAQ---MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 865 QGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIdkmrATSKLVGEVSLT-----DECNFGDFIAP-IAFEINSINQLE 938
Cdd:PLN02467 315 VKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFI----STAKSEGATILCggkrpEHLKKGFFIEPtIITDVTTSMQIW 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 939 NEQ-FGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQvgAVVGVQPFGGQGLSG 1017
Cdd:PLN02467 391 REEvFGPVLCVKTFSTED--EAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQ--PCFCQAPWGGIKRSG 466
|
490 500
....*....|....*....|..
gi 2030906275 1018 TGPKAGG---PHYLYrfTKQVV 1036
Cdd:PLN02467 467 FGRELGEwglENYLS--VKQVT 486
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
597-993 |
5.83e-36 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 143.36 E-value: 5.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 597 TPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQAIE 676
Cdd:PLN00412 51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 677 NFSVAKNQVR--FDGIAQQ----VTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLE 750
Cdd:PLN00412 131 ILGEGKFLVSdsFPGNERNkyclTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 751 AGLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGStETAQVINralakRDTNVATLIAETGGQNTMIVDSTALPEQVVR 830
Cdd:PLN00412 211 AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAIS-----KKAGMVPLQMELGGKDACIVLEDADLDLAAA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 831 DVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQhHHTDVGPVIDLLAKNKLQAHIdkMRATSKlvG 910
Cdd:PLN00412 285 NIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE-DDCDITPVVSESSANFIEGLV--MDAKEK--G 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 911 EVSLTDECNFGDFIAP-----------IAFEinsinqlenEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRne 979
Cdd:PLN00412 360 ATFCQEWKREGNLIWPllldnvrpdmrIAWE---------EPFGPVLPVIRINSVE--EGIHHCNASNFGLQGCVFTR-- 426
|
410
....*....|....
gi 2030906275 980 rtytDIERQIRVGN 993
Cdd:PLN00412 427 ----DINKAILISD 436
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
700-1019 |
1.78e-35 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 141.70 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 700 GVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEqtslIAARTMELMLE---AGLPKEAVHLLPGGGAAVGSLLTsdE 776
Cdd:PTZ00381 111 GVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSE----LSPHTSKLMAKlltKYLDPSYVRVIEGGVEVTTELLK--E 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 777 RIAGVVFTGSTETAQVINRALAKrdtNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDI 856
Cdd:PTZ00381 185 PFDHIFFTGSPRVGKLVMQAAAE---NLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 857 ADRITSLIQGAMQELhIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLVGEVSLTDEcnfgdFIAPIAF---EINS 933
Cdd:PTZ00381 262 KDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGKVVYGGEVDIENK-----YVAPTIIvnpDLDS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 934 InQLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINrDQVGAVVGVQ-PFGG 1012
Cdd:PTZ00381 336 P-LMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIN-DCVFHLLNPNlPFGG 411
|
....*..
gi 2030906275 1013 QGLSGTG 1019
Cdd:PTZ00381 412 VGNSGMG 418
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
614-1032 |
1.81e-35 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 142.28 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 614 TWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRY-YAMQAIENFSVAKNQvRFDGIAQ 692
Cdd:PLN02315 71 IWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFaVGLSRQLNGSIIPSE-RPNHMMM 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 693 QVTRQgQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAgLPKEAvhlLPG-------GG 765
Cdd:PLN02315 150 EVWNP-LGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEV-LEKNN---LPGaiftsfcGG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 766 AAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRdtnVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCS 845
Cdd:PLN02315 225 AEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR---FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 846 ALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSK--LVGEVSLTDEcnfGDF 923
Cdd:PLN02315 302 TCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGkiLTGGSAIESE---GNF 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 924 IAPIAFEIN-SINQLENEQFGPILHIVRYKAadLNNVIAEINATGFGLTMGIHSRNERTytdIERQI-----RVGNCYIN 997
Cdd:PLN02315 379 VQPTIVEISpDADVVKEELFGPVLYVMKFKT--LEEAIEINNSVPQGLSSSIFTRNPET---IFKWIgplgsDCGIVNVN 453
|
410 420 430
....*....|....*....|....*....|....*...
gi 2030906275 998 RDQVGAVVGvQPFGGQGLSGTGPKAGG---PHYLYRFT 1032
Cdd:PLN02315 454 IPTNGAEIG-GAFGGEKATGGGREAGSdswKQYMRRST 490
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
591-997 |
6.28e-35 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 139.61 E-value: 6.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 591 GQVL----WSTPAEVTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDF 666
Cdd:PRK13968 17 GEQLsvlpWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 667 CRYYA-----MQAIENFSVAKNQVrfdgiaqQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIA 741
Cdd:PRK13968 97 CDWYAehgpaMLKAEPTLVENQQA-------VIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 742 ARTMELMLEAGLPKEAVHLLPGGGAAVgSLLTSDERIAGVVFTGSTETAQVINralAKRDTNVATLIAETGGQNTMIVDS 821
Cdd:PRK13968 170 QLIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIG---AQAGAALKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 822 TALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDK 901
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 902 MRATSK--LVGEVSLTDECNF--GDFIAPIAFEINSINQlenEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSR 977
Cdd:PRK13968 326 TLAEGArlLLGGEKIAGAGNYyaPTVLANVTPEMTAFRE---ELFGPVAAITVAKDAE--HALELANDSEFGLSATIFTT 400
|
410 420
....*....|....*....|
gi 2030906275 978 NERTYTDIERQIRVGNCYIN 997
Cdd:PRK13968 401 DETQARQMAARLECGGVFIN 420
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
604-1036 |
3.49e-32 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 131.21 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 604 ALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTihdsldeVREAVDFCRYYAMQAIENFSVAKN 683
Cdd:cd07084 4 ALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-------WMFAENICGDQVQLRARAFVIYSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 684 QVRFD-------GIAQQVTRQ--GQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAG-L 753
Cdd:cd07084 77 RIPHEpgnhlgqGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 754 PKEAVHLLPGGGAAVGSLLTsDERIAGVVFTGSTETAQVInRALAKRdtnvATLIAETGGQNTMIVDSTAlPEQ--VVRD 831
Cdd:cd07084 157 PPEDVTLINGDGKTMQALLL-HPNPKMVLFTGSSRVAEKL-ALDAKQ----ARIYLELAGFNWKVLGPDA-QAVdyVAWQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 832 VMRSAFASAGQRCSALRVLFVQEDiaDRITSLIQGAMQELHIGLPQhhHTDVGPVI--DLLAK-NKLQAHID-KMRATSK 907
Cdd:cd07084 230 CVQDMTACSGQKCTAQSMLFVPEN--WSKTPLVEKLKALLARRKLE--DLLLGPVQtfTTLAMiAHMENLLGsVLLFSGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 908 LVGEVSLTDecNFGDFIAPIAF----EINSINQL-ENEQFGPILHIVRYKAADLNNVIAEINATGFGLTMGIHSrNERTY 982
Cdd:cd07084 306 ELKNHSIPS--IYGACVASALFvpidEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYS-NDPIF 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2030906275 983 TD--IERQIRVGNCY-INRDQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRFTKQVV 1036
Cdd:cd07084 383 LQelIGNLWVAGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHA 439
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
604-1019 |
1.96e-30 |
|
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: 125.80 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 604 ALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSldeVREAVDFCRYYAMQAIENFS---- 679
Cdd:cd07132 3 AVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEA---VLSEILLVKNEIKYAISNLPewmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 680 ---VAKNQVR-FDGIaqQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEqTSLIAARTMELMLEAGLPK 755
Cdd:cd07132 80 pepVKKNLATlLDDV--YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE-VSPATAKLLAELIPKYLDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 756 EAVHLLPGGGAAVGSLLtsDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPEQVVRDVMRS 835
Cdd:cd07132 157 ECYPVVLGGVEETTELL--KQRFDYIFYTGSTSVGKIVMQAAAKHLTPV-TL--ELGGKSPCYVDKSCDIDVAARRIAWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 836 AFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHiGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRatsklvgeVSLT 915
Cdd:cd07132 232 KFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFY-GEDPKESPDYGRIINDRHFQRLKKLLSGGK--------VAIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 916 DECNFGD-FIAP-IAFEINSINQL-ENEQFGPILHIVRYKAADlnNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVG 992
Cdd:cd07132 303 GQTDEKErYIAPtVLTDVKPSDPVmQEEIFGPILPIVTVNNLD--EAIEFINSREKPLALYVFSNNKKVINKILSNTSSG 380
|
410 420
....*....|....*....|....*..
gi 2030906275 993 NCYINRDQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07132 381 GVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
550-997 |
3.93e-30 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 127.17 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 550 ELSLQMQKTWQAAPVVNGQVITTELDNAKPVSAPYDRRIhVGQVLWSTPAEVTTALDTAADYFPTWSAVPVAERAACLNK 629
Cdd:PLN02419 103 EQSTQPQMPPRVPNLIGGSFVESQSSSFIDVINPATQEV-VSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 630 IADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDF----CRYYAMQAIENFSVAKNqvrfdGIAQQVTRQGQGVFVCI 705
Cdd:PLN02419 182 FQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVvehaCGMATLQMGEYLPNVSN-----GVDTYSIREPLGVCAGI 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 706 SPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAGLPKEAVHLLPGGGAAVGSlLTSDERIAGVVFTG 785
Cdd:PLN02419 257 CPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 786 S-TETAQVINRALAKRDtnvaTLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLI 864
Cdd:PLN02419 336 SnTAGMHIYARAAAKGK----RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 865 QGAmQELHIGLPQHHHTDVGPVIDLLAKNK----LQAHIDKmRATSKLVGEVSLTDECNFGDFIAPIAFE--INSINQLE 938
Cdd:PLN02419 412 ERA-KALKVTCGSEPDADLGPVISKQAKERicrlIQSGVDD-GAKLLLDGRDIVVPGYEKGNFIGPTILSgvTPDMECYK 489
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2030906275 939 NEQFGPILhiVRYKAADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYIN 997
Cdd:PLN02419 490 EEIFGPVL--VCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
612-1019 |
5.21e-27 |
|
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: 115.27 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 612 FPTWsavpvAERAACLNKIADLLEANLAELVALCHKEAG-KTIHDS-LDEVREAVDFCRYyamqAIEN------------ 677
Cdd:cd07133 16 PPSL-----EERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETlLAEILPSIAGIKH----ARKHlkkwmkpsrrhv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 678 ---FSVAKNQVRFdgiaqqvtrQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSliaaRTMEL---MLEA 751
Cdd:cd07133 87 gllFLPAKAEVEY---------QPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTP----RTSALlaeLLAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 752 GLPKEAVHLLpGGGAAVGSLLTS---DEriagVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPEQV 828
Cdd:cd07133 154 YFDEDEVAVV-TGGADVAAAFSSlpfDH----LLFTGSTAVGRHVMRAAAENLTPV-TL--ELGGKSPAIIAPDADLAKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 829 VRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPqhHHTDVGPVIDLLAKNKLQAHIDKMRATSKL 908
Cdd:cd07133 226 AERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLA--DNPDYTSIINERHYARLQGLLEDARAKGAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 909 VGEVSLTDECNFGD-FIAP-IAFEINSINQL-ENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDI 985
Cdd:cd07133 304 VIELNPAGEDFAATrKLPPtLVLNVTDDMRVmQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRV 381
|
410 420 430
....*....|....*....|....*....|....
gi 2030906275 986 ERQIRVGNCYINRDQVGAVVGVQPFGGQGLSGTG 1019
Cdd:cd07133 382 LRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMG 415
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
602-954 |
8.64e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 115.96 E-value: 8.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 602 TTALDTAADY-F------PTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLDEVREAVDFCRYYAMQA 674
Cdd:PRK11903 37 ATGLDLAAAFaFareqggAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 675 IenfSVAKNQVRFDGIAQQVTR----QGQ-------GVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAAR 743
Cdd:PRK11903 117 A---ALGDARLLRDGEAVQLGKdpafQGQhvlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 744 TMELMLEAG-LPKEAVHLLPGGGAavgSLLTSDERIAGVVFTGSTETAQVI--NRALAKRDTNVAtliAETGGQNTMIVD 820
Cdd:PRK11903 194 MVKDVVAAGiLPAGALSVVCGSSA---GLLDHLQPFDVVSFTGSAETAAVLrsHPAVVQRSVRVN---VEADSLNSALLG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 821 STALP-----EQVVRDVMRSAFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKL 895
Cdd:PRK11903 268 PDAAPgseafDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAV 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030906275 896 QAHIDKMRATSKLV---GEVSLTD-ECNFGDFIAPIAFEINSINQL----ENEQFGPILHIVRYKAA 954
Cdd:PRK11903 348 RAGLAALRAQAEVLfdgGGFALVDaDPAVAACVGPTLLGASDPDAAtavhDVEVFGPVATLLPYRDA 414
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
610-1019 |
2.15e-26 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 113.75 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 610 DYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS--------LDEVReavdfcryYAMQAIENFSVA 681
Cdd:cd07136 9 AFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAymteigfvLSEIN--------YAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 682 KnQVRFDgIAQQ-----VTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIaARTMELMLEAGLPKE 756
Cdd:cd07136 81 K-RVKTP-LLNFpsksyIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNT-SKVIAKIIEETFDEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 757 AVHLLPGGGAAVGSLLtsDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPEQVVRDVMRSA 836
Cdd:cd07136 158 YVAVVEGGVEENQELL--DQKFDYIFFTGSVRVGKIVMEAAAKHLTPV-TL--ELGGKSPCIVDEDANLKLAAKRIVWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 837 FASAGQRCSALRVLFVQEDIADRitsLIQGAMQELHIGLPQH--HHTDVGPVIDLLAKNKLQAHIDKmratsklvGEVSL 914
Cdd:cd07136 233 FLNAGQTCVAPDYVLVHESVKEK---FIKELKEEIKKFYGEDplESPDYGRIINEKHFDRLAGLLDN--------GKIVF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 915 TDECNFGD-FIAP-----IAFEINSinqLENEQFGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQ 988
Cdd:cd07136 302 GGNTDRETlYIEPtildnVTWDDPV---MQEEIFGPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLEN 376
|
410 420 430
....*....|....*....|....*....|..
gi 2030906275 989 IRVGNCYINrDQVGAVVGVQ-PFGGQGLSGTG 1019
Cdd:cd07136 377 LSFGGGCIN-DTIMHLANPYlPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
619-1019 |
2.13e-25 |
|
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: 110.58 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 619 PVAERAACLNKIADLLEANLAELVALCHKEAGKTIHDS-LDEVREAVDFCRYyAMQAIENFSV---AKNQVRFDGIAQQV 694
Cdd:cd07137 19 SAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCKL-AIKELKKWMApekVKTPLTTFPAKAEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 695 TRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAE---QTSLIAARTMELMLEaglpKEAVHLLPGGGAAVGSL 771
Cdd:cd07137 98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSElapATSALLAKLIPEYLD----TKAIKVIEGGVPETTAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 772 LtsDERIAGVVFTGSTETAQVINRALAKRDTNVaTLiaETGGQNTMIVDSTALPEQVVRDVMRSAFAS-AGQRCSALRVL 850
Cdd:cd07137 174 L--EQKWDKIFFTGSPRVGRIIMAAAAKHLTPV-TL--ELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 851 FVQEDIADRITSLIQGAMQELHiGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLV--GEVsltDECNFgdFIAP-I 927
Cdd:cd07137 249 LVEESFAPTLIDALKNTLEKFF-GENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVhgGER---DEKNL--YIEPtI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 928 AFEINSINQLENEQ-FGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQVGAVVG 1006
Cdd:cd07137 323 LLDPPLDSSIMTEEiFGPLLPIITVK--KIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
410
....*....|...
gi 2030906275 1007 VQPFGGQGLSGTG 1019
Cdd:cd07137 401 TLPFGGVGESGFG 413
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
621-955 |
5.84e-25 |
|
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: 110.44 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 621 AERAACLNKIADLLEANLAELVALCHKeAGKTIHDSLDEVREAVDFCRYYAmqaienfSVAKNQ-----VRFDGIAQQVT 695
Cdd:cd07128 59 HERAAMLKALAKYLMERKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYA-------SLGRRElpnahFLVEGDVEPLS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 696 RQG-----------QGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELMLEAG-LPKEAVHLLPG 763
Cdd:cd07128 131 KDGtfvgqhiltprRGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 764 GgaaVGSLLtsdERIAG---VVFTGSTETAQVInRALAKRDTNVATLIAETGGQNTMIVDSTALPEQ-----VVRDVMRS 835
Cdd:cd07128 211 S---VGDLL---DHLGEqdvVAFTGSAATAAKL-RAHPNIVARSIRFNAEADSLNAAILGPDATPGTpefdlFVKEVARE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 836 AFASAGQRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQHHHTDVGPVIDLLAKNKLQAHIDKMRATSKLVG----- 910
Cdd:cd07128 284 MTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFggpdr 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2030906275 911 -EVSLTDEcNFGDFIAPIAFEINSINQL----ENEQFGPILHIVRYKAAD 955
Cdd:cd07128 364 fEVVGADA-EKGAFFPPTLLLCDDPDAAtavhDVEAFGPVATLMPYDSLA 412
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
255-481 |
5.31e-21 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 97.46 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 255 SIKLSALH-PRYEV--------ANEARVMTEMHDTVLELLLRARDLDVGITIDAEEA------DRLELSLAL-FEKLYRH 318
Cdd:PLN02681 187 SFPLFADSsPLYHAtsepepltAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYTslqpaiDYITYDLAReFNKGKDR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 319 PRLQGwgkfgiVVQAYSKRALPTLIWLAALAKEQGDVIPLRLVKGAYWDTELKLSQQNGYDAyPVYTRKEATDVAYLACA 398
Cdd:PLN02681 267 PIVYG------TYQAYLKDARERLRLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 399 RFLLSEQIRGCIYPQFASHNAHTV-SAIATMAEHQEY------EFQRLHGMGDALYNhALEIYGVDVRIYAPVGSHKDLL 471
Cdd:PLN02681 340 EFLLEKASNGDGEVMLATHNVESGeLAAAKMNELGLHkgdprvQFAQLLGMSDNLSF-GLGNAGFRVSKYLPYGPVEEVI 418
|
250
....*....|
gi 2030906275 472 PYLVRRLLEN 481
Cdd:PLN02681 419 PYLLRRAEEN 428
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
601-976 |
2.09e-20 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 95.69 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 601 VTTALDTAADYFPTWSAVPVAERAACLNKIADLLEANLAELVALCHKEAGktihdsLDEVREAVDFCRyyamqaienfsv 680
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG------LPEARLQGELGR------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 681 AKNQVR-F-----DGIAQQVT----------------RQGQG------VFvciSPWNFPLAIFL--GQVAAALVAGNTVI 730
Cdd:cd07129 63 TTGQLRlFadlvrEGSWLDARidpadpdrqplprpdlRRMLVplgpvaVF---GASNFPLAFSVagGDTASALAAGCPVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 731 AK-----PAeqTSLIAARTMELMLEA-GLPKEAVHLLPGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRALAKRDTNV 804
Cdd:cd07129 140 VKahpahPG--TSELVARAIRAALRAtGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 805 AtLIAETGGQNTMIVDSTAL---PEQVVRDVMRSAFASAGQRCSALRVLFV---------QEDIADRITSLIQGAMqeLH 872
Cdd:cd07129 218 P-FYAELGSVNPVFILPGALaerGEAIAQGFVGSLTLGAGQFCTNPGLVLVpagpagdafIAALAEALAAAPAQTM--LT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 873 IGLPQHHHTDVG-----PVIDLLAKNKLQAHIDKMRATsklVGEVSLTdecnfgDFIAPIAfeinsinqLENEQFGPILH 947
Cdd:cd07129 295 PGIAEAYRQGVEalaaaPGVRVLAGGAAAEGGNQAAPT---LFKVDAA------AFLADPA--------LQEEVFGPASL 357
|
410 420
....*....|....*....|....*....
gi 2030906275 948 IVRYkaADLNNVIAEINATGFGLTMGIHS 976
Cdd:cd07129 358 VVRY--DDAAELLAVAEALEGQLTATIHG 384
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
620-1019 |
1.11e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 90.56 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 620 VAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSL-DEVREAVDFCRYyAMQAIENFSVAKNQ----VRFDGIAQqV 694
Cdd:PLN02203 27 LEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYrDEVGVLTKSANL-ALSNLKKWMAPKKAklplVAFPATAE-V 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 695 TRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAArtmelMLEAGLPK----EAVHLLPgGGAAVGS 770
Cdd:PLN02203 105 VPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPKyldsKAVKVIE-GGPAVGE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 771 LLTsDERIAGVVFTGSTETAQVINRALAKRDTNVATliaETGGQNTMIVDSTALP---EQVVRDVMRSAFAS-AGQRCSA 846
Cdd:PLN02203 179 QLL-QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVAL---ELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQACIA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 847 LRVLFVQEDIADRITSLIQGAMQELHIGLPQhhhtDVGPVIDLLAKN---KLQAHIDKMRATSKLVGEVSLtDECNFgdF 923
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPR----ESKSMARILNKKhfqRLSNLLKDPRVAASIVHGGSI-DEKKL--F 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 924 IAP-IAFEINSINQLENEQ-FGPILHIVRYKaaDLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQV 1001
Cdd:PLN02203 328 IEPtILLNPPLDSDIMTEEiFGPLLPIITVK--KIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAII 405
|
410
....*....|....*...
gi 2030906275 1002 GAVVGVQPFGGQGLSGTG 1019
Cdd:PLN02203 406 QYACDSLPFGGVGESGFG 423
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
675-980 |
3.40e-18 |
|
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: 89.09 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 675 IENFSvaKNQVRF---------DGIAQQV--TRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAAR 743
Cdd:cd07126 110 LENFA--GDQVRFlarsfnvpgDHQGQQSsgYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 744 TMELMLEAGLPKEAVHLLPGGGAAVGSLLtSDERIAGVVFTGSTETAQvinrALAkRDTNVATLIAETG------GQNTM 817
Cdd:cd07126 188 FLRLLHLCGMPATDVDLIHSDGPTMNKIL-LEANPRMTLFTGSSKVAE----RLA-LELHGKVKLEDAGfdwkilGPDVS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 818 IVDSTALpeQVVRDvmrsAFASAGQRCSALRVLFVQED-----IADRITSLI-QGAMQELhiglpqhhhtDVGPVIDLLA 891
Cdd:cd07126 262 DVDYVAW--QCDQD----AYACSGQKCSAQSILFAHENwvqagILDKLKALAeQRKLEDL----------TIGPVLTWTT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 892 KnKLQAHIDKMRA---TSKLVGEVSLTDECNFGDF--IAPIA--FEINSINQLEN------EQFGPILHIVRYKAADLNN 958
Cdd:cd07126 326 E-RILDHVDKLLAipgAKVLFGGKPLTNHSIPSIYgaYEPTAvfVPLEEIAIEENfelvttEVFGPFQVVTEYKDEQLPL 404
|
330 340
....*....|....*....|..
gi 2030906275 959 VIAEINATGFGLTMGIHSRNER 980
Cdd:cd07126 405 VLEALERMHAHLTAAVVSNDIR 426
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
691-1023 |
2.85e-15 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 79.70 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 691 AQQVTRQGQGVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARTMELmLEAGLPKEAVHLLPGGGAAVGS 770
Cdd:PLN02174 105 SAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 771 LLtsDERIAGVVFTGSTETAQVINRALAKRDTNVatlIAETGGQNTMIVDS-TALPEQVVRDVMRSAFASAGQRCSALRV 849
Cdd:PLN02174 184 LL--EQKWDKIFYTGSSKIGRVIMAAAAKHLTPV---VLELGGKSPVVVDSdTDLKVTVRRIIAGKWGCNNGQACISPDY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 850 LFVQEDIADRITSLIQGAMQELHiGLPQHHHTDVGPVIDllaknklQAHIDKMratSKLVGEVSLTDECNFGD------- 922
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETFY-GKNPMESKDMSRIVN-------STHFDRL---SKLLDEKEVSDKIVYGGekdrenl 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 923 FIAPIAFEINSINQL--ENEQFGPILHIVryKAADLNNVIAEINATGFGLTMGIHSRNERTYTDIERQIRVGNCYINRDQ 1000
Cdd:PLN02174 328 KIAPTILLDVPLDSLimSEEIFGPLLPIL--TLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIA 405
|
330 340
....*....|....*....|...
gi 2030906275 1001 VGAVVGVQPFGGQGLSGTGPKAG 1023
Cdd:PLN02174 406 VHLALHTLPFGGVGESGMGAYHG 428
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
599-855 |
1.00e-08 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 59.03 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 599 AEVTTALDTAADYFPTWS-AVPVAERAACLnKIADLLEANLAELV-ALCHK---------EAGKTihDSLDEVREAVDFC 667
Cdd:cd07127 84 CDPDALLAAARAAMPGWRdAGARARAGVCL-EILQRLNARSFEMAhAVMHTtgqafmmafQAGGP--HAQDRGLEAVAYA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 668 rYYAMQAIENFSV-AKNQVRFDGIAQQ----VTRQGQGVFVCISP---WNFPLAIFlgqvaAALVAGNTVIAKPAEQTSL 739
Cdd:cd07127 161 -WREMSRIPPTAEwEKPQGKHDPLAMEktftVVPRGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 740 IAARTM----ELMLEAGLPKEAVHLL---PGGGAAvgSLLTSDERIAGVVFTGSTETAQVInralaKRDTNVATLIAETG 812
Cdd:cd07127 235 PLAITVqvarEVLAEAGFDPNLVTLAadtPEEPIA--QTLATRPEVRIIDFTGSNAFGDWL-----EANARQAQVYTEKA 307
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2030906275 813 GQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQED 855
Cdd:cd07127 308 GVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRD 350
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
620-877 |
7.10e-07 |
|
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: 52.61 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 620 VAERAACLNKIADLLEANLAELVALCHKEAGKTIHDSLdevreavdfCRYYAMQAIENFSVAKNQVRFDGIA------QQ 693
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLI---------ANWIAMMGCSESKLYKNIDTERGITasvghiQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 694 VTR-QGQGVFVCISPWNFPLAIFLGQV--------AAALVAGNTVIAKP---AEQTSLIAARTMELMLEAGLPKEAVHLL 761
Cdd:cd07077 86 VLLpDNGETYVRAFPIGVTMHILPSTNplsgitsaLRGIATRNQCIFRPhpsAPFTNRALALLFQAADAAHGPKILVLYV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 762 PGGGAAVGSLLTSDERIAGVVFTGSTETAQVINRAlakrdTNVATLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASaG 841
Cdd:cd07077 166 PHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKH-----SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-Q 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 2030906275 842 QRCSALRVLFVQEDIADRITSLIQGAMQELHIGLPQ 877
Cdd:cd07077 240 NACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQ 275
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
698-823 |
5.62e-05 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 47.55 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 698 GQGVFVCISPwnfPLAIFLGQVAAALVAGNTVIAKPAEQTSLIAARtmelmleagLPKeavhlLPGGGAAVGSLLTSDER 777
Cdd:PRK11905 1078 PRGRVLCVAD---TEEALLRQLAAALATGNVAVVAADSGLAAALAD---------LPG-----LVAARIDWTQDWEADDP 1140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2030906275 778 IAGVVFTGSTETAQVINRALAKRDTNVATLIAETGGQNTMI----------VDSTA 823
Cdd:PRK11905 1141 FAGALLEGDAERARAVRQALAARPGAIVPLIAAEPTDAYDLarlveersvsINTTA 1196
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
700-987 |
2.39e-04 |
|
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: 44.95 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 700 GVFVCISPWNFPLAIFLGQVAAALVAGNTVIAKP---AEQTSLIAARTM-ELMLEAGLPKEAVHLLPGGGAAVGSLLTSD 775
Cdd:cd07081 97 GVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhprAKKVTQRAATLLlQAAVAAGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 776 ERIAGVVFTGSTETAQVinralAKRDTNvaTLIAETGGQNTMIVDSTALPEQVVRDVMRSAFASAGQRCSALRVLFVQED 855
Cdd:cd07081 177 PGIGLLLATGGPAVVKA-----AYSSGK--PAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 856 IADRITSLiqgaMQELHIGLPQHHHTD-VGPVI--------DLLAKNKLQ----AHIDKMRATSKLVGEVSLTDECNFgd 922
Cdd:cd07081 250 VYDEVMRL----FEGQGAYKLTAEELQqVQPVIlkngdvnrDIVGQDAYKiaaaAGLKVPQETRILIGEVTSLAEHEP-- 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2030906275 923 fiapiafeinsinqLENEQFGPILHIVRYKAADLNNVIAE--INATGFGLTMGIHSRNERTYTDIER 987
Cdd:cd07081 324 --------------FAHEKLSPVLAMYRAANFADADAKALalKLEGGCGHTSAMYSDNIKAIENMNQ 376
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
718-870 |
8.84e-03 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 39.67 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 718 QVAA-ALVAGNTVI---AKPAEQTSLIAARTM-ELMLEAGLPKEAVHLLPGGG-AAVGSLLTSDERIAGVVFTGStetAQ 791
Cdd:PRK00197 132 DAAAlCLKSGNAVIlrgGSEAIHSNRALVAVIqEALEEAGLPADAVQLVETTDrAAVGELLKLDGYVDVIIPRGG---AG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030906275 792 VINRalAKRDTNVATLiaETG-GQNTMIVDSTALPEQVVRDVmrsaFASAGQR---CSALRVLFVQEDIADRITSLIQGA 867
Cdd:PRK00197 209 LIRR--VVENATVPVI--EHGdGICHIYVDESADLDKALKIV----LNAKTQRpsvCNALETLLVHEAIAEEFLPKLAEA 280
|
...
gi 2030906275 868 MQE 870
Cdd:PRK00197 281 LAE 283
|
|
| |
