|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
19-1069 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1901.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 19 LLSPELPAPPNPFRQAITDGWLKDEASHVRELLAQARLPAEEQAKVQALAADLVGRVRVRAKDQGAIEAFMRQYDLGSEE 98
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGGIDAFLQEYSLSTEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 99 GVLLMCVAEALLRIPDQDTADKLIRDKLADADWEKHLGGSDSVLVNASTWGLMLTGKLVQMNDATRADAPSAFKRLVGRV 178
Cdd:PRK11904 81 GIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKADGTPSGVLKRLVNRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 179 GEPVVRLAVRQAMKIMGHQFVMGRTISEALSRSHKGDNANYRYSFDMLGEGALTMKDALRYLEDYRRAIHAIGGDHKarg 258
Cdd:PRK11904 161 GEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAG--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 259 grpDGDVNNAPGISIKLSALYPRYEHAKRARVLKDLVPGVLELAQLAKSYGIGCTVDAEESDRLELSLDIIEQVFSDASL 338
Cdd:PRK11904 238 ---GADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 339 AGWDGFGVVVQAYQKRTPYTIDHLADMARRAGRRLQVRLVKGAYWDAEIKRAQIEGYPGYPVFTRKQNTDVSYLACAKRL 418
Cdd:PRK11904 315 KGWGGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 419 FTHADAIYPMFATHNAHTIAAVRSIANGGVYEHQKLHGMGDDLYAEVVPAdrLNLPCRVYAPVGSHEDLLPYLVRRLLEN 498
Cdd:PRK11904 395 LSARGAIYPQFATHNAHTVAAILEMAGHRGFEFQRLHGMGEALYDALLDA--PGIPCRIYAPVGSHKDLLPYLVRRLLEN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 499 GANSSFVNRITDERVPIADLIRDPVEMVASFESIPHPKIPLPVDLLRsqnHDRKNSMGANLANDNELRALAEQINAAVKP 578
Cdd:PRK11904 473 GANSSFVHRLVDPDVPIEELVADPVEKLRSFETLPNPKIPLPRDIFG---PERKNSKGLNLNDRSELEPLAAAIAAFLEK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 579 -WQAAPLVPGAnpaGAALPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPE 657
Cdd:PRK11904 550 qWQAGPIINGE---GEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAE 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 658 FMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVA 737
Cdd:PRK11904 627 LIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVA 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 738 AALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAAR 817
Cdd:PRK11904 707 AALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAAR 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 818 DAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLS 897
Cdd:PRK11904 787 DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLS 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 898 TDVGPVIDADALKILQDHAERMDREARLIAAAELSAEAANGTFFAPRAYELKDLGQLQKEVFGPVLHVIRWKGDQLDAVI 977
Cdd:PRK11904 867 TDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDSISQLEREVFGPILHVIRYKASDLDKVI 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 978 DQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVN 1057
Cdd:PRK11904 947 DAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVN 1026
|
1050
....*....|..
gi 1590385370 1058 TTAAGGNASLLT 1069
Cdd:PRK11904 1027 TTAAGGNASLLS 1038
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
16-1056 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1642.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 16 PGALLSPELPaPPNPFRQAITDGWLKDEASHVRELLAQARLPAEEQAKVQALAADLVGRVRVRAKDQGaIEAFMRQYDLG 95
Cdd:PRK11905 1 MFQMFAPPFR-PQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTG-VEALLQEYSLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 96 SEEGVLLMCVAEALLRIPDQDTADKLIRDKLADADWEKHLGGSDSVLVNASTWGLMLTGKLVqmNDATRADAPSAFKRLV 175
Cdd:PRK11905 79 SQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLL--STVNDRGLSAALTRLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 176 GRVGEPVVRLAVRQAMKIMGHQFVMGRTISEALSRSHKGDNANYRYSFDMLGEGALTMKDALRYLEDYRRAIHAIGgdhK 255
Cdd:PRK11905 157 ARLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIG---K 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 256 ARGGRpdgDVNNAPGISIKLSALYPRYEHAKRARVLKDLVPGVLELAQLAKSYGIGCTVDAEESDRLELSLDIIEQVFSD 335
Cdd:PRK11905 234 AATGR---GVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 336 ASLAGWDGFGVVVQAYQKRTPYTIDHLADMARRAGRRLQVRLVKGAYWDAEIKRAQIEGYPGYPVFTRKQNTDVSYLACA 415
Cdd:PRK11905 311 PDLAGWNGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 416 KRLFTHADAIYPMFATHNAHTIAAVRSIANGG-VYEHQKLHGMGDDLYAEVVPADRLNLPCRVYAPVGSHEDLLPYLVRR 494
Cdd:PRK11905 391 RKLLAARDVIYPQFATHNAQTLAAIYELAGGKgDFEFQCLHGMGEPLYDQVVGKEKLGRPCRIYAPVGTHETLLAYLVRR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 495 LLENGANSSFVNRITDERVPIADLIRDPVEMVASFESIPHPKIPLPVDLLrsqNHDRKNSMGANLANDNELRALAEQINA 574
Cdd:PRK11905 471 LLENGANSSFVNRIVDENVPVEELIADPVEKVAAMGVAPHPQIPLPRDLY---GPERRNSKGLDLSDEATLAALDEALNA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 575 -AVKPWQAAPLVPGANPAGAALPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEA 653
Cdd:PRK11905 548 fAAKTWHAAPLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEA 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 654 RMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEKLPsptgesnelqlhgRGVFVCISPWNFPLAIFL 733
Cdd:PRK11905 628 HMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKP-------------LGPVVCISPWNFPLAIFT 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 734 GQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRA 813
Cdd:PRK11905 695 GQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRT 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 814 MAARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNP 893
Cdd:PRK11905 775 LAKRSGPPVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDP 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 894 GLLSTDVGPVIDADALKILQDHAERMDREARLIAAAELSAEAANGTFFAPRAYELKDLGQLQKEVFGPVLHVIRWKGDQL 973
Cdd:PRK11905 855 WRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADEL 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 974 DAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKT 1053
Cdd:PRK11905 935 DRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAP 1014
|
...
gi 1590385370 1054 VTV 1056
Cdd:PRK11905 1015 TPI 1017
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
16-1072 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1400.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 16 PGALLSPELPAPPNPFRQAITDGWLKDEASHVRELLAQARLPAEEQAKVQALAADLVGRVRVRAKDQGAiEAFMRQYDLG 95
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGG-LLLLLELSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 96 SEEGVLLMCVAEALLRIPDQDTADKLIRDKLADADWEKHLGGSDSVLVNASTWGLMLTGKLVQMNDATraDAPSAFKRLV 175
Cdd:COG4230 80 SSEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSL--SLASGLLRLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 176 GRVGEPVVRLAVRQAMKIMGHQFVMGRTISEALSRSHKGDNANYRYSFDMLGEGALTMKDALRYLEDYRRAIHAIGGDHK 255
Cdd:COG4230 158 GRLGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 256 ARGGRPDGDVNnaPGISIKLSALYPRYEHAKRARVLKDLVPGVLELAQLAKSYGIGCTVDAEESDRLELSLDIIEQVFSD 335
Cdd:COG4230 238 GGSGGPGPSIS--SSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 336 ASLAGWDGFGVVVQAYQKRTPYTIDHLADMARRAGRRLQVRLVKGAYWDAEIKRAQIEGYPGYPVFTRKQNTDVSYLACA 415
Cdd:COG4230 316 GGLGGGGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 416 KRLFTHADAIYPMFATHNAHTIAAVRSIANGGVYEHQKLHGMGDDLYAEVVPaDRLNLPCRVYAPVGSHEDLLPYLVRRL 495
Cdd:COG4230 396 LLLLAAQPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQVGR-GKLGRPCRIYAPVGSHEDLLAYLVRRL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 496 LENGANSSFVNRITDERVPIADLIRDPVEMVASFESIPHPKIPLPVDLLRsqnHDRKNSMGANLANDNELRALAEQINAA 575
Cdd:COG4230 475 LENGANSSFVNRIADEDVPVEELIADPVEKARALGGAPHPRIPLPRDLYG---PERRNSAGLDLSDEAVLAALSAALAAA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 576 V-KPWQAAPLVPGANPAGAALPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEAR 654
Cdd:COG4230 552 AeKQWQAAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAH 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 655 MPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEklpsptgesnelQLHGRGVFVCISPWNFPLAIFLG 734
Cdd:COG4230 632 RAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPT------------VLRGRGVFVCISPWNFPLAIFTG 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 735 QVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAM 814
Cdd:COG4230 700 QVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTL 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 815 AARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPG 894
Cdd:COG4230 780 AARDGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPA 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 895 LLSTDVGPVIDADALKILQDHAERMDREARLIAAAELSAEAANGTFFAPRAYELKDLGQLQKEVFGPVLHVIRWKGDQLD 974
Cdd:COG4230 860 DLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADELD 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 975 AVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1054
Cdd:COG4230 940 KVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTV 1019
|
1050
....*....|....*...
gi 1590385370 1055 TVNTTAAGGNASLLTLGD 1072
Cdd:COG4230 1020 TVNTTAAGGNASLLALGD 1037
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
27-1047 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 1383.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 27 PPNPFRQAITDGWLKDEASHVRELLAQARLPAEEQAKVQALAADLVGRVRVRAK---DQGAIEAFMRQYDLGSEEGVLLM 103
Cdd:PRK11809 87 PQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSaggRAGMVQGLLQEFSLSSQEGVALM 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 104 CVAEALLRIPDQDTADKLIRDKLADADWEKHLGGSDSVLVNASTWGLMLTGKLVQMNdaTRADAPSAFKRLVGRVGEPVV 183
Cdd:PRK11809 167 CLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTH--NEASLSSSLNRIIGKSGEPLI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 184 RLAVRQAMKIMGHQFVMGRTISEALSRSHKGDNANYRYSFDMLGEGALTMKDALRYLEDYRRAIHAIGgdhKARGGRpdg 263
Cdd:PRK11809 245 RKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIG---KASNGR--- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 264 DVNNAPGISIKLSALYPRYEHAKRARVLKDLVPGVLELAQLAKSYGIGCTVDAEESDRLELSLDIIEQVFSDASLAGWDG 343
Cdd:PRK11809 319 GIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNG 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 344 FGVVVQAYQKRTPYTIDHLADMARRAGRRLQVRLVKGAYWDAEIKRAQIEGYPGYPVFTRKQNTDVSYLACAKRLFTHAD 423
Cdd:PRK11809 399 IGFVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 424 AIYPMFATHNAHTIAAVRSIANG----GVYEHQKLHGMGDDLYAEVV---PADRLNLPCRVYAPVGSHEDLLPYLVRRLL 496
Cdd:PRK11809 479 LIYPQFATHNAHTLAAIYHLAGQnyypGQYEFQCLHGMGEPLYEQVVgkvADGKLNRPCRIYAPVGTHETLLAYLVRRLL 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 497 ENGANSSFVNRITDERVPIADLIRDPVEMVASFES------IPHPKIPLPVDLLrsqNHDRKNSMGANLANDNELRALAE 570
Cdd:PRK11809 559 ENGANTSFVNRIADTSLPLDELVADPVEAVEKLAQqegqlgLPHPKIPLPRDLY---GKGRANSAGLDLANEHRLASLSS 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 571 Q-INAAVKPWQAAPLVPGANPAGAALPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAAD 649
Cdd:PRK11809 636 AlLASAHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAAD 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 650 QLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEKLPsptgesnelqlhgRGVFVCISPWNFPL 729
Cdd:PRK11809 716 LMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRP-------------LGPVVCISPWNFPL 782
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 730 AIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARA 809
Cdd:PRK11809 783 AIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARL 862
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 810 INRAMAARDAAIG---VLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMK 886
Cdd:PRK11809 863 LQRNLAGRLDPQGrpiPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMA 942
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 887 ELKVGNPGLLSTDVGPVIDADALKILQDHAERMDREARLI--AAAELSAEAANGTFFAPRAYELKDLGQLQKEVFGPVLH 964
Cdd:PRK11809 943 ECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVfqAARENSEDWQSGTFVPPTLIELDSFDELKREVFGPVLH 1022
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 965 VIRWKGDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHY 1044
Cdd:PRK11809 1023 VVRYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLY 1102
|
...
gi 1590385370 1045 LLR 1047
Cdd:PRK11809 1103 LYR 1105
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
500-1068 |
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: 804.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 500 ANSSFVNRITDERVPiadlirdpvemvasfesiphpkiplpvdllrsqnhdrknsmganlandneLRALAEQINAA-VKP 578
Cdd:cd07125 1 ANSSFVNRIFDLEVP--------------------------------------------------LEALADALKAFdEKE 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 579 WQAAPLVPG-ANPAGAALPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPE 657
Cdd:cd07125 31 WEAIPIINGeETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 658 FMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEkLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVA 737
Cdd:cd07125 111 LIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPE-LPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 738 AALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAAR 817
Cdd:cd07125 190 AALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAER 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 818 DAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLS 897
Cdd:cd07125 270 DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 898 TDVGPVIDADALKILQDHAERMDREARLIaaAELSAEAANGTFFAPRAYELKDLGQLQKEVFGPVLHVIRWKGDQLDAVI 977
Cdd:cd07125 350 TDVGPLIDKPAGKLLRAHTELMRGEAWLI--APAPLDDGNGYFVAPGIIEIVGIFDLTTEVFGPILHVIRFKAEDLDEAI 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 978 DQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVN 1057
Cdd:cd07125 428 EDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLN 507
|
570
....*....|.
gi 1590385370 1058 TTAAGGNASLL 1068
Cdd:cd07125 508 TTAAGGNPSLL 518
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
54-1065 |
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: 649.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 54 ARLPAEEQAKVQALAADLVGRVRvrAKDQGAIEAFMRQYDLGSEEGVLLMCVAEALLRIPDQDTADKLIRDKLAdadwek 133
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIR--AAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 134 hlgGSDSVLVNASTWGLMLTgklvqmndatradapsafkrLVGRVGEPVVRLAVRQAMKIMGHQFVMGRTISEALSRSHK 213
Cdd:COG0506 75 ---KSPSFLVNASTWGLMLT--------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 214 GDNANYRYSFDMLGEGALTMKDALRYLEDYRRAIHAIGGDHKARggrpdgdvnnaPGISIKLSALYPRYEHAKRARVLKD 293
Cdd:COG0506 132 LRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAGVDR-----------PGVSVKLSALGPRYSPAQRERVVEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 294 LVPGVLELAQLAKSYGIGCTVDAEESDRLELSLDIIEQVFSDASLAGWDGFGVVVQAYQKRTPYTIDHLADMARRAGRRL 373
Cdd:COG0506 201 LLERLRPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 374 QVRLVKGAYWDAEIKRAQIEGYPgYPVFTRKQNTDVSYLACAKRLFTHADAIYPMFATHNAHTIAAVRSIA-----NGGV 448
Cdd:COG0506 281 RVRLVKGAYWDPEIVRAQVHGWP-YPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAgergrPPDR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 449 YEHQKLHGMGDDLYAEVVPAD--RLNLPCRVYAPVGSHEDLLPYLVRRLLENGANSSFVNRITDERVPIADLIRDPVEMV 526
Cdd:COG0506 360 FEFQMLYGMGEDLQRALAAVDggRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLA 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 527 ASFESIPHPKIPLPVDLLRSQnhdRKNSMGANLANDNELRALAEQINAAVKPWQAAPLVPGANPAGAALPVTNPADTREV 606
Cdd:COG0506 440 ALAAPTPPPPPPLRRQRRRRR---RARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAV 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 607 VGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRY 686
Cdd:COG0506 517 VAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAA 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 687 YAKQAREQFSHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLH 766
Cdd:COG0506 597 AAAAAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLL 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 767 DAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVLIAETGGQNAFIADSSALPEQLV 846
Cdd:COG0506 677 LGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAV 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 847 KDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDHAERMDREARLI 926
Cdd:COG0506 757 AASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLL 836
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 927 AAAELSAEAANGTFFAPRAYELKDLGQLQKEVFGPVLHVIRWKGDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGV 1006
Cdd:COG0506 837 PGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGG 916
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590385370 1007 HVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNTTAAGGNA 1065
Cdd:COG0506 917 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAAA 975
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
551-1048 |
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: 649.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 551 RKNSMGANLANDNELRALAEQI-NAAVKPWQAAPLVPGANPA-GAALPVTNPADTREVVGQWLAADAATVQKALANAVAA 628
Cdd:TIGR01238 7 RKNSLGIDLDNESELKPLEAQIhAWADKTWQAAPIIGHSYKAdGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 629 QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFshaeklPSPTGES 708
Cdd:TIGR01238 87 FPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVL------GEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 709 nelqlhgRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAA 788
Cdd:TIGR01238 161 -------RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 789 LTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLF 868
Cdd:TIGR01238 234 LTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLC 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 869 VQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDHAERMDREARLIAAAELSAEAA--NGTFFAPRAY 946
Cdd:TIGR01238 314 VQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRAcqHGTFVAPTLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 947 ELKDLGQLQKEVFGPVLHVIRWKGDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQP 1026
Cdd:TIGR01238 394 ELDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQP 473
|
490 500
....*....|....*....|..
gi 1590385370 1027 FGGQGLSGTGPKAGGPHYLLRF 1048
Cdd:TIGR01238 474 FGGQGLSGTGPKAGGPHYLYRL 495
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
579-1057 |
8.14e-176 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 523.68 E-value: 8.14e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 579 WQAAPLVPGAN--PAGAALPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMP 656
Cdd:cd07083 16 GRAYPLVIGGEwvDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 657 EFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQV 736
Cdd:cd07083 96 ELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 737 AAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMA- 815
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAr 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 816 --ARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNP 893
Cdd:cd07083 256 laPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 894 GLLSTDVGPVIDADALKILQDHAERMDREARLIaaAELSAEAANGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIRWKGD 971
Cdd:cd07083 336 EENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLV--LGGKRLEGEGYFVAPTVVEEVPPKAriAQEEIFGPVLSVIRYKDD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 972 QLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATE 1051
Cdd:cd07083 414 DFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRRFLEM 493
|
....*.
gi 1590385370 1052 KTVTVN 1057
Cdd:cd07083 494 KAVAER 499
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
595-1058 |
2.49e-143 |
|
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: 439.74 E-value: 2.49e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07124 48 IESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAREqfSHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQT 754
Cdd:cd07124 128 ADVAEAIDFLEYYAREMLR--LRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 755 NLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAmAARDA----AIGVLIAETGG 830
Cdd:cd07124 206 PVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYER-AAKVQpgqkWLKRVIAEMGG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 831 QNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALK 910
Cdd:cd07124 285 KNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARD 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 911 ILQDHAERMDREARLIAAAELSAEAANGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIrwKGDQLDAVIDQINATGYGLT 988
Cdd:cd07124 365 RIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHrlAQEEIFGPVLAVI--KAKDFDEALEIANDTEYGLT 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 989 LGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNT 1058
Cdd:cd07124 443 GGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTENF 512
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
207-507 |
1.07e-137 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 416.51 E-value: 1.07e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 207 ALSRSHKGDNANYRYSFDMLGEGALTMKDALRYLEDYRRAIHAIGGDHKArggrpdGDVNNAPGISIKLSALYPRYEHAK 286
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGP------WPLGPRPGISVKLSALHPRYEPLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 287 RARVLKDLVPGVLELAQLAKSYGIGCTVDAEESDRLELSLDIIEQVFSDASLAGWDGFGVVVQAYQKRTPYTIDHLADMA 366
Cdd:pfam01619 75 RERVMAELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 367 RRAGRRLQVRLVKGAYWDAEIKRAQIEGYPgYPVFTRKQNTDVSYLACAKRLFTHADAIYPMFATHNAHTIAAVRSIAN- 445
Cdd:pfam01619 155 RRRGRPLGVRLVKGAYWDSEIKRAQQGGWP-YPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEe 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590385370 446 ----GGVYEHQKLHGMGDDLYAEVVPADRlnlPCRVYAPVGSHEDLLPYLVRRLLENGANSSFVNR 507
Cdd:pfam01619 234 lgipPRRFEFQQLYGMGDNLSFALVAAGY---RVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
590-1058 |
1.28e-137 |
|
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: 423.38 E-value: 1.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:COG1012 18 ASGETFDVINPA-TGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIAEVREAVDFLRYYAKQAREQfsHAEKLPSP-TGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIA 748
Cdd:COG1012 97 LAEARGEVDRAADFLRYYAGEARRL--YGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 749 KPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARdaaIGVLIAET 828
Cdd:COG1012 175 KPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEN---LKRVTLEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADA 908
Cdd:COG1012 252 GGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 909 LKILQDHAER-MDREARLIaAAELSAEAANGTFFAP----------RAYelkdlgqlQKEVFGPVLHVIRWKGdqLDAVI 977
Cdd:COG1012 332 LERVLAYIEDaVAEGAELL-TGGRRPDGEGGYFVEPtvladvtpdmRIA--------REEIFGPVLSVIPFDD--EEEAI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 978 DQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGvQPFGGQGLSGTGPKaGGPHYLLRFATEKTVTVN 1057
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGRE-GGREGLEEYTETKTVTIR 478
|
.
gi 1590385370 1058 T 1058
Cdd:COG1012 479 L 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
590-1054 |
9.70e-128 |
|
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: 396.90 E-value: 9.70e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:pfam00171 4 SESETIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIAEVREAVDFLRYYAKQAREQfsHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAK 749
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARRL--DGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 750 PAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInraMAARDAAIGVLIAETG 829
Cdd:pfam00171 161 PSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHI---AEAAAQNLKRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 830 GQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADAL 909
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 910 KILQDHAER-MDREARLIaaAELSAEAANGTFFAPraYELKDLGQ----LQKEVFGPVLHVIRWKGdqLDAVIDQINATG 984
Cdd:pfam00171 318 ERVLKYVEDaKEEGAKLL--TGGEAGLDNGYFVEP--TVLANVTPdmriAQEEIFGPVLSVIRFKD--EEEAIEIANDTE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 985 YGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVqPFGGQGLSGTGpKAGGPHYLLRFATEKTV 1054
Cdd:pfam00171 392 YGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
619-1056 |
4.35e-123 |
|
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: 383.48 E-value: 4.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 619 QKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQfsHA 698
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRL--HG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 699 EKLPSPT-GESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQF 777
Cdd:cd07078 79 EVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 778 LPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARdaaIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSA 857
Cdd:cd07078 159 VTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAEN---LKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 858 GQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDHAERMDREARLIAAAELSAEAAN 937
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 938 GTFFAPRAYELKDLGQL--QKEVFGPVLHVIRWKgdQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNR 1015
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1590385370 1016 NQIGAVVGvQPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07078 394 YSVGAEPS-APFGGVKQSGIG-REGGPYGLEEYTEPKTVTI 432
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
595-1055 |
2.16e-113 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 361.17 E-value: 2.16e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:PRK03137 52 IVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAREqFSHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQT 754
Cdd:PRK03137 132 ADTAEAIDFLEYYARQMLK-LADGKPVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 755 NLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAmAARDAA----IGVLIAETGG 830
Cdd:PRK03137 211 PVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYER-AAKVQPgqiwLKRVIAEMGG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 831 QNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGlLSTDVGPVIDADALK 910
Cdd:PRK03137 290 KDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPE-DNAYMGPVINQASFD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 911 ILQDHAERMDREARLIAAAELSAEAanGTFFAPRAY-ELKDLGQL-QKEVFGPVLHVIrwKGDQLDAVIDQINATGYGLT 988
Cdd:PRK03137 369 KIMSYIEIGKEEGRLVLGGEGDDSK--GYFIQPTIFaDVDPKARImQEEIFGPVVAFI--KAKDFDHALEIANNTEYGLT 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 989 LGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVT 1055
Cdd:PRK03137 445 GAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVS 511
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
562-1057 |
2.71e-111 |
|
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: 355.33 E-value: 2.71e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 562 DNELRALAEQINAAVKPW--QAAPLVPGAN--PAGAALPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPA 637
Cdd:TIGR01237 11 DEENRQAFFKALATVKEQlgKTYPLVINGErvETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 638 ASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEKLPSPtGESNELQLHGRG 717
Cdd:TIGR01237 91 EERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSRE-GETNQYVYTPTG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 718 VFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAG 797
Cdd:TIGR01237 170 VTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 798 VAFTGSTDTARAINrAMAAR----DAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDI 873
Cdd:TIGR01237 250 ITFTGSREVGTRIF-ERAAKvqpgQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 874 ADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDHAERMDREARLIaaAELSAEAANGTFFAPRAYelKDLGQ 953
Cdd:TIGR01237 329 YDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLV--SGGCGDDSKGYFIGPTIF--ADVDR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 954 ----LQKEVFGPVLHVIRWKgdQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGG 1029
Cdd:TIGR01237 405 karlAQEEIFGPVVAFIRAS--DFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGG 482
|
490 500
....*....|....*....|....*...
gi 1590385370 1030 QGLSGTGPKAGGPHYLLRFATEKTVTVN 1057
Cdd:TIGR01237 483 FKMSGTDSKAGGPDYLALFMQAKTVTEM 510
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
625-1056 |
7.29e-100 |
|
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: 319.56 E-value: 7.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 625 AVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEKLPSP 704
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 705 TGESnELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGAT 784
Cdd:cd06534 83 GGEA-YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 785 VGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAigvLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAA 864
Cdd:cd06534 162 VGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKP---VTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 865 RVLFVQDDIADKVMTMLAGamkelkvgnpglLSTDVGPvidadALKIlqdhaermdrearliaaaelsaeaangtffapr 944
Cdd:cd06534 239 SRLLVHESIYDEFVEKLVT------------VLVDVDP-----DMPI--------------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 945 ayelkdlgqLQKEVFGPVLHVIRWkgDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGv 1024
Cdd:cd06534 269 ---------AQEEIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE- 336
|
410 420 430
....*....|....*....|....*....|..
gi 1590385370 1025 QPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd06534 337 APFGGVKNSGIG-REGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
590-1054 |
5.95e-96 |
|
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: 313.03 E-value: 5.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAALPVTNPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:cd07097 11 AGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIAEVREAVDFLRYYAKQAREQfsHAEKLPSpTGESNELQLHGR--GVFVCISPWNFPLAIFLGQVAAALAAGNSVI 747
Cdd:cd07097 91 LPEARGEVTRAGQIFRYYAGEALRL--SGETLPS-TRPGVEVETTREplGVVGLITPWNFPIAIPAWKIAPALAYGNTVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 748 AKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGvliAE 827
Cdd:cd07097 168 FKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQ---LE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 828 TGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDAD 907
Cdd:cd07097 245 MGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSER 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 908 ALKILQDHAERMDRE-ARLIAAAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGdqLDAVIDQINATG 984
Cdd:cd07097 325 QLEKDLRYIEIARSEgAKLVYGGERLKRPDEGYYLAPALFAgvTNDMRIAREEIFGPVAAVIRVRD--YDEALAIANDTE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590385370 985 YGLTLGVHSR----IDETVDRISNGVhvgnVYVNRNQIGAVVGVqPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1054
Cdd:cd07097 403 FGLSAGIVTTslkhATHFKRRVEAGV----VMVNLPTAGVDYHV-PFGGRKGSSYGPREQGEAALEFYTTIKTV 471
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
597-1056 |
5.50e-91 |
|
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: 298.96 E-value: 5.50e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAE 676
Cdd:cd07103 1 VINPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 677 VREAVDFLRYYAKQAREqfSHAEKLPSPTGesNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQ 753
Cdd:cd07103 80 VDYAASFLEWFAEEARR--IYGRTIPSPAP--GKRILVIKqpvGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 754 TNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInramaARDAAIGV--LIAETGGQ 831
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLL-----MAQAADTVkrVSLELGGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 832 NAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKI 911
Cdd:cd07103 231 APFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 912 LQDHAER-MDREARLIaaAELSAEAANGTFFAPRAyeLKDLGQ----LQKEVFGPVLHVIRWkgDQLDAVIDQINATGYG 986
Cdd:cd07103 311 VEALVEDaVAKGAKVL--TGGKRLGLGGYFYEPTV--LTDVTDdmliMNEETFGPVAPIIPF--DTEDEVIARANDTPYG 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 987 LTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVvgVQPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07103 385 LAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG-REGGKEGLEEYLETKYVSL 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
591-1054 |
2.47e-88 |
|
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: 292.25 E-value: 2.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSL 670
Cdd:cd07088 11 SGETIDVLNPA-TGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 671 PDSIAEVREAVDFLRYYAKQAREqfSHAEKLPS-PTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAK 749
Cdd:cd07088 90 SLARVEVEFTADYIDYMAEWARR--IEGEIIPSdRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 750 PAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInraMAARDAAIGVLIAETG 829
Cdd:cd07088 168 PSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKI---MEAAAENITKVSLELG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 830 GQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADAL 909
Cdd:cd07088 245 GKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 910 KILQDHAERMDREARLIAAAELSAEAANGTFFAPRAyeLKDLGQ----LQKEVFGPVLHVIRWkgDQLDAVIDQINATGY 985
Cdd:cd07088 325 DKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTV--LTNVRQdmeiVQEEIFGPVLPVVKF--SSLDEAIELANDSEY 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQpfGGQGLSGTGpKAGGPHYLLRFATEKTV 1054
Cdd:cd07088 401 GLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFH--AGWKKSGLG-GADGKHGLEEYLQTKVV 466
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
599-1057 |
4.65e-86 |
|
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: 286.55 E-value: 4.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 599 NPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVR 678
Cdd:cd07131 20 NPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 679 EAVDFLRYYAKQAREQFSHAekLPSptgESNELQLHGR----GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQT 754
Cdd:cd07131 100 EAIDMAQYAAGEGRRLFGET--VPS---ELPNKDAMTRrqpiGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 755 NLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGvliAETGGQNAF 834
Cdd:cd07131 175 PACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRVA---LEMGGKNPI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 835 IADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADAL-KILQ 913
Cdd:cd07131 252 IVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLeKVLN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 914 --DHAERMDREARLIAAAELSAEAANGTFFAPRAYEL--KDLGQLQKEVFGPVLHVIRWKGdqLDAVIDQINATGYGLTL 989
Cdd:cd07131 332 ynEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDvtPDMRIAQEEIFGPVVALIEVSS--LEEAIEIANDTEYGLSS 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590385370 990 GVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVqPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVN 1057
Cdd:cd07131 410 AIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGTTALDAFTEWKAVYVD 476
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
599-1054 |
3.82e-83 |
|
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: 279.86 E-value: 3.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 599 NPADTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARM-PEFMALCVKEAGKSL----PDS 673
Cdd:cd07123 52 MPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLGQGKNVwqaeIDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 674 IAEVreaVDFLRYYAKQArEQFSHAEKLPSPTGESNELQLHGRGVFV-CISPWNFPlAIFLGQVAAALAAGNSVIAKPAE 752
Cdd:cd07123 132 ACEL---IDFLRFNVKYA-EELYAQQPLSSPAGVWNRLEYRPLEGFVyAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 753 QTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARdaaIGV------LIA 826
Cdd:cd07123 207 TAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGEN---LDRyrtyprIVG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 827 ETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDA 906
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 907 DALKILQ---DHAeRMDREARLIAAAELSAEAanGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIRWKGDQLDAVIDQIN 981
Cdd:cd07123 364 KAFDRIKgyiDHA-KSDPEAEIIAGGKCDDSV--GYFVEPTVIETTDPKHklMTEEIFGPVLTVYVYPDSDFEETLELVD 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590385370 982 ATG-YGLTLGVHSR----IDETVDRISNGvhVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1054
Cdd:cd07123 441 TTSpYALTGAIFAQdrkaIREATDALRNA--AGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTI 516
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
590-1057 |
2.74e-80 |
|
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: 270.59 E-value: 2.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAALPVTNPADTREVVGQWLAAdAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:cd07086 10 SGGETFTSRNPANGEPIARVFPAS-PEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIAEVREAVDFLRYYAKQAReQFsHAEKLPS--PtGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVI 747
Cdd:cd07086 89 LPEGLGEVQEMIDICDYAVGLSR-ML-YGLTIPSerP-GHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 748 AKPAEQTNLIGYYAVKLLHDA----GVPAEVVQFLPGdGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARdaaIGV 823
Cdd:cd07086 166 WKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARR---FGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 824 LIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPV 903
Cdd:cd07086 242 VLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 904 IDADALKILQDHAER-MDREARLIAAAELSAEAANGTFFAPRAYELK--DLGQLQKEVFGPVLHVIRWKGdqLDAVIDQI 980
Cdd:cd07086 322 INQAAVEKYLNAIEIaKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVtdDARIVQEETFAPILYVIKFDS--LEEAIAIN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 981 NATGYGLTLGVHSRIDETVDRI--SNGVHVGNVYVNRNQIGAVVGVqPFGGQGLSGTGPKAGGPhyLLRFATE-KTVTVN 1057
Cdd:cd07086 400 NDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESGSD--AWKQYMRrSTCTIN 476
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
595-1056 |
7.63e-80 |
|
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: 268.31 E-value: 7.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPADtREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07149 1 IEVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAREqfSHAEKLP---SPTGEsNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVIA 748
Cdd:cd07149 80 KEVDRAIETLRLSAEEAKR--LAGETIPfdaSPGGE-GRIGFTIRepiGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 749 KPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInramaARDAAIGVLIAET 828
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI-----ARKAGLKKVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVID-AD 907
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISeAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 908 ALKILQDHAERMDREARLIaaaelSAEAANGTFFAPRAYEL--KDLGQLQKEVFGPVLHVIRWkgDQLDAVIDQINATGY 985
Cdd:cd07149 312 AERIEEWVEEAVEGGARLL-----TGGKRDGAILEPTVLTDvpPDMKVVCEEVFAPVVSLNPF--DTLDEAIAMANDSPY 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVN-----RnqigavVGVQPFGGQGLSGTGPKagGPHYLLRFATE-KTVTV 1056
Cdd:cd07149 385 GLQAGVFTNDLQKALKAARELEVGGVMINdsstfR------VDHMPYGGVKESGTGRE--GPRYAIEEMTEiKLVCF 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
597-1056 |
2.37e-79 |
|
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: 267.12 E-value: 2.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIA- 675
Cdd:cd07093 1 NFNPA-TGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 676 EVREAVDFLRYYAKQAREQfsHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTN 755
Cdd:cd07093 80 DIPRAAANFRFFADYILQL--DGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 756 LIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARdaaIGVLIAETGGQNAFI 835
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPN---LKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 836 ADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDH 915
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 916 AERMDRE-ARLIA--AAELSAEAANGTFFAPRAYE-LKDLGQL-QKEVFGPVLHVIRWKGDqlDAVIDQINATGYGLTLG 990
Cdd:cd07093 315 VELARAEgATILTggGRPELPDLEGGYFVEPTVITgLDNDSRVaQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAAY 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590385370 991 VHSRIDETVDRISNGVHVGNVYVN-------RnqigavvgvQPFGGQGLSGTGPKagGPHYLLRFATE-KTVTV 1056
Cdd:cd07093 393 VWTRDLGRAHRVARRLEAGTVWVNcwlvrdlR---------TPFGGVKASGIGRE--GGDYSLEFYTElKNVCI 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
597-1040 |
1.26e-74 |
|
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: 254.01 E-value: 1.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAA--QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07114 1 SINPA-TGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAkqareqfSHAEKLPS---PTGESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVIA 748
Cdd:cd07114 80 AQVRYLAEWYRYYA-------GLADKIEGaviPVDKGDYLNFTRReplGVVAAITPWNSPLLLLAKKLAPALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 749 KPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIgvlIAET 828
Cdd:cd07114 153 KPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPV---TLEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADA 908
Cdd:cd07114 230 GGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 909 LKILQDHAERMDRE-ARLIA--AAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDqlDAVIDQINAT 983
Cdd:cd07114 310 LEKVERYVARAREEgARVLTggERPSGADLGAGYFFEPTILAdvTNDMRIAQEEVFGPVLSVIPFDDE--EEAIALANDS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 984 GYGLTLGVHSRIDETVDRISNGVHVGNVYVN---RNQIGAvvgvqPFGGQGLSGTGPKAG 1040
Cdd:cd07114 388 EYGLAAGIWTRDLARAHRVARAIEAGTVWVNtyrALSPSS-----PFGGFKDSGIGRENG 442
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
595-1056 |
1.40e-73 |
|
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: 251.11 E-value: 1.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07145 1 IEVRNPA-NGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAREQfsHAEKLPSPTGESNELQL-----HGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAK 749
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVL--RGETIPVDAYEYNERRIaftvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 750 PAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInramAARDAAIGVLIA-ET 828
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLI----ASKAGGTGKKVAlEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADA 908
Cdd:cd07145 234 GGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 909 LKILQDH-AERMDREARLIAAAELSAeaanGTFFAPRAYEL--KDLGQLQKEVFGPVLHVIRWKGDqlDAVIDQINATGY 985
Cdd:cd07145 314 VERMENLvNDAVEKGGKILYGGKRDE----GSFFPPTVLENdtPDMIVMKEEVFGPVLPIAKVKDD--EEAVEIANSTEY 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVN---RNQIGAVvgvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07145 388 GLQASVFTNDINRALKVARELEAGGVVINdstRFRWDNL----PFGGFKKSGIG-REGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
595-1056 |
1.82e-73 |
|
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: 250.81 E-value: 1.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPADtREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07094 1 LDVHNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAREQFSHAEKLPSPTGESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPA 751
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIRepvGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 752 EQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAmaardAAIGVLIAETGGQ 831
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRAN-----AGGKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 832 NAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKI 911
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 912 LQDHAER-MDREARLIaaaelSAEAANGTFFAPRAYEL--KDLGQLQKEVFGPVLHVIRWkgDQLDAVIDQINATGYGLT 988
Cdd:cd07094 315 VERWVEEaVEAGARLL-----CGGERDGALFKPTVLEDvpRDTKLSTEETFGPVVPIIRY--DDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590385370 989 LGVHSR-IDETVDrISNGVHVGNVYVNRNQIgAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07094 388 AGIFTRdLNVAFK-AAEKLEVGGVMVNDSSA-FRTDWMPFGGVKESGVG-REGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
595-1056 |
4.50e-73 |
|
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: 250.57 E-value: 4.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPADtREVVGQWLAADAATVQKALANAVAAQPAWNRT-PAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDS 673
Cdd:cd07082 18 IEVYSPID-GEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 674 IAEVREAVDFLRYYAKQAREQFSHAEKLPSPTGESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKP 750
Cdd:cd07082 97 LKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRReplGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 751 AEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInramaARDAAIGVLIAETGG 830
Cdd:cd07082 177 ATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL-----KKQHPMKRLVLELGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 831 QNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVID---AD 907
Cdd:cd07082 252 KDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDpksAD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 908 ALKILQDHAErmDREARLIAAAELSAeaanGTFFAP----------RAYelkdlgqlQKEVFGPVLHVIRWKgdQLDAVI 977
Cdd:cd07082 332 FVEGLIDDAV--AKGATVLNGGGREG----GNLIYPtlldpvtpdmRLA--------WEEPFGPVLPIIRVN--DIEEAI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 978 DQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRN-QIGavVGVQPFGGQGLSGTGPKagGPHYLLRFATEKTVTV 1056
Cdd:cd07082 396 ELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcQRG--PDHFPFLGRKDSGIGTQ--GIGDALRSMTRRKGIV 471
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
618-1056 |
8.14e-73 |
|
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: 248.21 E-value: 8.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 618 VQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREqfSH 697
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRR--PE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 698 AEKLPSPT-GESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAV-KLLHDAGVPAEVV 775
Cdd:cd07104 80 GEILPSDVpGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 776 QFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAmAARDAAIGVLiaETGGQNAFIADSSALPEQLVKDAIGSAFT 855
Cdd:cd07104 160 NVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGEL-AGRHLKKVAL--ELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 856 SAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDHAER-MDREARLIaaaelSAE 934
Cdd:cd07104 237 HQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDaVAAGARLL-----TGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 935 AANGTFFAPraYELKDLGQ----LQKEVFGPVLHVIRWKGDqlDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGN 1010
Cdd:cd07104 312 TYEGLFYQP--TVLSDVTPdmpiFREEIFGPVAPVIPFDDD--EEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1590385370 1011 VYVNRNQI--GAVVgvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07104 388 VHINDQTVndEPHV---PFGGVKASGGG-RFGGPASLEEFTEWQWITV 431
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
597-1056 |
2.75e-72 |
|
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: 247.44 E-value: 2.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAE 676
Cdd:cd07106 1 VINPA-TGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 677 VREAVDFLRYYAKQAREQfshaEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNL 756
Cdd:cd07106 80 VGGAVAWLRYTASLDLPD----EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 757 IGYYAVKLLHDAgVPAEVVQFLPGDGAtVGAALTADPRVAGVAFTGSTDTARAInraMAARDAAIGVLIAETGGQNAFI- 835
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKV---MASAAKTLKRVTLELGGNDAAIv 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 836 ---ADSSALPEQLVkdaiGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDA---DAL 909
Cdd:cd07106 231 lpdVDIDAVAPKLF----WGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKmqyDKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 910 KILQDHAermdREARLIAAAELSAEAANGTFFAPR-AYELKDLGQL-QKEVFGPVLHVIRWkgDQLDAVIDQINATGYGL 987
Cdd:cd07106 307 KELVEDA----KAKGAKVLAGGEPLDGPGYFIPPTiVDDPPEGSRIvDEEQFGPVLPVLKY--SDEDEVIARANDSEYGL 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590385370 988 TLGVHSRIDETVDRISNGVHVGNVYVnrNQIGAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07106 381 GASVWSSDLERAEAVARRLEAGTVWI--NTHGALDPDAPFGGHKQSGIG-VEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
598-1056 |
3.00e-72 |
|
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: 247.52 E-value: 3.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 598 TNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEV 677
Cdd:cd07099 1 RNPA-TGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 678 REAVDFLRYYAKQArEQFSHAEKLPSPTGESN---ELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQT 754
Cdd:cd07099 80 LLALEAIDWAARNA-PRVLAPRKVPTGLLMPNkkaTVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 755 NLIGYYAVKLLHDAGVPAEVVQFLPGDGATvGAALtADPRVAGVAFTGSTDTARAINRAMAARdaaigvLI---AETGGQ 831
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAAL-IDAGVDKVAFTGSVATGRKVMAAAAER------LIpvvLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 832 NAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKI 911
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 912 LQDH-AERMDREARLIAAAELSAEAanGTFFAPRAyeLKDLGQ----LQKEVFGPVLHVIRWkgDQLDAVIDQINATGYG 986
Cdd:cd07099 311 VRRHvDDAVAKGAKALTGGARSNGG--GPFYEPTV--LTDVPHdmdvMREETFGPVLPVMPV--ADEDEAIALANDSRYG 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 987 LTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07099 385 LSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
585-1056 |
3.10e-71 |
|
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: 245.20 E-value: 3.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 585 VPGANpaGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPA--WNRTPAASRAAILEHAADQLEARMPEFMALC 662
Cdd:cd07091 13 VDSVS--GKTFPTINPA-TEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 663 VKEAGKSLPDSI-AEVREAVDFLRYYAKQA-----------REQFSHAEKLPsptgesnelqlhgrgVFVC--ISPWNFP 728
Cdd:cd07091 90 SLDNGKPLEESAkGDVALSIKCLRYYAGWAdkiqgktipidGNFLAYTRREP---------------IGVCgqIIPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 729 LAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTAR 808
Cdd:cd07091 155 LLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 809 AINRAMAARDAAIGVLiaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKEL 888
Cdd:cd07091 235 TIMEAAAKSNLKKVTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 889 KVGNPGLLSTDVGPVIDADALKILQDHAERMDRE-ARLIaaAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHV 965
Cdd:cd07091 313 VVGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEgATLL--TGGERHGSKGYFIQPTVFTdvKDDMKIAKEEIFGPVVTI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 966 IRWKgdQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNR-NQIGAVVgvqPFGGQGLSGTGPKAGgpHY 1044
Cdd:cd07091 391 LKFK--TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG--EE 463
|
490
....*....|...
gi 1590385370 1045 LLRFATE-KTVTV 1056
Cdd:cd07091 464 GLEEYTQvKAVTI 476
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
597-1057 |
6.33e-71 |
|
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: 243.82 E-value: 6.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAE 676
Cdd:cd07107 1 VINPA-TGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 677 VREAVDFLRYYAKQAREQfsHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNL 756
Cdd:cd07107 80 VMVAAALLDYFAGLVTEL--KGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 757 IGYYAVKLLHDAgVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARdaaIGVLIAETGGQNAFIA 836
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG---IKHVTLELGGKNALIV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 837 DSSALPEQLVKDAI-GSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDH 915
Cdd:cd07107 234 FPDADPEAAADAAVaGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 916 AERMDRE-ARLIA--AAELSAEAANGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIRWKGDqlDAVIDQINATGYGLTLG 990
Cdd:cd07107 314 IDSAKREgARLVTggGRPEGPALEGGFYVEPTVFADVTPGMriAREEIFGPVLSVLRWRDE--AEMVAQANGVEYGLTAA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 991 VHSRIDETVDRISNGVHVGNVYVN---RNQIGAvvgvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTVN 1057
Cdd:cd07107 392 IWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIG-REECLEELLSYTQEKNVNVR 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
597-1056 |
1.30e-70 |
|
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: 242.91 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPADTrEVVGQWLAADAATVQKALANAVAAQPA-WNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIA 675
Cdd:cd07109 1 VFDPSTG-EVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 676 EVREAVDFLRYYAKQArEQFsHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTN 755
Cdd:cd07109 80 DVEAAARYFEYYGGAA-DKL-HGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 756 LIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAarDAAIGVLIaETGGQNAFI 835
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA--ENVVPVTL-ELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 836 ADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGnPGLLSTDVGPVIDADALKILQDH 915
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 916 AER-MDREARLIAA-AELSAEAANGTFFAPRAYELKDLGQL--QKEVFGPVLHVIRWkgDQLDAVIDQINATGYGLTLGV 991
Cdd:cd07109 314 VARaRARGARIVAGgRIAEGAPAGGYFVAPTLLDDVPPDSRlaQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590385370 992 HSRIDETVDRISNGVHVGNVYVnrNQIGAVVGVQ-PFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFV--NNYGAGGGIElPFGGVKKSGHG-REKGLEALYNYTQTKTVAV 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
605-1056 |
7.43e-70 |
|
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: 240.27 E-value: 7.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 605 EVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFL 684
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 685 RYYAKQAREqfSHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAV-K 763
Cdd:cd07152 82 HEAAGLPTQ--PQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 764 LLHDAGVPAEVVQFLPGdGATVGAALTADPRVAGVAFTGSTDTARAINRAmAARDAAIGVLiaETGGQNAFIADSSALPE 843
Cdd:cd07152 160 LFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEA-AGRHLKKVSL--ELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 844 QLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALkilqDHAERMDREA 923
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQL----DRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 924 RLIAAAELSAEAANGTFFAP----------RAYElkdlgqlqKEVFGPVLHVIRWKGDqlDAVIDQINATGYGLTLGVHS 993
Cdd:cd07152 312 VAAGARLEAGGTYDGLFYRPtvlsgvkpgmPAFD--------EEIFGPVAPVTVFDSD--EEAVALANDTEYGLSAGIIS 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590385370 994 RIDETVDRISNGVHVGNVYVNrNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07152 382 RDVGRAMALADRLRTGMLHIN-DQTVNDEPHNPFGGMGASGNGSRFGGPANWEEFTQWQWVTV 443
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
599-1057 |
1.61e-68 |
|
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: 236.95 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 599 NPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDS-IAEV 677
Cdd:cd07115 3 NPA-TGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 678 REAVDFLRYYAKQAREQfsHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLI 757
Cdd:cd07115 82 PRAADTFRYYAGWADKI--EGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 758 GYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVliaETGGQNAFIAD 837
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSL---ELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 838 SSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDHAE 917
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 918 RMDRE-ARLIaaAELSAEAANGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIRWKGDQLDAVIdqINATGYGLTLGVHSR 994
Cdd:cd07115 317 VGREEgARLL--TGGKRPGARGFFVEPTIFAAVPPEMriAQEEIFGPVVSVMRFRDEEEALRI--ANGTEYGLAAGVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590385370 995 IDETVDRISNGVHVGNVYVnrNQIGAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTVTVN 1057
Cdd:cd07115 393 DLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFG-REMGREALDEYTEVKSVWVN 452
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
597-1036 |
2.50e-68 |
|
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: 236.48 E-value: 2.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAE 676
Cdd:cd07110 1 VINPA-TEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 677 VREAVDFLRYYAKQAREQFSHAEK---LPSPtGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQ 753
Cdd:cd07110 80 VDDVAGCFEYYADLAEQLDAKAERavpLPSE-DFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 754 TNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAmAARDaaIGVLIAETGGQNA 833
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQA-AAQD--IKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 834 FIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQ 913
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 914 DHAERMDRE-ARLIAAAELSAEAANGTFFAPRAY-ELKDLGQL-QKEVFGPVLHVIRWKGDqlDAVIDQINATGYGLTLG 990
Cdd:cd07110 316 SFIARGKEEgARLLCGGRRPAHLEKGYFIAPTVFaDVPTDSRIwREEIFGPVLCVRSFATE--DEAIALANDSEYGLAAA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1590385370 991 VHSRIDETVDRISNGVHVGNVYVNRNQIgaVVGVQPFGGQGLSGTG 1036
Cdd:cd07110 394 VISRDAERCDRVAEALEAGIVWINCSQP--CFPQAPWGGYKRSGIG 437
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
597-1056 |
2.73e-68 |
|
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: 236.49 E-value: 2.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSL-PDSIA 675
Cdd:cd07108 1 VINPA-TGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 676 EVREAVDFLRYYAKQAREQfsHAEKLPsptGESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAE 752
Cdd:cd07108 80 EAAVLADLFRYFGGLAGEL--KGETLP---FGPDVLTYTVReplGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 753 QTNLIGYYAVKLLHDAgVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVliaETGGQN 832
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSL---ELGGKS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 833 AFIADSSALPEQLVKDAI-GSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKI 911
Cdd:cd07108 231 PMIVFPDADLDDAVDGAIaGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 912 LQDHAE--RMDREARLIA--AAELSAEAANGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIRWKGDqlDAVIDQINATGY 985
Cdd:cd07108 311 VCGYIDlgLSTSGATVLRggPLPGEGPLADGFFVQPTIFSGVDNEWrlAREEIFGPVLCAIPWKDE--DEVIAMANDSHY 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVNRNqIGAVVGvQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07108 389 GLAAYVWTRDLGRALRAAHALEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREASLEGMLEHFTQKKTVNI 457
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
590-1036 |
1.45e-67 |
|
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: 234.70 E-value: 1.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAA-LPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGk 668
Cdd:cd07138 10 PAGTEtIDVINPA-TEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 669 sLPDSIAE---VREAVDFLRYYAKQAREqFSHAEKLpsptgESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNS 745
Cdd:cd07138 88 -APITLARaaqVGLGIGHLRAAADALKD-FEFEERR-----GNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 746 VIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAmAARDaaIGVLI 825
Cdd:cd07138 161 VVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA-AADT--VKRVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 826 AETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVID 905
Cdd:cd07138 238 LELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLAS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 906 ADALKILQDHAER-MDREARLIAAAELSAEAAN-GTFFAPR--AYELKDLGQLQKEVFGPVLHVIRWKGDQlDAVidQI- 980
Cdd:cd07138 318 AAQFDRVQGYIQKgIEEGARLVAGGPGRPEGLErGYFVKPTvfADVTPDMTIAREEIFGPVLSIIPYDDED-EAI--AIa 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 981 NATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNrnqiGAVVGVQ-PFGGQGLSGTG 1036
Cdd:cd07138 395 NDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
591-1057 |
2.47e-67 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 234.97 E-value: 2.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSL 670
Cdd:PLN02278 38 DGKTFPVYNPA-TGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 671 PDSIAEVREAVDFLRYYAKQAREQFShaEKLPSPTGESNELQLHGR-GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAK 749
Cdd:PLN02278 117 KEAIGEVAYGASFLEYFAEEAKRVYG--DIIPSPFPDRRLLVLKQPvGVVGAITPWNFPLAMITRKVGPALAAGCTVVVK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 750 PAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARainraMAARDAAIGV--LIAE 827
Cdd:PLN02278 195 PSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGK-----KLMAGAAATVkrVSLE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 828 TGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDAD 907
Cdd:PLN02278 270 LGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 908 ALKILQDH-AERMDREARLIAAAELSAEAanGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDQlDAvIDQINATG 984
Cdd:PLN02278 350 AVQKVESHvQDAVSKGAKVLLGGKRHSLG--GTFYEPTVLGdvTEDMLIFREEVFGPVAPLTRFKTEE-EA-IAIANDTE 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590385370 985 YGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTVN 1057
Cdd:PLN02278 426 AGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG-REGSKYGIDEYLEIKYVCLG 495
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
595-1056 |
4.27e-67 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 232.99 E-value: 4.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPADTrEVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07150 1 FDDLNPADG-SVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAREqfSHAEKLPS-PTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQ 753
Cdd:cd07150 80 FETTFTPELLRAAAGECRR--VRGETLPSdSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 754 TNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINrAMAARDAAIGVLiaETGGQNA 833
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIA-EKAGRHLKKITL--ELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 834 FIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQ 913
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 914 DHAER-MDREARLIaaaelSAEAANGTFFAPRAyeLKDLGQ----LQKEVFGPVLHVIRWKgDQLDAvIDQINATGYGLT 988
Cdd:cd07150 315 RQVEDaVAKGAKLL-----TGGKYDGNFYQPTV--LTDVTPdmriFREETFGPVTSVIPAK-DAEEA-LELANDTEYGLS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 989 LGVHSRIDETVDRISNGVHVGNVYVNRNQI--GAVVgvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07150 386 AAILTNDLQRAFKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGEWSMEEFTELKWITV 451
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
597-1056 |
6.19e-67 |
|
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: 232.63 E-value: 6.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPADTrEVVGQWLAADAATVQKALANAvAAQPAwnRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAE 676
Cdd:cd07146 3 VRNPYTG-EVVGTVPAGTEEALREALALA-ASYRS--TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 677 VREAVDFLRYYAKQAREQFSHAEKLP-SPTGESNELQLHGR--GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQ 753
Cdd:cd07146 79 VGRAADVLRFAAAEALRDDGESFSCDlTANGKARKIFTLREplGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 754 TNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInramaARDAAIGVLIAETGGQNA 833
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI-----AATAGYKRQLLELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 834 FIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQ 913
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 914 DHAER-MDREARLIaaaelSAEAANGTFFAPRAYEL--KDLGQLQKEVFGPVLHVIRWKGdqLDAVIDQINATGYGLTLG 990
Cdd:cd07146 314 NRVEEaIAQGARVL-----LGNQRQGALYAPTVLDHvpPDAELVTEETFGPVAPVIRVKD--LDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590385370 991 VHSRIDETVDRISNGVHVGNVYVNrNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
592-1036 |
1.08e-66 |
|
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: 232.11 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPADTReVVGQWLAADAATVQKALANAVAAQPA--WNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:cd07112 1 GETFATINPATGR-VLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIA-EVREAVDFLRYYAKQAREQFSHAeklpSPTGEsNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNS 745
Cdd:cd07112 80 ISDALAvDVPSAANTFRWYAEAIDKVYGEV----APTGP-DALALITReplGVVGAVVPWNFPLLMAAWKIAPALAAGNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 746 VIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAmAARDAAIGVLI 825
Cdd:cd07112 155 VVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEY-SGQSNLKRVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 826 aETGGQNAFI--ADSSALpEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPV 903
Cdd:cd07112 234 -ECGGKSPNIvfADAPDL-DAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 904 IDADALKILQDHAERMDRE-ARLIAAAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDqlDAVIDQI 980
Cdd:cd07112 312 VSEAHFDKVLGYIESGKAEgARLVAGGKRVLTETGGFFVEPTVFDgvTPDMRIAREEIFGPVLSVITFDSE--EEAVALA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1590385370 981 NATGYGLTLGVHSRIDETVDRISNGVHVGNVYVnrNQIGAVVGVQPFGGQGLSGTG 1036
Cdd:cd07112 390 NDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
618-1056 |
4.52e-66 |
|
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: 229.27 E-value: 4.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 618 VQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQArEQFSH 697
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENA-EAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 698 AEKLPSPTGESnELQLHGRGVFVCISPWNFPLAiflgQV----AAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAE 773
Cdd:cd07100 80 DEPIETDAGKA-YVRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 774 VVQFLPGDGATVgAALTADPRVAGVAFTGSTDTARAINrAMAARDAAIGVLiaETGGQNAFIADSSALPEQLVKDAIGSA 853
Cdd:cd07100 155 VFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVA-AEAGKNLKKSVL--ELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 854 FTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDHAERM-DREARLIaaAELS 932
Cdd:cd07100 231 LQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAvAAGATLL--LGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 933 AEAANGTFFAP----------RAYElkdlgqlqKEVFGPVLHVIRWKGDqlDAVIDQINATGYGLTLGVHSRIDETVDRI 1002
Cdd:cd07100 309 RPDGPGAFYPPtvltdvtpgmPAYD--------EELFGPVAAVIKVKDE--EEAIALANDSPFGLGGSVFTTDLERAERV 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 1003 SNGVHVGNVYVNrnqigAVVGVQ---PFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07100 379 ARRLEAGMVFIN-----GMVKSDprlPFGGVKRSGYG-RELGRFGIREFVNIKTVWV 429
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
618-1034 |
2.66e-64 |
|
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: 224.46 E-value: 2.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 618 VQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVdflryyAKQAREQFSH 697
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMA------GKIDISIKAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 698 AEKLPSPTGESNELQLHGR----GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAE 773
Cdd:cd07095 76 HERTGERATPMAQGRAVLRhrphGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 774 VVQFLPGdGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIgvLIAETGGQNAFIADSSALPEQLVKDAIGSA 853
Cdd:cd07095 156 VLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI--LALEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 854 FTSAGQRCSAARVLFV-QDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADAL-KILQDHAERMDREARLIaaAEL 931
Cdd:cd07095 233 FLTAGQRCTCARRLIVpDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAaRYLLAQQDLLALGGEPL--LAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 932 SAEAANGTFFAPRAYELKDLGQLQK-EVFGPVLHVIRWkgDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGN 1010
Cdd:cd07095 311 ERLVAGTAFLSPGIIDVTDAADVPDeEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGI 388
|
410 420
....*....|....*....|....
gi 1590385370 1011 VYVNRNQIGAvVGVQPFGGQGLSG 1034
Cdd:cd07095 389 VNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
591-1040 |
5.82e-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: 225.07 E-value: 5.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAA--QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGK 668
Cdd:cd07142 17 SGKTFPTIDPR-NGEVIAHVAEGDAEDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 669 SLPDS-IAEVREAVDFLRYYAKQAREqfSHAEKLPSpTGESNELQLHGR-GVFVCISPWNFPLAIFLGQVAAALAAGNSV 746
Cdd:cd07142 96 PYEQArYAEVPLAARLFRYYAGWADK--IHGMTLPA-DGPHHVYTLHEPiGVVGQIIPWNFPLLMFAWKVGPALACGNTI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 747 IAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDaaIGVLIA 826
Cdd:cd07142 173 VLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN--LKPVTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 827 ETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDA 906
Cdd:cd07142 251 ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 907 DAL-KILQDHAERMDREARLIaaAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKgdQLDAVIDQINAT 983
Cdd:cd07142 331 EQFeKILSYIEHGKEEGATLI--TGGDRIGSKGYYIQPTIFSdvKDDMKIARDEIFGPVQSILKFK--TVDEVIKRANNS 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590385370 984 GYGLTLGVHSRIDETVDRISNGVHVGNVYVN-RNQIGAVVgvqPFGGQGLSGTGPKAG 1040
Cdd:cd07142 407 KYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
603-1056 |
3.27e-63 |
|
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: 222.18 E-value: 3.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 603 TREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVD 682
Cdd:cd07101 5 TGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 683 FLRYYAKQArEQFSHAEKLPS--PTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYY 760
Cdd:cd07101 85 VARYYARRA-ERLLKPRRRRGaiPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 761 AVKLLHDAGVPAEVVQFLPGDGATVGAALTAdpRVAGVAFTGSTDTARAINRAMAARdaaigvLI---AETGGQNAFIAD 837
Cdd:cd07101 164 AVELLIEAGLPRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRR------LIgcsLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 838 SSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQDHAE 917
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 918 rmdrEARliaaAELSAEAANGT--------FFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDqlDAVIDQINATGYGL 987
Cdd:cd07101 316 ----DAV----AKGATVLAGGRarpdlgpyFYEPTVLTgvTEDMELFAEETFGPVVSIYRVADD--DEAIELANDTDYGL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 988 TLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQ-PFGGQGLSGTGPKAgGPHYLLRFATEKTVTV 1056
Cdd:cd07101 386 NASVWTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRH-GAEGLLKYTETQTVAV 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
591-1061 |
4.64e-63 |
|
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: 222.57 E-value: 4.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPADtREVVGQWLAADAATVQKALANAVAA--QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGK 668
Cdd:cd07119 11 SGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 669 SLPDSIAEVREAVDFLRYYAKQAReqfshaeklpSPTGESNEL--QLHGR------GVFVCISPWNFPLAIFLGQVAAAL 740
Cdd:cd07119 90 TLRESEIDIDDVANCFRYYAGLAT----------KETGEVYDVppHVISRtvrepvGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 741 AAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAA 820
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 821 IGVliaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDV 900
Cdd:cd07119 240 VAL---ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 901 GPVIDADAL-KILQDHAERMDREARLIA--AAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKgDQLDA 975
Cdd:cd07119 317 GPLVSAEHReKVLSYIQLGKEEGARLVCggKRPTGDELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERFD-TEEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 976 vIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVT 1055
Cdd:cd07119 396 -IRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEA--PWGGYKQSGIG-RELGPTGLEEYQETKHIN 471
|
....*.
gi 1590385370 1056 VNTTAA 1061
Cdd:cd07119 472 INLSPQ 477
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
590-1056 |
9.51e-63 |
|
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: 221.62 E-value: 9.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:cd07085 13 KTTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIAEVR---EAVDF--------LRYYAKQAREQF-SHAEKLPsptgesnelqlhgRGVFVCISPWNFPLAIFLGQVA 737
Cdd:cd07085 92 LADARGDVLrglEVVEFacsiphllKGEYLENVARGIdTYSYRQP-------------LGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 738 AALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTaDPRVAGVAFTGSTDTARAINramaAR 817
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIY----ER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 818 DAAIG--VLiAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGL 895
Cdd:cd07085 234 AAANGkrVQ-ALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 896 LSTDVGPVIDADALKILQDHAERMDRE-ARLIA--AAELSAEAANGTFFAP----------RAYelkdlgqlQKEVFGPV 962
Cdd:cd07085 313 PGADMGPVISPAAKERIEGLIESGVEEgAKLVLdgRGVKVPGYENGNFVGPtildnvtpdmKIY--------KEEIFGPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 963 LHVIRwkGDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNrnqIGAVVGVQ--PFGGQGLS------G 1034
Cdd:cd07085 385 LSIVR--VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLAffSFGGWKGSffgdlhF 459
|
490 500
....*....|....*....|...
gi 1590385370 1035 TGPKAggphylLRFATE-KTVTV 1056
Cdd:cd07085 460 YGKDG------VRFYTQtKTVTS 476
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
591-1056 |
9.90e-63 |
|
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: 221.45 E-value: 9.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAA---QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAG 667
Cdd:cd07141 20 SGKTFPTINPA-TGEKICEVQEGDKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 668 KS-LPDSIAEVREAVDFLRYYAKQAREqfSHAEKLPSpTGESNELQLHgRGVFVC--ISPWNFPLAIFLGQVAAALAAGN 744
Cdd:cd07141 99 KPfSKSYLVDLPGAIKVLRYYAGWADK--IHGKTIPM-DGDFFTYTRH-EPVGVCgqIIPWNFPLLMAAWKLAPALACGN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 745 SVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVL 824
Cdd:cd07141 175 TVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRVTL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 825 iaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVI 904
Cdd:cd07141 255 --ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 905 DADALKILQDHAERMDRE-ARLIAAAELSAEAanGTFFAPRAY-ELKDLGQLQK-EVFGPVLHVIRWKgdQLDAVIDQIN 981
Cdd:cd07141 333 DEEQFKKILELIESGKKEgAKLECGGKRHGDK--GYFIQPTVFsDVTDDMRIAKeEIFGPVQQIFKFK--TIDEVIERAN 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 982 ATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNrnqIGAVVGVQ-PFGGQGLSGTGPKAGgpHYLLRFATE-KTVTV 1056
Cdd:cd07141 409 NTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG--EYGLQEYTEvKTVTI 480
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
597-1054 |
1.08e-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: 220.58 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWN-RTPAASRAAILEHAADQLEARMPEFMALCVKEAGKslPDSIA 675
Cdd:cd07089 1 VINPA-TEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGA--PVMTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 676 E---VREAVDFLRYYAKQAREqFSHAEKLPSPTgesNELQLHGR-------GVFVCISPWNFPLAIFLGQVAAALAAGNS 745
Cdd:cd07089 78 RamqVDGPIGHLRYFADLADS-FPWEFDLPVPA---LRGGPGRRvvrrepvGVVAAITPWNFPFFLNLAKLAPALAAGNT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 746 VIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInramaARDAAIGV-- 823
Cdd:cd07089 154 VVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRI-----MAQAAATLkr 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 824 LIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPV 903
Cdd:cd07089 229 VLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 904 IDADALKILQDHAER-MDREARLIAAAELSAEAANGTFFAPRAyeLKDLGQ----LQKEVFGPVLHVIRWKGDqlDAVID 978
Cdd:cd07089 309 ISAAQRDRVEGYIARgRDEGARLVTGGGRPAGLDKGFYVEPTL--FADVDNdmriAQEEIFGPVLVVIPYDDD--DEAVR 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590385370 979 QINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNrnqiGAVVGV--QPFGGQGLSGTGpKAGGPHYLLRFATEKTV 1054
Cdd:cd07089 385 IANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG-RENGIEGLEEFLETKSI 457
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
600-1056 |
3.05e-61 |
|
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: 216.43 E-value: 3.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 600 PADTREVVGQWlAADAATVQKALAnavAAQPA-----WNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07118 4 PAHGVVVARYA-EGTVEDVDAAVA---AARKAfdkgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAR--EQFSHAEKLPSPTGesneLQLH-GRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPA 751
Cdd:cd07118 80 GEIEGAADLWRYAASLARtlHGDSYNNLGDDMLG----LVLRePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 752 EQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVliaETGGQ 831
Cdd:cd07118 156 EFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSL---ELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 832 NAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKI 911
Cdd:cd07118 233 NPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 912 LQDHAERMDREARLIAAAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWkgDQLDAVIDQINATGYGLTL 989
Cdd:cd07118 313 ITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 990 GVHSRIDETVDRISNGVHVGNVYVNRNQIGAVvgVQPFGGQGLSGTGPKAgGPHYLLRFATEKTVTV 1056
Cdd:cd07118 391 GVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGREL-GRYGVEEYTELKTVHL 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
597-1036 |
3.19e-61 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 216.42 E-value: 3.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIA- 675
Cdd:cd07092 1 VVDPA-TGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 676 EVREAVDFLRYYAKQAR--EQFSHAEKLPSPTGESNELQLhgrGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQ 753
Cdd:cd07092 80 ELPGAVDNFRFFAGAARtlEGPAAGEYLPGHTSMIRREPI---GVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 754 TNLIGYYAVKLLHDaGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAmAARDaaIGVLIAETGGQNA 833
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADT--LKRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 834 FIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQ 913
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 914 DHAERMDREARLIaaAELSAEAANGTFFAPR--AYELKDLGQLQKEVFGPVLHVIRWkgDQLDAVIDQINATGYGLTLGV 991
Cdd:cd07092 313 GFVERAPAHARVL--TGGRRAEGPGYFYEPTvvAGVAQDDEIVQEEIFGPVVTVQPF--DDEDEAIELANDVEYGLASSV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1590385370 992 HSRIDETVDRISNGVHVGNVYVNRNQIgaVVGVQPFGGQGLSGTG 1036
Cdd:cd07092 389 WTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
597-1058 |
4.00e-61 |
|
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: 216.02 E-value: 4.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAE 676
Cdd:cd07090 1 VIEPA-TGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 677 VREAVDFLRYYAKQAreqfshaeklPSPTGESNELQlHGR---------GVFVCISPWNFPLAIFLGQVAAALAAGNSVI 747
Cdd:cd07090 80 IDSSADCLEYYAGLA----------PTLSGEHVPLP-GGSfaytrreplGVCAGIGAWNYPIQIASWKSAPALACGNAMV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 748 AKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATvGAALTADPRVAGVAFTGSTDTARAInraMAARDAAIGVLIAE 827
Cdd:cd07090 149 YKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKV---MSAAAKGIKHVTLE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 828 TGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCS-AARVlFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDA 906
Cdd:cd07090 225 LGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSnGTRV-FVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 907 DALKILQDHAERMDRE-ARLI---AAAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDqlDAVIDQI 980
Cdd:cd07090 304 EHLEKVLGYIESAKQEgAKVLcggERVVPEDGLENGFYVSPCVLTdcTDDMTIVREEIFGPVMSILPFDTE--EEVIRRA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590385370 981 NATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVvgVQPFGGQGLSGTGpKAGGPHYLLRFATEKTVTVNT 1058
Cdd:cd07090 382 NDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPV--EVPFGGYKQSGFG-RENGTAALEHYTQLKTVYVEM 456
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
591-1056 |
4.55e-60 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 215.13 E-value: 4.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSL 670
Cdd:PRK09407 30 AGPTREVTAPF-TGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 671 PDSIAEVREAVDFLRYYAKQAREQFS---HAEKLPSPTgeSNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVI 747
Cdd:PRK09407 109 RHAFEEVLDVALTARYYARRAPKLLAprrRAGALPVLT--KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 748 AKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTAdpRVAGVAFTGSTDTARAINRAMAARdaaigvLI-- 825
Cdd:PRK09407 187 LKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGSTATGRVLAEQAGRR------LIgf 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 826 -AETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGnPGL-LSTDVGPV 903
Cdd:PRK09407 259 sLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLG-AGYdYSADMGSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 904 IDADALKILQDHAErmdrEARliaaaelsaeAANGTFFA---PRAyelkDLGQL-----------------QKEVFGPVL 963
Cdd:PRK09407 338 ISEAQLETVSAHVD----DAV----------AKGATVLAggkARP----DLGPLfyeptvltgvtpdmelaREETFGPVV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 964 HVIRWKGDqlDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQ-PFGGQGLSGTGPKAgGP 1042
Cdd:PRK09407 400 SVYPVADV--DEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLGRRH-GA 476
|
490
....*....|....
gi 1590385370 1043 HYLLRFATEKTVTV 1056
Cdd:PRK09407 477 EGLLKYTESQTIAT 490
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
599-1015 |
4.96e-60 |
|
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: 212.88 E-value: 4.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 599 NPADtREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVR 678
Cdd:cd07102 2 SPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 679 EAVDFLRYYAKQAreqfshAEKL-PSPTGESNELQLHGR----GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQ 753
Cdd:cd07102 81 GMLERARYMISIA------EEALaDIRVPEKDGFERYIRreplGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 754 TNLIGYYAVKLLHDAGVPAEVVQFLPGDGATvGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVliaETGGQNA 833
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGL---ELGGKDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 834 FIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKILQ 913
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 914 DH-AERMDREAR-LIAAAELSAEAANGTFFAPRAyeLKDLGQ----LQKEVFGPVLHVIRWKGDqlDAVIDQINATGYGL 987
Cdd:cd07102 311 AQiADAIAKGARaLIDGALFPEDKAGGAYLAPTV--LTNVDHsmrvMREETFGPVVGIMKVKSD--AEAIALMNDSEYGL 386
|
410 420
....*....|....*....|....*...
gi 1590385370 988 TLGVHSRIDETVDRISNGVHVGNVYVNR 1015
Cdd:cd07102 387 TASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
591-1034 |
7.67e-60 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 213.28 E-value: 7.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSL 670
Cdd:PRK09457 13 QGEAFESRNPV-SGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 671 PDSIAEVREAVdflryyAKQAREQFSHAEKlpspTGESNELQLHGR--------GVFVCISPWNFPLAIFLGQVAAALAA 742
Cdd:PRK09457 92 WEAATEVTAMI------NKIAISIQAYHER----TGEKRSEMADGAavlrhrphGVVAVFGPYNFPGHLPNGHIVPALLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 743 GNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATvGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIg 822
Cdd:PRK09457 162 GNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 823 vLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDI-ADKVMTMLAGAMKELKVGNPgllstD-- 899
Cdd:PRK09457 240 -LALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGRW-----Dae 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 900 ----VGPVIDAD-ALKILQDHAERMDREARLIaaAELSAEAANGTFFAPRAYELKDLGQL-QKEVFGPVLHVIRWkgDQL 973
Cdd:PRK09457 314 pqpfMGAVISEQaAQGLVAAQAQLLALGGKSL--LEMTQLQAGTGLLTPGIIDVTGVAELpDEEYFGPLLQVVRY--DDF 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590385370 974 DAVIDQINATGYGLTLGVHS----RIDETVDRISNGVhvgnvyVNRN-QIGAVVGVQPFGGQGLSG 1034
Cdd:PRK09457 390 DEAIRLANNTRFGLSAGLLSddreDYDQFLLEIRAGI------VNWNkPLTGASSAAPFGGVGASG 449
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
85-198 |
1.38e-59 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 199.27 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 85 IEAFMRQYDLGSEEGVLLMCVAEALLRIPDQDTADKLIRDKLADADWEKHLGGSDSVLVNASTWGLMLTGKLVQMNDatR 164
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEP--E 78
|
90 100 110
....*....|....*....|....*....|....
gi 1590385370 165 ADAPSAFKRLVGRVGEPVVRLAVRQAMKIMGHQF 198
Cdd:pfam14850 79 GTLAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
592-1036 |
1.47e-59 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 212.08 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLP 671
Cdd:PRK13473 16 GEKQPVYNPA-TGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 672 DSIA-EVREAVDFLRYYAKQAR--EQFSHAEKLPsptGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIA 748
Cdd:PRK13473 95 LALNdEIPAIVDVFRFFAGAARclEGKAAGEYLE---GHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 749 KPAEQTNLIGYYAVKLLHDAgVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInraMAARDAAIGVLIAET 828
Cdd:PRK13473 172 KPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHV---LSAAADSVKRTHLEL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADA 908
Cdd:PRK13473 248 GGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 909 LKILQDHAERMDREARLIAAAELSAEAANGTFFAPRAyeLKDLGQ----LQKEVFGPVLHVIRWKGDqlDAVIDQINATG 984
Cdd:PRK13473 328 RDRVAGFVERAKALGHIRVVTGGEAPDGKGYYYEPTL--LAGARQddeiVQREVFGPVVSVTPFDDE--DQAVRWANDSD 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1590385370 985 YGLTLGVHSRIDETVDRISNGVHVGNVYVNRNqiGAVVGVQPFGGQGLSGTG 1036
Cdd:PRK13473 404 YGLASSVWTRDVGRAHRVSARLQYGCTWVNTH--FMLVSEMPHGGQKQSGYG 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
599-1056 |
1.58e-59 |
|
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: 211.43 E-value: 1.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 599 NPAdTREVVGQWLAADAATVQKALANAVAA--QPAWNRTPAAsRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAE 676
Cdd:cd07120 3 DPA-TGEVIGTYADGGVAEAEAAIAAARRAfdETDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 677 VREAVDFLRYYAKQAREQFSHAEKlPSPtGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNL 756
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIE-PEP-GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 757 IGYYAVKLLHDA-GVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVliaETGGQNAFI 835
Cdd:cd07120 159 INAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGL---ELGGKTPCI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 836 ----ADSSALPEQLVKdaigSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKI 911
Cdd:cd07120 236 vfddADLDAALPKLER----ALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 912 LQDHAER-MDREAR-LIAAAELSAEAANGTFFAPRAYELKD--LGQLQKEVFGPVLHVIRWKgDQLDAViDQINATGYGL 987
Cdd:cd07120 312 VDRMVERaIAAGAEvVLRGGPVTEGLAKGAFLRPTLLEVDDpdADIVQEEIFGPVLTLETFD-DEAEAV-ALANDTDYGL 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 988 TLGVHSRIDETVDRISNGVHVGNVYVNR-NQIGAVVgvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07120 390 AASVWTRDLARAMRVARAIRAGTVWINDwNKLFAEA---EEGGYRQSGLG-RLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
595-1056 |
1.63e-58 |
|
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: 208.64 E-value: 1.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07147 1 LEVTNPY-TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAREQfsHAEKLPSPTGESNElqlhGR---------GVFVCISPWNFPLAIFLGQVAAALAAGNS 745
Cdd:cd07147 80 GEVARAIDTFRIAAEEATRI--YGEVLPLDISARGE----GRqglvrrfpiGPVSAITPFNFPLNLVAHKVAPAIAAGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 746 VIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLP--GDGAtvgAALTADPRVAGVAFTGSTdtarAINRAMAARDAAIGV 823
Cdd:cd07147 154 FVLKPASRTPLSALILGEVLAETGLPKGAFSVLPcsRDDA---DLLVTDERIKLLSFTGSP----AVGWDLKARAGKKKV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 824 LIaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPV 903
Cdd:cd07147 227 VL-ELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 904 IDADALKILQDHA-ERMDREARLIaaaelSAEAANGTFFAPRAYELKDLGQL--QKEVFGPVLHVIRWkgDQLDAVIDQI 980
Cdd:cd07147 306 ISESEAERVEGWVnEAVDAGAKLL-----TGGKRDGALLEPTILEDVPPDMEvnCEEVFGPVVTVEPY--DDFDEALAAV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 981 NATGYGLTLGVHSRIDETVDRISNGVHVGNVYVnrNQIGAV-VGVQPFGGQGLSGTGPKagGPHYLLRFATEKTVTV 1056
Cdd:cd07147 379 NDSKFGLQAGVFTRDLEKALRAWDELEVGGVVI--NDVPTFrVDHMPYGGVKDSGIGRE--GVRYAIEEMTEPRLLV 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
592-1036 |
6.95e-58 |
|
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: 207.58 E-value: 6.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMpEFMALC-VKEAGKSL 670
Cdd:cd07559 15 GEYFDNYNPV-NGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENL-ELLAVAeTLDNGKPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 671 PDSI-AEVREAVDFLRYYAKQAREQFSHAEKLpsptgESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSV 746
Cdd:cd07559 93 RETLaADIPLAIDHFRYFAGVIRAQEGSLSEI-----DEDTLSYHFHeplGVVGQIIPWNFPLLMAAWKLAPALAAGNTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 747 IAKPAEQTNLIGYYAVKLLHDAgVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInrAMAARDAAIGVLIa 826
Cdd:cd07559 168 VLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLI--MQYAAENLIPVTL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 827 ETGGQ--NAFIADSSALPEQLVKDAIGS----AFTSaGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDV 900
Cdd:cd07559 244 ELGGKspNIFFDDAMDADDDFDDKAEEGqlgfAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 901 GPVIDADALKILQDHAERMDRE-ARLIA--AAELSAEAANGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIRWKGDqlDA 975
Cdd:cd07559 323 GAQVSKDQLEKILSYVDIGKEEgAEVLTggERLTLGGLDKGYFYEPTLIKGGNNDMriFQEEIFGPVLAVITFKDE--EE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590385370 976 VIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVN-RNQIGAVVgvqPFGGQGLSGTG 1036
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
595-1056 |
7.47e-58 |
|
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: 207.16 E-value: 7.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI 674
Cdd:cd07151 12 IDVLNPY-TGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKAN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 675 AEVREAVDFLRYYAKQAREQfsHAEKLPSPT-GESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQ 753
Cdd:cd07151 91 IEWGAAMAITREAATFPLRM--EGRILPSDVpGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 754 TNLIGYYAV-KLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRaMAARDAAIGVLiaETGGQN 832
Cdd:cd07151 169 TPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGE-LAGRHLKKVAL--ELGGNN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 833 AFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADALKIL 912
Cdd:cd07151 246 PFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 913 QDHAERMDRE-ARLIaaaelSAEAANGTFFAPraYELKDLGQ----LQKEVFGPVLHVIRWKGDqlDAVIDQINATGYGL 987
Cdd:cd07151 326 LDKIEQAVEEgATLL-----VGGEAEGNVLEP--TVLSDVTNdmeiAREEIFGPVAPIIKADDE--EEALELANDTEYGL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590385370 988 TLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07151 397 SGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG-RFNGEWALEEFTTDKWISV 463
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
592-1057 |
7.51e-58 |
|
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: 207.38 E-value: 7.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPAdTREVVGQWLAADAATVQKALANAVAA-QPAWNRT-PAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:cd07143 21 GGTVKVYNPS-TGKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLMERNLDYLASIEALDNGKT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIA-EVREAVDFLRYYAkqareqfSHAEKLPSPTGESNELQL----HgRGVFVC--ISPWNFPLAIFLGQVAAALAA 742
Cdd:cd07143 100 FGTAKRvDVQASADTFRYYG-------GWADKIHGQVIETDIKKLtytrH-EPIGVCgqIIPWNFPLLMCAWKIAPALAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 743 GNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDaaIG 822
Cdd:cd07143 172 GNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSN--LK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 823 VLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGP 902
Cdd:cd07143 250 KVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 903 vidadalKILQDHAERM------DREARLIAAAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDQld 974
Cdd:cd07143 330 -------QVSQIQYERImsyiesGKAEGATVETGGKRHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKFKTEE-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 975 AVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVN-RNQIGAVVgvqPFGGQGLSGTGPKAGgpHYLLRFATE-K 1052
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG--EYALENYTQiK 475
|
....*
gi 1590385370 1053 TVTVN 1057
Cdd:cd07143 476 AVHIN 480
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
597-1056 |
9.71e-58 |
|
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: 206.91 E-value: 9.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 597 VTNPAdTREVVGQWLAADAATVQKALANAVAA-QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIA 675
Cdd:cd07113 19 ITNPA-TEQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 676 -EVREAVDFLRYYA----KQAREQFshAEKLPSPTGE--SNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIA 748
Cdd:cd07113 98 fEVGQSANFLRYFAgwatKINGETL--APSIPSMQGEryTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 749 KPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGAtVGAALTADPRVAGVAFTGSTDTARAINRAmAARDAAIGVLiaET 828
Cdd:cd07113 176 KPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ-AASDLTRVTL--EL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADA 908
Cdd:cd07113 252 GGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLANQPH 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 909 L-KILqdHAERMDREARLIAAAELSAEAANGTFFAPRAYELK--DLGQLQKEVFGPVLHVIRWKGDqlDAVIDQINATGY 985
Cdd:cd07113 332 FdKVC--SYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARsaDSRLMREETFGPVVSFVPYEDE--EELIQLINDTPF 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVNRNQI--GAVvgvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07113 408 GLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFldPAV----PFGGMKQSGIG-REFGSAFIDDYTELKSVMI 475
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
595-1056 |
1.25e-56 |
|
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: 203.58 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPAdTREVVGQWLAADAATVQKALANAVAA--QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGksLPD 672
Cdd:cd07139 16 IDVVSPA-TEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENG--MPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 673 SIAEVRE---AVDFLRYYAKQAREqFSHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAK 749
Cdd:cd07139 93 SWSRRAQgpgPAALLRYYAALARD-FPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 750 PAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDgATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVliaETG 829
Cdd:cd07139 172 PSPETPLDAYLLAEAAEEAGLPPGVVNVVPAD-REVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTL---ELG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 830 GQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSA-ARVLfVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADA 908
Cdd:cd07139 248 GKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVAlTRIL-VPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 909 LKILQDHAER-MDREARLIAAAELSAEAANGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIRWkgDQLDAVIDQINATGY 985
Cdd:cd07139 327 RERVEGYIAKgRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMriAQEEIFGPVLSVIPY--DDEDDAVRIANDSDY 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVN--RNQIGAvvgvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07139 405 GLSGSVWTADVERGLAVARRIRTGTVGVNgfRLDFGA-----PFGGFKQSGIG-REGGPEGLDAYLETKSIYL 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
592-1040 |
6.83e-55 |
|
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: 199.17 E-value: 6.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPAdTREVVGQWLAADAATVQKALANAVAA-QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSL 670
Cdd:cd07144 22 GETIKTVNPS-TGEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 671 -PDSIAEVREAVDFLRYYAKQAREQFS---------HAEKLPSPTGesnelqlhgrgvfVC--ISPWNFPLAIFLGQVAA 738
Cdd:cd07144 101 hSNALGDLDEIIAVIRYYAGWADKIQGktiptspnkLAYTLHEPYG-------------VCgqIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 739 ALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARD 818
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 819 AAIGVliaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKE-LKVGNPGLLS 897
Cdd:cd07144 248 KAVTL---ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFDDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 898 TDVGPVIDADALKILQDHAER-MDREARLIAA-AELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDql 973
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKgKKEGAKLVYGgEKAPEGLGKGYFIPPTIFTdvPQDMRIVKEEIFGPVVVISKFKTY-- 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 974 DAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAvVGVqPFGGQGLSGTGPKAG 1040
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSD-VGV-PFGGFKMSGIGRELG 467
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
588-1036 |
4.44e-54 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 196.64 E-value: 4.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 588 ANPAGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAG 667
Cdd:PRK13252 17 EATSGETFEVINPA-TGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 668 KSLPD-SIAEVREAVDFLRYYAKQAreqfshaeklpsPTGESNELQLHGR----------GVFVCISPWNFPLAIFLGQV 736
Cdd:PRK13252 96 KPIQEtSVVDIVTGADVLEYYAGLA------------PALEGEQIPLRGGsfvytrreplGVCAGIGAWNYPIQIACWKS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 737 AAALAAGNSVIAKPAEQTNLIgyyAVKL---LHDAGVPAEVVQFLPGDGAtVGAALTADPRVAGVAFTGSTDTARainRA 813
Cdd:PRK13252 164 APALAAGNAMIFKPSEVTPLT---ALKLaeiYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGK---KV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 814 MAARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCS-AARVlFVQDDIADKVMTMLAGAMKELKVGN 892
Cdd:PRK13252 237 MAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRV-FVQKSIKAAFEARLLERVERIRIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 893 PGLLSTDVGPVIDADALKILQDHAERMDRE-ARLIA--AAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIR 967
Cdd:PRK13252 316 PMDPATNFGPLVSFAHRDKVLGYIEKGKAEgARLLCggERLTEGGFANGAFVAPTVFTdcTDDMTIVREEIFGPVMSVLT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590385370 968 WkgDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVnrNQIGAVVGVQPFGGQGLSGTG 1036
Cdd:PRK13252 396 F--DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
590-1045 |
1.41e-53 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 195.13 E-value: 1.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:PRK11241 23 NNGEVIDVTNPA-NGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIAEVREAVDFLRYYAKQAREQFshAEKLPSPTGESNELQLHGR-GVFVCISPWNFPLAIFLGQVAAALAAGNSVIA 748
Cdd:PRK11241 102 LAEAKGEISYAASFIEWFAEEGKRIY--GDTIPGHQADKRLIVIKQPiGVTAAITPWNFPAAMITRKAGPALAAGCTMVL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 749 KPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInRAMAARDaaIGVLIAET 828
Cdd:PRK11241 180 KPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQL-MEQCAKD--IKKVSLEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADA 908
Cdd:PRK11241 257 GGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 909 LKILQDH-AERMDREARLIaaAELSAEAANGTFFAPR--AYELKDLGQLQKEVFGPVLHVIRWKGDqlDAVIDQINATGY 985
Cdd:PRK11241 337 VAKVEEHiADALEKGARVV--CGGKAHELGGNFFQPTilVDVPANAKVAKEETFGPLAPLFRFKDE--ADVIAQANDTEF 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGvqPFGG---QGLSGTGPKAGGPHYL 1045
Cdd:PRK11241 413 GLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
591-1040 |
1.67e-53 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 196.57 E-value: 1.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAA--QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGK 668
Cdd:PLN02466 71 SGKTFPTLDPR-TGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 669 SLPDSI-AEVREAVDFLRYYAKQAREQFShaekLPSPTGESNELQ-LHGR-GVFVCISPWNFPLAIFLGQVAAALAAGNS 745
Cdd:PLN02466 150 PYEQSAkAELPMFARLFRYYAGWADKIHG----LTVPADGPHHVQtLHEPiGVAGQIIPWNFPLLMFAWKVGPALACGNT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 746 VIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInRAMAARDAAIGVLI 825
Cdd:PLN02466 226 IVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIV-LELAAKSNLKPVTL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 826 aETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADK-VMTMLAGAMKELkVGNPGLLSTDVGPVI 904
Cdd:PLN02466 305 -ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEfVEKAKARALKRV-VGDPFKKGVEQGPQI 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 905 DADAL-KILQDHAERMDREARLIaaaelsaeaANGTFFAPRAYELK---------DLGQLQKEVFGPVLHVIRWKgdQLD 974
Cdd:PLN02466 383 DSEQFeKILRYIKSGVESGATLE---------CGGDRFGSKGYYIQptvfsnvqdDMLIAQDEIFGPVQSILKFK--DLD 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 975 AVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVN-RNQIGAVVgvqPFGGQGLSGTGPKAG 1040
Cdd:PLN02466 452 EVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
592-1048 |
1.03e-52 |
|
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: 192.61 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSlp 671
Cdd:cd07111 36 RKSFPTINPA-TGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKP-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 672 dsIAEVRE-----AVDFLRYYAKQAREQfshaeklpsptgesnELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAG 743
Cdd:cd07111 113 --IRESRDcdiplVARHFYHHAGWAQLL---------------DTELAGWkpvGVVGQIVPWNFPLLMLAWKICPALAMG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 744 NSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATvGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGV 823
Cdd:cd07111 176 NTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 824 liaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPV 903
Cdd:cd07111 255 ---ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 904 IDADALKILQDHAERMDREArLIAAAELSAEAANGTFFAPRAYElkDLGQ----LQKEVFGPVLHVIRWKgdQLDAVIDQ 979
Cdd:cd07111 332 VDPAQLKRIRELVEEGRAEG-ADVFQPGADLPSKGPFYPPTLFT--NVPPasriAQEEIFGPVLVVLTFR--TAKEAVAL 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 980 INATGYGLTLGVHSRIDETVDRISNGVHVGNVYVN-RNQIGAVVgvqPFGGQGLSGTGpKAGGPHYLLRF 1048
Cdd:cd07111 407 ANNTPYGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEY 472
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
618-1056 |
1.76e-51 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 187.78 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 618 VQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAreqfSH 697
Cdd:cd07105 2 ADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLI----TQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 698 AEKLPSPTGESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEV 774
Cdd:cd07105 78 IIGGSIPSDKPGTLAMVVKepvGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 775 VQFL---PGDGATVGAALTADPRVAGVAFTGSTDTARAInrAMAARDAAIGVLIaETGGQNAFIADSSALPEQLVKDAIG 851
Cdd:cd07105 158 LNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRII--AETAAKHLKPVLL-ELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 852 SAFTSAGQRC-SAARVLfVQDDIADKVMTMLAGAMKELKVGnpgllSTDVGPVIDADA---LKILQDHAerMDREARLIa 927
Cdd:cd07105 235 GAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAadrVKELVDDA--LSKGAKLV- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 928 AAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDqlDAVIDQINATGYGLTLGVHSRIDETVDRISNG 1005
Cdd:cd07105 306 VGGLADESPSGTSMPPTILDnvTPDMDIYSEESFGPVVSIIRVKDE--EEAVRIANDSEYGLSAAVFTRDLARALAVAKR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1590385370 1006 VHVGNVYVNrnqiGAVVGVQ---PFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07105 384 IESGAVHIN----GMTVHDEptlPHGGVKSSGYG-RFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
592-1057 |
7.69e-51 |
|
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: 187.03 E-value: 7.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPADTrEVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLP 671
Cdd:cd07130 11 GGVVTSISPANG-EPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 672 DSIAEVREAVDFLRYYAKQAReQFsHAEKLPS--PtGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAK 749
Cdd:cd07130 90 EGLGEVQEMIDICDFAVGLSR-QL-YGLTIPSerP-GHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 750 PAEQTNLIGYYAVKL----LHDAGVPAEVVQFLPGdGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARdaaIGVLI 825
Cdd:cd07130 167 PSPTTPLTAIAVTKIvarvLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR---FGRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 826 AETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVID 905
Cdd:cd07130 243 LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 906 ADALKILQDHAE--------------RMDREarliaaaelsaeaanGTFFAPRAYE-LKDLGQLQKEVFGPVLHVIRWKG 970
Cdd:cd07130 323 KAAVDNYLAAIEeaksqggtvlfggkVIDGP---------------GNYVEPTIVEgLSDAPIVKEETFAPILYVLKFDT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 971 dqLDAVIDQINATGYGLTLGVHSR-IDETVDRIS-NGVHVGNVYVNRNQIGAVVGvQPFGGQGLSGTGPKAGG---PHYL 1045
Cdd:cd07130 388 --LEEAIAWNNEVPQGLSSSIFTTdLRNAFRWLGpKGSDCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGSdawKQYM 464
|
490
....*....|..
gi 1590385370 1046 LRfateKTVTVN 1057
Cdd:cd07130 465 RR----STCTIN 472
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
592-1036 |
4.25e-50 |
|
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: 184.97 E-value: 4.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLP 671
Cdd:cd07117 15 GETIDSYNPA-NGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 672 DSIA-EVREAVDFLRYYAKQAREQFSHAEKLpsptgESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVI 747
Cdd:cd07117 94 ETRAvDIPLAADHFRYFAGVIRAEEGSANMI-----DEDTLSIVLRepiGVVGQIIPWNFPFLMAAWKLAPALAAGNTVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 748 AKPAEQTNLIGYYAVKLLHDAgVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAInrAMAARDAAIGVLIaE 827
Cdd:cd07117 169 IKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDV--AIAAAKKLIPATL-E 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 828 TGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDAD 907
Cdd:cd07117 245 LGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 908 ALKILQDHAERMDRE-ARLIA--AAELSAEAANGTFFAPRAYELKDLGQ--LQKEVFGPVLHVIRWKGDqlDAVIDQINA 982
Cdd:cd07117 325 QLDKILSYVDIAKEEgAKILTggHRLTENGLDKGFFIEPTLIVNVTNDMrvAQEEIFGPVATVIKFKTE--DEVIDMAND 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1590385370 983 TGYGLTLGVHSRIDETVDRISNGVHVGNVYVNR-NQIGAVVgvqPFGGQGLSGTG 1036
Cdd:cd07117 403 SEYGLGGGVFTKDINRALRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
579-1040 |
4.37e-50 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 185.71 E-value: 4.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 579 WQAAPLvpganpaGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAA-----QPAWNRTPAASRAAILEHAADQLEA 653
Cdd:PLN02467 16 WREPVL-------GKRIPVVNPA-TEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 654 RMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAE---KLPSPTGESNELQlHGRGVFVCISPWNFPLA 730
Cdd:PLN02467 88 RKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKapvSLPMETFKGYVLK-EPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 731 IFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAI 810
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 811 nraMAARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKV 890
Cdd:PLN02467 247 ---MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 891 GNPGLLSTDVGPVIDADALKILQDHAERMDRE-ARLIAAAELSAEAANGTFFAP-RAYELKDLGQLQK-EVFGPVLHVIR 967
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEgATILCGGKRPEHLKKGFFIEPtIITDVTTSMQIWReEVFGPVLCVKT 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590385370 968 WKGDqlDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQigAVVGVQPFGGQGLSGTGPKAG 1040
Cdd:PLN02467 404 FSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQ--PCFCQAPWGGIKRSGFGRELG 472
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
603-1054 |
1.28e-49 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 184.25 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 603 TREVVGQWLAADAATVQKALANAVAA--QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLP-DSIAEVRE 679
Cdd:PLN02766 45 TGEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 680 AVDFLRYYAKQAREqfSHAEKLPSPTgesnelQLHGR------GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQ 753
Cdd:PLN02766 125 AAGLLRYYAGAADK--IHGETLKMSR------QLQGYtlkepiGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 754 TNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVLiaETGGQNA 833
Cdd:PLN02766 197 TPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKQVSL--ELGGKSP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 834 FIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADAL-KIL 912
Cdd:PLN02766 275 LLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFeKIL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 913 Q--DHAERmdREARLIaaAELSAEAANGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKgdQLDAVIDQINATGYGLT 988
Cdd:PLN02766 355 SyiEHGKR--EGATLL--TGGKPCGDKGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKFK--TVEEAIKKANNTKYGLA 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590385370 989 LGVHSRIDETVDRISNGVHVGNVYVnrNQIGAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTV 1054
Cdd:PLN02766 429 AGIVTKDLDVANTVSRSIRAGTIWV--NCYFAFDPDCPFGGYKMSGFG-RDQGMDALDKYLQVKSV 491
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
599-1057 |
2.06e-48 |
|
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: 179.80 E-value: 2.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 599 NPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPD-SIAEV 677
Cdd:cd07098 2 DPA-TGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDaSLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 678 REAVDFLRYYAKQArEQFSHAEKLPSPTGE---SNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQT 754
Cdd:cd07098 81 LVTCEKIRWTLKHG-EKALRPESRPGGLLMfykRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 755 NLIGYYAV----KLLHDAGVPAEVVQFLPGDGATvGAALTADPRVAGVAFTGSTDTARAInrAMAARDAAIGVlIAETGG 830
Cdd:cd07098 160 AWSSGFFLsiirECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKV--MAAAAESLTPV-VLELGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 831 QNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVI-DADAL 909
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIsPARFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 910 KILQDHAERMDREARLIA--AAELSAEAANGTFFAPR--AYELKDLGQLQKEVFGPVLHVIRWKGDqlDAVIDQINATGY 985
Cdd:cd07098 316 RLEELVADAVEKGARLLAggKRYPHPEYPQGHYFPPTllVDVTPDMKIAQEEVFGPVMVVMKASDD--EEAVEIANSTEY 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVnrNQIGAVVGVQ--PFGGQGLSGTGpKAGGPHYLLRFATEKTVTVN 1057
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAI--NDFGVNYYVQqlPFGGVKGSGFG-RFAGEEGLRGLCNPKSVTED 464
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
644-1054 |
1.97e-47 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 175.31 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 644 LEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQfsHAEKLPSP-TGESNELQLHGRGVFVCI 722
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRY--EGEIIQSDrPGENILLFKRALGVTTGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 723 SPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTG 802
Cdd:PRK10090 79 LPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 803 STDTARAInraMAARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLA 882
Cdd:PRK10090 159 SVSAGEKI---MAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 883 GAMKELKVGNPGLLST-DVGPVIDADALKILQDHAERMDREARLIaAAELSAEAANGTFFAPRAyeLKDLGQ----LQKE 957
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARV-ALGGKAVEGKGYYYPPTL--LLDVRQemsiMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 958 VFGPVLHVIRWkgDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQpfGGQGLSGTGp 1037
Cdd:PRK10090 313 TFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFH--AGWRKSGIG- 387
|
410
....*....|....*..
gi 1590385370 1038 KAGGPHYLLRFATEKTV 1054
Cdd:PRK10090 388 GADGKHGLHEYLQTQVV 404
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
591-1056 |
9.95e-47 |
|
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: 175.38 E-value: 9.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPADtREVVGQWLAADAATVQKALANAVAA--QPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGK 668
Cdd:cd07140 19 GGKTYNTINPTD-GSVICKVSLATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 669 SLPDSI-AEVREAVDFLRYYAKQAREqfSHAEKLP-SPTGESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAG 743
Cdd:cd07140 98 VYTLALkTHVGMSIQTFRYFAGWCDK--IQGKTIPiNQARPNRNLTLTKRepiGVCGIVIPWNYPLMMLAWKMAACLAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 744 NSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAarDAAIGV 823
Cdd:cd07140 176 NTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA--VSNLKK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 824 LIAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPV 903
Cdd:cd07140 254 VSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 904 IDADALKILQDHAERMDRE-ARLIAAAELSAEAanGTFFAPRAYE--LKDLGQLQKEVFGPVLHVIRWKGDQLDAVIDQI 980
Cdd:cd07140 334 NHKAHLDKLVEYCERGVKEgATLVYGGKQVDRP--GFFFEPTVFTdvEDHMFIAKEESFGPIMIISKFDDGDVDGVLQRA 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590385370 981 NATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVTV 1056
Cdd:cd07140 412 NDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAA--PFGGFKQSGFG-KDLGEEALNEYLKTKTVTI 484
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
595-1056 |
1.22e-46 |
|
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: 174.14 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 595 LPVTNPADtREVVGQWLAADAATVQKAL--ANAVAAQPAwNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPD 672
Cdd:cd07148 1 LEVVNPFD-LKPIGEVPTVDWAAIDKALdtAHALFLDRN-NWLPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 673 SIAEVREAVDFLRYYAKQAREQFSHAEKL---PSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAK 749
Cdd:cd07148 79 AKVEVTRAIDGVELAADELGQLGGREIPMgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 750 PAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGAtVGAALTADPRVAGVAFTGSTDTARAINRAMAArdaaiGVLIA-ET 828
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLAP-----GTRCAlEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADA 908
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 909 LKILQDHA-ERMDREARLIAAAELSAEaangTFFAPRAY--ELKDLGQLQKEVFGPVLHVirWKGDQLDAVIDQINATGY 985
Cdd:cd07148 313 VDRVEEWVnEAVAAGARLLCGGKRLSD----TTYAPTVLldPPRDAKVSTQEIFGPVVCV--YSYDDLDEAIAQANSLPV 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590385370 986 GLTLGVHSRIDETVDRISNGVHVGNVYVNrNQIGAVVGVQPFGGQGLSGTGpkAGGPHYLLRFATEKTVTV 1056
Cdd:cd07148 387 AFQAAVFTKDLDVALKAVRRLDATAVMVN-DHTAFRVDWMPFAGRRQSGYG--TGGIPYTMHDMTQEKMAV 454
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
594-1054 |
9.45e-45 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 168.76 E-value: 9.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 594 ALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDS 673
Cdd:PRK09406 2 PIATINPA-TGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 674 IAEVREAVDFLRYYAKQArEQFSHAEklPSPTGESNELQLHGR----GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAK 749
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHA-EALLADE--PADAAAVGASRAYVRyqplGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 750 PAEQTNLIGYYAVKLLHDAGVPAEVVQ-FLPGDGATvgAALTADPRVAGVAFTGSTDTARAINrAMAARDAAIGVLiaET 828
Cdd:PRK09406 158 HASNVPQTALYLADLFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAVA-AIAGDEIKKTVL--EL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVID--- 905
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATeqg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 906 -ADALKILQDHA----------ERMDRearliaaaelsaeaaNGTFFAPR--AYELKDLGQLQKEVFGPVLHVIRwkGDQ 972
Cdd:PRK09406 313 rDEVEKQVDDAVaagatilcggKRPDG---------------PGWFYPPTviTDITPDMRLYTEEVFGPVASLYR--VAD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 973 LDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNrnqiGAVVGVQ--PFGGQGLSGTGPKAGGpHYLLRFAT 1050
Cdd:PRK09406 376 IDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN----GMTVSYPelPFGGVKRSGYGRELSA-HGIREFCN 450
|
....
gi 1590385370 1051 EKTV 1054
Cdd:PRK09406 451 IKTV 454
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
591-1014 |
1.43e-42 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 163.00 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSL 670
Cdd:PLN00412 29 SGKSVAITNPS-TRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 671 PDSIAEVREAVDFLRYYAKQAREQFSHAEKLPS---PTGESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGN 744
Cdd:PLN00412 108 KDAVTEVVRSGDLISYTAEEGVRILGEGKFLVSdsfPGNERNKYCLTSKiplGVVLAIPPFNYPVNLAVSKIAPALIAGN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 745 SVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGStDTARAInramaARDAAIGVL 824
Cdd:PLN00412 188 AVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAI-----SKKAGMVPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 825 IAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGlLSTDVGPVI 904
Cdd:PLN00412 262 QMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPE-DDCDITPVV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 905 ---DADALKILQDHAERMD--------REARLIAAAELSAEAAngtffaprayelkDLGQLQKEVFGPVLHVIRWKGDQl 973
Cdd:PLN00412 341 sesSANFIEGLVMDAKEKGatfcqewkREGNLIWPLLLDNVRP-------------DMRIAWEEPFGPVLPVIRINSVE- 406
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1590385370 974 dAVIDQINATGYGLTLGVHSR-IDETVdRISNGVHVGNVYVN 1014
Cdd:PLN00412 407 -EGIHHCNASNFGLQGCVFTRdINKAI-LISDAMETGTVQIN 446
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
613-1036 |
1.05e-41 |
|
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: 160.31 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 613 ADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSI-AEVREAVDFLRYYAKQA 691
Cdd:cd07116 35 STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFAGCI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 692 REQFSHAEKLpsptgESNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDA 768
Cdd:cd07116 115 RAQEGSISEI-----DENTVAYHFHeplGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 769 gVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRamAARDAAIGVLIaETGGQ--NAFIADSSALPEQLV 846
Cdd:cd07116 190 -LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQ--YASENIIPVTL-ELGGKspNIFFADVMDADDAFF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 847 KDAIGSAFTSA---GQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADAL-KILQDHAERMDRE 922
Cdd:cd07116 266 DKALEGFVMFAlnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLeKILSYIDIGKEEG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 923 ARLIA--AAELSAEAANGTFFAPRAYEL-KDLGQLQKEVFGPVLHVIRWKgDQLDAvIDQINATGYGLTLGVHSRIDETV 999
Cdd:cd07116 346 AEVLTggERNELGGLLGGGYYVPTTFKGgNKMRIFQEEIFGPVLAVTTFK-DEEEA-LEIANDTLYGLGAGVWTRDGNTA 423
|
410 420 430
....*....|....*....|....*....|....*..
gi 1590385370 1000 DRISNGVHVGNVYVnrNQIGAVVGVQPFGGQGLSGTG 1036
Cdd:cd07116 424 YRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
592-1054 |
7.98e-41 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 158.14 E-value: 7.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPAdTREVVGQWLAADAATVQKAL--ANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:PRK09847 34 NETFETVDPV-TQAPLAKIARGKSVDIDRAVsaARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIAE-VREAVDFLRYYAKQAREQFSHAeklpSPTGeSNELQLHGR---GVFVCISPWNFPLAIFLGQVAAALAAGNS 745
Cdd:PRK09847 113 IRHSLRDdIPGAARAIRWYAEAIDKVYGEV----ATTS-SHELAMIVRepvGVIAAIVPWNFPLLLTCWKLGPALAAGNS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 746 VIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRamAARDAAIGVLI 825
Cdd:PRK09847 188 VILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLK--DAGDSNMKRVW 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 826 AETGGQNAFI--ADSSALpEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPV 903
Cdd:PRK09847 266 LEAGGKSANIvfADCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 904 IDADALKILQDHAERMDREARLIAAAELSAEAAngtFFAPRAYELKD--LGQLQKEVFGPVLHVIRWKGDQldAVIDQIN 981
Cdd:PRK09847 345 IDCAHADSVHSFIREGESKGQLLLDGRNAGLAA---AIGPTIFVDVDpnASLSREEIFGPVLVVTRFTSEE--QALQLAN 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590385370 982 ATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVvgVQPFGGQGLSGTGpKAGGPHYLLRFATEKTV 1054
Cdd:PRK09847 420 DSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG-RDKSLHALEKFTELKTI 489
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
627-1054 |
1.01e-37 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 147.37 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 627 AAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS---------LPdSIAEVREAVDFLRYYAKqareqfsh 697
Cdd:cd07134 9 AHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPaaevdlteiLP-VLSEINHAIKHLKKWMK-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 698 AEKLPSPT---GESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEV 774
Cdd:cd07134 80 PKRVRTPLllfGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 775 VQFlPGDgATVGAALTADPrVAGVAFTGSTDTARAINRAmAARDAAIGVLiaETGGQNAFIADSSALPEQLVKDAIGSAF 854
Cdd:cd07134 160 AVF-EGD-AEVAQALLELP-FDHIFFTGSPAVGKIVMAA-AAKHLASVTL--ELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 855 TSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLL-STDVGPVID---ADALKILQDHAerMDREARLIaaaE 930
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNdrhFDRLKGLLDDA--VAKGAKVE---F 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 931 LSAEAANGTFFAPRAyeLKDLGQ----LQKEVFGPVLHVIRWkgDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGV 1006
Cdd:cd07134 309 GGQFDAAQRYIAPTV--LTNVTPdmkiMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1590385370 1007 HVGNVYVNRNQIGAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTV 1054
Cdd:cd07134 385 SSGGVVVNDVVLHFLNPNLPFGGVNNSGIG-SYHGVYGFKAFSHERAV 431
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
592-1057 |
1.11e-36 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 145.75 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 592 GAALPVTNPADTrEVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLP 671
Cdd:PLN02315 33 GPLVSSVNPANN-QPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 672 DSIAEVREAVDFLRYYAKQAREQfsHAEKLPSPTGESNELQL-HGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKP 750
Cdd:PLN02315 112 EGIGEVQEIIDMCDFAVGLSRQL--NGSIIPSERPNHMMMEVwNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 751 AEQTNLIGYYAVKL----LHDAGVPAEVVQFLPGdGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARdaaIGVLIA 826
Cdd:PLN02315 190 APTTPLITIAMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR---FGKCLL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 827 ETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDA 906
Cdd:PLN02315 266 ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 907 DALKILQDHAERMDREARLIaAAELSAEAANGTFFAPRAYELK-DLGQLQKEVFGPVLHVIRWKgdQLDAVIDQINATGY 985
Cdd:PLN02315 346 ESKKNFEKGIEIIKSQGGKI-LTGGSAIESEGNFVQPTIVEISpDADVVKEELFGPVLYVMKFK--TLEEAIEINNSVPQ 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590385370 986 GLTLGVHSRIDETVDRI--SNGVHVGNVYVNRNQIGAVVGvQPFGGQGLSGTGPKAGGPHYlLRFATEKTVTVN 1057
Cdd:PLN02315 423 GLSSSIFTRNPETIFKWigPLGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSDSW-KQYMRRSTCTIN 494
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
590-1014 |
4.03e-34 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 137.30 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAALPVtNPAdTREVVGQWLAADAATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKS 669
Cdd:PRK13968 5 PATHAISV-NPA-TGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 670 LPDSIAEVREAVDFLRYYAKQAREQFShaeklPSPTGESNE---LQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSV 746
Cdd:PRK13968 83 INQARAEVAKSANLCDWYAEHGPAMLK-----AEPTLVENQqavIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 747 IAKPAeqTNLIGYYAV--KLLHDAGVPAEVVQFLPGDGATVGAALTaDPRVAGVAFTGSTDTARAINramAARDAAIGVL 824
Cdd:PRK13968 158 LLKHA--PNVMGCAQLiaQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIG---AQAGAALKKC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 825 IAETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGLLSTDVGPVI 904
Cdd:PRK13968 232 VLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 905 DADALKILQDHAER-MDREARLIAAAELSAEAANgtFFAPR--AYELKDLGQLQKEVFGPVLHVIRWKgdQLDAVIDQIN 981
Cdd:PRK13968 312 RFDLRDELHHQVEAtLAEGARLLLGGEKIAGAGN--YYAPTvlANVTPEMTAFREELFGPVAAITVAK--DAEHALELAN 387
|
410 420 430
....*....|....*....|....*....|...
gi 1590385370 982 ATGYGLTLGVHSRIDETVDRISNGVHVGNVYVN 1014
Cdd:PRK13968 388 DSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
717-1036 |
7.05e-33 |
|
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: 132.65 E-value: 7.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 717 GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQT----NLIgyyaVKLLHDAgVPAEVVQFLPGdGATVGAALTAD 792
Cdd:cd07087 102 GVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELApatsALL----AKLIPKY-FDPEAVAVVEG-GVEVATALLAE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 793 PrVAGVAFTGSTDTARAINRAmAARDAAIGVLiaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDD 872
Cdd:cd07087 176 P-FDHIFFTGSPAVGKIVMEA-AAKHLTPVTL--ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 873 IADKVMTMLAGAMKELkVGNPGLLSTDVGPVIDadalkilQDHAERMdreARLIAAAELSA---EAANGTFFAPRAYELK 949
Cdd:cd07087 252 IKDELIEELKKAIKEF-YGEDPKESPDYGRIIN-------ERHFDRL---ASLLDDGKVVIggqVDKEERYIAPTILDDV 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 950 DLGQ--LQKEVFGPVLHVIRWkgDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPF 1027
Cdd:cd07087 321 SPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPF 398
|
....*....
gi 1590385370 1028 GGQGLSGTG 1036
Cdd:cd07087 399 GGVGNSGMG 407
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
618-1051 |
1.08e-32 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 132.75 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 618 VQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSlPDSIAEVREAVDFLRYYAKQAREQFSH 697
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 698 ---AEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAG-VPAE 773
Cdd:cd07084 80 hepGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 774 VVQFLPGDGATvGAALTADPRVAGVAFTGSTDTARAInramaARDAAIGVLIAETGGQN-AFIADSSALPEQLVKDAIGS 852
Cdd:cd07084 160 DVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKL-----ALDAKQARIYLELAGFNwKVLGPDAQAVDYVAWQCVQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 853 AFTSAGQRCSAARVLFV-QDDIADKVMTMLAGAMKELKVGnpgllSTDVGPVIDADALKILQdHAERMD--------REA 923
Cdd:cd07084 234 MTACSGQKCTAQSMLFVpENWSKTPLVEKLKALLARRKLE-----DLLLGPVQTFTTLAMIA-HMENLLgsvllfsgKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 924 RLIAAAELSAEAANGTFFAPRAYELKDLGQLQKEVFGPVLHVIRWKGDQLDAVIDQINATGYGLTLGVHSRIDETVDRI- 1002
Cdd:cd07084 308 KNHSIPSIYGACVASALFVPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELi 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1590385370 1003 ----SNGVHVGNvyvNRNQIGAVVGVQPFGGQGLSGTGPKAGGP---HYLLRFATE 1051
Cdd:cd07084 388 gnlwVAGRTYAI---LRGRTGVAPNQNHGGGPAADPRGAGIGGPeaiKLVWRCHAE 440
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
621-980 |
1.25e-28 |
|
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: 120.72 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 621 ALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQARE------Q 694
Cdd:cd07129 4 AAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgswldaR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 695 FSHAEKLPSPTGESN-ELQLHGRGVFVCISPWNFPLAIFL--GQVAAALAAGNSVIAK--PA--EQTNLIGYYAVKLLHD 767
Cdd:cd07129 84 IDPADPDRQPLPRPDlRRMLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhpGTSELVARAIRAALRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 768 AGVPAEVVQFLPGDGATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAIGVLiAETGGQNAFIADSSAL---PEQ 844
Cdd:cd07129 164 TGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIPFY-AELGSVNPVFILPGALaerGEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 845 LVKDAIGSAFTSAGQRCSAARVLFVQDDIA-DKVMTMLAGAMKELKVG---NPGLLSTdvgpviDADALKILQDHAermD 920
Cdd:cd07129 243 IAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQtmlTPGIAEA------YRQGVEALAAAP---G 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590385370 921 REARLIAAAELSAEAANGTFFAPRAYELKDLGQLQKEVFGPVLHVIRWKG-DQLDAVIDQI 980
Cdd:cd07129 314 VRVLAGGAAAEGGNQAAPTLFKVDAAAFLADPALQEEVFGPASLVVRYDDaAELLAVAEAL 374
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
693-1036 |
5.50e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 119.36 E-value: 5.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 693 EQFSHAEKLPSPTG---ESNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEqtnlIGYYAVKLLH--- 766
Cdd:PTZ00381 84 DEYLKPEKVDTVGVfgpGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSE----LSPHTSKLMAkll 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 767 DAGVPAEVVQFLPGdGATVGAALTADPrVAGVAFTGSTDTARAINRAmAARDAAIGVLiaETGGQNAFIADSSALPEQLV 846
Cdd:PTZ00381 160 TKYLDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQA-AAENLTPCTL--ELGGKSPVIVDKSCNLKVAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 847 KDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELkVGNPGLLSTDVGPVIDADALKILQD----------HA 916
Cdd:PTZ00381 235 RRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAElikdhggkvvYG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 917 ERMDREARLIaaaelsaeaangtffAPRAYELKDLGQ--LQKEVFGPVLHVIRWKgdQLDAVIDQINATGYGLTLGVHSR 994
Cdd:PTZ00381 314 GEVDIENKYV---------------APTIIVNPDLDSplMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGE 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1590385370 995 IDETVDRISNGVHVGNVYVNRnqigAVVGVQ----PFGGQGLSGTG 1036
Cdd:PTZ00381 377 DKRHKELVLENTSSGAVVIND----CVFHLLnpnlPFGGVGNSGMG 418
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
716-1054 |
9.47e-27 |
|
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: 114.62 E-value: 9.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 716 RGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNligyYAVKLLHD---AGVPAEVVQFLPGDGATVGAALtaD 792
Cdd:cd07135 109 LGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTP----HTAALLAElvpKYLDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 793 PRVAGVAFTGSTDTARAINRAmAARDAAIGVLiaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDD 872
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIAEA-AAKHLTPVTL--ELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 873 IADKVMTMLAGAMKELkvgNPGLLSTD------VGP--------VIDADALKILQDHaeRMDREARliaaaelsaeaang 938
Cdd:cd07135 260 VYDEFVEELKKVLDEF---YPGGANASpdytriVNPrhfnrlksLLDTTKGKVVIGG--EMDEATR-------------- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 939 tFFAP--RAYELKDLGQLQKEVFGPVLHVIrwKGDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRN 1016
Cdd:cd07135 321 -FIPPtiVSDVSWDDSLMSEELFGPVLPII--KVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDT 397
|
330 340 350
....*....|....*....|....*....|....*...
gi 1590385370 1017 QIGAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTV 1054
Cdd:cd07135 398 LIHVGVDNAPFGGVGDSGYG-AYHGKYGFDTFTHERTV 434
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
563-1014 |
4.34e-26 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 114.84 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 563 NELRALAEQINAAVKPW-----------QAAPLVPG-------ANPAGAALPVTNPAdTREVVGQWLAADAATVQKALAN 624
Cdd:PLN02419 81 NNLRPLRPQFLALRSSWlstspeqstqpQMPPRVPNliggsfvESQSSSFIDVINPA-TQEVVSKVPLTTNEEFKAAVSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 625 AVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFshAEKLPSP 704
Cdd:PLN02419 160 AKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQM--GEYLPNV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 705 TGESNELQL-HGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGA 783
Cdd:PLN02419 238 SNGVDTYSIrEPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTND 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 784 TVGaALTADPRVAGVAFTGSTDTARAInramAARDAAIGVLI-AETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCS 862
Cdd:PLN02419 318 TVN-AICDDEDIRAVSFVGSNTAGMHI----YARAAAKGKRIqSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCM 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 863 A-ARVLFVQDdiADKVMTMLAGAMKELKVGNPGLLSTDVGPVIDADAL-KILQDHAERMDREARLIAAAELSAEA--ANG 938
Cdd:PLN02419 393 AlSTVVFVGD--AKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKeRICRLIQSGVDDGAKLLLDGRDIVVPgyEKG 470
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590385370 939 TFFAPRAYE--LKDLGQLQKEVFGPVLhvIRWKGDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVN 1014
Cdd:PLN02419 471 NFIGPTILSgvTPDMECYKEEIFGPVL--VCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
673-1054 |
5.59e-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: 109.11 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 673 SIAEVREAVDFLRYYAKQAREqfsHAEKLPSPTgeSNELQLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAE 752
Cdd:cd07133 64 SIAGIKHARKHLKKWMKPSRR---HVGLLFLPA--KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 753 ---QTN-LIgyyaVKLLHDAGVPAEVVQFLpgDGATVGAALTADPrVAGVAFTGSTDTARAINRAmAARDAAIGVLiaET 828
Cdd:cd07133 139 ftpRTSaLL----AELLAEYFDEDEVAVVT--GGADVAAAFSSLP-FDHLLFTGSTAVGRHVMRA-AAENLTPVTL--EL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 829 GGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKEL---KVGNPgllstDVGPVID 905
Cdd:cd07133 209 GGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIIN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 906 ADALKILQ---DHAErmDREARLIAAAELSAEAANGTFFAPRA-YELKDLGQL-QKEVFGPVLHVIRWkgDQLDAVIDQI 980
Cdd:cd07133 284 ERHYARLQgllEDAR--AKGARVIELNPAGEDFAATRKLPPTLvLNVTDDMRVmQEEIFGPILPILTY--DSLDEAIDYI 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590385370 981 NATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQGLSGTGpkaggpHY-----LLRFATEKTV 1054
Cdd:cd07133 360 NARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMG------AYhgkegFLTFSHAKPV 432
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
591-926 |
5.82e-20 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 94.77 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 591 AGAALPVTNPADTREVVgqwlAADAATVQKALANAVAAQ---PAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAG 667
Cdd:PRK11903 17 SGAGTPLFDPVTGEELV----RVSATGLDLAAAFAFAREqggAALRALTYAQRAALLAAIVKVLQANRDAYYDIATANSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 668 KSLPDSIAEVREAVDFLRYYAKqAREQFSHAEKLP---------SPTGESNELQLHGRGVFVCISPWNFPLAIFLGQVAA 738
Cdd:PRK11903 93 TTRNDSAVDIDGGIFTLGYYAK-LGAALGDARLLRdgeavqlgkDPAFQGQHVLVPTRGVALFINAFNFPAWGLWEKAAP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 739 ALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGV-PAEVVQFLPGDGATVGAALTADPRVAgvaFTGSTDTARAI--NRAMA 815
Cdd:PRK11903 172 ALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVVS---FTGSAETAAVLrsHPAVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 816 ARDAAIGVliaETGGQNAFI-----ADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELKV 890
Cdd:PRK11903 249 QRSVRVNV---EADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTV 325
|
330 340 350
....*....|....*....|....*....|....*.
gi 1590385370 891 GNPGLLSTDVGPVIDADALKILQDHAERMDREARLI 926
Cdd:PRK11903 326 GNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVL 361
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
590-962 |
7.58e-20 |
|
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: 94.26 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 590 PAGAALPVTNPAdTREVVgqwlaADAATVQKALANAVA-----AQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVK 664
Cdd:cd07128 12 GTGDGRTLHDAV-TGEVV-----ARVSSEGLDFAAAVAyarekGGPALRALTFHERAAMLKALAKYLMERKEDLYALSAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 665 eAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEKLPSPTGE--SNELQLHGR-------GVFVCISPWNFPLAIFLGQ 735
Cdd:cd07128 86 -TGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVEplSKDGTFVGQhiltprrGVAVHINAFNFPVWGMLEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 736 VAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGV-PAEVVQFLPGDGATVGAALtaDPRVAgVAFTGSTDTARAINRAM 814
Cdd:cd07128 165 FAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHL--GEQDV-VAFTGSAATAAKLRAHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 815 AARDAAIGVlIAETGGQNAFIADSSALPEQ-----LVKDAIGSAFTSAGQRCSAARVLFVQDDIADKVMTMLAGAMKELK 889
Cdd:cd07128 242 NIVARSIRF-NAEADSLNAAILGPDATPGTpefdlFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 890 VGNPGLLSTDVGPVIDADALKILQDHAERMDREARLI-----AAAELSAEAANGTFFAP---RAYELKDLGQL-QKEVFG 960
Cdd:cd07128 321 VGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVfggpdRFEVVGADAEKGAFFPPtllLCDDPDAATAVhDVEAFG 400
|
..
gi 1590385370 961 PV 962
Cdd:cd07128 401 PV 402
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
717-1036 |
1.01e-18 |
|
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: 90.36 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 717 GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNligyyavkllHDAGVPAEVV-QFLPGDGATV---GAALTA- 791
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP----------ATAKLLAELIpKYLDKECYPVvlgGVEETTe 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 792 --DPRVAGVAFTGSTDTARAINRAmAARDAAIGVLiaETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFV 869
Cdd:cd07132 172 llKQRFDYIFYTGSTSVGKIVMQA-AAKHLTPVTL--ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 870 QDDIADKVMTMLAGAMKELkVGNPGLLSTDVGPVIDADALKILQD--------HAERMDREARLIaaaelsaeaangtff 941
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKKllsggkvaIGGQTDEKERYI--------------- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 942 APRAyeLKDLGQ----LQKEVFGPVLHVIRWKGdqLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQ 1017
Cdd:cd07132 313 APTV--LTDVKPsdpvMQEEIFGPILPIVTVNN--LDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTI 388
|
330
....*....|....*....
gi 1590385370 1018 IGAVVGVQPFGGQGLSGTG 1036
Cdd:cd07132 389 MHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
717-1036 |
5.43e-18 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 87.94 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 717 GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQT----NLIgyyaVKLLHDAgVPAEVVQFLPGDGATVGAALtaD 792
Cdd:cd07136 102 GVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTpntsKVI----AKIIEET-FDEEYVAVVEGGVEENQELL--D 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 793 PRVAGVAFTGSTDTARAINRAmAARDaaigvLIA---ETGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFV 869
Cdd:cd07136 175 QKFDYIFFTGSVRVGKIVMEA-AAKH-----LTPvtlELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 870 QDDIADKVMTMLAGAMKELKVGNPgLLSTDVGPVIDA---DALKILQDHAE-----RMDREARLIaaaeLSAEAANGTFF 941
Cdd:cd07136 249 HESVKEKFIKELKEEIKKFYGEDP-LESPDYGRIINEkhfDRLAGLLDNGKivfggNTDRETLYI----EPTILDNVTWD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 942 APrayelkdlgQLQKEVFGPVLHVIRWkgDQLDAVIDQINATGYGLTLGVHSRiDETV-----DRISNG--------VHV 1008
Cdd:cd07136 324 DP---------VMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSE-DKKVekkvlENLSFGggcindtiMHL 391
|
330 340
....*....|....*....|....*...
gi 1590385370 1009 GNVYVnrnqigavvgvqPFGGQGLSGTG 1036
Cdd:cd07136 392 ANPYL------------PFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
717-1036 |
4.15e-17 |
|
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: 85.16 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 717 GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEqtnlIGYYAVKLLHD---AGVPAEVVQFLPGdGATVGAALTaDP 793
Cdd:cd07137 103 GVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSE----LAPATSALLAKlipEYLDTKAIKVIEG-GVPETTALL-EQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 794 RVAGVAFTGSTDTARAInraMAARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAIGSAFTS-AGQRCSAARVLFVQDD 872
Cdd:cd07137 177 KWDKIFFTGSPRVGRII---MAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVEES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 873 IADKVMTMLAGAMKELKVGNPgLLSTDVGPVIDADALKILQD------------HAERMDREARLIAAAELSAeaangtf 940
Cdd:cd07137 254 FAPTLIDALKNTLEKFFGENP-KESKDLSRIVNSHHFQRLSRllddpsvadkivHGGERDEKNLYIEPTILLD------- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 941 fAPRAYELkdlgqLQKEVFGPVLHVIRWKGdqLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGA 1020
Cdd:cd07137 326 -PPLDSSI-----MTEEIFGPLLPIITVKK--IEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQY 397
|
330
....*....|....*.
gi 1590385370 1021 VVGVQPFGGQGLSGTG 1036
Cdd:cd07137 398 AIDTLPFGGVGESGFG 413
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
663-830 |
4.49e-17 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 86.84 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 663 VKEAGKSLPDSIAEVREAVDFLRYYAKQAREQFSHAEKLPSPTGESNELQLHGRGVFVCISPwnfPLAIFLGQVAAALAA 742
Cdd:PRK11905 1026 TDAAARDFLAWLDKEGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCVAD---TEEALLRQLAAALAT 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 743 GNSVIakpaeqtnligyyavklLHDAGVPAEVVQFLPGD---GATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDA 819
Cdd:PRK11905 1103 GNVAV-----------------VAADSGLAAALADLPGLvaaRIDWTQDWEADDPFAGALLEGDAERARAVRQALAARPG 1165
|
170
....*....|.
gi 1590385370 820 AIGVLIAETGG 830
Cdd:PRK11905 1166 AIVPLIAAEPT 1176
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
722-993 |
1.43e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 81.00 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 722 ISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGAALT-ADPRVagVAF 800
Cdd:cd07126 149 ITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLeANPRM--TLF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 801 TGSTDTARAINRAMAARdaaigVLIAETG------GQNafIADSSALPEQLVKDaigsAFTSAGQRCSAARVLF-----V 869
Cdd:cd07126 227 TGSSKVAERLALELHGK-----VKLEDAGfdwkilGPD--VSDVDYVAWQCDQD----AYACSGQKCSAQSILFahenwV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 870 QDDIADKvMTMLAGAMKelkvgnpgLLSTDVGPVIDADALKILqDHAERMDR--EARLI----AAAELSAEAANGTF--- 940
Cdd:cd07126 296 QAGILDK-LKALAEQRK--------LEDLTIGPVLTWTTERIL-DHVDKLLAipGAKVLfggkPLTNHSIPSIYGAYept 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 941 --FAP--RAYELKDLGQLQKEVFGPVLHVIRWKGDQLDAVIDQINATGYGLTLGVHS 993
Cdd:cd07126 366 avFVPleEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVS 422
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
717-1055 |
6.57e-13 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 72.45 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 717 GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQT--------NLIGYY----AVKllhdagvpaeVVQflpgDGAT 784
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELApatsaflaANIPKYldskAVK----------VIE----GGPA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 785 VGAALTaDPRVAGVAFTGSTDTARAInraMAARDAAIGVLIAETGGQNAFIADSSALP---EQLVKDAIGSAFTS-AGQR 860
Cdd:PLN02203 176 VGEQLL-QHKWDKIFFTGSPRVGRII---MTAAAKHLTPVALELGGKCPCIVDSLSSSrdtKVAVNRIVGGKWGScAGQA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 861 CSAARVLFVQDDIADKVMTMLAGAMKELKVGNPGllstdvgpviDADAL-KILQDHaeRMDREARLIAAAELSAEAANGT 939
Cdd:PLN02203 252 CIAIDYVLVEERFAPILIELLKSTIKKFFGENPR----------ESKSMaRILNKK--HFQRLSNLLKDPRVAASIVHGG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 940 FFAPRAYELK---------DLGQLQKEVFGPVLHVIRWKgdQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGN 1010
Cdd:PLN02203 320 SIDEKKLFIEptillnpplDSDIMTEEIFGPLLPIITVK--KIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGS 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1590385370 1011 VYVNRNQIGAVVGVQPFGGQGLSGTGpKAGGPHYLLRFATEKTVT 1055
Cdd:PLN02203 398 VTFNDAIIQYACDSLPFGGVGESGFG-RYHGKYSFDTFSHEKAVL 441
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
29-76 |
6.82e-13 |
|
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: 64.02 E-value: 6.82e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1590385370 29 NPFRQAITDGWLKDEASHVRELLAQARLPAEEQAKVQALAADLVGRVR 76
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
300-498 |
9.31e-13 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 71.66 E-value: 9.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 300 ELAQLAKSYGIGCTVDAEES------DRLELSLDIieqVFSDAslagwDGFGVV---VQAYQKRTPytiDHLADMARRAG 370
Cdd:PLN02681 224 KLCERAAQLGVPLLIDAEYTslqpaiDYITYDLAR---EFNKG-----KDRPIVygtYQAYLKDAR---ERLRLDLERSE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 371 RR---LQVRLVKGAYWDAEIKRAQIEGYPGyPVFTRKQNTDVSYLACAKRLFTHA----DAIypMFATHNAHTI-AAVRS 442
Cdd:PLN02681 293 REgvpLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAEFLLEKAsngdGEV--MLATHNVESGeLAAAK 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590385370 443 IA-------NGGVYEHQkLHGMGDDLYAEVVPADrlnlpCRV--YAPVGSHEDLLPYLVRRLLEN 498
Cdd:PLN02681 370 MNelglhkgDPRVQFAQ-LLGMSDNLSFGLGNAG-----FRVskYLPYGPVEEVIPYLLRRAEEN 428
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
717-1040 |
1.19e-11 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 68.53 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 717 GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDAGVPAeVVQFLpgDGATVGAALTADPRVA 796
Cdd:PLN02174 114 GVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS-AVRVV--EGAVTETTALLEQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 797 GVAFTGSTDTARAInraMAARDAAIGVLIAETGGQNAFIADSSALPEQLVKDAI-GSAFTSAGQRCSAARVLFVQDDIAD 875
Cdd:PLN02174 191 KIFYTGSSKIGRVI---MAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIaGKWGCNNGQACISPDYILTTKEYAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 876 KVMTMLAGAMKELKVGNPgLLSTDVGPVIDA---DALKILQDHAERMDRearliaAAELSAEAANGTFFAPRAYELKDLG 952
Cdd:PLN02174 268 KVIDAMKKELETFYGKNP-MESKDMSRIVNSthfDRLSKLLDEKEVSDK------IVYGGEKDRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 953 QL--QKEVFGPVLHVIrwKGDQLDAVIDQINATGYGLTLGVHSRIDETVDRISNGVHVGNVYVNRNQIGAVVGVQPFGGQ 1030
Cdd:PLN02174 341 SLimSEEIFGPLLPIL--TLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGV 418
|
330
....*....|
gi 1590385370 1031 GLSGTGPKAG 1040
Cdd:PLN02174 419 GESGMGAYHG 428
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
693-833 |
1.33e-11 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 69.20 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 693 EQFSHAEKLPSPTGESNELQLHGRGVFVCISPwnfPLAIFLGQVAAALAAGNSVIAKPAEQTnligyyavkllhdAGVPA 772
Cdd:COG4230 1040 ASLLGALTLPGPTGERNTLTLRPRGRVLCLAD---SLEALLAQLAAALATGNRAVVAADLAL-------------AGLPA 1103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590385370 773 EVvqflpgdgatvgaaltaDPRVAGVAFTGstdTARAINRAMAARDAAI-GV---------LIAETGGqNA 833
Cdd:COG4230 1104 VL-----------------LPPFDAVLFEG---RLRALRQALAARDGAIvPVidagydlerLLEEAGG-NA 1153
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
619-821 |
3.30e-10 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 64.61 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 619 QKALANAVAAQPAWNRTPAASRAAILE-HAA--DQLEARMPEFMALCvkeagkslpdsiaevreavdflRYYAKQAreQF 695
Cdd:PRK11809 1112 EDALAVTLARQDAEYPVDAQLRAALLApLTAlrEWAAEREPELAALC----------------------DQYAELA--QA 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 696 SHAEKLPSPTGESNELQLHGRGVFVCISPWNFPLAIflgQVAAALAAGNSVIAKPAEQTNligyyavKLLhdAGVPAEVV 775
Cdd:PRK11809 1168 GTTRLLPGPTGERNTYTLLPRERVLCLADTEQDALT---QLAAVLAVGSQALWPDDALHR-------ALV--AALPAAVQ 1235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1590385370 776 QFLpgdgATVGAALTADPRVAGVAFTGSTDTARAINRAMAARDAAI 821
Cdd:PRK11809 1236 ARI----QLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPI 1277
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
616-1014 |
1.82e-09 |
|
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: 61.73 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 616 ATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMALCVKEAGKSL--------PDSIAEVREAVDflryY 687
Cdd:cd07127 84 CDPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFmmafqaggPHAQDRGLEAVA----Y 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 688 AKQAREQFSHAEKLPSPTGESNELQLH------GRGVFVCIS-----PWNFPLAIFlgqvaAALAAGNSVIAKPAEQTNL 756
Cdd:cd07127 160 AWREMSRIPPTAEWEKPQGKHDPLAMEktftvvPRGVALVIGcstfpTWNGYPGLF-----ASLATGNPVIVKPHPAAIL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 757 IGYYAVK----LLHDAGVPAEVVQ---FLPGDGATvgAALTADPRVAGVAFTGSTDTARAINRamAARDAaigVLIAETG 829
Cdd:cd07127 235 PLAITVQvareVLAEAGFDPNLVTlaaDTPEEPIA--QTLATRPEVRIIDFTGSNAFGDWLEA--NARQA---QVYTEKA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 830 GQNAFIADSSalpEQLVKDAIGSAFTSA---GQRCSAARVLFV-QDDIA--------DKVMTMLAGAMKELkVGNPGLLS 897
Cdd:cd07127 308 GVNTVVVDST---DDLKAMLRNLAFSLSlysGQMCTTPQNIYVpRDGIQtddgrksfDEVAADLAAAIDGL-LADPARAA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 898 TDVGPVIDadalkilQDHAERMDREARLIAAAELSAEAANGTFFAPR-------AYELKDLGQLQKEVFGPVLHVIrwKG 970
Cdd:cd07127 384 ALLGAIQS-------PDTLARIAEARQLGEVLLASEAVAHPEFPDARvrtplllKLDASDEAAYAEERFGPIAFVV--AT 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590385370 971 DQLDAVID---QINATGYGLTLGVHSRIDETVDRISN-----GVHV-----GNVYVN 1014
Cdd:cd07127 455 DSTDHSIElarESVREHGAMTVGVYSTDPEVVERVQEaaldaGVALsinltGGVFVN 511
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
717-1003 |
9.17e-06 |
|
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: 49.57 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 717 GVFVCISPWNFPLAIFLGQVAAALAAGNSVIAKPAEQTNLIGYYAVKLLHDA----GVPAEVVQFLPGDGATVGAALTAD 792
Cdd:cd07081 97 GVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 793 PRVAGVAFTGSTDTARAinrAMAARDAAIGVliaeTGGQNAFIADSSALPEQLVKDAIGSAFTSAGQRCSAARVLFVQDD 872
Cdd:cd07081 177 PGIGLLLATGGPAVVKA---AYSSGKPAIGV----GAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 873 IADKVMTMLAG------AMKELKVGNPGLLST-DVGP-VIDADALKILQDHAERMDREARLIAAAELSAEAANgtFFApr 944
Cdd:cd07081 250 VYDEVMRLFEGqgayklTAEELQQVQPVILKNgDVNRdIVGQDAYKIAAAAGLKVPQETRILIGEVTSLAEHE--PFA-- 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590385370 945 ayelkdlgqlqKEVFGPVLHVIRWKG--DQLDAVIDQINATGYGLTLGVHSRIDETVDRIS 1003
Cdd:cd07081 326 -----------HEKLSPVLAMYRAANfaDADAKALALKLEGGCGHTSAMYSDNIKAIENMN 375
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
638-914 |
1.77e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 48.37 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 638 ASRAAILEHAADQLEARMPEFMALCVKEAGKSLPDSIAEVREAV----DFLRYYAKQAREQFSHAEKLPSPTGESN---E 710
Cdd:cd07077 16 EQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMgcseSKLYKNIDTERGITASVGHIQDVLLPDNgetY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 711 LQLHGRGVFVCISPWNFPLAIfLGQVAAALAAGNSVIAKP---AEQTNLIGYYAVKLLHDAGVPAEVVQFLPGDGATVGA 787
Cdd:cd07077 96 VRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPhpsAPFTNRALALLFQAADAAHGPKILVLYVPHPSDELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 788 ALTADPRVAGVAFTGSTDTARAINRAMAARDaaigvLIAETGGQNAFIADSSALPEQLVKDAIGSAFTSaGQRCSAARVL 867
Cdd:cd07077 175 ELLSHPKIDLIVATGGRDAVDAAVKHSPHIP-----VIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNL 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1590385370 868 FVQDDIADKVMTMLAGAMKELKVG---NPGLLSTDVGPVIDADALKILQD 914
Cdd:cd07077 249 YVVDDVLDPLYEEFKLKLVVEGLKvpqETKPLSKETTPSFDDEALESMTP 298
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
615-890 |
1.40e-04 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 45.44 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 615 AATVQKALANAVAAQPAWNRTPAASRAAILEHAADQLEARMPEFMA------LCVKEAGKSLP------------DSIAE 676
Cdd:PRK00197 3 MEYLEELGRRAKAASRKLAQLSTAQKNRALLAIADALEANAAEILAanakdlAAARANGLSAAmldrlllteariEGIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 677 -VREAVdflryyakqareqfshaeKLPSPTGEsnelqlhgrgvfvCISPWNFPLAIFLGQV------------------- 736
Cdd:PRK00197 83 gLRQVA------------------ALPDPVGE-------------VLDGWTLPNGLRIGRVrvplgvigviyesrpnvtv 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 737 -AAALA--AGNSVI---AKPAEQTNLIgyyAVKLLHDA----GVPAEVVQFLPG-DGATVGAALTAD-------PRvagv 798
Cdd:PRK00197 132 dAAALClkSGNAVIlrgGSEAIHSNRA---LVAVIQEAleeaGLPADAVQLVETtDRAAVGELLKLDgyvdviiPR---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590385370 799 aftGStdtARAINRAMaaRDAAIGVLiaETG-GQNAFIADSSALPEQlvkdAIGSAFTSAGQR---CSAARVLFVQDDIA 874
Cdd:PRK00197 205 ---GG---AGLIRRVV--ENATVPVI--EHGdGICHIYVDESADLDK----ALKIVLNAKTQRpsvCNALETLLVHEAIA 270
|
330
....*....|....*.
gi 1590385370 875 DKVMTMLAGAMKELKV 890
Cdd:PRK00197 271 EEFLPKLAEALAEAGV 286
|
|
| |
