|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
1-1202 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 2030.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1 MFNFAFPTQTPLRQAVTDAYRRDEIEAVQDMLQRAQMTDEERNAASELARRLVTQVRSSRTKaSGVDALMHEFSLSSEEG 80
Cdd:PRK11905 4 MFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKG-TGVEALLQEYSLSSQEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 81 VALMCLAEALLRIPDNATRDRLIADKISEGNWKSHLNNSPSLFVNAAAWGLLITGKLTTNTSEKNMGSALSRMISKGGAP 160
Cdd:PRK11905 83 VALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLIARLGEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 161 LIRQGVNYAMRLLGKQFVTGQTIEEALQNGKEREKMGYRFSFDMLGEAAYTEEDANRYYNDYVQAIHAIGKDAAGQGVYE 240
Cdd:PRK11905 163 VIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGVYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 241 GNGISVKLSAIHPRYSRAQHERVMSELLPRLKELFLLGKKYDIGINIDAEEANRLELSLDLMEALVSDPDLAGYKGIGFV 320
Cdd:PRK11905 243 GPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIGFV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 321 VQAYQKRCPFVIDYLIDLARRNNQKLMIRLVKGAYWDSEVKWAQVDGMEGYPTYTRKVHTDISYLACARKLLDAQDAVFP 400
Cdd:PRK11905 323 VQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAARDVIYP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 401 QFATHNAYTLGAIYQMGKG-KDFEHQCLHGMGETLYDQVVGPQNLGRRVRVYAPVGTHETLLAYLVRRLLENGANSSFVN 479
Cdd:PRK11905 403 QFATHNAQTLAAIYELAGGkGDFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVN 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 480 QIVDENISIDRLIKSPFDTIAEQGIHLHPALPLPRDLYGKGRLNSQGVDFSNENVLQNLQEKLNQASSEDFHAASIVNGE 559
Cdd:PRK11905 483 RIVDENVPVEELIADPVEKVAAMGVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLAGG 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 560 ArNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAG 639
Cdd:PRK11905 563 D-VDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 640 KTLNNAVAEVREAVDFCRYYANEAENTLPKD-AKAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATY 718
Cdd:PRK11905 642 KTLANAIAEVREAVDFLRYYAAQARRLLNGPgHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAAR 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 719 AVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKR-DDSPVLIAETGGQNAMIVDSTA 796
Cdd:PRK11905 722 AVRLLHEAGVPKDALQLLPGDGRtVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRsGPPVPLIAETGGQNAMIVDSSA 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 797 LPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKMK 876
Cdd:PRK11905 802 LPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMR 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 877 GVAKAYHEIKTAADVdeNNSTFVRPILFELNNLNELQREVFGPVLHVVRYRASELDQLIDQINAKGYALTSGVHSRIEGT 956
Cdd:PRK11905 882 AAGRLVHQLPLPAET--EKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGLHSRIDET 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 957 VDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAGGSFYLQRLVRTPEWVAPTLSRIGQADEDALKRLETLVH 1036
Cdd:PRK11905 960 IAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTPIPPAHESVDTDAAARDFLAWLDK 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1037 KlpfnaeEKKAAAAALGHARVRTLRKAEAVLVGPTGERNSLSWRSPKRVWVHGGNLLQAFSALTELAAAGIQTVVEPNSP 1116
Cdd:PRK11905 1040 E------GKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVADTEEALLRQLAAALATGNVAVVAADSG 1113
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1117 LASYSADLDGLLQVNSK-----PENAGISHVAAIEPLSSER--KQELAGRDGALIRILPSEQ--GLDILQVFEEISCSIN 1187
Cdd:PRK11905 1114 LAAALADLPGLVAARIDwtqdwEADDPFAGALLEGDAERARavRQALAARPGAIVPLIAAEPtdAYDLARLVEERSVSIN 1193
|
1210
....*....|....*
gi 1080520335 1188 TTAAGGNASLMAVAD 1202
Cdd:PRK11905 1194 TTAAGGNASLMALGE 1208
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
9-1198 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1673.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 9 QTPLRQAVTDAYRRDEIEAVQDMLQRAQMTDEERNAASELARRLVTQVRSSRT---KASGVDALMHEFSLSSEEGVALMC 85
Cdd:PRK11809 88 QSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSaggRAGMVQGLLQEFSLSSQEGVALMC 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 86 LAEALLRIPDNATRDRLIADKISEGNWKSHLNNSPSLFVNAAAWGLLITGKLTTNTSEKNMGSALSRMISKGGAPLIRQG 165
Cdd:PRK11809 168 LAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSGEPLIRKG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 166 VNYAMRLLGKQFVTGQTIEEALQNGKEREKMGYRFSFDMLGEAAYTEEDANRYYNDYVQAIHAIGKDAAGQGVYEGNGIS 245
Cdd:PRK11809 248 VDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGIYEGPGIS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 246 VKLSAIHPRYSRAQHERVMSELLPRLKELFLLGKKYDIGINIDAEEANRLELSLDLMEALVSDPDLAGYKGIGFVVQAYQ 325
Cdd:PRK11809 328 IKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQ 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 326 KRCPFVIDYLIDLARRNNQKLMIRLVKGAYWDSEVKWAQVDGMEGYPTYTRKVHTDISYLACARKLLDAQDAVFPQFATH 405
Cdd:PRK11809 408 KRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLIYPQFATH 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 406 NAYTLGAIYQMGKGK----DFEHQCLHGMGETLYDQVVGPQ---NLGRRVRVYAPVGTHETLLAYLVRRLLENGANSSFV 478
Cdd:PRK11809 488 NAHTLAAIYHLAGQNyypgQYEFQCLHGMGEPLYEQVVGKVadgKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFV 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 479 NQIVDENISIDRLIKSPFD---TIAEQGIHL---HPALPLPRDLYGKGRLNSQGVDFSNENVLQNLQEKLNQASSEDFHA 552
Cdd:PRK11809 568 NRIADTSLPLDELVADPVEaveKLAQQEGQLglpHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLASAHQKWQA 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 553 ASIVnGEARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMM 632
Cdd:PRK11809 648 APML-EDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMG 726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 633 LAVREAGKTLNNAVAEVREAVDFCRYYANEAENTLPKDA-KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQ 711
Cdd:PRK11809 727 LLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDThRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQ 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 712 TSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDS---PV-LIAETGG 786
Cdd:PRK11809 807 TPLIAAQAVRILLEAGVPAGVVQLLPGRGEtVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPqgrPIpLIAETGG 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 787 QNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQ 866
Cdd:PRK11809 887 QNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKA 966
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 867 NLLAHINKMKGVAKAYHEIKTAADVDENNSTFVRPILFELNNLNELQREVFGPVLHVVRYRASELDQLIDQINAKGYALT 946
Cdd:PRK11809 967 NIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQINASGYGLT 1046
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 947 SGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAGGSFYLQRLV--RTPEWVAPTLSR---IG 1021
Cdd:PRK11809 1047 LGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLatRPEDALAVTLARqdaEY 1126
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1022 QADEDALKRLETLVHKLPFNAEEKKAAAAAL-GHARVRTLRKAEAVLVGPTGERNSLSWRSPKRVWVHGGNllqAFSALT 1100
Cdd:PRK11809 1127 PVDAQLRAALLAPLTALREWAAEREPELAALcDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADT---EQDALT 1203
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1101 ELAAA---GIQTVVEPNSP----LASYSADLDGLLQVNSKPENAGISHVAAIEPLSSERKQEL----AGRDGALIRIL-- 1167
Cdd:PRK11809 1204 QLAAVlavGSQALWPDDALhralVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDSDQLRALceqvAQRDGPIVSVQgf 1283
|
1210 1220 1230
....*....|....*....|....*....|..
gi 1080520335 1168 -PSEQGLDILQVFEEISCSINTTAAGGNASLM 1198
Cdd:PRK11809 1284 aRGETNILLERLLIERSLSVNTAAAGGNASLM 1315
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
1-1007 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1613.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1 MFNFAFPTQTPLRQAVTDAYRRDEIEAVQDMLQRAQMTDEERNAASELARRLVTQVRSSRTKASGVDALMHEFSLSSEEG 80
Cdd:PRK11904 2 LGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGGIDAFLQEYSLSTEEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 81 VALMCLAEALLRIPDNATRDRLIADKISEGNWKSHLNNSPSLFVNAAAWGLLITGKL--TTNTSEKNMGSALSRMISKGG 158
Cdd:PRK11904 82 IALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVvkLDKKADGTPSGVLKRLVNRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 159 APLIRQGVNYAMRLLGKQFVTGQTIEEALQNGKEREKMGYRFSFDMLGEAAYTEEDANRYYNDYVQAIHAIGKDAAGQGV 238
Cdd:PRK11904 162 EPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 239 YEGNGISVKLSAIHPRYSRAQHERVMSELLPRLKELFLLGKKYDIGINIDAEEANRLELSLDLMEALVSDPDLAGYKGIG 318
Cdd:PRK11904 242 PARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 319 FVVQAYQKRCPFVIDYLIDLARRNNQKLMIRLVKGAYWDSEVKWAQVDGMEGYPTYTRKVHTDISYLACARKLLDAQDAV 398
Cdd:PRK11904 322 LAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSARGAI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 399 FPQFATHNAYTLGAIYQMGKGKDFEHQCLHGMGETLYDQVVgpQNLGRRVRVYAPVGTHETLLAYLVRRLLENGANSSFV 478
Cdd:PRK11904 402 YPQFATHNAHTVAAILEMAGHRGFEFQRLHGMGEALYDALL--DAPGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSFV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 479 NQIVDENISIDRLIKSPFDTIAEQGIHLHPALPLPRDLYGKGRLNSQGVDFSNENVLQNLQEKLNQASSEDFHAASIVNG 558
Cdd:PRK11904 480 HRLVDPDVPIEELVADPVEKLRSFETLPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPIING 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 559 EarnvGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREA 638
Cdd:PRK11904 560 E----GEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREA 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 639 GKTLNNAVAEVREAVDFCRYYANEAENTLpkdAKAV-----------------GAIVAISPWNFPLAIFTGEVVSALAAG 701
Cdd:PRK11904 636 GKTLQDAIAEVREAVDFCRYYAAQARRLF---GAPEklpgptgesnelrlhgrGVFVCISPWNFPLAIFLGQVAAALAAG 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 702 NTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPV- 779
Cdd:PRK11904 713 NTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGAtVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVp 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 780 LIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPV 859
Cdd:PRK11904 793 LIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPV 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 860 IDAEAQQNLLAHINKMKGVAKAYHeiKTAADVDENNSTFVRPILFELNNLNELQREVFGPVLHVVRYRASELDQLIDQIN 939
Cdd:PRK11904 873 IDAEAKANLDAHIERMKREARLLA--QLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVIDAIN 950
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080520335 940 AKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAGGSFYLQRLV 1007
Cdd:PRK11904 951 ATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFA 1018
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
1-1198 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1497.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1 MFNFAFPTQTPLRQAVTDAYRRDEIEAVQDMLQRAQMTDEERNAASELARRLVTQVRSSRTkASGVDALMHEFSLSSEEG 80
Cdd:COG4230 5 LFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRG-GGGGLLLLLELSSLSSEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 81 VALMCLAEALLRIPDNATRDRLIADKISEGNWKSHLNNSPSLFVNAAAWGLLITGKLTTNTSEKNMGSALSRMISKGGAP 160
Cdd:COG4230 84 LALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSLASGLLRLLGRLGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 161 LIRQGVNYAMR----LLGKQFVTGQTIEEALQNGKEREKMGYRFSFDMLGEAAYTEEDANRYYNDYVQAIHAIGKDAAGQ 236
Cdd:COG4230 164 GIRRAMRAAMMmmmgLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGSGGP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 237 GVYEGNGISVKLSAIHPRYSRAQHERVMSELLPRLKELFLLGKKYDIGINIDAEEANRLELSLDLMEALVSDPDLAGYKG 316
Cdd:COG4230 244 GPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 317 IGFVVQAYQKRCPFVIDYLIDLARRNNQKLMIRLVKGAYWDSEVKWAQVDGMEGYPTYTRKVHTDISYLACARKLLDAQD 396
Cdd:COG4230 324 VGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAAQP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 397 AVFPQFATHNAYTLGAIYQMGKGKDFEHQCLHGMGETLYDQVvGPQNLGRRVRVYAPVGTHETLLAYLVRRLLENGANSS 476
Cdd:COG4230 404 AFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQV-GRGKLGRPCRIYAPVGSHEDLLAYLVRRLLENGANSS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 477 FVNQIVDENISIDRLIKSPFDTIAEQGIHLHPALPLPRDLYGKGRLNSQGVDFSNENVLQNLQEKLNQASSEDFHAASIV 556
Cdd:COG4230 483 FVNRIADEDVPVEELIADPVEKARALGGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSAALAAAAEKQWQAAPLI 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 557 NGEARNvGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVR 636
Cdd:COG4230 563 AGEAAS-GEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 637 EAGKTLNNAVAEVREAVDFCRYYANEAENTL--PKDAKAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSL 714
Cdd:COG4230 642 EAGKTLPDAIAEVREAVDFCRYYAAQARRLFaaPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPL 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 715 IATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPV-LIAETGGQNAMIV 792
Cdd:COG4230 722 IAARAVRLLHEAGVPADVLQLLPGDGEtVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVpLIAETGGQNAMIV 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHI 872
Cdd:COG4230 802 DSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHI 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 873 NKMKGVAKAYHEikTAADVDENNSTFVRPILFELNNLNELQREVFGPVLHVVRYRASELDQLIDQINAKGYALTSGVHSR 952
Cdd:COG4230 882 ERMRAEGRLVHQ--LPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGVHSR 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 953 IEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAGGSFYLQRLVRTPEWVAPTLSRIGQAdedALKRLE 1032
Cdd:COG4230 960 IDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTAAGGNA---SLLALG 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1033 TLVHKLpfnaeekkaaaaaLGHarvrtlrkaeAVLVGPTGERNSLSWRSPKRVWVHGGNLLQAFSALTELAAAGIQTVVE 1112
Cdd:COG4230 1037 DWLASL-------------LGA----------LTLPGPTGERNTLTLRPRGRVLCLADSLEALLAQLAAALATGNRAVVA 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 1113 PNSPLASYSADLDgllqvnskpenAGISHVAAiEPLSSERKQELAGRDGALIRILpsEQGLDILQVFEEiscsinttaAG 1192
Cdd:COG4230 1094 ADLALAGLPAVLL-----------PPFDAVLF-EGRLRALRQALAARDGAIVPVI--DAGYDLERLLEE---------AG 1150
|
....*.
gi 1080520335 1193 GNASLM 1198
Cdd:COG4230 1151 GNASLM 1156
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
515-1011 |
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: 837.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 515 DLYGKGRLNSQGVDFSNENVLQNLQEKLNQASSEDFHAASIVNGEARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAI 594
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 595 GAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAENTLPKD-AKA 673
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFsVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 674 VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARI 752
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGaDVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 753 GGVIFTGSTEVARLINKALSKRDDSPV-LIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVAD 831
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDAPVpLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 832 KMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKMKGVAKAYHEIKTAADVDENNSTFVRPILFELNNLNE 911
Cdd:TIGR01238 321 RVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFELDDIAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 912 LQREVFGPVLHVVRYRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLS 991
Cdd:TIGR01238 401 LSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLS 480
|
490 500
....*....|....*....|
gi 1080520335 992 GTGPKAGGSFYLQRLVRTPE 1011
Cdd:TIGR01238 481 GTGPKAGGPHYLYRLTQVQY 500
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
473-1008 |
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: 721.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 473 ANSSFVNQIVDENISidrlikspfdtiaeqgihlhpalplprdlygkgrlnsqgvdfsnenvLQNLQEKLNQASSEDFHA 552
Cdd:cd07125 1 ANSSFVNRIFDLEVP-----------------------------------------------LEALADALKAFDEKEWEA 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 553 ASIVNGEARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMM 632
Cdd:cd07125 34 IPIINGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 633 LAVREAGKTLNNAVAEVREAVDFCRYYANEAE---------------NTLPKDAKavGAIVAISPWNFPLAIFTGEVVSA 697
Cdd:cd07125 114 LAAAEAGKTLADADAEVREAIDFCRYYAAQARelfsdpelpgptgelNGLELHGR--GVFVCISPWNFPLAIFTGQIAAA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 698 LAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDD 776
Cdd:cd07125 192 LAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEeIGEALVAHPRIDGVIFTGSTETAKLINRALAERDG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 777 S-PVLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTD 855
Cdd:cd07125 272 PiLPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 856 IGPVIDAEAQQNLLAHINKMKGVAKAYHEiktaADVDENNSTFVRPILFELNNLNELQREVFGPVLHVVRYRASELDQLI 935
Cdd:cd07125 352 VGPLIDKPAGKLLRAHTELMRGEAWLIAP----APLDDGNGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEAI 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080520335 936 DQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAGGSFYLQRLVR 1008
Cdd:cd07125 428 EDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGN 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
35-1016 |
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: 694.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 35 AQMTDEERNAASELARRLVTQVRSSRtkASGVDALMHEFSLSSEEGVALMCLAEALLRIPDNATRDRLIADKISegnwks 114
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAAP--EGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 115 hlnNSPSLFVNAAAWGLLITgklttntseknmgsalsrMISKGGAPLIRQGVNYAMRLLGKQFVTGQTIEEALQNGKERE 194
Cdd:COG0506 75 ---KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 195 KMGYRFSFDMLGEAAYTEEDANRYYNDYVQAIHAIGKDAagqgvYEGNGISVKLSAIHPRYSRAQHERVMSELLPRLKEL 274
Cdd:COG0506 134 AKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 275 FLLGKKYDIGINIDAEEANRLELSLDLMEALVSDPDLAGYKGIGFVVQAYQKRCPFVIDYLIDLARRNNQKLMIRLVKGA 354
Cdd:COG0506 209 ARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 355 YWDSEVKWAQVDGMeGYPTYTRKVHTDISYLACARKLLDAQDAVFPQFATHNAYTLGAIYQMGK-----GKDFEHQCLHG 429
Cdd:COG0506 289 YWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGergrpPDRFEFQMLYG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 430 MGETLYDQV--VGPQNLGRRVRVYAPVGTHETLLAYLVRRLLENGANSSFVNQIVDENISIDRLIKSPFDTIAEQGIHLH 507
Cdd:COG0506 368 MGEDLQRALaaVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 508 PALPLPRDLYGKGRLNSQGVDFSNENVLQNLQEKLNQASSEDFHAASIVNGEARNVGEAQPVRNPADHNDVVGTVsfADA 587
Cdd:COG0506 448 PPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAA--AAA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 588 ALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAENTL 667
Cdd:COG0506 526 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARA 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 668 PKDAKAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGDVG---- 743
Cdd:COG0506 606 AAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGggvl 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 744 -----------SALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDS 812
Cdd:COG0506 686 vlgagggaggaAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASAS 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 813 AGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKMKGVAKAYHEIKTAADVD 892
Cdd:COG0506 766 ASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPG 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 893 EnNSTFVRPILFELNNLNELQREVFGPVLHVVRYRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVN 972
Cdd:COG0506 846 L-LTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGG 924
|
970 980 990 1000
....*....|....*....|....*....|....*....|....
gi 1080520335 973 RNIVGAVVGVQPFGGHGLSGTGPKAGGSFYLQRLVRTPEWVAPT 1016
Cdd:COG0506 925 GGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALA 968
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
538-1016 |
7.64e-152 |
|
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: 464.74 E-value: 7.64e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 538 LQEKLNQASSEDFHAASIVNG-EARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCL 616
Cdd:cd07083 4 MREALRRVKEEFGRAYPLVIGgEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 617 RRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAENTLPKDAKAV--------------GAIVAISP 682
Cdd:cd07083 84 LKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVpypgednesfyvglGAGVVISP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 683 WNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGST 761
Cdd:cd07083 164 WNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEeVGAYLTEHERIRGINFTGSL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 762 EVARLINKALSKRDDS----PVLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINII 837
Cdd:cd07083 244 ETGKKIYEAAARLAPGqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 838 KGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKMKGVAKayheIKTAADVDENNSTFVRPILFELNNLNE--LQRE 915
Cdd:cd07083 324 LKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQ----LVLGGKRLEGEGYFVAPTVVEEVPPKAriAQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 916 VFGPVLHVVRYRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGP 995
Cdd:cd07083 400 IFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNA 479
|
490 500
....*....|....*....|.
gi 1080520335 996 KAGGSFYLQRLVrTPEWVAPT 1016
Cdd:cd07083 480 KTGGPHYLRRFL-EMKAVAER 499
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
186-480 |
4.89e-147 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 444.24 E-value: 4.89e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 186 ALQNGKEREKMGYRFSFDMLGEAAYTEEDANRYYNDYVQAIHAIGKDAAGQGVYEGNGISVKLSAIHPRYSRAQHERVMS 265
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 266 ELLPRLKELFLLGKKYDIGINIDAEEANRLELSLDLMEALVSDPDLAGYKGIGFVVQAYQKRCPFVIDYLIDLARRNNQK 345
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 346 LMIRLVKGAYWDSEVKWAQVdGMEGYPTYTRKVHTDISYLACARKLLDAQDAVFPQFATHNAYTLGAIYQMGK-----GK 420
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEelgipPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 421 DFEHQCLHGMGETLYDQVVgpqNLGRRVRVYAPVGTHETLLAYLVRRLLENGANSSFVNQ 480
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALV---AAGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
556-1005 |
9.42e-121 |
|
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: 381.78 E-value: 9.42e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEARNV--GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMML 633
Cdd:COG1012 10 IGGEWVAAasGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 634 AVREAGKTLNNAVAEVREAVDFCRYYANEAEN----TLPKDA---------KAVGAIVAISPWNFPLAIFTGEVVSALAA 700
Cdd:COG1012 89 LTLETGKPLAEARGEVDRAADFLRYYAGEARRlygeTIPSDApgtrayvrrEPLGVVGAITPWNFPLALAAWKLAPALAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 701 GNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRddSPV 779
Cdd:COG1012 169 GNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGsEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN--LKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 780 LIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPV 859
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 860 IDAEAQQNLLAHINkmKGVAKayhEIKTAAD---VDENNSTFVRPILFE-LNNLNEL-QREVFGPVLHVVRYRasELDQL 934
Cdd:COG1012 327 ISEAQLERVLAYIE--DAVAE---GAELLTGgrrPDGEGGYFVEPTVLAdVTPDMRIaREEIFGPVLSVIPFD--DEEEA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080520335 935 IDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGvQPFGGHGLSGTGPKAGG---SFYLQR 1005
Cdd:COG1012 400 IALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGReglEEYTET 472
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
555-1008 |
7.76e-119 |
|
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: 378.10 E-value: 7.76e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 555 IVNGEARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLA 634
Cdd:cd07124 36 VIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 635 VREAGKTLNNAVAEVREAVDFCRYYANEAENTLPKDA------------KAVGAIVAISPWNFPLAIFTGEVVSALAAGN 702
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVemvpgednryvyRPLGVGAVISPWNFPLAILAGMTTAALVTGN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 703 TVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPV-- 779
Cdd:cd07124 196 TVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEeVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKwl 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 780 --LIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIG 857
Cdd:cd07124 276 krVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 858 PVIDAEAQQNLLAHInkmkGVAKAYHEIKTAADVDENNST--FVRPILFELNNLNE--LQREVFGPVLHVVRYRasELDQ 933
Cdd:cd07124 356 PVIDKGARDRIRRYI----EIGKSEGRLLLGGEVLELAAEgyFVQPTIFADVPPDHrlAQEEIFGPVLAVIKAK--DFDE 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080520335 934 LIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAGGSFYLQRLVR 1008
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQ 504
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
564-1004 |
5.82e-118 |
|
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: 373.79 E-value: 5.82e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLN 643
Cdd:pfam00171 6 SETIEVINPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 644 NAVAEVREAVDFCRYYANEAEN----TLPKDA--------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQ 711
Cdd:pfam00171 85 EARGEVDRAIDVLRYYAGLARRldgeTLPSDPgrlaytrrEPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 712 TSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRddSPVLIAETGGQNAM 790
Cdd:pfam00171 165 TPLTALLLAELFEEAGLPAGVLNVVTGSGaEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQN--LKRVTLELGGKNPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 791 IVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLA 870
Cdd:pfam00171 243 IVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 871 HINkmKGVAKAYhEIKTAADVDENNSTFVRP-ILFELNNLNELQR-EVFGPVLHVVRYraSELDQLIDQINAKGYALTSG 948
Cdd:pfam00171 323 YVE--DAKEEGA-KLLTGGEAGLDNGYFVEPtVLANVTPDMRIAQeEIFGPVLSVIRF--KDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080520335 949 VHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVqPFGGHGLSGTG---PKAGGSFYLQ 1004
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFGregGPYGLEEYTE 455
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
591-1003 |
1.77e-106 |
|
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: 341.88 E-value: 1.77e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 591 QEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAE------ 664
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARrlhgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 665 -NTLPKDAKA------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVL 737
Cdd:cd07078 81 iPSPDPGELAivrrepLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 738 GAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRdDSPVlIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQR 816
Cdd:cd07078 161 GDGDeVGAALASHPRVDKISFTGSTAVGKAIMRAAAEN-LKRV-TLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 817 CSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKMKGvakayHEIKTAAD---VDE 893
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKA-----EGAKLLCGgkrLEG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 894 NNSTFVRPILFELNNLNEL--QREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYV 971
Cdd:cd07078 314 GKGYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWI 391
|
410 420 430
....*....|....*....|....*....|..
gi 1080520335 972 NRNIVGAVVGvQPFGGHGLSGTGpKAGGSFYL 1003
Cdd:cd07078 392 NDYSVGAEPS-APFGGVKQSGIG-REGGPYGL 421
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
528-1004 |
6.62e-100 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 327.28 E-value: 6.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 528 DFSNENVLQNLQEKLNQASSE-DFHAASIVNGEARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSA 606
Cdd:PRK03137 12 DFSVEENVEAFEEALKKVEKElGQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 607 KPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEA---------------ENTLpkDA 671
Cdd:PRK03137 92 WSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMlkladgkpvesrpgeHNRY--FY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 672 KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDA 750
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSeVGDYLVDHP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 751 RIGGVIFTGSTEVARLINKALSKRDDSPV----LIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQ 826
Cdd:PRK03137 250 KTRFITFTGSREVGLRIYERAAKVQPGQIwlkrVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 827 EDVADKMINIIKGAMDELVVGKPIQlTTDIGPVIDAEAQQNLLAHINKMKGVAKayheIKTAADVDENNSTFVRPILFEl 906
Cdd:PRK03137 330 EDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEGR----LVLGGEGDDSKGYFIQPTIFA- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 907 nNLNE----LQREVFGPVLHVVryRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGV 982
Cdd:PRK03137 404 -DVDPkariMQEEIFGPVVAFI--KAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGY 480
|
490 500
....*....|....*....|..
gi 1080520335 983 QPFGGHGLSGTGPKAGGSFYLQ 1004
Cdd:PRK03137 481 HPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
528-1003 |
4.88e-97 |
|
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: 319.50 E-value: 4.88e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 528 DFSNENVLQNLQEKLNQASSE-DFHAASIVNGE-ARNVGEAQPVrNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWS 605
Cdd:TIGR01237 8 DFADEENRQAFFKALATVKEQlGKTYPLVINGErVETENKIVSI-NPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 606 AKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAE--------NTLPKDAKA---- 673
Cdd:TIGR01237 87 KTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIelakgkpvNSREGETNQyvyt 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 674 -VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDAR 751
Cdd:TIGR01237 167 pTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGsEVGDYLVDHPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 752 IGGVIFTGSTEVARLINKALSK----RDDSPVLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQE 827
Cdd:TIGR01237 247 TSLITFTGSREVGTRIFERAAKvqpgQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 828 DVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINkmkgVAKAYHEIKTAADVDENNSTFVRPILFEln 907
Cdd:TIGR01237 327 KVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIE----IGKAEGRLVSGGCGDDSKGYFIGPTIFA-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 908 NLNE----LQREVFGPVLHVVryRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQ 983
Cdd:TIGR01237 401 DVDRkarlAQEEIFGPVVAFI--RASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQ 478
|
490 500
....*....|....*....|
gi 1080520335 984 PFGGHGLSGTGPKAGGSFYL 1003
Cdd:TIGR01237 479 PFGGFKMSGTDSKAGGPDYL 498
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
556-1004 |
9.70e-92 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 303.40 E-value: 9.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAV 635
Cdd:cd07097 5 IDGEWVAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 636 REAGKTLNNAVAEVREAVDFCRYYANEAEN----TLPKDAK---------AVGAIVAISPWNFPLAIFTGEVVSALAAGN 702
Cdd:cd07097 85 REEGKTLPEARGEVTRAGQIFRYYAGEALRlsgeTLPSTRPgvevettrePLGVVGLITPWNFPIAIPAWKIAPALAYGN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 703 TVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSpvLI 781
Cdd:cd07097 165 TVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGsEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR--VQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 782 AETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVID 861
Cdd:cd07097 243 LEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 862 AEAQQNLLAHINKMKGVAkAYHEIKTAADVDENNSTFVRPILFElNNLNEL---QREVFGPVLHVVRYRasELDQLIDQI 938
Cdd:cd07097 323 ERQLEKDLRYIEIARSEG-AKLVYGGERLKRPDEGYYLAPALFA-GVTNDMriaREEIFGPVAAVIRVR--DYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 939 NAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVqPFGGHGLSGTGPKAGGS----FYLQ 1004
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGEaaleFYTT 467
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
596-1009 |
1.23e-84 |
|
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: 279.88 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 596 AAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAE-----NTLPKD 670
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADklggpELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 671 AKA--------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD- 741
Cdd:cd06534 82 PGGeayvrrepLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 742 VGSALTGDARIGGVIFTGSTEVARLINKALSKRdDSPVlIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALR 821
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAAEN-LKPV-TLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 822 ILCVQEDVADKMIniikgamDELVvgkpiQLTTDIGPvidaeaqqnllahinKMkgvaKAYHEiktaadvdennstfvrp 901
Cdd:cd06534 240 RLLVHESIYDEFV-------EKLV-----TVLVDVDP---------------DM----PIAQE----------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 902 ilfelnnlnelqrEVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVG 981
Cdd:cd06534 272 -------------EIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE 336
|
410 420
....*....|....*....|....*...
gi 1080520335 982 vQPFGGHGLSGTGpKAGGSFYLQRLVRT 1009
Cdd:cd06534 337 -APFGGVKNSGIG-REGGPYGLEEYTRT 362
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
554-1000 |
2.05e-83 |
|
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: 280.77 E-value: 2.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 554 SIVNGE--ARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALM 631
Cdd:cd07131 1 NYIGGEwvDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 632 MLAVREAGKTLNNAVAEVREAVDFCRYYANEAE----NTLP-----KDAKAV----GAIVAISPWNFPLAIFTGEVVSAL 698
Cdd:cd07131 81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRrlfgETVPselpnKDAMTRrqpiGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 699 AAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDS 777
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEeVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 778 PVLiaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIG 857
Cdd:cd07131 241 VAL--EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 858 PVIDAEAQQNLLAHINKMKGV-AKAYHEIKTAADVDENNSTFVRPILFEL--NNLNELQREVFGPVLHVVRYraSELDQL 934
Cdd:cd07131 319 PLINEAQLEKVLNYNEIGKEEgATLLLGGERLTGGGYEKGYFVEPTVFTDvtPDMRIAQEEIFGPVVALIEV--SSLEEA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080520335 935 IDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVqPFGGHGLSGTGPKAGGS 1000
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
569-994 |
2.70e-80 |
|
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: 270.84 E-value: 2.70e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07103 1 VINPAT-GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAEN----TLPKDA---------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLI 715
Cdd:cd07103 80 VDYAASFLEWFAEEARRiygrTIPSPApgkrilvikQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 716 ATYAVSLMHQAGIPTSALQLVLG-AGDVGSALTGDARIGGVIFTGSTEVARLINKALS---KRddspvLIAETGGqNA-M 790
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAAdtvKR-----VSLELGG-NApF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 791 IVDSTALPEQVCLDVLNSAFDSAGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLL 869
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCvCANRIY-VHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 870 AHIN--KMKGvAKayheIKTAADVDENNSTFVRPILfeLNNLNE----LQREVFGPVLHVVRYraSELDQLIDQINAKGY 943
Cdd:cd07103 313 ALVEdaVAKG-AK----VLTGGKRLGLGGYFYEPTV--LTDVTDdmliMNEETFGPVAPIIPF--DTEDEVIARANDTPY 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1080520335 944 ALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVvgVQPFGGHGLSGTG 994
Cdd:cd07103 384 GLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
554-998 |
7.57e-78 |
|
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: 265.20 E-value: 7.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 554 SIVNGEAR-NVGEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMM 632
Cdd:cd07086 1 GVIGGEWVgSGGETFTSRNPAN-GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 633 LAVREAGKTLNNAVAEVREAVDFCRYYANEAE----NTLP-----KDAKA----VGAIVAISPWNFPLAIFTGEVVSALA 699
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRmlygLTIPserpgHRLMEqwnpLGVVGVITAFNFPVAVPGWNAAIALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 700 AGNTVIAKPAEQTSLIATYAVSLMHQA----GIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRD 775
Cdd:cd07086 160 CGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 776 DSPVLiaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTD 855
Cdd:cd07086 240 GRVLL--ELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 856 IGPVIDAEAQQNLLAHINKMKGV-AKAYHEIKTAADVDENNstFVRPILFE-LNNLNEL-QREVFGPVLHVVRYraSELD 932
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQgGTVLTGGKRIDGGEPGN--YVEPTIVTgVTDDARIvQEETFAPILYVIKF--DSLE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080520335 933 QLIDQINAKGYALTSGVHSRIEGTVDHIRDR--IEAGNIYVNRNIVGAVVGVqPFGGHGLSGTGPKAG 998
Cdd:cd07086 394 EAIAINNDVPQGLSSSIFTEDLREAFRWLGPkgSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
531-1015 |
3.65e-76 |
|
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: 261.75 E-value: 3.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 531 NENVL---------QNLQEKLNQASSEDFHAASIVNGEARNVGEAQPVRNPADHNDVVGTVSFADAALAQEAIGAAVAAL 601
Cdd:cd07123 3 NEPVLsyapgsperAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 602 PEWSAKPASERADCLRRFADLLEqhTP------ALMMLAvreAGKTLNNavAEVR---EAVDFCR---YYANEAENTLPK 669
Cdd:cd07123 83 KEWARMPFEDRAAIFLKAADLLS--GKyryelnAATMLG---QGKNVWQ--AEIDaacELIDFLRfnvKYAEELYAQQPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 670 DAKAV-----------GAIVAISPWNFPlAIfTGEVVSALA-AGNTVIAKPAEqTSLIATYAV-SLMHQAGIPTSALQLV 736
Cdd:cd07123 156 SSPAGvwnrleyrpleGFVYAVSPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 737 LGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDS----PVLIAETGGQNAMIVDSTALPEQVCLDVLNSAFD 811
Cdd:cd07123 233 PGDGpVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRyrtyPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 812 SAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKmkgvAKAYHEIKTAADV 891
Cdd:cd07123 313 YQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDH----AKSDPEAEIIAGG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 892 DENNST--FVRPILFELNNLNE--LQREVFGPVLHVVRYRASELD---QLIDQinAKGYALTSGVHSR----IEGTVDHI 960
Cdd:cd07123 389 KCDDSVgyFVEPTVIETTDPKHklMTEEIFGPVLTVYVYPDSDFEetlELVDT--TSPYALTGAIFAQdrkaIREATDAL 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1080520335 961 RDriEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAGGSFYLQRlvrtpeWVAP 1015
Cdd:cd07123 467 RN--AAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLR------WVSP 513
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
592-992 |
9.03e-74 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 252.19 E-value: 9.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 592 EAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVRE-------AVDFCRYYANEAE 664
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAmagkidiSIKAYHERTGERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 665 NTLPkDAKAV------GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLG 738
Cdd:cd07095 84 TPMA-QGRAVlrhrphGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 739 AGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDspVLIA-ETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRC 817
Cdd:cd07095 163 GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPG--KILAlEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 818 S-ALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINK-MKGVAKAYHEIKtaadVDENN 895
Cdd:cd07095 241 TcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDlLALGGEPLLAME----RLVAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 896 STFVRPILFELNNLNELQ-REVFGPVLHVvrYRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRN 974
Cdd:cd07095 317 TAFLSPGIIDVTDAADVPdEEIFGPLLQV--YRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRP 394
|
410
....*....|....*...
gi 1080520335 975 IVGAvVGVQPFGGHGLSG 992
Cdd:cd07095 395 TTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
569-994 |
2.16e-73 |
|
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: 251.72 E-value: 2.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 V--REAVDFcRYYAN----EAENTLPKDAKA--------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSL 714
Cdd:cd07093 80 DipRAAANF-RFFADyilqLDGESYPQDGGAlnyvlrqpVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 715 IATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSpvLIAETGGQNAMIV- 792
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGpEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKP--VSLELGGKNPNIVf 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTALPEqvCLD-VLNSAFDSAGQRCSA-LRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEaqqnlla 870
Cdd:cd07093 237 ADADLDR--AVDaAVRSSFSNNGEVCLAgSRIL-VQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKE------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 871 HINKMKG---VAKAY-HEIKTAADVDE----NNSTFVRPILFE-LNNLNEL-QREVFGPVLHVVRYRaSElDQLIDQINA 940
Cdd:cd07093 307 HLEKVLGyveLARAEgATILTGGGRPElpdlEGGYFVEPTVITgLDNDSRVaQEEIFGPVVTVIPFD-DE-EEAIELAND 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1080520335 941 KGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVvgVQPFGGHGLSGTG 994
Cdd:cd07093 385 TPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDL--RTPFGGVKASGIG 436
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
569-994 |
4.27e-73 |
|
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: 250.52 E-value: 4.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPAdHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07106 1 VINPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANeaeNTLPKDA-------------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLI 715
Cdd:cd07106 80 VGGAVAWLRYTAS---LDLPDEViedddtrrvelrrKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 716 ATYAVSLMHQAgIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALS---KRddspvLIAETGGQNAMIV 792
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAktlKR-----VTLELGGNDAAIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVidaeaqQNlLAHI 872
Cdd:cd07106 231 LPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPV------QN-KMQY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 873 NKMKGV---AKAYH-EIKTAADVDENNSTFVRPILfeLNNLNELQR----EVFGPVLHVVRYraSELDQLIDQINAKGYA 944
Cdd:cd07106 304 DKVKELvedAKAKGaKVLAGGEPLDGPGYFIPPTI--VDDPPEGSRivdeEQFGPVLPVLKY--SDEDEVIARANDSEYG 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1080520335 945 LTSGVHSRIEGTVDHIRDRIEAGNIYVNRNivGAVVGVQPFGGHGLSGTG 994
Cdd:cd07106 380 LGASVWSSDLERAEAVARRLEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
567-994 |
6.28e-71 |
|
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: 244.81 E-value: 6.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 567 QPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAV 646
Cdd:cd07149 1 IEVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 647 AEVREAVDFCRYYANEAEN----TLPKDAKA-------------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPA 709
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKRlageTIPFDASPggegrigftirepIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 710 EQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLI-NKALSKRddspvLIAETGGQ 787
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIaRKAGLKK-----VTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 788 NAMIVDSTALPEQVCLDVLNSAFDSAGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQ 866
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 867 NLLAHINK-MKGVAK---------AYHEIKTAADVDENNSTFvrpilfelnnlnelQREVFGPVLHVVRYRasELDQLID 936
Cdd:cd07149 314 RIEEWVEEaVEGGARlltggkrdgAILEPTVLTDVPPDMKVV--------------CEEVFAPVVSLNPFD--TLDEAIA 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080520335 937 QINAKGYALTSGVH-SRIEGTVDHIRdRIEAGNIYVNrNIVGAVVGVQPFGGHGLSGTG 994
Cdd:cd07149 378 MANDSPYGLQAGVFtNDLQKALKAAR-ELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
556-1007 |
8.50e-71 |
|
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: 244.87 E-value: 8.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGE---ARNvGEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMM 632
Cdd:cd07088 2 INGEfvpSSS-GETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 633 LAVREAGKTLNNAVAEVREAVDFCRYYANEA--------ENTLPK-----DAKAVGAIVAISPWNFPLAIFTGEVVSALA 699
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWArriegeiiPSDRPNenifiFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 700 AGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSP 778
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGsVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 779 VLiaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGP 858
Cdd:cd07088 240 SL--ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 859 VIDAEAqqnlLAHINKMkgVAKAyheIKTAADV-------DENNSTFVRPILFE--LNNLNELQREVFGPVLHVVRYraS 929
Cdd:cd07088 318 LVNEAA----LDKVEEM--VERA---VEAGATLltggkrpEGEKGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKF--S 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 930 ELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAvvgVQPFggH------GLSGTGPKAGGSFYL 1003
Cdd:cd07088 387 SLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEA---MQGF--HagwkksGLGGADGKHGLEEYL 461
|
....
gi 1080520335 1004 QRLV 1007
Cdd:cd07088 462 QTKV 465
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
569-998 |
1.14e-69 |
|
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: 241.30 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAAL--PEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAV 646
Cdd:cd07114 1 SINPAT-GEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 647 AEVREAVDFCRYYANEAE----NTLPKDAK---------AVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTS 713
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADkiegAVIPVDKGdylnftrrePLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 714 LIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKAlSKRDDSPVlIAETGGQNAMIV 792
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGpETGEALVEHPLVAKIAFTGGTETGRHIARA-AAENLAPV-TLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHI 872
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 873 NKMK---GVAKAYHEIKTAADVDENNstFVRPILFE--LNNLNELQREVFGPVLHVVRYRaSElDQLIDQINAKGYALTS 947
Cdd:cd07114 318 ARAReegARVLTGGERPSGADLGAGY--FFEPTILAdvTNDMRIAQEEVFGPVLSVIPFD-DE-EEAIALANDSEYGLAA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1080520335 948 GVHSRIEGTVDHIRDRIEAGNIYVN--RnivgAVVGVQPFGGHGLSGTGPKAG 998
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
555-994 |
2.26e-69 |
|
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: 240.94 E-value: 2.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 555 IVNGEAR-NVGEAQPVRNPADHNdVVGTVSFADAALAQEAIGAAVAALPEWSA-KPASERADCLRRFADLLEQHTPALMM 632
Cdd:cd07082 5 LINGEWKeSSGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 633 LAVREAGKTLNNAVAEVREAVDFCRYYANEAEN----TLPKDAK-------------AVGAIVAISPWNFPLAIFTGEVV 695
Cdd:cd07082 84 LLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRldgdSLPGDWFpgtkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 696 SALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKR 774
Cdd:cd07082 164 PALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGrEIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 775 DdspvLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTT 854
Cdd:cd07082 244 R----LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 855 DIGPVIDAEAQQNLLAHIN--KMKGvAKAYHEIKTAADvdennsTFVRPILFElnNLNELQR----EVFGPVLHVVRYra 928
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDdaVAKG-ATVLNGGGREGG------NLIYPTLLD--PVTPDMRlaweEPFGPVLPIIRV-- 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 929 SELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVN----RNIvgavvGVQPFGGHGLSGTG 994
Cdd:cd07082 389 NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINskcqRGP-----DHFPFLGRKDSGIG 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
556-1012 |
7.35e-68 |
|
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: 236.64 E-value: 7.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEARNV--GEAQPVRNPAdHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMML 633
Cdd:cd07085 5 INGEWVESktTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 634 AVREAGKTLNNAVAEVR---EAVDFCRYYANEAE-NTLPKDAKAV---------GAIVAISPWNFPLAIFTGEVVSALAA 700
Cdd:cd07085 84 ITLEHGKTLADARGDVLrglEVVEFACSIPHLLKgEYLENVARGIdtysyrqplGVVAGITPFNFPAMIPLWMFPMAIAC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 701 GNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINK---ALSKRdds 777
Cdd:cd07085 164 GNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYEraaANGKR--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 778 pVLiAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIG 857
Cdd:cd07085 241 -VQ-ALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 858 PVIDAEAQQNLLAHINkmKGV---AKAYHEIKTAADVDENNSTFVRPILFELNNLNE--LQREVFGPVLHVVryRASELD 932
Cdd:cd07085 319 PVISPAAKERIEGLIE--SGVeegAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMkiYKEEIFGPVLSIV--RVDTLD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 933 QLIDQINAKGYA------LTSGVHSRiegtvdHIRDRIEAGNIYVNRNIvgAV-VGVQPFGGHGLSGTG-----PKAGGS 1000
Cdd:cd07085 395 EAIAIINANPYGngaaifTRSGAAAR------KFQREVDAGMVGINVPI--PVpLAFFSFGGWKGSFFGdlhfyGKDGVR 466
|
490
....*....|..
gi 1080520335 1001 FYLQRLVRTPEW 1012
Cdd:cd07085 467 FYTQTKTVTSRW 478
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
536-994 |
2.21e-67 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 236.13 E-value: 2.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 536 QNLQEKLNQASSedFHAASIVNGEARNV--GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERA 613
Cdd:PLN02278 11 QSALVKLRNAGL--LRTQGLIGGKWTDAydGKTFPVYNPAT-GEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 614 DCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEA--------ENTLPkDAK------AVGAIVA 679
Cdd:PLN02278 88 KILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAkrvygdiiPSPFP-DRRllvlkqPVGVVGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 680 ISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLG-AGDVGSALTGDARIGGVIFT 758
Cdd:PLN02278 167 ITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGdAPEIGDALLASPKVRKITFT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 759 GSTEVARLINKALS---KRddspvLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRC-SALRILcVQEDVADKMI 834
Cdd:PLN02278 247 GSTAVGKKLMAGAAatvKR-----VSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 835 NIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKM--KGvAKAYHEIKTAADvdenNSTFVRP-ILFELNNLNE 911
Cdd:PLN02278 321 EAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAvsKG-AKVLLGGKRHSL----GGTFYEPtVLGDVTEDML 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 912 LQR-EVFGPVLHVVRYRASEldQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGvqPFGGHGL 990
Cdd:PLN02278 396 IFReEVFGPVAPLTRFKTEE--EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQ 471
|
....
gi 1080520335 991 SGTG 994
Cdd:PLN02278 472 SGLG 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
568-994 |
5.84e-67 |
|
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: 233.39 E-value: 5.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 568 PVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVA 647
Cdd:cd07145 2 EVRNPAN-GEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYYANEAE----NTLPKDA-------------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAE 710
Cdd:cd07145 81 EVERTIRLFKLAAEEAKvlrgETIPVDAyeynerriaftvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 711 QTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINK---ALSKRddspvLIAETGG 786
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSeVGDEIVTNPKVNMISFTGSTAVGLLIASkagGTGKK-----VALELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 787 QNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQ 866
Cdd:cd07145 236 SDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 867 NLLAHINkmKGVAKAyHEIKTAADVDENNstFVRPILFELNNLNE--LQREVFGPVLHVVRYRASEldQLIDQINAKGYA 944
Cdd:cd07145 316 RMENLVN--DAVEKG-GKILYGGKRDEGS--FFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDDE--EAVEIANSTEYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520335 945 LTSGVHSRIEGTVDHIRDRIEAGNIYVNR-------NIvgavvgvqPFGGHGLSGTG 994
Cdd:cd07145 389 LQASVFTNDINRALKVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG 437
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
570-994 |
6.07e-66 |
|
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: 230.57 E-value: 6.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 570 RNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEV 649
Cdd:cd07099 1 RNPAT-GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 650 REAVDFCRYYANEAENTLPKDAKAVGAIVA----------------ISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTS 713
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRKVPTGLLMPnkkatveyrpygvvgvISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 714 LIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTgDARIGGVIFTGSTEVARLINKALSKRdDSPVLIaETGGQNAMIVD 793
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATGRKVMAAAAER-LIPVVL-ELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 794 STALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAeAQQNLL-AHI 872
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTA-RQLDIVrRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 873 N--KMKGvAKAyheiKTAADVDENNSTFVRPILfeLNNLNE----LQREVFGPVLHVVRYraSELDQLIDQINAKGYALT 946
Cdd:cd07099 316 DdaVAKG-AKA----LTGGARSNGGGPFYEPTV--LTDVPHdmdvMREETFGPVLPVMPV--ADEDEAIALANDSRYGLS 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1080520335 947 SGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTG 994
Cdd:cd07099 387 ASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
564-992 |
1.13e-65 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 230.62 E-value: 1.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLN 643
Cdd:PRK09457 14 GEAFESRNPVS-GEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 644 NAVAEV-----REAVDFCRYYAN--EAENTLPkDAKAV------GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAE 710
Cdd:PRK09457 93 EAATEVtaminKIAISIQAYHERtgEKRSEMA-DGAAVlrhrphGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 711 QTSLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSpVLIAETGGQNAM 790
Cdd:PRK09457 172 LTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEK-ILALEMGGNNPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 791 IVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDV-ADKMINIIKGAMDELVVGKPIQLTTD-IGPVIDA------ 862
Cdd:PRK09457 251 VIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEqaaqgl 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 863 -EAQQNLLAhinkmKGvAKAYHEIKTAADvdenNSTFVRPILFELNNLNEL-QREVFGPVLHVVRYraSELDQLIDQINA 940
Cdd:PRK09457 331 vAAQAQLLA-----LG-GKSLLEMTQLQA----GTGLLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDFDEAIRLANN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1080520335 941 KGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAvVGVQPFGGHGLSG 992
Cdd:PRK09457 399 TRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
568-998 |
2.08e-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: 229.79 E-value: 2.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 568 PVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAK--PASERADCLRRFADLLEQHTPALMMLAVREAGKTLN-N 644
Cdd:cd07091 22 PTINPAT-EEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEeS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 645 AVAEVREAVDFCRYYANEAE----NTLPKDAK--------AVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQT 712
Cdd:cd07091 101 AKGDVALSIKCLRYYAGWADkiqgKTIPIDGNflaytrrePIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 713 SLIATYAVSLMHQAGIPTSALQLVLGAGDV-GSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLIaETGGQNAMI 791
Cdd:cd07091 181 PLSALYLAELIKEAGFPPGVVNIVPGFGPTaGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNLKKVTL-ELGGKSPNI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 792 VDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAH 871
Cdd:cd07091 260 VFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 872 INKMKgVAKAyhEIKTAADVDENNSTFVRPILFelNNLNE----LQREVFGPVLHVVRYraSELDQLIDQINAKGYALTS 947
Cdd:cd07091 340 IESGK-KEGA--TLLTGGERHGSKGYFIQPTVF--TDVKDdmkiAKEEIFGPVVTILKF--KTEDEVIERANDTEYGLAA 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1080520335 948 GVHSRIEGTVDHIRDRIEAGNIYVNR-NIVGAVVgvqPFGGHGLSGTGPKAG 998
Cdd:cd07091 413 GVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
564-994 |
1.04e-64 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 227.96 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAAL--PEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKT 641
Cdd:cd07119 12 GKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 642 LNNAVAEVREAVDFCRYYANEAE------NTLPKDAKA------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPA 709
Cdd:cd07119 91 LRESEIDIDDVANCFRYYAGLATketgevYDVPPHVISrtvrepVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 710 EQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALS---KRddspvlIA-ET 784
Cdd:cd07119 171 EVTPLTTIALFELIEEAGLPAGVVNLVTGSGAtVGAELAESPDVDLVSFTGGTATGRSIMRAAAgnvKK------VAlEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 785 GGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEA 864
Cdd:cd07119 245 GGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 865 QQNLLAHIN--KMKGvAKAYHEIKTAADVDENNSTFVRPILFE--LNNLNELQREVFGPVLHVVRYRaSElDQLIDQINA 940
Cdd:cd07119 325 REKVLSYIQlgKEEG-ARLVCGGKRPTGDELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERFD-TE-EEAIRLAND 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1080520335 941 KGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRniVGAVVGVQPFGGHGLSGTG 994
Cdd:cd07119 402 TPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGIG 453
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
564-998 |
1.25e-64 |
|
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: 227.38 E-value: 1.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPE--WSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKT 641
Cdd:cd07142 18 GKTFPTIDPRN-GEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 642 LNNA-VAEVREAVDFCRYYANEAEN----TLPKDA--------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKP 708
Cdd:cd07142 97 YEQArYAEVPLAARLFRYYAGWADKihgmTLPADGphhvytlhEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 709 AEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLIaETGGQ 787
Cdd:cd07142 177 AEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPtAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSNLKPVTL-ELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 788 NAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQN 867
Cdd:cd07142 256 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 868 LLAHINKMKgvaKAYHEIKTAADVDENNSTFVRPILFE--LNNLNELQREVFGPVLHVVRYraSELDQLIDQINAKGYAL 945
Cdd:cd07142 336 ILSYIEHGK---EEGATLITGGDRIGSKGYYIQPTIFSdvKDDMKIARDEIFGPVQSILKF--KTVDEVIKRANNSKYGL 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1080520335 946 TSGVHSRIEGTVDHIRDRIEAGNIYVN-RNIVGAVVgvqPFGGHGLSGTGPKAG 998
Cdd:cd07142 411 AAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
564-994 |
1.11e-63 |
|
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: 224.40 E-value: 1.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPE--WSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKT 641
Cdd:cd07112 1 GETFATINPAT-GRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 642 LNNAVA-EVREAVDFCRYYAnEAENTL-------PKDAKA------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAK 707
Cdd:cd07112 80 ISDALAvDVPSAANTFRWYA-EAIDKVygevaptGPDALAlitrepLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 708 PAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLIaETGG 786
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHtAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWL-ECGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 787 QNAMIV-DSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQ 865
Cdd:cd07112 238 KSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 866 QNLLAHINkmKGVAKayhEIKTAA----DVDENNSTFVRPILFE-LNNLNEL-QREVFGPVLHVVRYraSELDQLIDQIN 939
Cdd:cd07112 318 DKVLGYIE--SGKAE---GARLVAggkrVLTETGGFFVEPTVFDgVTPDMRIaREEIFGPVLSVITF--DSEEEAVALAN 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1080520335 940 AKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVnrNIVGAVVGVQPFGGHGLSGTG 994
Cdd:cd07112 391 DSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
568-1004 |
7.45e-63 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 221.43 E-value: 7.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 568 PVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVA 647
Cdd:cd07150 2 DDLNPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYYANEAEN----TLPKDA---------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSL 714
Cdd:cd07150 81 ETTFTPELLRAAAGECRRvrgeTLPSDSpgtvsmsvrRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 715 IATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSkRDDSPVLIaETGGQNAMIVD 793
Cdd:cd07150 161 IGLKIAEIMEEAGLPKGVFNVVTGGGAeVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITL-ELGGKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 794 STALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHIN 873
Cdd:cd07150 239 ADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 874 kmKGVAK------------AYHEIKTAADVDENNSTFvrpilfelnnlnelQREVFGPVlhVVRYRASELDQLIDQINAK 941
Cdd:cd07150 319 --DAVAKgaklltggkydgNFYQPTVLTDVTPDMRIF--------------REETFGPV--TSVIPAKDAEEALELANDT 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080520335 942 GYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIV--GAVVgvqPFGGHGLSGTGpKAGGSFYLQ 1004
Cdd:cd07150 381 EYGLSAAILTNDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSME 441
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
66-177 |
1.26e-62 |
|
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: 208.13 E-value: 1.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 66 VDALMHEFSLSSEEGVALMCLAEALLRIPDNATRDRLIADKISEGNWKSHLNNSPSLFVNAAAWGLLITGKLTTNTSEKN 145
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 1080520335 146 MGSALSRMISKGGAPLIRQGVNYAMRLLGKQF 177
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
592-994 |
2.81e-62 |
|
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: 219.32 E-value: 2.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 592 EAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAEN----TL 667
Cdd:cd07104 4 RAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRpegeIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 668 PKDA---------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTS-----LIAtyavSLMHQAGIPTSAL 733
Cdd:cd07104 84 PSDVpgkesmvrrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 734 QLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNAMIVDSTALPEQVCLDVLNSAFDS 812
Cdd:cd07104 160 NVVPGGGSeIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVAL--ELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 813 AGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINkmKGVAK-AyhEIKTAAD 890
Cdd:cd07104 238 QGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVE--DAVAAgA--RLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 891 VDENnstFVRP-ILFELNNLNEL-QREVFGPVLHVVryRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGN 968
Cdd:cd07104 313 YEGL---FYQPtVLSDVTPDMPIfREEIFGPVAPVI--PFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
410 420
....*....|....*....|....*...
gi 1080520335 969 IYVNRNIV--GAVVgvqPFGGHGLSGTG 994
Cdd:cd07104 388 VHINDQTVndEPHV---PFGGVKASGGG 412
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
569-994 |
6.35e-62 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 219.04 E-value: 6.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWS-AKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVA 647
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 -EVREAVDFCRYYANEAEN-----TLPKDAK------------AVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPA 709
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSfpwefDLPVPALrggpgrrvvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 710 EQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALS---KRddspVLIaETG 785
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNaVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAatlKR----VLL-ELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 786 GQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSAL-RILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEA 864
Cdd:cd07089 235 GKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTtRLL-VPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 865 QQNLLAHINkmKGV---AKAYHEIKTAADVDenNSTFVRPILF-ELNNLNEL-QREVFGPVLHVVRYRasELDQLIDQIN 939
Cdd:cd07089 314 RDRVEGYIA--RGRdegARLVTGGGRPAGLD--KGFYVEPTLFaDVDNDMRIaQEEIFGPVLVVIPYD--DDDEAVRIAN 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520335 940 AKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNrnivGAVVGV--QPFGGHGLSGTG 994
Cdd:cd07089 388 DSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
571-998 |
9.24e-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: 215.38 E-value: 9.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 571 NPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAV-AEV 649
Cdd:cd07115 3 NPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 650 REAVDFCRYYANEAE----NTLPKDAKA--------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIAT 717
Cdd:cd07115 82 PRAADTFRYYAGWADkiegEVIPVRGPFlnytvrepVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 718 YAVSLMHQAGIPTSALQLVLGAGDV-GSALTGDARIGGVIFTGSTEVARLINKALS---KRddspvLIAETGGQNAMIVD 793
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVaGAALVEHPDVDKITFTGSTAVGRKIMQGAAgnlKR-----VSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 794 STALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHIN 873
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 874 KMKgvaKAYHEIKTAADVDENNSTFVRPILFElNNLNEL---QREVFGPVLHVVRYRASELDQLIdqINAKGYALTSGVH 950
Cdd:cd07115 317 VGR---EEGARLLTGGKRPGARGFFVEPTIFA-AVPPEMriaQEEIFGPVVSVMRFRDEEEALRI--ANGTEYGLAAGVW 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1080520335 951 SRIEGTVDHIRDRIEAGNIYVnrNIVGAVVGVQPFGGHGLSGTGPKAG 998
Cdd:cd07115 391 TRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
569-998 |
9.39e-61 |
|
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: 215.30 E-value: 9.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAkpaSERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07146 3 VRNPYT-GEVVGTVPAGTEEALREALALAASYRSTLTR---YQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAEN----TLPKDAKA-------------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQ 711
Cdd:cd07146 79 VGRAADVLRFAAAEALRddgeSFSCDLTAngkarkiftlrepLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 712 TSLIATYAVSLMHQAGIPTSALQLVLGA-GDVGSALTGDARIGGVIFTGSTEVARLI-NKALSKRddspvLIAETGGQNA 789
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIaATAGYKR-----QLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 790 MIV-DSTALPEQVCLDVlNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNL 868
Cdd:cd07146 234 LIVmDDADLERAATLAV-AGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 869 LAHINKM--KGVAKAYHeiktaadvDENNSTFVRPILfeLNNLN---EL-QREVFGPVLHVVRYRasELDQLIDQINAKG 942
Cdd:cd07146 313 ENRVEEAiaQGARVLLG--------NQRQGALYAPTV--LDHVPpdaELvTEETFGPVAPVIRVK--DLDEAIAISNSTA 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080520335 943 YALTSGVHSRIEGTVDHIRDRIEAGNIYVNrNIVGAVVGVQPFGGHGLSGTGPKAG 998
Cdd:cd07146 381 YGLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
569-994 |
4.42e-60 |
|
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: 213.45 E-value: 4.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07094 3 VHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAEN----TLPKDAKA-------------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQ 711
Cdd:cd07094 82 VDRAIDTLRLAAEEAERirgeEIPLDATQgsdnrlawtirepVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 712 TSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKrddsPVLIAETGGQNAM 790
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEReVLGDAFAADERVAMLSFTGSAAVGEALRANAGG----KRIALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 791 IVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLA 870
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 871 HINKmkgVAKAYHEIKTAAdvdENNSTFVRPILFELNNLNELQR--EVFGPVLHVVRYRasELDQLIDQINAKGYALTSG 948
Cdd:cd07094 318 WVEE---AVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSteETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1080520335 949 VHSRIEGTVDHIRDRIEAGNIYVNRNIVgAVVGVQPFGGHGLSGTG 994
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG 434
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
556-994 |
5.84e-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: 213.52 E-value: 5.84e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEARNV--GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMML 633
Cdd:cd07138 3 IDGAWVAPagTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 634 AVREAGKTLNNA-VAEVREAVDFCRYYANEAEN-----TLPKDA---KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTV 704
Cdd:cd07138 82 ITLEMGAPITLArAAQVGLGIGHLRAAADALKDfefeeRRGNSLvvrEPIGVCGLITPWNWPLNQIVLKVAPALAAGCTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 705 IAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALS---KRddspvL 780
Cdd:cd07138 162 VLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGpVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAAdtvKR-----V 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 781 IAETGGQNAMIV-DSTALPEQVcLDVLNSAFDSAGQRCSAL-RILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGP 858
Cdd:cd07138 237 ALELGGKSANIIlDDADLEKAV-PRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 859 VIDAEAQQNLLAHINKmkGVAKAYHEIKTAADVDENNST--FVRPILF-ELNNLNELQR-EVFGPVLHVVRYRasELDQL 934
Cdd:cd07138 315 LASAAQFDRVQGYIQK--GIEEGARLVAGGPGRPEGLERgyFVKPTVFaDVTPDMTIAReEIFGPVLSIIPYD--DEDEA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080520335 935 IDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNrnivGAVVGVQ-PFGGHGLSGTG 994
Cdd:cd07138 391 IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
569-994 |
8.63e-60 |
|
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: 212.86 E-value: 8.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAK-PASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVA 647
Cdd:cd07109 1 VFDPST-GEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYYANEAE----NTLPKDAKAVGAIV--------AISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLI 715
Cdd:cd07109 80 DVEAAARYFEYYGGAADklhgETIPLGPGYFVYTVrephgvtgHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 716 ATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNAMIVDS 794
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGaEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTL--ELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 795 TALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQlTTDIGPVIDAEAQqnllAHINK 874
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQL----DRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 875 MKGVAKAYH-EIKTAADVDENNST---FVRPILF-ELNNLNEL-QREVFGPVLHVVRYRasELDQLIDQINAKGYALTSG 948
Cdd:cd07109 313 FVARARARGaRIVAGGRIAEGAPAggyFVAPTLLdDVPPDSRLaQEEIFGPVLAVMPFD--DEAEAIALANGTDYGLVAG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1080520335 949 VHSRIEGTVDHIRDRIEAGNIYVNRniVGAVVGVQ-PFGGHGLSGTG 994
Cdd:cd07109 391 VWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
546-998 |
1.82e-59 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 212.64 E-value: 1.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 546 SSEDFHAASIVNGEARNV--GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLL 623
Cdd:cd07111 16 DAHDRSFGHFINGKWVKPenRKSFPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 624 EQHTPALMMLAVREAGKtlnnAVAEVRE-----AVDFCRYYANEA---ENTLPkDAKAVGAIVAISPWNFPLAIFTGEVV 695
Cdd:cd07111 95 QKHQRLFAVLESLDNGK----PIRESRDcdiplVARHFYHHAGWAqllDTELA-GWKPVGVVGQIVPWNFPLLMLAWKIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 696 SALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSkrD 775
Cdd:cd07111 170 PALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATA--G 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 776 DSPVLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSA-LRILcVQEDVADKMINIIKGAMDELVVGKPIQLTT 854
Cdd:cd07111 248 TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAgSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 855 DIGPVIDAEAQQNllahINKMKGVAKAY-HEIKTAADVDENNSTFVRPILFElnNLNE----LQREVFGPVLHVVRYRAs 929
Cdd:cd07111 327 DMGAIVDPAQLKR----IRELVEEGRAEgADVFQPGADLPSKGPFYPPTLFT--NVPPasriAQEEIFGPVLVVLTFRT- 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 930 eLDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVN-RNIVGAVVgvqPFGGHGLSGTGPKAG 998
Cdd:cd07111 400 -AKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFGREGG 465
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
569-997 |
1.92e-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: 211.84 E-value: 1.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPAdHNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTL-NNAVA 647
Cdd:cd07108 1 VINPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYY---ANEAE-NTLPKDA--------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLi 715
Cdd:cd07108 80 EAAVLADLFRYFgglAGELKgETLPFGPdvltytvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 716 ATYAVSLMHQAGIPTSALQLVLGAGDV-GSALTGDARIGGVIFTGSTEVARLINKALSKRdDSPVLIaETGGQNAMIVDS 794
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEEcGAALVDHPDVDKVTFTGSTEVGKIIYRAAADR-LIPVSL-ELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 795 TALPEQVCLDVLNSA-FDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHIN 873
Cdd:cd07108 237 DADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 874 ---KMKGvAKAYHEIKTAADVDENNSTFVRPILFE-LNNLNELQR-EVFGPVLHVVRYraSELDQLIDQINAKGYALTSG 948
Cdd:cd07108 317 lglSTSG-ATVLRGGPLPGEGPLADGFFVQPTIFSgVDNEWRLAReEIFGPVLCAIPW--KDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1080520335 949 VHSRIEGTVDHIRDRIEAGNIYVNRNiVGAVVGvQPFGGHGLSGTGPKA 997
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
569-994 |
7.12e-59 |
|
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: 210.29 E-value: 7.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAEN---------TLPKDA-------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQT 712
Cdd:cd07110 80 VDDVAGCFEYYADLAEQldakaeravPLPSEDfkarvrrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 713 SLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSkRDDSPVLIaETGGQNAMI 791
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDeAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSL-ELGGKSPII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 792 VDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAH 871
Cdd:cd07110 238 VFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 872 INKMKGV-AKAYHEIKTAADVDEnnSTFVRPILF-ELNNLNELQR-EVFGPVLhVVRYRASElDQLIDQINAKGYALTSG 948
Cdd:cd07110 318 IARGKEEgARLLCGGRRPAHLEK--GYFIAPTVFaDVPTDSRIWReEIFGPVL-CVRSFATE-DEAIALANDSEYGLAAA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1080520335 949 VHSRIEGTVDHIRDRIEAGNIYVnrNIVGAVVGVQPFGGHGLSGTG 994
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
555-947 |
4.14e-58 |
|
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: 208.60 E-value: 4.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 555 IVNGEARNVGEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLA 634
Cdd:cd07130 2 VYDGEWGGGGGVVTSISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 635 VREAGKTLNNAVAEVREAVDFCRY------------YANEAEN-TLPKDAKAVGAIVAISPWNFPLAIFTGEVVSALAAG 701
Cdd:cd07130 81 SLEMGKILPEGLGEVQEMIDICDFavglsrqlygltIPSERPGhRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 702 NTVIAKPAEQTSL--IATYAV--SLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDS 777
Cdd:cd07130 161 NVVVWKPSPTTPLtaIAVTKIvaRVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 778 PVLiaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIG 857
Cdd:cd07130 241 SLL--ELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 858 PVIDAEAQQNLLAHINKmkgvAKAYH-EIKTAADVDENNSTFVRPILFELNNLNEL-QREVFGPVLHVVRYraSELDQLI 935
Cdd:cd07130 319 PLHTKAAVDNYLAAIEE----AKSQGgTVLFGGKVIDGPGNYVEPTIVEGLSDAPIvKEETFAPILYVLKF--DTLEEAI 392
|
410
....*....|..
gi 1080520335 936 DQINAKGYALTS 947
Cdd:cd07130 393 AWNNEVPQGLSS 404
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
550-1004 |
7.99e-58 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 207.84 E-value: 7.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 550 FHAASIVNGEARNV--GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHT 627
Cdd:PRK11241 9 FRQQALINGEWLDAnnGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 628 PALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAE----NTLPKD---------AKAVGAIVAISPWNFPLAIFTGEV 694
Cdd:PRK11241 88 DDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKriygDTIPGHqadkrliviKQPIGVTAAITPWNFPAAMITRKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 695 VSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLG-AGDVGSALTGDARIGGVIFTGSTEVARLINKALSK 773
Cdd:PRK11241 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGsAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 774 rdDSPVLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLT 853
Cdd:PRK11241 248 --DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 854 TDIGPVIDAEAQQNLLAHInkMKGVAKAyHEIKTAADVDENNSTFVRP-ILFEL-NNLNELQREVFGPVLHVVRYRasEL 931
Cdd:PRK11241 326 VTIGPLIDEKAVAKVEEHI--ADALEKG-ARVVCGGKAHELGGNFFQPtILVDVpANAKVAKEETFGPLAPLFRFK--DE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080520335 932 DQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGvqPFGG---HGLSGTGPKAGGSFYLQ 1004
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYLE 474
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
577-998 |
1.16e-57 |
|
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: 206.78 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 577 DVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFC 656
Cdd:cd07101 7 EPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 657 RYYANEAENTLpKDAKAVGAI---------------VA-ISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAV 720
Cdd:cd07101 87 RYYARRAERLL-KPRRRRGAIpvltrttvnrrpkgvVGvISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 721 SLMHQAGIPTSALQLVLGAG-DVGSALTgdARIGGVIFTGSTEVARLINKALSKRddspvLI---AETGGQNAMIVDSTA 796
Cdd:cd07101 166 ELLIEAGLPRDLWQVVTGPGsEVGGAIV--DNADYVMFTGSTATGRVVAERAGRR-----LIgcsLELGGKNPMIVLEDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 797 LPEQVCLDVLNSAFDSAGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINkm 875
Cdd:cd07101 239 DLDKAAAGAVRACFSNAGQLCvSIERIY-VHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 876 KGVAK----------------AYHEIKTAADVDENNSTFVrpilfelnnlnelqREVFGPVLHVvrYRASELDQLIDQIN 939
Cdd:cd07101 316 DAVAKgatvlaggrarpdlgpYFYEPTVLTGVTEDMELFA--------------EETFGPVVSI--YRVADDDEAIELAN 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 940 AKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQ-PFGGHGLSGTGPKAG 998
Cdd:cd07101 380 DTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
569-1001 |
2.98e-57 |
|
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: 206.14 E-value: 2.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAAL-PEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLN-NAV 646
Cdd:cd07113 19 ITNPAT-EQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHlSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 647 AEVREAVDFCRYYA------------------NEAENTLPKDAKAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKP 708
Cdd:cd07113 98 FEVGQSANFLRYFAgwatkingetlapsipsmQGERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 709 AEQTSLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSkrDDSPVLIAETGGQN 788
Cdd:cd07113 178 SEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAA--SDLTRVTLELGGKN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 789 AMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAeaqqnl 868
Cdd:cd07113 256 AAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQ------ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 869 lAHINKMKG---VAKAYH-EIKTAADVDENNSTFVRPILFELNNLNE--LQREVFGPVLHVVRYRASEldQLIDQINAKG 942
Cdd:cd07113 330 -PHFDKVCSyldDARAEGdEIVRGGEALAGEGYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDEE--ELIQLINDTP 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 943 YALTSGVHSRIEGTVDHIRDRIEAGNIYVN-RNIVGAVVgvqPFGGHGLSGTGPKAGGSF 1001
Cdd:cd07113 407 FGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIGREFGSAF 463
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
556-998 |
9.99e-57 |
|
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: 204.68 E-value: 9.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGE-ARNV-GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALP-EWSAK-PASERADCLRRFADLLEQHTPALM 631
Cdd:cd07143 11 INGEfVDSVhGGTVKVYNPST-GKLITKIAEATEADVDIAVEVAHAAFEtDWGLKvSGSKRGRCLSKLADLMERNLDYLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 632 MLAVREAGKTLNNAVA-EVREAVDFCRYYANEAE----NTLPKDAKA--------VGAIVAISPWNFPLAIFTGEVVSAL 698
Cdd:cd07143 90 SIEALDNGKTFGTAKRvDVQASADTFRYYGGWADkihgQVIETDIKKltytrhepIGVCGQIIPWNFPLLMCAWKIAPAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 699 AAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDS 777
Cdd:cd07143 170 AAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRtCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNLK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 778 PVLIaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIG 857
Cdd:cd07143 250 KVTL-ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 858 PVIDAEAQQNLLAHINKMKgvaKAYHEIKTAADVDENNSTFVRPILFE--LNNLNELQREVFGPVLHVVRYRASEldQLI 935
Cdd:cd07143 329 PQVSQIQYERIMSYIESGK---AEGATVETGGKRHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKFKTEE--EAI 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080520335 936 DQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVN-RNIVGAVVgvqPFGGHGLSGTGPKAG 998
Cdd:cd07143 404 KRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
571-973 |
1.35e-56 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 203.25 E-value: 1.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 571 NPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVR 650
Cdd:cd07102 2 SPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 651 EAVDFCRYYANEAENTL-----PKDA--------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIAT 717
Cdd:cd07102 81 GMLERARYMISIAEEALadirvPEKDgferyirrEPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 718 YAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRddspvLIA---ETGGQNAMIVDS 794
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGR-----FIKvglELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 795 TALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVAD----KMINIIKGamdeLVVGKPIQLTTDIGPVIDAEAQQNLLA 870
Cdd:cd07102 236 DADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDafveAFVAVVKG----YKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 871 HIN--KMKGvAKAYHEIKTAADVDEnNSTFVRPILfeLNNLNE----LQREVFGPVLHVvrYRASELDQLIDQINAKGYA 944
Cdd:cd07102 312 QIAdaIAKG-ARALIDGALFPEDKA-GGAYLAPTV--LTNVDHsmrvMREETFGPVVGI--MKVKSDAEAIALMNDSEYG 385
|
410 420
....*....|....*....|....*....
gi 1080520335 945 LTSGVHSRIEGTVDHIRDRIEAGNIYVNR 973
Cdd:cd07102 386 LTASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
556-994 |
1.89e-56 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 203.60 E-value: 1.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEarnvGEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAV 635
Cdd:PRK13473 12 VAGE----GEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 636 REAGKTLNNAVA-EVREAVDFCRYYANEAENTLPKDA-------------KAVGAIVAISPWNFPLAIFTGEVVSALAAG 701
Cdd:PRK13473 87 LNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAgeyleghtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALAAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 702 NTVIAKPAEQTSLIATYAVSLMHQAgIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALS---KRdds 777
Cdd:PRK13473 167 NTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGaTVGDALVGHPKVRMVSLTGSIATGKHVLSAAAdsvKR--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 778 pvLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCS-ALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDI 856
Cdd:PRK13473 243 --THLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTaACRIY-AQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 857 GPVIDAEAQQNLLAHINKMKGVAKAyhEIKTAADVDENNSTFVRPILfeLNNLNE----LQREVFGPVLHVVRYraSELD 932
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGHI--RVVTGGEAPDGKGYYYEPTL--LAGARQddeiVQREVFGPVVSVTPF--DDED 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080520335 933 QLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVgaVVGVQPFGGHGLSGTG 994
Cdd:PRK13473 394 QAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
577-999 |
3.95e-56 |
|
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: 201.75 E-value: 3.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 577 DVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFC 656
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 657 RYYANEAEN----TLPKDA--------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVS-LM 723
Cdd:cd07152 82 HEAAGLPTQpqgeILPSAPgrlslarrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIArLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 724 HQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNAMIVDSTALPEqvcL 803
Cdd:cd07152 162 EEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL--ELGGKNALIVLDDADLD---L 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 804 DVLNSAFDS---AGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDaeaqQNLLAHINKMkgVA 879
Cdd:cd07152 237 AASNGAWGAflhQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLIN----ARQLDRVHAI--VD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 880 KAyheIKTAADVD---ENNSTFVRP-ILFELNNLNEL-QREVFGPVLHVVRYraSELDQLIDQINAKGYALTSGVHSRIE 954
Cdd:cd07152 310 DS---VAAGARLEaggTYDGLFYRPtVLSGVKPGMPAfDEEIFGPVAPVTVF--DSDEEAVALANDTEYGLSAGIISRDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1080520335 955 GTVDHIRDRIEAGNIYVNRNIVGAVVgVQPFGGHGLSGTGPKAGG 999
Cdd:cd07152 385 GRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGG 428
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
564-998 |
8.56e-56 |
|
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: 201.81 E-value: 8.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAAL---PEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGK 640
Cdd:cd07141 21 GKTFPTINPAT-GEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 641 T-LNNAVAEVREAVDFCRYYANEAE----NTLPKDAKA--------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAK 707
Cdd:cd07141 100 PfSKSYLVDLPGAIKVLRYYAGWADkihgKTIPMDGDFftytrhepVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 708 PAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGDV-GSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLIaETGG 786
Cdd:cd07141 180 PAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTaGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRVTL-ELGG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 787 QNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQ 866
Cdd:cd07141 259 KSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 867 NLLAHINKMKgvaKAYHEIKTAADVDENNSTFVRPILFE--LNNLNELQREVFGPVLHVVRYraSELDQLIDQINAKGYA 944
Cdd:cd07141 339 KILELIESGK---KEGAKLECGGKRHGDKGYFIQPTVFSdvTDDMRIAKEEIFGPVQQIFKF--KTIDEVIERANNTTYG 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1080520335 945 LTSGVHSRIEGTVDHIRDRIEAGNIYVNrniVGAVVGVQ-PFGGHGLSGTGPKAG 998
Cdd:cd07141 414 LAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
553-994 |
2.72e-55 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 201.65 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 553 ASIVNGEARnvgEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMM 632
Cdd:PRK09407 23 TARVDGAAG---PTREVTAPFT-GEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 633 LAVREAGKTLNNAVAEVREAVDFCRYYANEAENTLpKDAKAVGAI---------------VA-ISPWNFPLAIFTGEVVS 696
Cdd:PRK09407 99 LVQLETGKARRHAFEEVLDVALTARYYARRAPKLL-APRRRAGALpvltkttelrqpkgvVGvISPWNYPLTLAVSDAIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 697 ALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTgdARIGGVIFTGSTEVARLINKALSKRd 775
Cdd:PRK09407 178 ALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGpVVGTALV--DNADYLMFTGSTATGRVLAEQAGRR- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 776 dspvLI---AETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQ 851
Cdd:PRK09407 255 ----LIgfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCiSIERIY-VHESIYDEFVRAFVAAVRAMRLGAGYD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 852 LTTDIGPVIDAEAQQNLLAHIN--KMKG------------VAKAYHEIKTAADVDENNSTFVrpilfelnnlnelqREVF 917
Cdd:PRK09407 330 YSADMGSLISEAQLETVSAHVDdaVAKGatvlaggkarpdLGPLFYEPTVLTGVTPDMELAR--------------EETF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080520335 918 GPVLHVvrYRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQ-PFGGHGLSGTG 994
Cdd:PRK09407 396 GPVVSV--YPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
569-994 |
3.60e-55 |
|
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: 199.09 E-value: 3.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVA- 647
Cdd:cd07092 1 VVDPAT-GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYYANeAENTLPKDAKA--------------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTS 713
Cdd:cd07092 80 ELPGAVDNFRFFAG-AARTLEGPAAGeylpghtsmirrepIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 714 LiATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSkrDDSPVLIAETGGQNAMIV 792
Cdd:cd07092 159 L-TTLLLAELAAEVLPPGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVARAAA--DTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTALPEQVCLDVLNSAFDSAGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAH 871
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 872 INKmkgvAKAYHEIKTAADVDENNSTFVRP-ILFELNNLNEL-QREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGV 949
Cdd:cd07092 315 VER----APAHARVLTGGRRAEGPGYFYEPtVVAGVAQDDEIvQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1080520335 950 HSRIEGTVDHIRDRIEAGNIYVNRNIVgaVVGVQPFGGHGLSGTG 994
Cdd:cd07092 389 WTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
590-994 |
5.04e-55 |
|
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: 198.07 E-value: 5.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 590 AQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAEN---- 665
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAflad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 666 -TLPKDAK-------AVGAIVAISPWNFPL---AIFtgeVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQ 734
Cdd:cd07100 81 ePIETDAGkayvryePLGVVLGIMPWNFPFwqvFRF---AAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 735 LVLGAGDVGSALTGDARIGGVIFTGST----EVARLINKALSKrddsPVLiaETGGQNAMIVDSTALPEQVCLDVLNSAF 810
Cdd:cd07100 158 NLLIDSDQVEAIIADPRVRGVTLTGSEragrAVAAEAGKNLKK----SVL--ELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 811 DSAGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKM--KGvAK------- 880
Cdd:cd07100 232 QNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAvaAG-ATlllggkr 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 881 -----AYHEIKTAADVDENNSTFvrpilfelnnlNElqrEVFGPVLHVvrYRASELDQLIDQINAKGYALTSGVHSRIEG 955
Cdd:cd07100 310 pdgpgAFYPPTVLTDVTPGMPAY-----------DE---ELFGPVAAV--IKVKDEEEAIALANDSPFGLGGSVFTTDLE 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 1080520335 956 TVDHIRDRIEAGNIYVNRnIVGAVVGVqPFGGHGLSGTG 994
Cdd:cd07100 374 RAERVARRLEAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
577-1010 |
3.47e-54 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 198.88 E-value: 3.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 577 DVVGTVSFADAALAQEAIGAAVAALPE--WSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAV-AEVREAV 653
Cdd:PLN02466 84 EVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMFA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 654 DFCRYYANEAEN----TLPKDA--------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVS 721
Cdd:PLN02466 164 RLFRYYAGWADKihglTVPADGphhvqtlhEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 722 LMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLIaETGGQNAMIVDSTALPEQ 800
Cdd:PLN02466 244 LLHEAGLPPGVLNVVSGFGpTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL-ELGGKSPFIVCEDADVDK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 801 VCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHInkmKGVAK 880
Cdd:PLN02466 323 AVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYI---KSGVE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 881 AYHEIKTAADVDENNSTFVRPILFE--LNNLNELQREVFGPVLHVVRYraSELDQLIDQINAKGYALTSGVHSRIEGTVD 958
Cdd:PLN02466 400 SGATLECGGDRFGSKGYYIQPTVFSnvQDDMLIAQDEIFGPVQSILKF--KDLDEVIRRANNTRYGLAAGVFTQNLDTAN 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520335 959 HIRDRIEAGNIYVN-RNIVGAVVgvqPFGGHGLSGTGPKAGG---SFYLQ-RLVRTP 1010
Cdd:PLN02466 478 TLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKGIyslNNYLQvKAVVTP 531
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
570-998 |
7.33e-54 |
|
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: 195.63 E-value: 7.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 570 RNPAdHNDVVGTVSFADAALAQEAIGAAVAALPE--WSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVA 647
Cdd:cd07118 2 RSPA-HGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYYAN-------EAENTLPKDA------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSL 714
Cdd:cd07118 81 EIEGAADLWRYAASlartlhgDSYNNLGDDMlglvlrEPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 715 IATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNAMIVD 793
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYGAtVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSL--ELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 794 STALPEQVCLDVLNSAFDSAGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHI 872
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCnSGSRLL-VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 873 NkmKGVAKAYHEIKTAADVDENNSTFVRPILFE--LNNLNELQREVFGPVLHVVRYRAseLDQLIDQINAKGYALTSGVH 950
Cdd:cd07118 318 D--AGRAEGATLLLGGERLASAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTFDT--VDEAIALANDTVYGLSAGVW 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1080520335 951 SR-IEGTVDHIRdRIEAGNIYVNRNIVGAVvgVQPFGGHGLSGTGPKAG 998
Cdd:cd07118 394 SKdIDTALTVAR-RIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
577-1017 |
5.30e-53 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 194.27 E-value: 5.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 577 DVVGTVSFADAALAQEAIGAAVAALP--EWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGK--TLNNAVaEVREA 652
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKlfALGKAV-DIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 653 VDFCRYYANEAEN---------------TLPKDAKAVGAIVaisPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIAT 717
Cdd:PLN02766 126 AGLLRYYAGAADKihgetlkmsrqlqgyTLKEPIGVVGHII---PWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 718 YAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLIaETGGQNAMIV-DST 795
Cdd:PLN02766 203 FYAHLAKLAGVPDGVINVVTGFGpTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKQVSL-ELGGKSPLLIfDDA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 796 ALPEQVCLDVLNSAFDSaGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKM 875
Cdd:PLN02766 282 DVDMAVDLALLGIFYNK-GEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 876 KGVAKAyheIKTAADVDENNSTFVRPILFelNNLNE----LQREVFGPVLHVVRYRAseLDQLIDQINAKGYALTSGVHS 951
Cdd:PLN02766 361 KREGAT---LLTGGKPCGDKGYYIEPTIF--TDVTEdmkiAQDEIFGPVMSLMKFKT--VEEAIKKANNTKYGLAAGIVT 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 952 RIEGTVDHIRDRIEAGNIYVNRNIvgAVVGVQPFGGHGLSGTGPKAGGSF---YLQ-RLVRTPEWVAPTL 1017
Cdd:PLN02766 434 KDLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQGMDAldkYLQvKSVVTPLYNSPWL 501
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
564-1004 |
1.16e-52 |
|
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: 193.01 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAK-PASERADCLRRFADLLEQHTPALMMLAVREAGKTL 642
Cdd:cd07144 22 GETIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 643 N-NAVAEVREAVDFCRYYANEAE--------NTLPKDAKAV----GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPA 709
Cdd:cd07144 101 HsNALGDLDEIIAVIRYYAGWADkiqgktipTSPNKLAYTLhepyGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 710 EQTSLIATYAVSLMHQAGIPTSALQLVLGAGDV-GSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQN 788
Cdd:cd07144 181 ENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVaGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTL--ECGGKS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 789 AMIVDSTALPEQVCLDVLNSAFDSAGQRCSAL-RILcVQEDVADKMIN-IIKGAMDELVVGKPIQLTTDIGPVIDAEAQQ 866
Cdd:cd07144 259 PALVFEDADLDQAVKWAAAGIMYNSGQNCTATsRIY-VQESIYDKFVEkFVEHVKQNYKVGSPFDDDTVVGPQVSKTQYD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 867 NLLAHINKMKGVAKAYHEIKTAADVDENNSTFVRPILFelNNLNE----LQREVFGPVLHVVRYraSELDQLIDQINAKG 942
Cdd:cd07144 338 RVLSYIEKGKKEGAKLVYGGEKAPEGLGKGYFIPPTIF--TDVPQdmriVKEEIFGPVVVISKF--KTYEEAIKKANDTT 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080520335 943 YALTSGVHSRiEGTVDH-IRDRIEAGNIYVNRNIVGAvVGVqPFGGHGLSGTGP---KAGGSFYLQ 1004
Cdd:cd07144 414 YGLAAAVFTK-DIRRAHrVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRelgEYGLETYTQ 476
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
569-994 |
3.76e-52 |
|
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: 190.66 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAE----NTLPKDAKAV--------GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIA 716
Cdd:cd07107 80 VMVAAALLDYFAGLVTelkgETIPVGGRNLhytlrepyGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 717 TYAVSLMHQAgIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGSTEVARLINKALSKRdDSPVLIaETGGQNAMIVDST 795
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGAtAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTL-ELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 796 ALPEQVCLDVLNSA-FDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHIN- 873
Cdd:cd07107 237 ADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDs 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 874 -KMKGvAKAYHEIKTAADVDENNSTFVRPILFE--LNNLNELQREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVH 950
Cdd:cd07107 317 aKREG-ARLVTGGGRPEGPALEGGFYVEPTVFAdvTPGMRIAREEIFGPVLSVLRWR--DEAEMVAQANGVEYGLTAAIW 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1080520335 951 SRIEGTVDHIRDRIEAGNIYVN---RNIVGAvvgvqPFGGHGLSGTG 994
Cdd:cd07107 394 TNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
569-994 |
4.88e-52 |
|
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: 190.21 E-value: 4.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07090 1 VIEPAT-GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAEN------TLPKDAKA------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIA 716
Cdd:cd07090 80 IDSSADCLEYYAGLAPTlsgehvPLPGGSFAytrrepLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 717 TYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKrDDSPVLIaETGGQNAMIVDSTA 796
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTL-ELGGKSPLIIFDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 797 LPEQVCLDVLNSAFDSAGQRCS-ALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKM 875
Cdd:cd07090 238 DLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 876 K--GVAKAYHEIKTAADVDENNSTFVRPILFelNNLNE----LQREVFGPVLHVVRYRaSElDQLIDQINAKGYALTSGV 949
Cdd:cd07090 317 KqeGAKVLCGGERVVPEDGLENGFYVSPCVL--TDCTDdmtiVREEIFGPVMSILPFD-TE-EEVIRRANDTTYGLAAGV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1080520335 950 HSRIEGTVDHIRDRIEAGNIYVNR-NIVGAVVgvqPFGGHGLSGTG 994
Cdd:cd07090 393 FTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
568-994 |
6.21e-52 |
|
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: 189.76 E-value: 6.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 568 PVRNPADHnDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVA 647
Cdd:cd07147 2 EVTNPYTG-EVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYYANEAE----NTLPKDAKA-------------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAE 710
Cdd:cd07147 81 EVARAIDTFRIAAEEATriygEVLPLDISArgegrqglvrrfpIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 711 QTSLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRddSPVLiaETGGQNAM 790
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVL--ELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 791 IVDSTALPEQVCLDVLNSAFDSAGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLL 869
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 870 AHINKmkgVAKAYHEIKTAADVDENnstFVRP-ILFELNNLNELQR-EVFGPVLHVVRYraSELDQLIDQINAKGYALTS 947
Cdd:cd07147 316 GWVNE---AVDAGAKLLTGGKRDGA---LLEPtILEDVPPDMEVNCeEVFGPVVTVEPY--DDFDEALAAVNDSKFGLQA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1080520335 948 GVHSRIEGTVDHIRDRIEAGNIYVNrNIVGAVVGVQPFGGHGLSGTG 994
Cdd:cd07147 388 GVFTRDLEKALRAWDELEVGGVVIN-DVPTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
569-994 |
2.30e-49 |
|
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: 182.77 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADhNDVVGTVSFADAALAQEAIGAAVAALPE--WSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAV 646
Cdd:cd07139 18 VVSPAT-EEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 647 -AEVREAVDFCRYYANEAENTLPKDAKA-------------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQT 712
Cdd:cd07139 97 rAQGPGPAALLRYYAALARDFPFEERRPgsggghvlvrrepVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPET 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 713 SLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNAMIV 792
Cdd:cd07139 177 PLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTL--ELGGKSAAIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTALPEQVCLDVLNSAFDSAGQRCSAL-RILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAH 871
Cdd:cd07139 255 LDDADLDAAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 872 INkmKGVAKAYHEI---KTAADVDENNstFVRPILF-ELNNLNEL-QREVFGPVLHVVRYRasELDQLIDQINAKGYALT 946
Cdd:cd07139 334 IA--KGRAEGARLVtggGRPAGLDRGW--FVEPTLFaDVDNDMRIaQEEIFGPVLSVIPYD--DEDDAVRIANDSDYGLS 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1080520335 947 SGVHSRIEGTVDHIRDRIEAGNIYVNrnivGAVVGVQ-PFGGHGLSGTG 994
Cdd:cd07139 408 GSVWTADVERGLAVARRIRTGTVGVN----GFRLDFGaPFGGFKQSGIG 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
590-994 |
6.10e-49 |
|
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: 180.47 E-value: 6.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 590 AQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEA----EN 665
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLItqiiGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 666 TLPKDA---------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLV 736
Cdd:cd07105 82 SIPSDKpgtlamvvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 737 L----GAGDVGSALTGDARIGGVIFTGSTEVARLINKaLSKRDDSPVLIaETGGQNAMIVDSTALPEQVCLDVLNSAFDS 812
Cdd:cd07105 162 ThspeDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAE-TAAKHLKPVLL-ELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 813 AGQRC-SALRILcVQEDVADKMINIIKGAMDELVVGKpiqltTDIGPVIDAEAQQNLLAHINkmKGVAKAYHEIKTAADV 891
Cdd:cd07105 240 SGQICmSTERII-VHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVD--DALSKGAKLVVGGLAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 892 DENNSTFVRPILfeLNNLNELQR----EVFGPVLHVVRYraSELDQLIDQINAKGYALTSGVHSRiegtvDHIR-----D 962
Cdd:cd07105 312 ESPSGTSMPPTI--LDNVTPDMDiyseESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR-----DLARalavaK 382
|
410 420 430
....*....|....*....|....*....|....*
gi 1080520335 963 RIEAGNIYVNrnivGAVVGVQ---PFGGHGLSGTG 994
Cdd:cd07105 383 RIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
556-994 |
6.19e-49 |
|
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: 181.35 E-value: 6.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEARNVgeaQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAV 635
Cdd:cd07151 4 RDGTSERT---IDVLNPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 636 REAGKT-------LNNAVAEVREAVDF-CRYYANEAENTLP-KDAK----AVGAIVAISPWNFPLAIFTGEVVSALAAGN 702
Cdd:cd07151 80 RESGSTrikanieWGAAMAITREAATFpLRMEGRILPSDVPgKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 703 TVIAKPAEQTS-----LIAtyavSLMHQAGIPTSALQLVLGAG-DVGSALTGDaRIGGVI-FTGSTEVARLINKALSKRD 775
Cdd:cd07151 160 AVVLKPASDTPitgglLLA----KIFEEAGLPKGVLNVVVGAGsEIGDAFVEH-PVPRLIsFTGSTPVGRHIGELAGRHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 776 DSPVLiaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSAL-RILcVQEDVADKMINIIKGAMDELVVGKPIQLTT 854
Cdd:cd07151 235 KKVAL--ELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAInRII-VHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 855 DIGPVIDAEAQQNLLAHINKMKgvaKAYHEIKTAADVDENnstFVRP-ILFELNNLNELQR-EVFGPVLHVVRYRASEld 932
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAV---EEGATLLVGGEAEGN---VLEPtVLSDVTNDMEIAReEIFGPVAPIIKADDEE-- 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080520335 933 QLIDQINAKGYALTSGVHSR-IEGTVDhIRDRIEAGNIYVNRNIVGAVVGVqPFGGHGLSGTG 994
Cdd:cd07151 384 EALELANDTEYGLSGAVFTSdLERGVQ-FARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
571-994 |
1.39e-46 |
|
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: 174.07 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 571 NPADhNDVVGTVSFADAALAQEAIGAAVAAL--PEWSAKPAsERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:cd07120 3 DPAT-GEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAENT--------------LPKDAKAVGAIvaISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSL 714
Cdd:cd07120 81 ISGAISELRYYAGLARTEagrmiepepgsfslVLREPMGVAGI--IVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 715 IATYAVSLMHQA-GIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNAMIV 792
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGsEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGL--ELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 --DS---TALPEqvcldVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQN 867
Cdd:cd07120 237 fdDAdldAALPK-----LERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 868 LLAHINK-MKGVAKAYHEiKTAADVDENNSTFVRPILFEL--NNLNELQREVFGPVLHVVRYraSELDQLIDQINAKGYA 944
Cdd:cd07120 312 VDRMVERaIAAGAEVVLR-GGPVTEGLAKGAFLRPTLLEVddPDADIVQEEIFGPVLTLETF--DDEAEAVALANDTDYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1080520335 945 LTSGVHSRIEGTVDHIRDRIEAGNIYVN---RNIVGAvvgvqPFGGHGLSGTG 994
Cdd:cd07120 389 LAASVWTRDLARAMRVARAIRAGTVWINdwnKLFAEA-----EEGGYRQSGLG 436
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
556-994 |
4.58e-45 |
|
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: 170.60 E-value: 4.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGE--ARNVGEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHtpaLMML 633
Cdd:cd07559 5 INGEwvAPSKGEYFDNYNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEEN---LELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 634 AVREagkTLNNAVAeVRE--------AVDFCRYYAN--EAE----NTLPKDAKAV------GAIVAISPWNFPLAIFTGE 693
Cdd:cd07559 81 AVAE---TLDNGKP-IREtlaadiplAIDHFRYFAGviRAQegslSEIDEDTLSYhfheplGVVGQIIPWNFPLLMAAWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 694 VVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAgIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALS 772
Cdd:cd07559 157 LAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGsEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 773 KRddspvLIA---ETGGQNAMIVDSTALPEQVCLD------VLNSAFDSaGQRCSA-LRILcVQEDVADKMINIIKGAMD 842
Cdd:cd07559 236 EN-----LIPvtlELGGKSPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCpSRAL-VQESIYDEFIERAVERFE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 843 ELVVGKPIQLTTDIGPVIDAEAQQNLLAH--INKMKGvAKAYHEIKTAADVDENNSTFVRPILFEL--NNLNELQREVFG 918
Cdd:cd07559 309 AIKVGNPLDPETMMGAQVSKDQLEKILSYvdIGKEEG-AEVLTGGERLTLGGLDKGYFYEPTLIKGgnNDMRIFQEEIFG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520335 919 PVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVN-RNIVGAVVgvqPFGGHGLSGTG 994
Cdd:cd07559 388 PVLAVITFK--DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
569-994 |
2.48e-44 |
|
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: 167.60 E-value: 2.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADHNdVVGTVSFADAALAQEAIGAAVAALPEWSAK-PASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVA 647
Cdd:cd07148 3 VVNPFDLK-PIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYYANEAEN----TLPKDAKA-------------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAE 710
Cdd:cd07148 82 EVTRAIDGVELAADELGQlggrEIPMGLTPasagriafttrepIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 711 QTSLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVliaETGGQNAM 790
Cdd:cd07148 162 ATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGTRCAL---EHGGAAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 791 IVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLA 870
Cdd:cd07148 239 IVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 871 HINkmKGVAKAYHEIKTAADVDEnnSTFVRPILFE-LNNLNELQREVFGPVlhVVRYRASELDQLIDQINAKGYALTSGV 949
Cdd:cd07148 319 WVN--EAVAAGARLLCGGKRLSD--TTYAPTVLLDpPRDAKVSTQEIFGPV--VCVYSYDDLDEAIAQANSLPVAFQAAV 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1080520335 950 HSRIEGTVDHIRDRIEAGNIYVNRNiVGAVVGVQPFGGHGLSGTG 994
Cdd:cd07148 393 FTKDLDVALKAVRRLDATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
571-998 |
6.63e-44 |
|
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: 167.29 E-value: 6.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 571 NPADhNDVVGTVSFADAALAQEAIGAAVAALP--EWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAV-A 647
Cdd:cd07140 27 NPTD-GSVICKVSLATVEDVDRAVAAAKEAFEngEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALkT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 648 EVREAVDFCRYYANEAE----NTLP-KDAKA-----------VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQ 711
Cdd:cd07140 106 HVGMSIQTFRYFAGWCDkiqgKTIPiNQARPnrnltltkrepIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 712 TSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLIaETGGQNAM 790
Cdd:cd07140 186 TPLTALKFAELTVKAGFPKGVINILPGSGsLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLKKVSL-ELGGKSPL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 791 IVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPvidaeaqQNLLA 870
Cdd:cd07140 265 IIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP-------QNHKA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 871 HINKM-----KGVAKAYHEIKTAADVDENNSTFVRPILFELNNLNEL-QREVFGPVLHVVRYRASELDQLIDQINAKGYA 944
Cdd:cd07140 338 HLDKLveyceRGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIaKEESFGPIMIISKFDDGDVDGVLQRANDTEYG 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520335 945 LTSGVHSRIEGTVDHIRDRIEAGNIYVN---RNIVGAvvgvqPFGGHGLSGTGPKAG 998
Cdd:cd07140 418 LASGVFTKDINKALYVSDKLEAGTVFVNtynKTDVAA-----PFGGFKQSGFGKDLG 469
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
564-994 |
6.19e-43 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 164.28 E-value: 6.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLN 643
Cdd:PRK13252 21 GETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 644 NA-VAEVREAVDFCRYYANEAE----NTLPKDA--------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAE 710
Cdd:PRK13252 100 ETsVVDIVTGADVLEYYAGLAPalegEQIPLRGgsfvytrrEPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 711 QTSLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLI--NKALSKRDdspvLIAETGGQN 788
Cdd:PRK13252 180 VTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVmaAAAASLKE----VTMELGGKS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 789 AMIVDSTALPEQVCLDVLNSAFDSAGQRCS-ALRILcVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQN 867
Cdd:PRK13252 256 PLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 868 LLAHINkmKGVAKAYHEIKTAADVDENNS---TFVRPILFE--LNNLNELQREVFGPVLHVVRYRaSElDQLIDQINAKG 942
Cdd:PRK13252 335 VLGYIE--KGKAEGARLLCGGERLTEGGFangAFVAPTVFTdcTDDMTIVREEIFGPVMSVLTFD-DE-DEVIARANDTE 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1080520335 943 YALTSGVHSRIEGTVDHIRDRIEAGNIYVNRniVGAVVGVQPFGGHGLSGTG 994
Cdd:PRK13252 411 YGLAAGVFTADLSRAHRVIHQLEAGICWINT--WGESPAEMPVGGYKQSGIG 460
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
571-994 |
2.73e-42 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 161.83 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 571 NPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLL--EQHTPALMMlaVREAGKTLNNAVAE 648
Cdd:PRK09406 7 NPAT-GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLeaEADQVAALM--TLEMGKTLASAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAENTL---PKDAKAVGA------------IVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTS 713
Cdd:PRK09406 84 ALKCAKGFRYYAEHAEALLadePADAAAVGAsrayvryqplgvVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 714 LIATYAVSLMHQAGIPTSALQ-LVLGAGDVgSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNAMIV 792
Cdd:PRK09406 164 QTALYLADLFRRAGFPDGCFQtLLVGSGAV-EAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVL--ELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLlahI 872
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV---E 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 873 NKMKGVAKAYHEIKTAADVDENNSTFVRP-ILFELNNLNELQR-EVFGPVLHVvrYRASELDQLIDQINAKGYALTSGVH 950
Cdd:PRK09406 318 KQVDDAVAAGATILCGGKRPDGPGWFYPPtVITDITPDMRLYTeEVFGPVASL--YRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1080520335 951 SRIEGTVDHIRDRIEAGNIYVNrnivGAVVGVQ--PFGGHGLSGTG 994
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYG 437
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
554-1009 |
6.31e-42 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 161.93 E-value: 6.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 554 SIVNGEARNVGEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMML 633
Cdd:PLN02315 23 CYVGGEWRANGPLVSSVNPAN-NQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 634 AVREAGKTLNNAVAEVREAVDFCRYYANEAE----NTLPKDA---------KAVGAIVAISPWNFPLAIFTGEVVSALAA 700
Cdd:PLN02315 102 VSLEMGKILAEGIGEVQEIIDMCDFAVGLSRqlngSIIPSERpnhmmmevwNPLGIVGVITAFNFPCAVLGWNACIALVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 701 GNTVIAKPAEQTSLIaTYAV-----SLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKRD 775
Cdd:PLN02315 182 GNCVVWKGAPTTPLI-TIAMtklvaEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 776 DSPVLiaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTD 855
Cdd:PLN02315 261 GKCLL--ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 856 IGPVIDAEAQQNLLAHINKMKGVAKayhEIKTAADVDENNSTFVRPILFELN-NLNELQREVFGPVLHVVRYRAseLDQL 934
Cdd:PLN02315 339 LGPLHTPESKKNFEKGIEIIKSQGG---KILTGGSAIESEGNFVQPTIVEISpDADVVKEELFGPVLYVMKFKT--LEEA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 935 IDQINAKGYALTSGVHSRIEGTV-----DHIRDrieAGNIYVNRNIVGAVVGvQPFGGHGLSGTGPKAGGSFYLQRLVRT 1009
Cdd:PLN02315 414 IEINNSVPQGLSSSIFTRNPETIfkwigPLGSD---CGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSDSWKQYMRRS 489
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
556-972 |
1.70e-41 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 160.28 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEARN--VGEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALP-----EWSAKPASERADCLRRFADLLEQHTP 628
Cdd:PLN02467 12 IGGEWREpvLGKRIPVVNPAT-EETIGDIPAATAEDVDAAVEAARKAFKrnkgkDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 629 ALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAEN---------TLPKDA-------KAVGAIVAISPWNFPLAIFTG 692
Cdd:PLN02467 91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEAldakqkapvSLPMETfkgyvlkEPLGVVGLITPWNYPLLMATW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 693 EVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKAL 771
Cdd:PLN02467 171 KVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGtEAGAPLASHPGVDKIAFTGSTATGRKIMTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 772 SKrDDSPVLIaETGGQNAMIVDstalpEQVCLDV-----LNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVV 846
Cdd:PLN02467 251 AQ-MVKPVSL-ELGGKSPIIVF-----DDVDLDKavewaMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 847 GKPIQLTTDIGPVIDAEAQQNLLAHIN--KMKGVakayhEIKTAADVDENNST--FVRP-ILFELNNLNELQR-EVFGPV 920
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFIStaKSEGA-----TILCGGKRPEHLKKgfFIEPtIITDVTTSMQIWReEVFGPV 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1080520335 921 LhVVRYRASElDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVN 972
Cdd:PLN02467 399 L-CVKTFSTE-DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
571-998 |
2.43e-41 |
|
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: 159.00 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 571 NPADHNdVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAV-AEV 649
Cdd:cd07098 2 DPATGQ-HLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASlGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 650 REAVDFCRYYANEAENTLPKDAKAV----------------GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTS 713
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGgllmfykrarveyeplGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 714 LIATYAVSLMHQA----GIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLINKALSKrDDSPVlIAETGGQNA 789
Cdd:cd07098 161 WSSGFFLSIIREClaacGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAE-SLTPV-VLELGGKDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 790 MIV-DSTALPEQVCLdVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVI-------- 860
Cdd:cd07098 239 AIVlDDADLDQIASI-IMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIsparfdrl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 861 -----DAEAQ-QNLLA------HINKMKGvakAYHEIKTAADVDENNSTFvrpilfelnnlnelQREVFGPVLHVVryRA 928
Cdd:cd07098 318 eelvaDAVEKgARLLAggkrypHPEYPQG---HYFPPTLLVDVTPDMKIA--------------QEEVFGPVMVVM--KA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 929 SELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAG 998
Cdd:cd07098 379 SDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
564-994 |
6.28e-40 |
|
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: 154.92 E-value: 6.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLN 643
Cdd:cd07117 15 GETIDSYNPAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 644 NAVA-EVREAVDFCRYYAN--EAE----NTLPKDA------KAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAE 710
Cdd:cd07117 94 ETRAvDIPLAADHFRYFAGviRAEegsaNMIDEDTlsivlrEPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 711 QTSLIATYAVSLMHQAgIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNA 789
Cdd:cd07117 174 TTSLSLLELAKIIQDV-LPKGVVNIVTGKGsKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPATL--ELGGKSA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 790 MIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLL 869
Cdd:cd07117 251 NIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKIL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 870 AH--INKMKGvAKAYHEIKTAADVDENNSTFVRPILFEL--NNLNELQREVFGPVLHVVRYRASelDQLIDQINAKGYAL 945
Cdd:cd07117 331 SYvdIAKEEG-AKILTGGHRLTENGLDKGFFIEPTLIVNvtNDMRVAQEEIFGPVATVIKFKTE--DEVIDMANDSEYGL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1080520335 946 TSGVHSRIEGTVDHIRDRIEAGNIYVNR-NIVGAVVgvqPFGGHGLSGTG 994
Cdd:cd07117 408 GGGVFTKDINRALRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
680-994 |
8.76e-40 |
|
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: 153.45 E-value: 8.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 680 ISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQT--------SLIATYavslmhqagIPTSALQLVLGAGDVGSALTgDAR 751
Cdd:cd07087 107 IGPWNYPLQLALAPLIGAIAAGNTVVLKPSELApatsallaKLIPKY---------FDPEAVAVVEGGVEVATALL-AEP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 752 IGGVIFTGSTEVARLINKALSKRDdSPVlIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVAD 831
Cdd:cd07087 177 FDHIFFTGSPAVGKIVMEAAAKHL-TPV-TLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 832 KMINIIKGAMDELVvGKPIQLTTDIGPVIDAeaqqnllAHINKMKGVAKaYHEIKTAADVDENnSTFVRPILFELNNLNE 911
Cdd:cd07087 255 ELIEELKKAIKEFY-GEDPKESPDYGRIINE-------RHFDRLASLLD-DGKVVIGGQVDKE-ERYIAPTILDDVSPDS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 912 --LQREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHG 989
Cdd:cd07087 325 plMQEEIFGPILPILTYD--DLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVG 402
|
....*
gi 1080520335 990 LSGTG 994
Cdd:cd07087 403 NSGMG 407
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
616-1007 |
1.14e-39 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 152.58 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 616 LRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFCRYYANEAE----NTLPKD---------AKAVGAIVAISP 682
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegEIIQSDrpgenillfKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 683 WNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGD-VGSALTGDARIGGVIFTGST 761
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGEtVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 762 EVARLINKALSKRDDSPVLiaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAM 841
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCL--ELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 842 DELVVGKPIQ-LTTDIGPVIDAEAqqnlLAHINKMkgVAKAYHE---IKTAADVDENNSTFVRPILFeLNNLNE---LQR 914
Cdd:PRK10090 239 QAVQFGNPAErNDIAMGPLINAAA----LERVEQK--VARAVEEgarVALGGKAVEGKGYYYPPTLL-LDVRQEmsiMHE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 915 EVFGPVLHVVRYraSELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQP-FGGHGLSGT 993
Cdd:PRK10090 312 ETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAgWRKSGIGGA 389
|
410
....*....|....
gi 1080520335 994 GPKAGGSFYLQRLV 1007
Cdd:PRK10090 390 DGKHGLHEYLQTQV 403
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
556-994 |
1.56e-37 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 148.51 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEARNVGEAQ--PVRNPAdhndvvGTVSFADAALAQEA-IGAAVAALPE------WSAKPASERADCLRRFADLLEQH 626
Cdd:PRK09847 24 INGEYTAAAENEtfETVDPV------TQAPLAKIARGKSVdIDRAVSAARGvfergdWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 627 TPALMMLAVREAGKTLNNAVAE-VREAVDFCRYYANEAENTLPKDA------------KAVGAIVAISPWNFPLAIFTGE 693
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSLRDdIPGAARAIRWYAEAIDKVYGEVAttsshelamivrEPVGVIAAIVPWNFPLLLTCWK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 694 VVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALS 772
Cdd:PRK09847 178 LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 773 KRDDSPVLIaETGGQNAMIV--DSTALpEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPI 850
Cdd:PRK09847 258 DSNMKRVWL-EAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 851 QLTTDIGPVIDAEAQQNLLAHINKmkgvakayHEIKTAADVDENNSTF---VRPILF-ELNNLNELQR-EVFGPVLHVVR 925
Cdd:PRK09847 336 DPATTMGTLIDCAHADSVHSFIRE--------GESKGQLLLDGRNAGLaaaIGPTIFvDVDPNASLSReEIFGPVLVVTR 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080520335 926 YRASEldQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVvgVQPFGGHGLSGTG 994
Cdd:PRK09847 408 FTSEE--QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
556-972 |
5.79e-37 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 146.82 E-value: 5.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 556 VNGEARNV--GEAQPVRNPADHNdvvgtVSFADAALAQE----AIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPA 629
Cdd:PLN00412 20 ADGEWRTSssGKSVAITNPSTRK-----TQYKVQACTQEevnkAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 630 LMMLAVREAGKTLNNAVAEVREAVDFCRYYANEA-----------ENTLPKDAKA---------VGAIVAISPWNFPLAI 689
Cdd:PLN00412 95 IAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGvrilgegkflvSDSFPGNERNkycltskipLGVVLAIPPFNYPVNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 690 FTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFT-GSTEVarli 767
Cdd:PLN00412 175 AVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGsEIGDFLTMHPGVNCISFTgGDTGI---- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 768 nkALSKRDDSPVLIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVG 847
Cdd:PLN00412 251 --AISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 848 KPiQLTTDIGPVIdAEAQQNL---LAHINKMKGvAKAYHEIKTaadvdENNstFVRPILfeLNNLNELQR----EVFGPV 920
Cdd:PLN00412 329 PP-EDDCDITPVV-SESSANFiegLVMDAKEKG-ATFCQEWKR-----EGN--LIWPLL--LDNVRPDMRiaweEPFGPV 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1080520335 921 LHVVRYRASEldQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVN 972
Cdd:PLN00412 397 LPVIRINSVE--EGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN 446
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
591-1001 |
1.21e-36 |
|
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: 144.29 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 591 QEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKtlnnAVAEVR---------EAVDFCRyyaN 661
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRK----PAAEVDlteilpvlsEINHAIK---H 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 662 EAENTLPKDAK---------------AVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQA 726
Cdd:cd07134 74 LKKWMKPKRVRtplllfgtkskiryePKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 727 gIPTSALQLVLGAGDVGSALTgDARIGGVIFTGSTEVARLINKALSKRDDSPVLiaETGGQNAMIVDSTALPEQVCLDVL 806
Cdd:cd07134 154 -FDEDEVAVFEGDAEVAQALL-ELPFDHIFFTGSPAVGKIVMAAAAKHLASVTL--ELGGKSPTIVDETADLKKAAKKIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 807 NSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDElVVGK--PIQLTTDIGPVIDAeaqqnllAHINKMKG-----VA 879
Cdd:cd07134 230 WGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEK-FYGKdaARKASPDLARIVND-------RHFDRLKGllddaVA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 880 KAyHEIKTAADVDEnNSTFVRPILfeLNNLNE----LQREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEG 955
Cdd:cd07134 302 KG-AKVEFGGQFDA-AQRYIAPTV--LTNVTPdmkiMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKA 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1080520335 956 TVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGpKAGGSF 1001
Cdd:cd07134 376 NVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIG-SYHGVY 420
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
593-994 |
1.25e-34 |
|
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: 139.51 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 593 AIGAAVAALPEWSAKPASERADCLRRFADLLEQHtpaLMMLAVREA---GKTLNNAV-AEVREAVDFCRYYAN---EAEN 665
Cdd:cd07116 43 ALDAAHAAKEAWGKTSVAERANILNKIADRMEAN---LEMLAVAETwdnGKPVRETLaADIPLAIDHFRYFAGcirAQEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 666 TLPK-DAKAV--------GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAgIPTSALQLV 736
Cdd:cd07116 120 SISEiDENTVayhfheplGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 737 LGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKrDDSPVLIaETGGQNAMIVDSTALPEQvcldvlNSAFDSA-- 813
Cdd:cd07116 199 NGFGlEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NIIPVTL-ELGGKSPNIFFADVMDAD------DAFFDKAle 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 814 ---------GQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHIN--KMKGVAKAY 882
Cdd:cd07116 271 gfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDigKEEGAEVLT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 883 HEIKTAADVDENNSTFVRPILFELNNLNELQREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRD 962
Cdd:cd07116 351 GGERNELGGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTFK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGR 428
|
410 420 430
....*....|....*....|....*....|..
gi 1080520335 963 RIEAGNIYVnrNIVGAVVGVQPFGGHGLSGTG 994
Cdd:cd07116 429 GIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
675-994 |
1.74e-33 |
|
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: 135.04 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 675 GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAgIPTSALQLVLGAGDVGSALTgDARIGG 754
Cdd:cd07135 110 GVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL-EQKFDK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 755 VIFTGSTEVARLINKALSKRdDSPVLIaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMI 834
Cdd:cd07135 188 IFYTGSGRVGRIIAEAAAKH-LTPVTL-ELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 835 NIIKGAMDELVVGKPIQLtTDIGPVIDAEAQQNLLAHINKMKG--VAKAYHEIKT-------AADVDENNSTfvrpilfe 905
Cdd:cd07135 266 EELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLDTTKGkvVIGGEMDEATrfipptiVSDVSWDDSL-------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 906 lnnlneLQREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPF 985
Cdd:cd07135 337 ------MSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPF 408
|
....*....
gi 1080520335 986 GGHGLSGTG 994
Cdd:cd07135 409 GGVGDSGYG 417
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
675-994 |
1.90e-33 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 135.93 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 675 GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEqtslIATYAVSLMHQ---AGIPTSALQLVLGAGDVGSALTgDAR 751
Cdd:PTZ00381 111 GVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSE----LSPHTSKLMAKlltKYLDPSYVRVIEGGVEVTTELL-KEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 752 IGGVIFTGSTEVARLINKALSKrDDSPVlIAETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVAD 831
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAE-NLTPC-TLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKD 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 832 KMINIIKGAMDELvVGKPIQLTTDIGPVIDAEAQQNLLAHINKMKGvaKAYHeiktAADVDENNStFVRPILFELNNLNE 911
Cdd:PTZ00381 264 KFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDHGG--KVVY----GGEVDIENK-YVAPTIIVNPDLDS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 912 --LQREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHG 989
Cdd:PTZ00381 336 plMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVG 413
|
....*
gi 1080520335 990 LSGTG 994
Cdd:PTZ00381 414 NSGMG 418
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
591-1000 |
5.13e-31 |
|
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: 127.74 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 591 QEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVREAVDFcRYYA---------N 661
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQL-RARAfviysyripH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 662 EAENTLPKDAK--------AVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGI-PTSA 732
Cdd:cd07084 81 EPGNHLGQGLKqqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 733 LQLVLGAGDVGSALTGDARIGGVIFTGSTEVAR-LINKALSKRddspvLIAETGGQNAMIVDSTAlpEQVCLDVLNSAFD 811
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEkLALDAKQAR-----IYLELAGFNWKVLGPDA--QAVDYVAWQCVQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 812 S---AGQRCSALRILCVQEDVA-DKMINIIKGAMDELVVGkpiqlTTDIGPVIDAEAQQNLLAHINKMKGVAKAYHEIKT 887
Cdd:cd07084 234 MtacSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLE-----DLLLGPVQTFTTLAMIAHMENLLGSVLLFSGKELK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 888 AADVDENNSTFVRPILF----ELNNLNEL-QREVFGPVLHVVRYRASELDQLIDQINAKGYALTSGVHSRIEGTVDHIRD 962
Cdd:cd07084 309 NHSIPSIYGACVASALFvpidEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIG 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 1080520335 963 RIE-AGNIYVNRNIVGavvGVQPFGGHGLSGTGPKAGGS 1000
Cdd:cd07084 389 NLWvAGRTYAILRGRT---GVAPNQNHGGGPAADPRGAG 424
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
571-972 |
6.02e-31 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 128.06 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 571 NPADhNDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAEVR 650
Cdd:PRK13968 13 NPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 651 EAVDFCRYYAN------EAENTLPKDAKAV------GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATY 718
Cdd:PRK13968 92 KSANLCDWYAEhgpamlKAEPTLVENQQAVieyrplGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 719 AVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLIN----KALSKrddspvLIAETGGQNAMIVDS 794
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGaqagAALKK------CVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 795 TALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQLTTDIGPVI-----DAEAQQ--- 866
Cdd:PRK13968 246 DADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMArfdlrDELHHQvea 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 867 ------NLLAHINKMKGvAKAYHEIKTAADVDENNSTFvrpilfelnnlnelQREVFGPVLHVVryRASELDQLIDQINA 940
Cdd:PRK13968 326 tlaegaRLLLGGEKIAG-AGNYYAPTVLANVTPEMTAF--------------REELFGPVAAIT--VAKDAEHALELAND 388
|
410 420 430
....*....|....*....|....*....|..
gi 1080520335 941 KGYALTSGVHSRIEGTVDHIRDRIEAGNIYVN 972
Cdd:PRK13968 389 SEFGLSATIFTTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
607-994 |
1.27e-28 |
|
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: 120.59 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 607 KPASERADCLRRFADLLEQHTPALMMLAVREAGK-TLNNAVAEVREAVDFCRYYANEAEN------------TLPKDAKA 673
Cdd:cd07137 18 RSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKpSAESFRDEVSVLVSSCKLAIKELKKwmapekvktpltTFPAKAEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 674 V----GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEqtslIATYAVSLMHQAgIP----TSALQLVLGAGDVGSA 745
Cdd:cd07137 98 VseplGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSE----LAPATSALLAKL-IPeyldTKAIKVIEGGVPETTA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 746 LTgDARIGGVIFTGSTEVARLINKALSKRdDSPVLIaETGGQNAMIVDSTALPEQVCLDVLNSAFDS-AGQRCSALRILC 824
Cdd:cd07137 173 LL-EQKWDKIFFTGSPRVGRIIMAAAAKH-LTPVTL-ELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 825 VQEDVADKMINIIKGAMDELVVGKPIQlTTDIGPVIDAEAQQnLLAHINKMKGVAKayhEIKTAADVDENNsTFVRPILF 904
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKE-SKDLSRIVNSHHFQ-RLSRLLDDPSVAD---KIVHGGERDEKN-LYIEPTIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 905 ELNNLNEL--QREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGV 982
Cdd:cd07137 324 LDPPLDSSimTEEIFGPLLPIITVK--KIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
410
....*....|..
gi 1080520335 983 QPFGGHGLSGTG 994
Cdd:cd07137 402 LPFGGVGESGFG 413
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
674-994 |
4.29e-28 |
|
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: 118.86 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 674 VGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEqtslIATYAVSLMHQAgIP----TSALQLVLGAGDVGSALTgD 749
Cdd:cd07132 101 LGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE----VSPATAKLLAEL-IPkyldKECYPVVLGGVEETTELL-K 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 750 ARIGGVIFTGSTEVARLINKALSKRdDSPVLIaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALR-ILCVQEd 828
Cdd:cd07132 175 QRFDYIFYTGSTSVGKIVMQAAAKH-LTPVTL-ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDyVLCTPE- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 829 VADKMINIIKGAMDELvVGKPIQLTTDIGPVIDAEAQQNLLAHINKMKgvakayheIKTAADVDEnNSTFVRPILfeLNN 908
Cdd:cd07132 252 VQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKLLSGGK--------VAIGGQTDE-KERYIAPTV--LTD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 909 LNE----LQREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQP 984
Cdd:cd07132 320 VKPsdpvMQEEIFGPILPIVTVN--NLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLP 397
|
330
....*....|
gi 1080520335 985 FGGHGLSGTG 994
Cdd:cd07132 398 FGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
569-1012 |
7.69e-28 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 120.62 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 569 VRNPADHnDVVGTVSFADAALAQEAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTLNNAVAE 648
Cdd:PLN02419 133 VINPATQ-EVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 649 VREAVDFCRYYANEAE----NTLPKDAKAV---------GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLI 715
Cdd:PLN02419 212 IFRGLEVVEHACGMATlqmgEYLPNVSNGVdtysireplGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 716 ATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGGVIFTGSTEVARLI---NKALSKRDDSpvliaETGGQNAMIV 792
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIyarAAAKGKRIQS-----NMGAKNHGLV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVA---DKMINIIKgAMDELVVGKPiqlTTDIGPVIDAEAQQNLL 869
Cdd:PLN02419 367 LPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVERAK-ALKVTCGSEP---DADLGPVISKQAKERIC 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 870 AHINkmKGVAKAYHEIKTAADV---DENNSTFVRPILFE--LNNLNELQREVFGPVLhvVRYRASELDQLIDQINAKGYA 944
Cdd:PLN02419 443 RLIQ--SGVDDGAKLLLDGRDIvvpGYEKGNFIGPTILSgvTPDMECYKEEIFGPVL--VCMQANSFDEAISIINKNKYG 518
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080520335 945 LTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIvGAVVGVQPFGGHGLSGTGP-----KAGGSFYLQRLVRTPEW 1012
Cdd:PLN02419 519 NGAAIFTSSGAAARKFQMDIEAGQIGINVPI-PVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQIKLVTQKQ 590
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
680-994 |
2.55e-25 |
|
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: 110.65 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 680 ISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSliATYAV--SLMHQAgIPTSALQLVLGAGDVGSALTG---DArigg 754
Cdd:cd07133 108 IVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTP--RTSALlaELLAEY-FDEDEVAVVTGGADVAAAFSSlpfDH---- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 755 VIFTGSTEVARLINKALSKrDDSPVLIaETGGQNAMIVDSTALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMI 834
Cdd:cd07133 181 LLFTGSTAVGRHVMRAAAE-NLTPVTL-ELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 835 NIIKGAMDEL---VVGKPiqlttDIGPVIDAEAQQNLLAHIN--KMKGvAKAyHEIKTAADVDENNSTFVRPILFELNN- 908
Cdd:cd07133 259 AAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEdaRAKG-ARV-IELNPAGEDFAATRKLPPTLVLNVTDd 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 909 LNELQREVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGH 988
Cdd:cd07133 332 MRVMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGV 409
|
....*.
gi 1080520335 989 GLSGTG 994
Cdd:cd07133 410 GASGMG 415
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
586-951 |
2.23e-23 |
|
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: 104.93 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 586 DAALAqeaigAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAG-----------KT---LNNAVAEVRE 651
Cdd:cd07129 2 DAAAA-----AAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpearlqgelgRTtgqLRLFADLVRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 652 ------AVDFcryyANEAENTLPK-DAK----AVGAIVAISPWNFPLAIFT--GEVVSALAAGNTVIAK--PA--EQTSL 714
Cdd:cd07129 77 gswldaRIDP----ADPDRQPLPRpDLRrmlvPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhpGTSEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 715 IATYAVSLMHQAGIPTSALQLVLGAG-DVGSALTGDARIGGVIFTGSTEVARLINKALSKRDDS-PVLiAETGGQNAMIV 792
Cdd:cd07129 153 VARAIRAALRATGLPAGVFSLLQGGGrEVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPiPFY-AELGSVNPVFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 793 DSTAL---PEQVCLDVLNSAFDSAGQRCSALRILCVQEDVA-DKMINIIKGAMDELVVGkpIQLTTDIgpvidaeaQQNL 868
Cdd:cd07129 232 LPGALaerGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQ--TMLTPGI--------AEAY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 869 LAHINKMKGVAKAYHEIKTAADVDENNstfVRPILFE-----LNNLNELQREVFGPVLHVVRYRAseLDQLIDQINAKGY 943
Cdd:cd07129 302 RQGVEALAAAPGVRVLAGGAAAEGGNQ---AAPTLFKvdaaaFLADPALQEEVFGPASLVVRYDD--AAELLAVAEALEG 376
|
....*...
gi 1080520335 944 ALTSGVHS 951
Cdd:cd07129 377 QLTATIHG 384
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
553-1005 |
3.38e-22 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 101.96 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 553 ASIVNGEAR-NVGEAQPVRNPADhNDVVGTVS-----FADA-ALAQEAIGAAVAALPewsakpASERADCLRRFADLLEQ 625
Cdd:cd07128 2 QSYVAGQWHaGTGDGRTLHDAVT-GEVVARVSsegldFAAAvAYAREKGGPALRALT------FHERAAMLKALAKYLME 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 626 HTPALMMLAVReAGKTLNNAVAEVREAVDFCRYYANEAENTLP--------------KDAKAV---------GAIVAISP 682
Cdd:cd07128 75 RKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELPnahflvegdveplsKDGTFVgqhiltprrGVAVHINA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 683 WNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGI-PTSALQLVLG-AGDVGSALTG-DAriggVIFTG 759
Cdd:cd07128 154 FNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGsVGDLLDHLGEqDV----VAFTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 760 STEVARLI--NKALSKRddSPVLIAETGGQNAMIVDSTALPEQVCLD-----VLNSAFDSAGQRCSALRILCVQEDVADK 832
Cdd:cd07128 230 SAATAAKLraHPNIVAR--SIRFNAEADSLNAAILGPDATPGTPEFDlfvkeVAREMTVKAGQKCTAIRRAFVPEARVDA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 833 MINIIKGAMDELVVGKPIQLTTDIGPVIDAEAQQNLLAHINKMKGVAKAYH---EIKTAADVDENNSTFVRPILFELNNL 909
Cdd:cd07128 308 VIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFggpDRFEVVGADAEKGAFFPPTLLLCDDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 910 NELQR----EVFGPVLHVVRYRasELDQLIDQINAKGYALTSGVHSrieGTVDHIRDRIEA-----GNIYV-NRNIVGAV 979
Cdd:cd07128 388 DAATAvhdvEAFGPVATLMPYD--SLAEAIELAARGRGSLVASVVT---NDPAFARELVLGaapyhGRLLVlNRDSAKES 462
|
490 500 510
....*....|....*....|....*....|....*.
gi 1080520335 980 VG---VQP---FGGHGLSGTGPKAGG----SFYLQR 1005
Cdd:cd07128 463 TGhgsPLPqlvHGGPGRAGGGEELGGlrgvKHYMQR 498
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
675-994 |
1.11e-21 |
|
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: 99.50 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 675 GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSliATYAV-SLMHQAGIPTSALQLVLGAGDVGSALTgDARIG 753
Cdd:cd07136 102 GVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTP--NTSKViAKIIEETFDEEYVAVVEGGVEENQELL-DQKFD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 754 GVIFTGSTEVARLINKALSKRdDSPVLIaETGGQNAMIVDSTAlpeqvCLDV----------LNsafdsAGQRCSALRIL 823
Cdd:cd07136 179 YIFFTGSVRVGKIVMEAAAKH-LTPVTL-ELGGKSPCIVDEDA-----NLKLaakrivwgkfLN-----AGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 824 CVQEDVADKMINIIKGAMDELvVGKPIQLTTDIGPVIDAEaqqnllaHINKMKGVAKaYHEIKTAADVDENNsTFVRPIL 903
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKKF-YGEDPLESPDYGRIINEK-------HFDRLAGLLD-NGKIVFGGNTDRET-LYIEPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 904 FELNNLNE--LQREVFGPVLHVVRYraSELDQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVG 981
Cdd:cd07136 317 LDNVTWDDpvMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANP 394
|
330
....*....|...
gi 1080520335 982 VQPFGGHGLSGTG 994
Cdd:cd07136 395 YLPFGGVGNSGMG 407
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
564-927 |
3.15e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 99.01 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 564 GEAQPVRNPADHNDVVGT----VSFADA-ALAQEAIGAAVAALPewsakpASERADCLRRFADLLEQHTPALMMLAVREA 638
Cdd:PRK11903 18 GAGTPLFDPVTGEELVRVsatgLDLAAAfAFAREQGGAALRALT------YAQRAALLAAIVKVLQANRDAYYDIATANS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 639 GKTLNNAVAEVREAVDFCRYYANEA----ENTLPKDAKAV------------------GAIVAISPWNFPLAIFTGEVVS 696
Cdd:PRK11903 92 GTTRNDSAVDIDGGIFTLGYYAKLGaalgDARLLRDGEAVqlgkdpafqgqhvlvptrGVALFINAFNFPAWGLWEKAAP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 697 ALAAGNTVIAKPAEQTSLIATYAVSLMHQAGI-PTSALQLVLG-AGDVGSALTG-DAriggVIFTGSTEVARLINKALSK 773
Cdd:PRK11903 172 ALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGsSAGLLDHLQPfDV----VSFTGSAETAAVLRSHPAV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 774 RDDSPVLIAETGGQNAMIVDSTALPEQVCLD-----VLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGK 848
Cdd:PRK11903 248 VQRSVRVNVEADSLNSALLGPDAAPGSEAFDlfvkeVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 849 PIQLTTDIGPVIDAEAQQNLLAHINKMKGVAKAYHEIKTAA--DVDENNSTFVRPILFELNNLNELQR----EVFGPVLH 922
Cdd:PRK11903 328 PRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFAlvDADPAVAACVGPTLLGASDPDAATAvhdvEVFGPVAT 407
|
....*
gi 1080520335 923 VVRYR 927
Cdd:PRK11903 408 LLPYR 412
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
666-1012 |
9.13e-20 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 94.02 E-value: 9.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 666 TLPKDAKAV----GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSliatyAVSLMHQAGIPT----SALQLVL 737
Cdd:PLN02203 97 AFPATAEVVpeplGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAP-----ATSAFLAANIPKyldsKAVKVIE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 738 GAGDVGSALTgDARIGGVIFTGSTEVARLINKALSKRdDSPVLIaETGGQNAMIVDSTALP---EQVCLDVLNSAFDS-A 813
Cdd:PLN02203 172 GGPAVGEQLL-QHKWDKIFFTGSPRVGRIIMTAAAKH-LTPVAL-ELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 814 GQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQlTTDIGPVIDAEAQQNLLAHINKMKGVAKAYHeiktAADVDE 893
Cdd:PLN02203 249 GQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRE-SKSMARILNKKHFQRLSNLLKDPRVAASIVH----GGSIDE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 894 NNsTFVRPILFeLN---NLNELQREVFGPVLHVVRYRASEldQLIDQINAKGYALTSGVHSRIEGTVDHIRDRIEAGNIY 970
Cdd:PLN02203 324 KK-LFIEPTIL-LNpplDSDIMTEEIFGPLLPIITVKKIE--DSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVT 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520335 971 VNRNIVGAVVGVQPFGGHGLSGTGPKAG---------------GSFYLQRLVRTPEW 1012
Cdd:PLN02203 400 FNDAIIQYACDSLPFGGVGESGFGRYHGkysfdtfshekavlrRSLLTEFEFRYPPW 456
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
629-998 |
2.07e-19 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 93.19 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 629 ALMMLAVREAGKTLNNAVAEVReavdfcryyANEAENTLPKDAKAV----GAIVAISPWNFPLAIFTGEVVSALAAGNTV 704
Cdd:PLN02174 73 SLLRNSIKLALKQLKNWMAPEK---------AKTSLTTFPASAEIVseplGVVLVISAWNYPFLLSIDPVIGAISAGNAV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 705 IAKPAEQTSLIATYAVSLMHQAgIPTSALQLVLGAGDVGSALTgDARIGGVIFTGSTEVARLINKALSKRdDSPVLIaET 784
Cdd:PLN02174 144 VLKPSELAPASSALLAKLLEQY-LDSSAVRVVEGAVTETTALL-EQKWDKIFYTGSSKIGRVIMAAAAKH-LTPVVL-EL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 785 GGQNAMIVDS-TALPEQVCLDVLNSAFDSAGQRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQlTTDIGPVIDAe 863
Cdd:PLN02174 220 GGKSPVVVDSdTDLKVTVRRIIAGKWGCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNS- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 864 aqqNLLAHINKMKGVAKAYHEIKTAADVDENNSTFVRPILFE--LNNLnELQREVFGPVLHVVryRASELDQLIDQINAK 941
Cdd:PLN02174 298 ---THFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDvpLDSL-IMSEEIFGPLLPIL--TLNNLEESFDVIRSR 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1080520335 942 GYALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAVVGVQPFGGHGLSGTGPKAG 998
Cdd:PLN02174 372 PKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHG 428
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
10-57 |
1.35e-18 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 80.20 E-value: 1.35e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1080520335 10 TPLRQAVTDAYRRDEIEAVQDMLQRAQMTDEERNAASELARRLVTQVR 57
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
675-951 |
1.56e-14 |
|
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: 77.92 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 675 GAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAGDVGSALTGDARIGG 754
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRM 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 755 VIFTGSTEVARLINKALSKRddspVLIAETG------GQNAMIVDSTAlpeQVClDvlNSAFDSAGQRCSALRILCVQED 828
Cdd:cd07126 224 TLFTGSSKVAERLALELHGK----VKLEDAGfdwkilGPDVSDVDYVA---WQC-D--QDAYACSGQKCSAQSILFAHEN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 829 VADK-MINIIKgamdELVVGKPIQLTTdIGPVIDAEAQQnLLAHINKMKGVAKAY----------HEIKTAADVDENNST 897
Cdd:cd07126 294 WVQAgILDKLK----ALAEQRKLEDLT-IGPVLTWTTER-ILDHVDKLLAIPGAKvlfggkpltnHSIPSIYGAYEPTAV 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1080520335 898 FVrPILFELNNLN-EL-QREVFGPVLHVVRYRASELDQLIDQINAKGYALTSGVHS 951
Cdd:cd07126 368 FV-PLEEIAIEENfELvTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVS 422
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
592-960 |
9.75e-07 |
|
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: 52.65 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 592 EAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAGKTL-------NNAVAE----VREAVDFCRYYA 660
Cdd:cd07081 3 DAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRvedkvikNHFAAEyiynVYKDEKTCGVLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 661 NEAENTLPKDAKAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQLVLGAG 740
Cdd:cd07081 83 GDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIGWI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 741 D-----VGSALTGDARIGGVIFTGSTEVARlinkalSKRDDSPVLIAETGGQNAMIVDSTA-LPEQVCLDVLNSAFDSaG 814
Cdd:cd07081 163 DnpsieLAQRLMKFPGIGLLLATGGPAVVK------AAYSSGKPAIGVGAGNTPVVIDETAdIKRAVQSIVKSKTFDN-G 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 815 QRCSALRILCVQEDVADKMINIIKGAMDELVVGKPIQlttDIGPVIDAEAQQNllahinkMKGVAKAYHEIKTAADVDEN 894
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQ---QVQPVILKNGDVN-------RDIVGQDAYKIAAAAGLKVP 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080520335 895 NSTfvRPILFELNNLNE---LQREVFGPVLHVVRYR--ASELDQLIDQINAKGYALTSGVHSRIEGTVDHI 960
Cdd:cd07081 306 QET--RILIGEVTSLAEhepFAHEKLSPVLAMYRAAnfADADAKALALKLEGGCGHTSAMYSDNIKAIENM 374
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
258-471 |
3.79e-06 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 50.86 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 258 AQHERVMSELLPRLKELFLLGKKYDIGINIDAEEaNRLE-----LSLDLMEALVSDPDLAGYKGigfVVQAYQKRCPFVI 332
Cdd:PLN02681 209 AEEERLLELAHERLQKLCERAAQLGVPLLIDAEY-TSLQpaidyITYDLAREFNKGKDRPIVYG---TYQAYLKDARERL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 333 DYLIDLARRNNQKLMIRLVKGAYWDSEVKWAQVDGMEGyPTYTRKVHTDISYLACARKLLDA----QDAVFpqFATHN-- 406
Cdd:PLN02681 285 RLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAEFLLEKasngDGEVM--LATHNve 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080520335 407 --------AYTLGaiyqMGKGKDFEH--QcLHGMGETLydqVVGPQNLGRRVRVYAPVGTHETLLAYLVRRLLEN 471
Cdd:PLN02681 362 sgelaaakMNELG----LHKGDPRVQfaQ-LLGMSDNL---SFGLGNAGFRVSKYLPYGPVEEVIPYLLRRAEEN 428
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
592-960 |
6.62e-06 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 50.29 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 592 EAIGAAVAALPEWSAKPASERA---DCLRRfadLLEQHTPALMMLAVREAG------KTL-NNAVAEVREAVDFCRYYAN 661
Cdd:PRK15398 40 DAVAAAKVAQQRYQQKSLAMRQriiDAIRE---ALLPHAEELAELAVEETGmgrvedKIAkNVAAAEKTPGVEDLTTEAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 662 EAEN--TLPKDAkAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQ-LVLG 738
Cdd:PRK15398 117 TGDNglTLIEYA-PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAGGPEnLVVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 739 AG----DVGSALTGDARIGGVIFTGSTEVarlINKALS--KRddspvLIAETGGQNAMIVDSTALPEQVCLDVLNSA-FD 811
Cdd:PRK15398 196 VAeptiETAQRLMKHPGIALLVVTGGPAV---VKAAMKsgKK-----AIGAGAGNPPVVVDETADIEKAARDIVKGAsFD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 812 SagqrcsalRILCVQE-------DVADKMINIIK--GAMdelvvgkpiqlttdigpVIDAEAQQNLLA-------HINKm 875
Cdd:PRK15398 268 N--------NLPCIAEkevivvdSVADELMRLMEknGAV-----------------LLTAEQAEKLQKvvlknggTVNK- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 876 KGVAKAYHEIKTAADVDENNSTfvRPILFELNNLNEL-QREVFGPVLHVVryRASELDQLIDqiNAK----GYALTSGVH 950
Cdd:PRK15398 322 KWVGKDAAKILEAAGINVPKDT--RLLIVETDANHPFvVTELMMPVLPVV--RVKDVDEAIA--LAVklehGNRHTAIMH 395
|
410
....*....|
gi 1080520335 951 SRiegTVDHI 960
Cdd:PRK15398 396 SR---NVDNL 402
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
592-952 |
1.36e-05 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 49.16 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 592 EAIGAAVAALPEWSAKPASERADCLRRFADLLEQHTPALMMLAVREAG------KTL-NNAVAEVREAVDFCRYYANEAE 664
Cdd:cd07121 8 DAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGmgrvedKIAkNHLAAEKTPGTEDLTTTAWSGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 665 N--TLPKDAkAVGAIVAISPWNFPLAIFTGEVVSALAAGNTVIAKPAEQTSLIATYAVSLMHQAGIPTSALQ-LVLGAG- 740
Cdd:cd07121 88 NglTLVEYA-PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGGPDnLVVTVEe 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 741 ---DVGSALTGDARIGGVIFTGSTEVARlinKALS--KRddspvLIAETGGQNAMIVDSTALPEQVCLDVLNSA-FDSag 814
Cdd:cd07121 167 ptiETTNELMAHPDINLLVVTGGPAVVK---AALSsgKK-----AIGAGAGNPPVVVDETADIEKAARDIVQGAsFDN-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 815 qrcsalRILCVQE-------DVADKMINIIK--GAMdELVVGKPIQLTTDIgpvidaeAQQNLLAHINKmKGVAKAYHEI 885
Cdd:cd07121 237 ------NLPCIAEkeviavdSVADYLIAAMQrnGAY-VLNDEQAEQLLEVV-------LLTNKGATPNK-KWVGKDASKI 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080520335 886 KTAADVDENNSTfvRPILFELNNLNEL-QREVFGPVLHVVryRASELDQLIDQinAK----GYALTSGVHSR 952
Cdd:cd07121 302 LKAAGIEVPADI--RLIIVETDKDHPFvVEEQMMPILPVV--RVKNFDEAIEL--AVelehGNRHTAIIHSK 367
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
591-979 |
4.86e-05 |
|
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: 47.47 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 591 QEAIGAAVAALPEWSAKPASERA----DCLRRFADLLEQHTPALM-------MLAVREAGKtlnNAVAEVREAVDfcryY 659
Cdd:cd07127 87 DALLAAARAAMPGWRDAGARARAgvclEILQRLNARSFEMAHAVMhttgqafMMAFQAGGP---HAQDRGLEAVA----Y 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 660 ANEAENTLPKDA----------------------KAVGAIVAISP---WNFPLAIFtgevvSALAAGNTVIAKPAEQTSL 714
Cdd:cd07127 160 AWREMSRIPPTAewekpqgkhdplamektftvvpRGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 715 IATYAV----SLMHQAGIPTSALQLVLG--AGDVGSALTGDARIGGVIFTGSTEVArlinKALSKRDDSPVLIAETGGQN 788
Cdd:cd07127 235 PLAITVqvarEVLAEAGFDPNLVTLAADtpEEPIAQTLATRPEVRIIDFTGSNAFG----DWLEANARQAQVYTEKAGVN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 789 AMIVDSTALPEQVCldvLNSAFDSA---GQRCSALRILCVQED---------VADKMINIIKGAMDELvVGKPIQLTTDI 856
Cdd:cd07127 311 TVVVDSTDDLKAML---RNLAFSLSlysGQMCTTPQNIYVPRDgiqtddgrkSFDEVAADLAAAIDGL-LADPARAAALL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080520335 857 GpVIDAEAQQNLLAHINKMKGVAKAYHEIKTAADVDENNSTfvrPILFELNNLNE--LQREVFGPVLHVVRYRASE--LD 932
Cdd:cd07127 387 G-AIQSPDTLARIAEARQLGEVLLASEAVAHPEFPDARVRT---PLLLKLDASDEaaYAEERFGPIAFVVATDSTDhsIE 462
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1080520335 933 QLIDQINAKGyALTSGVHSRIEGTVDHIRDRIEAGNIYVNRNIVGAV 979
Cdd:cd07127 463 LARESVREHG-AMTVGVYSTDPEVVERVQEAALDAGVALSINLTGGV 508
|
|
| |
