|
Name |
Accession |
Description |
Interval |
E-value |
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
1-1320 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 2914.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1 MGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLENSDTLPELPALLSGAANESDEAPTPAEEPHQPFLD 80
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADTPAEEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 81 FAEQILPQSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRNQKNASGRAGMVQGLLQEFSLSSQ 160
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGRAGMVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEASLSRSLNRIIGKSG 240
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGI 320
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 401 FVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLI 480
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 481 YPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 561 GANTSFVNRIADTSLPLDELVADPVTAVEKLAQQEGQTGLPHPKIPLPRDLYGHGRDNSAGLDLANEHRLASLSSALLNS 640
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLAS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 641 ALQKWQALPMLEQPVAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQ 720
Cdd:PRK11809 641 AHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQ 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 721 MQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:PRK11809 721 MQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 801 AKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPL 880
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 881 IAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVI 960
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 961 DSEAKVNIERHIQTMRSKGRPVFQAVRENSEDareWQSGTFVAPTLIELDDFAELQKEVFGPVLHVVRYNRNQLPELIEQ 1040
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSED---WQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQ 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLANRPESALAV 1120
Cdd:PRK11809 1038 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAV 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1121 TLARQDAEYPVDAQLKAALTQPLNALREWAANR-PELQALCTQYGELAQAGTQRLLPGPTGERNTWTLLPRERVLCIADD 1199
Cdd:PRK11809 1118 TLARQDAEYPVDAQLRAALLAPLTALREWAAERePELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADT 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1200 EQDALTQLAAVLAVGSQVLWPDDALHRQLVKALPSAVSERIQLAKAENITAQPFDAVIFHGDSDQLRALCEAVAARDGAI 1279
Cdd:PRK11809 1198 EQDALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPI 1277
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|.
gi 157066218 1280 VSVQGFARGESNILLERLYIERSLSVNTAAAGGNASLMTIG 1320
Cdd:PRK11809 1278 VSVQGFARGETNILLERLLIERSLSVNTAAAGGNASLMTIG 1318
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
77-1320 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 2047.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 77 PFLDFAEQILPQSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRnqknASGRAGMVQGLLQEFS 156
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALR----AKRKGTGVEALLQEYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 157 LSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEASLSRSLNRII 236
Cdd:PRK11905 77 LSSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASN 316
Cdd:PRK11905 157 ARLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 317 GRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGW 396
Cdd:PRK11905 237 GRGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 397 NGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAV 476
Cdd:PRK11905 317 NGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 477 PNLIYPQFATHNAHTLAAIYQLAGQNYypgQYEFQCLHGMGEPLYEQVTGKvadGKLNRPCRIYAPVGTHETLLAYLVRR 556
Cdd:PRK11905 397 RDVIYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGK---EKLGRPCRIYAPVGTHETLLAYLVRR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 557 LLENGANTSFVNRIADTSLPLDELVADPVTAVEKLAqqegqtGLPHPKIPLPRDLYGHGRDNSAGLDLANEHRLASLSSA 636
Cdd:PRK11905 471 LLENGANSSFVNRIVDENVPVEELIADPVEKVAAMG------VAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 637 LLNSALQKWQALPMLEQPVAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVL 716
Cdd:PRK11905 545 LNAFAAKTWHAAPLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADL 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 717 MESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAG 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 797 NSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqGR 876
Cdd:PRK11905 705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GP 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 877 PIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:PRK11905 782 PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDV 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 957 GPVIDSEAKVNIERHIQTMRSKGRPVFQAvrensEDAREWQSGTFVAPTLIELDDFAELQKEVFGPVLHVVRYNRNQLPE 1036
Cdd:PRK11905 862 GPVIDAEAQANIEAHIEAMRAAGRLVHQL-----PLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDR 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1037 LIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLANRPES 1116
Cdd:PRK11905 937 VIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTP 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1117 ALAVTlarqdaeypVDAQLKAALTQPLNALREWAanRPELQALCTQYGELAQAGTQRLLPGPTGERNTWTLLPRERVLCI 1196
Cdd:PRK11905 1017 IPPAH---------ESVDTDAAARDFLAWLDKEG--KAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCV 1085
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1197 ADDEQDALTQLAAVLAVGSQVLWPDDALHRQLVKALPSAVSERIQLAKAENiTAQPFDAVIFHGDSDQLRALCEAVAARD 1276
Cdd:PRK11905 1086 ADTEEALLRQLAAALATGNVAVVAADSGLAAALADLPGLVAARIDWTQDWE-ADDPFAGALLEGDAERARAVRQALAARP 1164
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 157066218 1277 GAIVSVQGfARGESNILLERLYIERSLSVNTAAAGGNASLMTIG 1320
Cdd:PRK11905 1165 GAIVPLIA-AEPTDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
77-1317 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1593.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 77 PFLDFAEQILPQSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHklayqlADKLRNQKNASGRAGMVQGLLQEFS 156
Cdd:COG4230 2 PFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAA------AAALAARERVRARRGGGGGLLLLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 157 LSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEAS--LSRSLNR 234
Cdd:COG4230 76 LSSLSSEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSlsLASGLLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 235 IIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKA 314
Cdd:COG4230 156 LLGRLGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 315 SNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELA 394
Cdd:COG4230 236 AGGGSGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 395 GWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRR----LMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACA 470
Cdd:COG4230 316 GGLGGGGGVGQAVQAYAKALLLVLDLLARRRRRrrrrLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 471 KKLLAVPNLIYPQFATHNAHTLAAIYQLAGQnyypGQYEFQCLHGMGEPLYEQvtgkVADGKLNRPCRIYAPVGTHETLL 550
Cdd:COG4230 396 LLLLAAQPAFAPQFATHAAATAAAAAAAGGG----GEFEFQCLHGMGEYLYDQ----VGRGKLGRPCRIYAPVGSHEDLL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 551 AYLVRRLLENGANTSFVNRIADTSLPLDELVADPVTAVEKLAqqegqtGLPHPKIPLPRDLYGHGRDNSAGLDLANEHRL 630
Cdd:COG4230 468 AYLVRRLLENGANSSFVNRIADEDVPVEELIADPVEKARALG------GAPHPRIPLPRDLYGPERRNSAGLDLSDEAVL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 631 ASLSSALLNSALQKWQALPMLEQPVAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAIL 710
Cdd:COG4230 542 AALSAALAAAAEKQWQAAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAIL 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 711 HRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANET-HRPLGPVVCISPWNFPLAIFTGQI 789
Cdd:COG4230 622 ERAADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvLRGRGVFVCISPWNFPLAIFTGQV 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 790 AAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIAS 869
Cdd:COG4230 702 AAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAA 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 870 RldaQGRPIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNP 949
Cdd:COG4230 782 R---DGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDP 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 950 GRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRensedAREWQSGTFVAPTLIELDDFAELQKEVFGPVLHVVRY 1029
Cdd:COG4230 859 ADLSTDVGPVIDAEARANLEAHIERMRAEGRLVHQLPL-----PEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRY 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1030 NRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRL 1109
Cdd:COG4230 934 KADELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRF 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1110 LANRPESALAVTLARQDAeypvdaqlkaaltqpLNALREWaanrpelqalctqygeLAQAGTQRLLPGPTGERNTWTLLP 1189
Cdd:COG4230 1014 ATERTVTVNTTAAGGNAS---------------LLALGDW----------------LASLLGALTLPGPTGERNTLTLRP 1062
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1190 RERVLCIADDEQDALTQLAAVLAVGSQVLWPDDALHRQLVKALpsavseriqlakaenitAQPFDAVIFHGdsdQLRALC 1269
Cdd:COG4230 1063 RGRVLCLADSLEALLAQLAAALATGNRAVVAADLALAGLPAVL-----------------LPPFDAVLFEG---RLRALR 1122
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*...
gi 157066218 1270 EAVAARDGAIVSVQGFArgesnILLERLYIErslsvntaaAGGNASLM 1317
Cdd:COG4230 1123 QALAARDGAIVPVIDAG-----YDLERLLEE---------AGGNASLM 1156
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
79-1113 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1552.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 79 LDFAEQILPQSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRNQKnasGRAGMVQGLLQEFSLS 158
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKK---KKLGGIDAFLQEYSLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 159 SQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEA--SLSRSLNRII 236
Cdd:PRK11904 78 TEEGIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKAdgTPSGVLKRLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASN 316
Cdd:PRK11904 158 NRLGEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 317 GRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGW 396
Cdd:PRK11904 238 GADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 397 NGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAV 476
Cdd:PRK11904 318 GGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 477 PNLIYPQFATHNAHTLAAIYQLAGQnyypGQYEFQCLHGMGEPLYEQVTgkvadGKLNRPCRIYAPVGTHETLLAYLVRR 556
Cdd:PRK11904 398 RGAIYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 557 LLENGANTSFVNRIADTSLPLDELVADPVTAVEKLAQqegqtgLPHPKIPLPRDLYGHGRDNSAGLDLANEHRLASLSSA 636
Cdd:PRK11904 469 LLENGANSSFVHRLVDPDVPIEELVADPVEKLRSFET------LPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 637 LLNSALQKWQALPMleqPVAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVL 716
Cdd:PRK11904 543 IAAFLEKQWQAGPI---INGEGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 717 MESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRPlGPV--------------VCISPWNFPL 782
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLP-GPTgesnelrlhgrgvfVCISPWNFPL 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 783 AIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATL 862
Cdd:PRK11904 699 AIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARI 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 863 LQRNIASRldaQGRPIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMA 942
Cdd:PRK11904 779 INRTLAAR---DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMA 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 943 ECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAvrensEDAREWQSGTFVAPTLIELDDFAELQKEVFGP 1022
Cdd:PRK11904 856 ELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQL-----PLPAGTENGHFVAPTAFEIDSISQLEREVFGP 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1023 VLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGG 1102
Cdd:PRK11904 931 ILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGG 1010
|
1050
....*....|.
gi 157066218 1103 PLYLYRLLANR 1113
Cdd:PRK11904 1011 PHYLLRFATEK 1021
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
610-1114 |
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: 830.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 610 DLYGHGRDNSAGLDLANEHRLASLSSALLNSALQKWQALPML-EQPVAAGEMSPVINPAEPKDIVGFVREATPREVEQAL 688
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIgHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 689 ESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRP 768
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 769 LGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRV 848
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 849 RGVMFTGSTEVATLLQRNIASRLDAqgrPIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDE 928
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 929 IADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSedaREWQSGTFVAPTLIE 1008
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDS---RACQHGTFVAPTLFE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1009 LDDFAELQKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPF 1088
Cdd:TIGR01238 395 LDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPF 474
|
490 500
....*....|....*....|....*.
gi 157066218 1089 GGEGLSGTGPKAGGPLYLYRLLANRP 1114
Cdd:TIGR01238 475 GGQGLSGTGPKAGGPHYLYRLTQVQY 500
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
114-1123 |
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: 682.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 114 ARLPQPVAEQAHKLAYQLADKLRNQknasgRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISngn 193
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAA-----PEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 194 wqshigRSPSLFVNAATWGLLFTgklvsthneaslsrslnrIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANAR 273
Cdd:COG0506 75 ------KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 274 KLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASngrgiYEGPGISIKLSALHPRYSRAQYDRVMEELYPRL 353
Cdd:COG0506 131 KLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 354 KSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLV 433
Cdd:COG0506 206 RPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 434 KGAYWDSEIKRAQMDGLeGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQ-NYYPGQYEFQC 512
Cdd:COG0506 286 KGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 513 LHGMGEPLYEQVTgKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVTAVEKLA 592
Cdd:COG0506 365 LYGMGEDLQRALA-AVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 593 qqegqtGLPHPKIPLPRDLYGHGRDNSAGLDLANEHRLASLSSALLNSALQKWQALPMLEQPVAAGEMSPVINPAEPKDI 672
Cdd:COG0506 444 ------PTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 673 VGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHY 752
Cdd:COG0506 518 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAA 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 753 YAGQVRDDFANETHRP--------LGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVP 824
Cdd:COG0506 598 AAAAAARAAAPPPPPPgglvallpLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLL 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 825 PGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVID 904
Cdd:COG0506 678 GGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVA 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 905 VLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQ 984
Cdd:COG0506 758 ASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLP 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 985 AVRENSEDAREWqsgtFVAPTLIELDDFAELQKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVT 1064
Cdd:COG0506 838 GGGPLVPGLLTA----PLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGR 913
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 157066218 1065 GSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLANRPESALAVTLA 1123
Cdd:COG0506 914 VGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAA 972
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
627-1109 |
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: 668.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 627 EHRLASLSSALLNSALQKWQALPML-EQPVAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVE 705
Cdd:cd07125 13 EVPLEALADALKAFDEKEWEAIPIInGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 706 RAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFA-----------NETH-RPLGPVV 773
Cdd:cd07125 93 RAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 774 CISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMF 853
Cdd:cd07125 173 CISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 854 TGSTEVATLLQRNIASRldaQGRPIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHT 933
Cdd:cd07125 253 TGSTETAKLINRALAER---DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 934 LKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEdarewqsGTFVAPTLIELDDFA 1013
Cdd:cd07125 330 IEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGN-------GYFVAPGIIEIVGIF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1014 ELQKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGL 1093
Cdd:cd07125 403 DLTTEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGL 482
|
490
....*....|....*.
gi 157066218 1094 SGTGPKAGGPLYLYRL 1109
Cdd:cd07125 483 SGTGPKAGGPNYLLRF 498
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
643-1110 |
6.03e-149 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 460.12 E-value: 6.03e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 643 QKWQALPML--EQPVAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQ 720
Cdd:cd07083 14 EFGRAYPLVigGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 721 MQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFA------------NET-HRPLGPVVCISPWNFPLAIFTG 787
Cdd:cd07083 94 RRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYpavevvpypgedNESfYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 788 QIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNI 867
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 868 ASRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMG 947
Cdd:cd07083 254 ARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 948 NPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEdarewqsGTFVAPTLIELDDFAE--LQKEVFGPVLH 1025
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGE-------GYFVAPTVVEEVPPKAriAQEEIFGPVLS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1026 VVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLY 1105
Cdd:cd07083 407 VIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHY 486
|
....*
gi 157066218 1106 LYRLL 1110
Cdd:cd07083 487 LRRFL 491
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
268-569 |
2.94e-146 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 444.63 E-value: 2.94e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 268 ALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVME 347
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 348 ELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRR 427
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 428 LMIRLVKGAYWDSEIKRAQMdGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQ-NYYPG 506
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157066218 507 QYEFQCLHGMGEPLYEQVtgkVADGklnRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNR 569
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFAL---VAAG---YRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
653-1107 |
8.91e-131 |
|
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: 412.39 E-value: 8.91e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 653 QPVAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:cd07124 40 KEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 GKTFSNAIAEVREAVDFLHYYAGQV----------RDDFANETH-RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07124 120 GKNWAEADADVAEAIDFLEYYAREMlrlrgfpvemVPGEDNRYVyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 802 KPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPLI 881
Cdd:cd07124 200 KPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 882 AETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVID 961
Cdd:cd07124 280 AEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVID 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 962 SEAKVNIERHIQTMRSKGRpvfqaVRENSEDAREWQSGTFVAPTLIE-LDDFAEL-QKEVFGPVLHVVRYnrNQLPELIE 1039
Cdd:cd07124 360 KGARDRIRRYIEIGKSEGR-----LLLGGEVLELAAEGYFVQPTIFAdVPPDHRLaQEEIFGPVLAVIKA--KDFDEALE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157066218 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1107
Cdd:cd07124 433 IANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLL 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
656-1102 |
1.33e-119 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 381.01 E-value: 1.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKT 735
Cdd:COG1012 18 ASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 736 FSNAIAEVREAVDFLHYYAGQVR------------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:COG1012 97 LAEARGEVDRAADFLRYYAGEARrlygetipsdapGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 804 AEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAE 883
Cdd:COG1012 177 AEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVTLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 884 TGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSE 963
Cdd:COG1012 251 LGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 964 AKVNIERHIQTMRSKG-RPVFQAVRensedaREWQSGTFVAPTLIE-LDDFAEL-QKEVFGPVLHVVRYnrNQLPELIEQ 1040
Cdd:COG1012 331 QLERVLAYIEDAVAEGaELLTGGRR------PDGEGGYFVEPTVLAdVTPDMRIaREEIFGPVLSVIPF--DDEEEAIAL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157066218 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1102
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
656-1106 |
4.97e-116 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 370.71 E-value: 4.97e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPAePKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKT 735
Cdd:pfam00171 4 SESETIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 736 FSNAIAEVREAVDFLHYYAGQVR-----------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARrldgetlpsdpGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 805 EQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAET 884
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEA 964
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 965 KVNIERHIQTMRSKG-RPVFQAVRENSEdarewqsGTFVAPTLIE-LDDFAEL-QKEVFGPVLHVVRYnrNQLPELIEQI 1041
Cdd:pfam00171 317 LERVLKYVEDAKEEGaKLLTGGEAGLDN-------GYFVEPTVLAnVTPDMRIaQEEIFGPVLSVIRF--KDEEEAIEIA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157066218 1042 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGpKAGGPLYL 1106
Cdd:pfam00171 388 NDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGL 450
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
663-1107 |
4.46e-112 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 361.94 E-value: 4.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE 742
Cdd:PRK03137 54 SINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 743 VREAVDFLHYYAGQV-----------RDDFANETH-RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:PRK03137 134 TAEAIDFLEYYARQMlkladgkpvesRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPLIAETGGMNAM 890
Cdd:PRK03137 214 AAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRlTTDIGPVIDSEAKVNIER 970
Cdd:PRK03137 294 VVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 971 HIQTMRSKGRPVFQAVRENSEdarewqsGTFVAPTLI-ELDDFAEL-QKEVFGPVLHVVRYNRNQlpELIEQINASGYGL 1048
Cdd:PRK03137 373 YIEIGKEEGRLVLGGEGDDSK-------GYFIQPTIFaDVDPKARImQEEIFGPVVAFIKAKDFD--HALEIANNTEYGL 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 157066218 1049 TLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1107
Cdd:PRK03137 444 TGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
664-1106 |
1.01e-108 |
|
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: 353.02 E-value: 1.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 664 INPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEV 743
Cdd:TIGR01237 51 INPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 744 REAVDFLHYYA--------GQVRDDFANETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:TIGR01237 131 AEAIDFMEYYArqmielakGKPVNSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 812 AQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPLIAETGGMNAMI 891
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 892 VDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERH 971
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 972 IQTMRSKGRPVFQAVRENSEdarewqsGTFVAPTLI-ELDDFAEL-QKEVFGPVLHVVRYNRNQlpELIEQINASGYGLT 1049
Cdd:TIGR01237 371 IEIGKAEGRLVSGGCGDDSK-------GYFIGPTIFaDVDRKARLaQEEIFGPVVAFIRASDFD--EALEIANNTEYGLT 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 157066218 1050 LGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1106
Cdd:TIGR01237 442 GGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYL 498
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
685-1108 |
3.72e-108 |
|
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: 348.43 E-value: 3.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 685 EQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVR------ 758
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARrlhgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 759 ------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLP 832
Cdd:cd07078 81 ipspdpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 833 GQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNiasrldAQGRPIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDS 912
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRA------AAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 913 AGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKG-RPVFQAVRENSE 991
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGaKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 992 DarewqsGTFVAPTLIE-LDDFAEL-QKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHV 1069
Cdd:cd07078 315 K------GYFVPPTVLTdVDPDMPIaQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEA 386
|
410 420 430
....*....|....*....|....*....|....*....
gi 157066218 1070 GNLYVNRNMVGAVVGvQPFGGEGLSGTGpKAGGPLYLYR 1108
Cdd:cd07078 387 GTVWINDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEE 423
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
655-1103 |
2.24e-89 |
|
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: 298.01 E-value: 2.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 655 VAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGK 734
Cdd:cd07097 10 VAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 735 TFSNAIAEVREAVDFLHYYAGQ-----------VRDDFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07097 90 TLPEARGEVTRAGQIFRYYAGEalrlsgetlpsTRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 803 PAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDAQGRPIPLia 882
Cdd:cd07097 170 PAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVG----RRIAAAAAARGARVQL-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 883 ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDS 962
Cdd:cd07097 244 EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 963 EAKVNIERHIQTMRSKG-RPVFQAVRENSEDarewqSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPELIE 1039
Cdd:cd07097 324 RQLEKDLRYIEIARSEGaKLVYGGERLKRPD-----EGYYLAPALFAgvTNDMRIAREEIFGPVAAVIRV--RDYDEALA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157066218 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1103
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
654-1103 |
4.85e-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: 288.86 E-value: 4.85e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 654 PVAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAG 733
Cdd:cd07131 9 DSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 734 KTFSNAIAEVREAVDFLHYYAGQVR------------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07131 89 KPLAEGRGDVQEAIDMAQYAAGEGRrlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 802 KPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRniasrldAQGRPIPLI 881
Cdd:cd07131 169 KPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE-------TCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 882 A-ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVI 960
Cdd:cd07131 242 AlEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 961 DSEAKVNIERHIQTMRSKGRPVFQAvrENSEDAREWQSGTFVAPTLIEL--DDFAELQKEVFGPVLHVVRYnrNQLPELI 1038
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLG--GERLTGGGYEKGYFVEPTVFTDvtPDMRIAQEEIFGPVVALIEV--SSLEEAI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157066218 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1103
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
663-1097 |
3.47e-85 |
|
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: 285.48 E-value: 3.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAePKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE 742
Cdd:cd07103 1 VINPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 743 VREAVDFLHYYAGQVR--------DDFANE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07103 80 VDYAASFLEWFAEEARriygrtipSPAPGKrilvIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGmNA- 889
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGG-NAp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 890 MIVDSSALTEQVVIDVLASAFDSAGQRC-SALRVLClQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNI 968
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 969 ERHIQTMRSKG-RPVFQAVRENSedarewqSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPELIEQINASG 1045
Cdd:cd07103 312 EALVEDAVAKGaKVLTGGKRLGL-------GGYFYEPTVLTdvTDDMLIMNEETFGPVAPIIPF--DTEDEVIARANDTP 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 157066218 1046 YGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:cd07103 383 YGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
656-1101 |
9.81e-85 |
|
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: 285.23 E-value: 9.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPAEPKDIVGfVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKT 735
Cdd:cd07086 10 SGGETFTSRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 736 FSNAIAEVREAVDFLHYYAGQVR------------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07086 89 LPEGLGEVQEMIDICDYAVGLSRmlygltipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 804 AEQTPLIAAQGIAILLEA----GVPPGVVQLLPGQGEtVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqGRPIp 879
Cdd:cd07086 169 SETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRVL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 880 liAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPV 959
Cdd:cd07086 244 --LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 960 IDSEAKVNIERHIQTMRSKGRPVF--QAVRENSEDarewqsGTFVAPTLIEL--DDFAELQKEVFGPVLHVVRYnrNQLP 1035
Cdd:cd07086 322 INQAAVEKYLNAIEIAKSQGGTVLtgGKRIDGGEP------GNYVEPTIVTGvtDDARIVQEETFAPILYVIKF--DSLE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157066218 1036 ELIEQINASGYGLTLGVHT---RIDETIAQVTGSaHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAG 1101
Cdd:cd07086 394 EAIAINNDVPQGLSSSIFTedlREAFRWLGPKGS-DCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
689-1110 |
3.27e-83 |
|
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: 277.19 E-value: 3.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 689 ESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRD--------- 759
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKlggpelpsp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 760 --DFANET-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGE 836
Cdd:cd06534 81 dpGGEAYVrREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 837 TVGAQLTGDDRVRGVMFTGSTEVATLLQRNiasrldAQGRPIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQR 916
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKA------AAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 917 CSALRVLCLQDEIADhtlkmlrgamaecrmgnpgrlttdigPVIDseakvnierhiqtmrsKGRPVFQAVRENSEDAREw 996
Cdd:cd06534 235 CTAASRLLVHESIYD--------------------------EFVE----------------KLVTVLVDVDPDMPIAQE- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 997 qsgtfvaptlielddfaelqkEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR 1076
Cdd:cd06534 272 ---------------------EIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYIND 328
|
410 420 430
....*....|....*....|....*....|....
gi 157066218 1077 NMVGAVVGvQPFGGEGLSGTGpKAGGPLYLYRLL 1110
Cdd:cd06534 329 SSIGVGPE-APFGGVKNSGIG-REGGPYGLEEYT 360
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
662-1097 |
9.26e-79 |
|
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: 267.68 E-value: 9.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 662 PVINPAEPKdIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIA 741
Cdd:cd07145 2 EVRNPANGE-VIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYAGQVR---------DDFANETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07145 81 EVERTIRLFKLAAEEAKvlrgetipvDAYEYNERRiaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 806 QTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLlqrnIASRLDAQGRPIplIAETG 885
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLL----IASKAGGTGKKV--ALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAK 965
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 966 VNIERHIQTMRSKGRPVFQAVREnsedarewQSGTFVAPTLIELD--DFAELQKEVFGPVLHVVRYNRNQlpELIEQINA 1043
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKR--------DEGSFFPPTVLENDtpDMIVMKEEVFGPVLPIAKVKDDE--EAVEIANS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157066218 1044 SGYGLTLGVHTRiDETIAqvtgsahvgnLYVNRNM-VGAVV---------GVQPFGGEGLSGTG 1097
Cdd:cd07145 385 TEYGLQASVFTN-DINRA----------LKVARELeAGGVVindstrfrwDNLPFGGFKKSGIG 437
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
636-1108 |
8.95e-75 |
|
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: 258.67 E-value: 8.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 636 ALLNSALQKWQALPmLEQP-------VAAGEMSPVINPAEPKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAA 708
Cdd:cd07123 17 AKLQEALAELKSLT-VEIPlviggkeVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 709 ILHRAAVLMESQMQQLI------GilvreAGKTFSNA-IAEVREAVDFLHY--------YAGQVRDDFANET----HRPL 769
Cdd:cd07123 96 IFLKAADLLSGKYRYELnaatmlG-----QGKNVWQAeIDAACELIDFLRFnvkyaeelYAQQPLSSPAGVWnrleYRPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 770 -GPVVCISPWNFPlAIfTGQIAAALA-AGNSVLAKPAEqTPLIAAQGI-AILLEAGVPPGVVQLLPGQGETVGAQLTGDD 846
Cdd:cd07123 171 eGFVYAVSPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 847 RVRGVMFTGSTEVATLLQRNIASRLDAQgRPIP-LIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSAL-RV-- 922
Cdd:cd07123 248 HLAGLHFTGSTPTFKSLWKQIGENLDRY-RTYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAAsRAyv 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 923 -LCLQDEIADHTLKMLrgamAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQtmRSKGRPVFQAVRENSEDAREwqsGTF 1001
Cdd:cd07123 327 pESLWPEVKERLLEEL----KEIKMGDPDDFSNFMGAVIDEKAFDRIKGYID--HAKSDPEAEIIAGGKCDDSV---GYF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1002 VAPTLIELDD--FAELQKEVFGPVLHVVRYNRNQLPELIEQIN-ASGYGLTLGVHTRiDETIAQVTGSAH---VGNLYVN 1075
Cdd:cd07123 398 VEPTVIETTDpkHKLMTEEIFGPVLTVYVYPDSDFEETLELVDtTSPYALTGAIFAQ-DRKAIREATDALrnaAGNFYIN 476
|
490 500 510
....*....|....*....|....*....|...
gi 157066218 1076 RNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1108
Cdd:cd07123 477 DKPTGAVVGQQPFGGARASGTNDKAGSPLNLLR 509
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
662-1097 |
9.06e-75 |
|
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: 256.37 E-value: 9.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 662 PVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIA 741
Cdd:cd07149 2 EVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYA-------GQV---------RDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07149 81 EVDRAIETLRLSAeeakrlaGETipfdaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 806 QTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRldaqgrpiPLIAETG 885
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--------KVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRC-SALRVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEA 964
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 965 KVNIERHIQTMRSKG-RPVFQAVREnsedarewqsGTFVAPTLIE-LDDFAELQK-EVFGPVLHVVRYNRnqLPELIEQI 1041
Cdd:cd07149 312 AERIEEWVEEAVEGGaRLLTGGKRD----------GAILEPTVLTdVPPDMKVVCeEVFAPVVSLNPFDT--LDEAIAMA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157066218 1042 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1097
Cdd:cd07149 380 NDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdsstfR------VDHMPYGGVKESGTG 434
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
663-1101 |
4.92e-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: 254.40 E-value: 4.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPKdIVGFVREATPREVEQALESAVN--NAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAI 740
Cdd:cd07114 1 SINPATGE-PWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 741 AEVREAVDFLHYYAGQVR------------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADkiegavipvdkgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 809 LIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMN 888
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 889 AMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNI 968
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 969 ERHIQTMRSKG-RPVFQAVRENSEDareWQSGTFVAPTLIELD--DFAELQKEVFGPVLHVVRYNRNQlpELIEQINASG 1045
Cdd:cd07114 314 ERYVARAREEGaRVLTGGERPSGAD---LGAGYFFEPTILADVtnDMRIAQEEVFGPVLSVIPFDDEE--EAIALANDSE 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 157066218 1046 YGLTLGVHTRiDETIA-QVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07114 389 YGLAAGIWTR-DLARAhRVARAIEAGTVWV--NTYRALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
663-1097 |
3.95e-73 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 251.72 E-value: 3.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIA- 741
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYAG----------QVRDDFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07093 80 DIPRAAANFRFFADyilqldgesyPQDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAM 890
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIER 970
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 971 HIQTMRSKGRPVfqAVRENSEDAREWQSGTFVAPTLIE-LDDFAEL-QKEVFGPVLHVVRYNRNQlpELIEQINASGYGL 1048
Cdd:cd07093 314 YVELARAEGATI--LTGGGRPELPDLEGGYFVEPTVITgLDNDSRVaQEEIFGPVVTVIPFDDEE--EAIELANDTPYGL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 157066218 1049 TLGVHTRiDETIAQVTGSA-HVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:cd07093 390 AAYVWTR-DLGRAHRVARRlEAGTVWVNCWLVRDL--RTPFGGVKASGIG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
683-1095 |
1.49e-71 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 246.41 E-value: 1.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 683 EVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVRE-------AVDFLHYYAG 755
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAmagkidiSIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 756 QVRDDFANE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLL 831
Cdd:cd07095 81 ERATPMAQGravlRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 832 PGQGETvGAQLTGDDRVRGVMFTGSTEVATLLQRNIAsrldaqGRPIPLIA-ETGGMNAMIVDSSALTEQVVIDVLASAF 910
Cdd:cd07095 161 QGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 911 DSAGQRCS-ALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRen 989
Cdd:cd07095 234 LTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 990 sedaREWQSGTFVAPTLIELDDFAELQK-EVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAH 1068
Cdd:cd07095 312 ----RLVAGTAFLSPGIIDVTDAADVPDeEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420
....*....|....*....|....*..
gi 157066218 1069 VGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:cd07095 386 AGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
658-1097 |
1.91e-71 |
|
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: 247.48 E-value: 1.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 658 GEMSPVINPAEPKdIVGFVREATPREVEQALESAVNNAPIWFATPPV-ERAAILHRAAVLMESQMQQLIGILVREAGKTF 736
Cdd:cd07082 15 GKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTMPLeERIDCLHKFADLLKENKEEVANLLMWEIGKTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 737 SNAIAEVREAVDFLHYYAGQVRD--------DFANETHR--------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07082 94 KDALKEVDRTIDYIRDTIEELKRldgdslpgDWFPGTKGkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 801 AKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRnIASRLdaqgrpiPL 880
Cdd:cd07082 174 FKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK-QHPMK-------RL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 881 IAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVI 960
Cdd:cd07082 246 VLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 961 DsEAKVN-IERHIQTMRSKG-RPVFQAVREnsedarewqSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPE 1036
Cdd:cd07082 326 D-PKSADfVEGLIDDAVAKGaTVLNGGGRE---------GGNLIYPTLLDpvTPDMRLAWEEPFGPVLPIIRV--NDIEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157066218 1037 LIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-KCQRGPDHFPFLGRKDSGIG 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
654-1076 |
2.47e-71 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 246.79 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 654 PVAAGEMSPVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAG 733
Cdd:cd07088 8 PSSSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 734 KTFSNAIAEVREAVDFLHYYAGQVR--------DDFANET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07088 87 KTLSLARVEVEFTADYIDYMAEWARriegeiipSDRPNENififKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 802 KPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLI 881
Cdd:cd07088 167 KPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 882 AETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVID 961
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 962 SEAKVNIERHIQtmrskgRPVFQAVRENSEDAR-EWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPELI 1038
Cdd:cd07088 321 EAALDKVEEMVE------RAVEAGATLLTGGKRpEGEKGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKF--SSLDEAI 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 157066218 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR 1076
Cdd:cd07088 393 ELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
665-1103 |
1.91e-70 |
|
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: 243.78 E-value: 1.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 665 NPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVR 744
Cdd:cd07150 5 NPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 745 EAVDFLHYYAGQVR------------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAA 812
Cdd:cd07150 84 FTPELLRAAAGECRrvrgetlpsdspGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 813 QGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDAQGRPIPLiaETGGMNAMIV 892
Cdd:cd07150 164 KIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRHLKKITL--ELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 893 DSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHI 972
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 973 QTMRSKGRPVFqavrensedAREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRNQlpELIEQINASGYGLTL 1050
Cdd:cd07150 318 EDAVAKGAKLL---------TGGKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPAKDAE--EALELANDTEYGLSA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 157066218 1051 GVHTR-IDETIAQV----TGSAHVGNLYVNRNmvgAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07150 387 AILTNdLQRAFKLAerleSGMVHINDPTILDE---AHV---PFGGVKASGFG-REGGE 437
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
657-1097 |
9.20e-70 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 242.81 E-value: 9.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 657 AGEMSPVINPAePKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTF 736
Cdd:cd07085 14 TTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 737 SNAIAEVR---EAVDF--------LHYYAGQVRDDFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07085 93 ADARGDVLrglEVVEFacsiphllKGEYLENVARGIDTYSYRqPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 805 EQTPLiAAQGIAILL-EAGVPPGVVQLLPGQGETVGAQLTgDDRVRGVMFTGSTEVAtllqRNIASRLDAQGRPIplIAE 883
Cdd:cd07085 173 ERVPG-AAMRLAELLqEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVG----EYIYERAAANGKRV--QAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 884 TGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSE 963
Cdd:cd07085 245 GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 964 AKVNIERHIQtmrskgrpvfQAVRENSE---DARE-----WQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQ 1033
Cdd:cd07085 325 AKERIEGLIE----------SGVEEGAKlvlDGRGvkvpgYENGNFVGPTILDnvTPDMKIYKEEIFGPVLSIVRV--DT 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157066218 1034 LPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmVGAVVGVQ--PFGGEGLSGTG 1097
Cdd:cd07085 393 LDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLAffSFGGWKGSFFG 455
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
683-1103 |
2.71e-69 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 239.74 E-value: 2.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 683 EVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVR---- 758
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRrpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 759 ----DDFANETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIA-ILLEAGVPPGVVQ 829
Cdd:cd07104 81 eilpSDVPGKESMvrrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAeIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 830 LLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASrldAQGRPIPLIA-ETGGMNAMIVDSSALTEQVVIDVLAS 908
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIGE---LAGRHLKKVAlELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 909 AFDSAGQRC-SALRVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGrpvfqAVR 987
Cdd:cd07104 234 AFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAG-----ARL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 988 EnsedAREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVHTRIDETIAQVTG 1065
Cdd:cd07104 308 L----TGGTYEGLFYQPTVLSdvTPDMPIFREEIFGPVAPVIPFDDDE--EAVELANDTEYGLSAAVFTRDLERAMAFAE 381
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 157066218 1066 SAHVGNLYVNRNMV--GAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07104 382 RLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
658-1097 |
4.48e-67 |
|
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: 234.42 E-value: 4.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 658 GEMSPVINPAEPKdIVGFVREATPREVEQALESA--VNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKT 735
Cdd:cd07112 1 GETFATINPATGR-VLAEVAACDAADVDRAVAAArrAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 736 FSNAIA-EVREAVDFLHYYA-------GQV----RDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07112 80 ISDALAvDVPSAANTFRWYAeaidkvyGEVaptgPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 804 AEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIAsrlDAQGRPIPLiaE 883
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSG---QSNLKRVWL--E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 884 TGGMNAMIV-DSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDS 962
Cdd:cd07112 235 CGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 963 EAKVNIERHIQTMRSKGrpvfQAVRENSEDAREWQSGTFVAPTLIE-LDDFAEL-QKEVFGPVLHVVRYNRNQlpELIEQ 1040
Cdd:cd07112 315 AHFDKVLGYIESGKAEG----ARLVAGGKRVLTETGGFFVEPTVFDgVTPDMRIaREEIFGPVLSVITFDSEE--EAVAL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 157066218 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07112 389 ANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
663-1097 |
6.10e-67 |
|
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: 233.67 E-value: 6.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPKDIVGFVReATPREVEQALESAVNNAPI-WFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIA 741
Cdd:cd07109 1 VFDPSTGEVFARIAR-GGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYAGQVR----------DDFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07109 80 DVEAAARYFEYYGGAADklhgetiplgPGYFVYTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAM 890
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGnPGRLTTDIGPVIDSEAKVNIER 970
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 971 HIQTMRSKGRPVF---QAVRENSEDarewqsGTFVAPTLI-ELDDFAEL-QKEVFGPVLHVVRYnrNQLPELIEQINASG 1045
Cdd:cd07109 313 FVARARARGARIVaggRIAEGAPAG------GYFVAPTLLdDVPPDSRLaQEEIFGPVLAVMPF--DDEAEAIALANGTD 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 157066218 1046 YGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnmVGAVVGVQ-PFGGEGLSGTG 1097
Cdd:cd07109 385 YGLVAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
663-1097 |
3.20e-66 |
|
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: 231.55 E-value: 3.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPKdIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE 742
Cdd:cd07094 3 VHNPYDGE-VIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 743 VREAVDFLHYYAGQVR---------DDFANETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQ 806
Cdd:cd07094 82 VDRAIDTLRLAAEEAErirgeeiplDATQGSDNRlawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 807 TPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIasrldaqgrPIPLIA-ETG 885
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA---------GGKRIAlELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAK 965
Cdd:cd07094 233 GNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 966 VNIERHIQtmrskgrpvfQAVRENSE----DAREwqsGTFVAPTLIELDDF-AELQK-EVFGPVLHVVRYnrNQLPELIE 1039
Cdd:cd07094 313 ERVERWVE----------EAVEAGARllcgGERD---GALFKPTVLEDVPRdTKLSTeETFGPVVPIIRY--DDFEEAIR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157066218 1040 QINASGYGLTLGVHTRiDETIAqvtgsahvgnLYVNRNM-VGAVV---------GVQPFGGEGLSGTG 1097
Cdd:cd07094 378 IANSTDYGLQAGIFTR-DLNVA----------FKAAEKLeVGGVMvndssafrtDWMPFGGVKESGVG 434
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
664-1097 |
6.97e-66 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 230.57 E-value: 6.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 664 INPAEPKDiVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEV 743
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 744 REAVDFLHYYAGQVRDDFANE---------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRkvptgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 809 LIAAQGIAILLEAGVPPGVVQLLPGQGETvGAQLTgDDRVRGVMFTGSteVATllQRNIASRldAQGRPIPLIAETGGMN 888
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGS--VAT--GRKVMAA--AAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 889 AMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVID-SEAKVn 967
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTaRQLDI- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 968 IERHIQTMRSKG-RPVFQAVRENSedarewqSGTFVAPT-LIELD-DFAELQKEVFGPVLHVVRYnrNQLPELIEQINAS 1044
Cdd:cd07099 311 VRRHVDDAVAKGaKALTGGARSNG-------GGPFYEPTvLTDVPhDMDVMREETFGPVLPVMPV--ADEDEAIALANDS 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 157066218 1045 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07099 382 RYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
663-1097 |
3.08e-64 |
|
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: 225.49 E-value: 3.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPkDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE 742
Cdd:cd07106 1 VINPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 743 VREAVDFLHYYAGQ------VRDD---FANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQ 813
Cdd:cd07106 80 VGGAVAWLRYTASLdlpdevIEDDdtrRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 814 GIAILLEAgVPPGVVQLLPGQGEtVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgRPIPLiaETGGMNAMIVD 893
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 894 SSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVidseakvnierhiQ 973
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPV-------------Q 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 974 TmrskgRPVFQAVRENSEDAR------------EWQSGTFVAPTLI-ELDDFAEL-QKEVFGPVLHVVRYnrNQLPELIE 1039
Cdd:cd07106 299 N-----KMQYDKVKELVEDAKakgakvlaggepLDGPGYFIPPTIVdDPPEGSRIvDEEQFGPVLPVLKY--SDEDEVIA 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 157066218 1040 QINASGYGLTLGVHTRiDETIAQVTGSA-HVGNLYVNRNmvGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07106 372 RANDSEYGLGASVWSS-DLERAEAVARRlEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
663-1101 |
9.02e-64 |
|
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: 224.63 E-value: 9.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNA-IA 741
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYAG----------QVRDDFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07115 80 DVPRAADTFRYYAGwadkiegeviPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgRPIPLiaETGGMNAM 890
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNL----KRVSL--ELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIER 970
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 971 HIQTMRSKGrpvfqaVRENSEDAREWQSGTFVAPTLIEL--DDFAELQKEVFGPVLHVVRYNRNQlpELIEQINASGYGL 1048
Cdd:cd07115 314 YVDVGREEG------ARLLTGGKRPGARGFFVEPTIFAAvpPEMRIAQEEIFGPVVSVMRFRDEE--EALRIANGTEYGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 157066218 1049 TLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07115 386 AAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
632-1097 |
1.50e-63 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 225.34 E-value: 1.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 632 SLSSALLNSALQKWQALPMLEQPVA-AGEMSPVINPAEPKDIVGFVREATpREVEQALESAVNNAPIWFATPPVERAAIL 710
Cdd:PLN02278 12 SALVKLRNAGLLRTQGLIGGKWTDAyDGKTFPVYNPATGEVIANVPCMGR-AETNDAIASAHDAFPSWSKLTASERSKIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 711 HRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVR--------DDFANE----THRPLGPVVCISPW 778
Cdd:PLN02278 91 RRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKrvygdiipSPFPDRrllvLKQPVGVVGAITPW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 779 NFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI--AAQGIAilLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGS 856
Cdd:PLN02278 171 NFPLAMITRKVGPALAAGCTVVVKPSELTPLTalAAAELA--LQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 857 TEVATLLQRNIASRLdaqgRPIPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRC-SALRVLcLQDEIADHTLK 935
Cdd:PLN02278 249 TAVGKKLMAGAAATV----KRVSL--ELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 936 MLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAvrenseDAREWQSGTFVAPTLIE--LDDFA 1013
Cdd:PLN02278 322 AFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLG------GKRHSLGGTFYEPTVLGdvTEDML 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1014 ELQKEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGGEGL 1093
Cdd:PLN02278 396 IFREEVFGPVAPLTRFKTEE--EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQ 471
|
....
gi 157066218 1094 SGTG 1097
Cdd:PLN02278 472 SGLG 475
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
654-1101 |
2.14e-63 |
|
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: 224.01 E-value: 2.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 654 PVAAGEMSPVINPAEPKDIvGFVREATPREVEQALESAVNNAPI--WFATPPVERAAILHRAAVLMESQMQQLIGILVRE 731
Cdd:cd07091 14 DSVSGKTFPTINPATEEVI-CQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 732 AGKTFS-NAIAEVREAVDFLHYYAG----------QVRDDFANETHR-PLGpvVC--ISPWNFPLAIFTGQIAAALAAGN 797
Cdd:cd07091 93 NGKPLEeSAKGDVALSIKCLRYYAGwadkiqgktiPIDGNFLAYTRRePIG--VCgqIIPWNFPLLMLAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 798 SVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIA-SRLdaqgR 876
Cdd:cd07091 171 TVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAkSNL----K 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 877 PIPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:cd07091 247 KVTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 957 GPVIDSEAKVNIERHIQTMRSKGRPVFQAvrensedAREWQS-GTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQ 1033
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTG-------GERHGSkGYFIQPTVFTdvKDDMKIAKEEIFGPVVTILKF--KT 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157066218 1034 LPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
148-259 |
2.23e-63 |
|
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: 210.44 E-value: 2.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 148 VQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEAS 227
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 157066218 228 LSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQF 259
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
663-1097 |
2.44e-62 |
|
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: 220.64 E-value: 2.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPKdIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE 742
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 743 VREAVDFLHYYAGQV-----------RDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07090 80 IDSSADCLEYYAGLAptlsgehvplpGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 812 AQGIAILLEAGVPPGVVQLLPGQGETvGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgRPIPLiaETGGMNAMI 891
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 892 VDSSALTEQVVIDVLASAFDSAGQRCS-ALRVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIER 970
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 971 HIQTMRSKGRPVFQ-AVRENSEDAREwqSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRNQlpELIEQINASGYG 1047
Cdd:cd07090 312 YIESAKQEGAKVLCgGERVVPEDGLE--NGFYVSPCVLTdcTDDMTIVREEIFGPVMSILPFDTEE--EVIRRANDTTYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 157066218 1048 LTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07090 388 LAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
653-1097 |
1.37e-61 |
|
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: 219.10 E-value: 1.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 653 QPVAAGEMSPVINPAEpKDIVGFVREATPREVEQALESAVN--NAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVR 730
Cdd:cd07119 7 VEAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRafDSGEWPHLPAQERAALLFRIADKIREDAEELARLETL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 731 EAGKTFSNAIAEVREAVDFLHYYAGQV--RDDFANET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07119 86 NTGKTLRESEIDIDDVANCFRYYAGLAtkETGEVYDVpphvisrtvREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 800 LAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgRPIP 879
Cdd:cd07119 166 VIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV----KKVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 880 LiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPV 959
Cdd:cd07119 242 L--ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 960 IDSEAKVNIERHIQTMRSKGRPVFQAVRENSEDarEWQSGTFVAPTLI-ELD-DFAELQKEVFGPVLHVVRYNRNQlpEL 1037
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTGD--ELAKGYFVEPTIFdDVDrTMRIVQEEIFGPVLTVERFDTEE--EA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157066218 1038 IEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1097
Cdd:cd07119 396 IRLANDTPYGLAGAVWTK-DIARANrVARRLRAGTVWINDYHPYFAEA--PWGGYKQSGIG 453
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
679-1103 |
4.39e-61 |
|
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: 216.39 E-value: 4.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 679 ATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYA---- 754
Cdd:cd07152 10 ADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAglpt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 755 ---GQV------RDDFAneTHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLE-AGVP 824
Cdd:cd07152 90 qpqGEIlpsapgRLSLA--RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLFEeAGLP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 825 PGVVQLLPGQGEtVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASrldAQGRPIPLIA-ETGGMNAMIVDSSALTEQVVI 903
Cdd:cd07152 168 AGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVG----RKVGE---AAGRHLKKVSlELGGKNALIVLDDADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 904 DVLASAFDSAGQRC-SALRVLCLQDeIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGrpv 982
Cdd:cd07152 240 NGAWGAFLHQGQICmAAGRHLVHES-VADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 983 fqavrensedAREWQSGT----FVAPTLI-----ELDDFAElqkEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVH 1053
Cdd:cd07152 316 ----------ARLEAGGTydglFYRPTVLsgvkpGMPAFDE---EIFGPVAPVTVFDSDE--EAVALANDTEYGLSAGII 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 157066218 1054 TRIDETIAQVTGSAHVGNLYVNRNMVGAVVgVQPFGGEGLSGTGPKAGGP 1103
Cdd:cd07152 381 SRDVGRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
672-1101 |
5.33e-61 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 216.46 E-value: 5.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 672 IVGFVREATPREVEQALESAVNNAPiwfATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLH 751
Cdd:cd07146 11 VVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 752 YYAGQVR---------DDFANE------THR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGI 815
Cdd:cd07146 88 FAAAEALrddgesfscDLTANGkarkifTLRePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 816 AILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIAsrldAQGRPIPLIAETGGMNAMIVDSS 895
Cdd:cd07146 168 DLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVG----KAIA----ATAGYKRQLLELGGNDPLIVMDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 896 ALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHI-QT 974
Cdd:cd07146 240 ADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVeEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 975 MRSKGRPVFQAVREnsedarewqsGTFVAPTLIE-LDDFAEL-QKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGV 1052
Cdd:cd07146 320 IAQGARVLLGNQRQ----------GALYAPTVLDhVPPDAELvTEETFGPVAPVIRV--KDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 157066218 1053 HTRIDETIAQVTGSAHVGNLYVNrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
663-1100 |
7.13e-61 |
|
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: 216.07 E-value: 7.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTF-SNAIA 741
Cdd:cd07108 1 VINPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYAG----------QVRDDFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLi 810
Cdd:cd07108 80 EAAVLADLFRYFGGlagelkgetlPFGPDVLTYTVRePLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAM 890
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 891 IVDSSALTEQVVIDVLASA-FDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIE 969
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 970 RHIQTMRSkgRPVFQAVR--ENSEDAReWQSGTFVAPTLI-ELDDFAEL-QKEVFGPVLHVVRYNRNQlpELIEQINASG 1045
Cdd:cd07108 313 GYIDLGLS--TSGATVLRggPLPGEGP-LADGFFVQPTIFsGVDNEWRLaREEIFGPVLCAIPWKDED--EVIAMANDSH 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 157066218 1046 YGLTLGVHTRiDETIAQVTGSA-HVGNLYVNRNmVGAVVGvQPFGGEGLSGTGPKA 1100
Cdd:cd07108 388 YGLAAYVWTR-DLGRALRAAHAlEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
653-1097 |
7.35e-60 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 213.52 E-value: 7.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 653 QPVAAGEMSPVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:cd07138 8 VAPAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 G--KTFSNAiAEVREAVDFLHYYAGQVRDdFANETHR--------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07138 87 GapITLARA-AQVGLGIGHLRAAADALKD-FEFEERRgnslvvrePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 803 PAEQTPLiAAQGIA-ILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLD--AQgrpip 879
Cdd:cd07138 165 PSEVAPL-SAIILAeILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKrvAL----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 880 liaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSAL-RVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGP 958
Cdd:cd07138 239 ---ELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 959 VIDSEAKVNIERHIQTMRSKG---------RPvfqavrensedaREWQSGTFVAPTLielddFAEL-------QKEVFGP 1022
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGarlvaggpgRP------------EGLERGYFVKPTV-----FADVtpdmtiaREEIFGP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157066218 1023 VLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmvGAVVGVQ-PFGGEGLSGTG 1097
Cdd:cd07138 378 VLSIIPY--DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
655-1102 |
3.00e-59 |
|
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: 212.07 E-value: 3.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 655 VAAGEMSPVINPAEPKDIVGfVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGK 734
Cdd:cd07130 8 GGGGGVVTSISPANGEPIAR-VRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 735 TFSNAIAEVREAVDFLHYYAGQVR------------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07130 87 ILPEGLGEVQEMIDICDFAVGLSRqlygltipserpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 803 PAEQTPL--IAAQGIA--ILLEAGVPPGVVQLLPGQGEtVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqGRpi 878
Cdd:cd07130 167 PSPTTPLtaIAVTKIVarVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---GR-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 879 pLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGP 958
Cdd:cd07130 241 -SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 959 VIDSEAKVNIERHIQTMRSKGRPVFqavrenSEDAREWQSGTFVAPTLIE-LDDFAELQKEVFGPVLHVVRYnrNQLPEL 1037
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQGGTVL------FGGKVIDGPGNYVEPTIVEgLSDAPIVKEETFAPILYVLKF--DTLEEA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157066218 1038 IEQINASGYGLTLGVHTRIDETIAQ---VTGSaHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1102
Cdd:cd07130 392 IAWNNEVPQGLSSSIFTTDLRNAFRwlgPKGS-DCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
663-1097 |
3.60e-59 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 211.33 E-value: 3.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEpKDIVGFVREATPREVEQALESAVNNAPIW-FATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNA-- 739
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTAra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 740 ------IAEVREAVD----FLHYYAGQVRDDFANETHR-----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07089 80 mqvdgpIGHLRYFADladsFPWEFDLPVPALRGGPGRRvvrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 805 EQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgRPIPLiaET 884
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEA 964
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 965 KVNIERHIQTMRSKG-RPVFQAVRENSEDarewqSGTFVAPTLI-ELDDFAEL-QKEVFGPVLHVVRYNRNQlpELIEQI 1041
Cdd:cd07089 314 RDRVEGYIARGRDEGaRLVTGGGRPAGLD-----KGFYVEPTLFaDVDNDMRIaQEEIFGPVLVVIPYDDDD--EAVRIA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 157066218 1042 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmvGAVVGV--QPFGGEGLSGTG 1097
Cdd:cd07089 387 NDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
656-1101 |
5.66e-59 |
|
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: 211.20 E-value: 5.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPaEPKDIVGFVREATPREVEQALESA---VNNAPiWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:cd07142 16 ASGKTFPTIDP-RNGEVIAHVAEGDAEDVDRAVKAArkaFDEGP-WPRMTGYERSRILLRFADLLEKHADELAALETWDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 GKTFSNA-IAEVREAVDFLHYYAGQVrDDFANET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07142 94 GKPYEQArYAEVPLAARLFRYYAGWA-DKIHGMTlpadgphhvytlHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 800 LAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqrNIASRLDAQGRPIP 879
Cdd:cd07142 173 VLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVG-----KIIMQLAAKSNLKP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 880 LIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPV 959
Cdd:cd07142 248 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 960 IDSEAKVNIERHIQTMRSKGrpvfqaVRENSEDAREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPEL 1037
Cdd:cd07142 328 VDKEQFEKILSYIEHGKEEG------ATLITGGDRIGSKGYYIQPTIFSdvKDDMKIARDEIFGPVQSILKF--KTVDEV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157066218 1038 IEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
663-1101 |
6.48e-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: 208.54 E-value: 6.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPKDIVGfVREATPREVEQALESAVN--NAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAI 740
Cdd:cd07143 26 VYNPSTGKLITK-IAEATEADVDIAVEVAHAafETDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 741 A-EVREAVDFLHYYAGQVRDDFAN--ET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07143 105 RvDVQASADTFRYYGGWADKIHGQviETdikkltytrHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 809 LIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVA-TLLQRNIASRLdaqgRPIPLiaETGGM 887
Cdd:cd07143 185 LSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGrKVMEAAAKSNL----KKVTL--ELGGK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 888 NAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVN 967
Cdd:cd07143 259 SPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 968 IERHIQTMRSKGRPVFQAVRensedaREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRNQlpELIEQINASG 1045
Cdd:cd07143 339 IMSYIESGKAEGATVETGGK------RHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKFKTEE--EAIKRANDST 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 157066218 1046 YGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07143 411 YGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
655-1110 |
1.36e-57 |
|
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: 207.25 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 655 VAAGEMSPVINPAEPKDIVGfVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGK 734
Cdd:cd07111 33 PENRKSFPTINPATGEVLAS-VLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 735 tfsnAIAEVRE-----AVDFLHYYAGQVR-DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07111 112 ----PIRESRDcdiplVARHFYHHAGWAQlLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 809 LIAAQGIAILLEAGVPPGVVQLLPGQGETvGAQLTGDDRVRGVMFTGSTEVATLLQRNIAsrldAQGRPIPLiaETGGMN 888
Cdd:cd07111 188 LTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA----GTGKKLSL--ELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 889 AMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNI 968
Cdd:cd07111 261 PFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 969 ERHIQTMRSKGRPVFQAVRENSEDarewqsGTFVAPTLIELDDFAE--LQKEVFGPVLHVVRYnRNqLPELIEQINASGY 1046
Cdd:cd07111 341 RELVEEGRAEGADVFQPGADLPSK------GPFYPPTLFTNVPPASriAQEEIFGPVLVVLTF-RT-AKEAVALANNTPY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157066218 1047 GLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGpKAGGPLYLYRLL 1110
Cdd:cd07111 413 GLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEYL 473
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
663-1097 |
7.52e-57 |
|
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: 204.48 E-value: 7.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPKDIvGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIA- 741
Cdd:cd07092 1 VVDPATGEEI-ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYAGQVRD-----------DFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPL 809
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTlegpaageylpGHTSMIRRePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 810 iAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDAQGRPIPLiaETGGMNA 889
Cdd:cd07092 160 -TTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTG----KKVARAAADTLKRVHL--ELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 890 MIVDSSALTEQVVIDVLASAFDSAGQRC-SALRVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNI 968
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 969 ERHIQTMRSKGRPVfqavrenSEDAREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRNQlpELIEQINASGY 1046
Cdd:cd07092 312 AGFVERAPAHARVL-------TGGRRAEGPGYFYEPTVVAgvAQDDEIVQEEIFGPVVTVQPFDDED--EAIELANDVEY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 157066218 1047 GLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1097
Cdd:cd07092 383 GLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
678-1101 |
8.87e-57 |
|
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: 204.11 E-value: 8.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 678 EATPREVEQALESA---VNNAPiWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYA 754
Cdd:cd07118 15 EGTVEDVDAAVAAArkaFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 755 GQVR------------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAG 822
Cdd:cd07118 94 SLARtlhgdsynnlgdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 823 VPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGrpipliAETGGMNAMIVDSSALTEQVV 902
Cdd:cd07118 174 LPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQIVFADADLDAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 903 IDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPV 982
Cdd:cd07118 248 DAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 983 fqAVRENSEDAREwqsGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETI 1060
Cdd:cd07118 328 --LLGGERLASAA---GLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 157066218 1061 AQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTGPKAG 1101
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
679-1095 |
1.42e-56 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 204.42 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 679 ATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVRE-------AVDFLH 751
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiaiSIQAYH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 752 YYAGQVRDDFANET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGV 827
Cdd:PRK09457 114 ERTGEKRSEMADGAavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 828 VQLLPGQGETvGAQLTGDDRVRGVMFTGSTEVATLLQRNIAsrldaqGRPIPLIA-ETGGMNAMIVDSSALTEQVVIDVL 906
Cdd:PRK09457 194 LNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFA------GQPEKILAlEMGGNNPLVIDEVADIDAAVHLII 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 907 ASAFDSAGQRCS-ALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTD-IGPVIDSEAK---VNIERHIQTMrsKGRP 981
Cdd:PRK09457 267 QSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAqglVAAQAQLLAL--GGKS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 982 VFQAVRensedaREWQSGtFVAPTLIELDDFAEL-QKEVFGPVLHVVRYNRnqLPELIEQINASGYGLTLGVHTRIDETI 1060
Cdd:PRK09457 345 LLEMTQ------LQAGTG-LLTPGIIDVTGVAELpDEEYFGPLLQVVRYDD--FDEAIRLANNTRFGLSAGLLSDDREDY 415
|
410 420 430
....*....|....*....|....*....|....*
gi 157066218 1061 AQVTGSAHVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:PRK09457 416 DQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
662-1097 |
2.04e-56 |
|
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: 203.25 E-value: 2.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 662 PVINPAEPKdIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIA 741
Cdd:cd07147 2 EVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYAGQVRD----------DFANETHR------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07147 81 EVARAIDTFRIAAEEATRiygevlpldiSARGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 806 QTPLIAAQGIAILLEAGVPPGVVQLLPGQGETvGAQLTGDDRVRGVMFTGSTEVATLLqRNIASRldaqgRPIPLiaETG 885
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-----KKVVL--ELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRC-SALRVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEA 964
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 965 KVNIERHIQTMRSKGRPVFQAVRENsedarewqsGTFVAPTLIE---LDDFAELQkEVFGPVLHVVRYNRnqLPELIEQI 1041
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGKRD---------GALLEPTILEdvpPDMEVNCE-EVFGPVVTVEPYDD--FDEALAAV 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157066218 1042 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1097
Cdd:cd07147 379 NDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSGIG 433
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
673-1101 |
2.07e-56 |
|
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: 203.31 E-value: 2.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 673 VGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHY 752
Cdd:cd07101 9 LGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 753 YAGQVRDDFA--------------NETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAIL 818
Cdd:cd07101 89 YARRAERLLKprrrrgaipvltrtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 819 LEAGVPPGVVQLLPGQGETVGAQLTgdDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALT 898
Cdd:cd07101 169 IEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 899 EQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSK 978
Cdd:cd07101 241 DKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 979 GRPVFQAVRensedAREWQSGTFVAPT-LIELDDFAEL-QKEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVHTRI 1056
Cdd:cd07101 321 GATVLAGGR-----ARPDLGPYFYEPTvLTGVTEDMELfAEETFGPVVSIYRVADDD--EAIELANDTDYGLNASVWTRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 157066218 1057 DETIAQVTGSAHVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTGPKAG 1101
Cdd:cd07101 394 GARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
653-1097 |
2.96e-56 |
|
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: 202.92 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 653 QPVAAGEMSPVINPAEPKDIVGfVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:cd07151 4 RDGTSERTIDVLNPYTGETLAE-IPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 GKTFSNAIAEV-------REAVDFLHYYAGQ-VRDDFANETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07151 83 GSTRIKANIEWgaamaitREAATFPLRMEGRiLPSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 801 AKPAEQTPLIAAQGIA-ILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASrldAQGRPIP 879
Cdd:cd07151 163 LKPASDTPITGGLLLAkIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG----RHIGE---LAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 880 LIA-ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGP 958
Cdd:cd07151 236 KVAlELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 959 VIDSEAKVNIERHIQTMRSKGrpvfqAVRENSEDArewqSGTFVAPT-LIELDDFAEL-QKEVFGPVLHVVRYNRNQlpE 1036
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEG-----ATLLVGGEA----EGNVLEPTvLSDVTNDMEIaREEIFGPVAPIIKADDEE--E 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157066218 1037 LIEQINASGYGLTLGVHTRIDETIAQV-----TGSAHVGNLYVNR--NMvgavvgvqPFGGEGLSGTG 1097
Cdd:cd07151 385 ALELANDTEYGLSGAVFTSDLERGVQFarridAGMTHINDQPVNDepHV--------PFGGEKNSGLG 444
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
658-1103 |
3.20e-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: 203.19 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 658 GEMSPVINPAEPKdIVGFVREATPREVEQALESA---VNNAPiWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGK 734
Cdd:cd07139 13 SETIDVVSPATEE-VVGRVPEATPADVDAAVAAArraFDNGP-WPRLSPAERAAVLRRLADALEARADELARLWTAENGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 735 TFS-NAIAEVREAVDFLHYYAGQVRDdFANETHR-------------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07139 91 PISwSRRAQGPGPAALLRYYAALARD-FPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 801 AKPAEQTPLIA---AQGIAillEAGVPPGVVQLLPGQGEtVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDAQGRP 877
Cdd:cd07139 170 LKPSPETPLDAyllAEAAE---EAGLPPGVVNVVPADRE-VGEYLVRHPGVDKVSFTGSTAAG----RRIAAVCGERLAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 878 IPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSAL-RVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:cd07139 242 VTL--ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 957 GPVIDSEAKVNIERHIQTMRSKG--------RPvfqavrenSEDAREWqsgtFVAPTLI-ELDDFAEL-QKEVFGPVLHV 1026
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGarlvtgggRP--------AGLDRGW----FVEPTLFaDVDNDMRIaQEEIFGPVLSV 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157066218 1027 VRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07139 387 IPY--DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA---PFGGFKQSGIG-REGGP 457
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
664-1076 |
4.57e-56 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 202.09 E-value: 4.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 664 INPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEV 743
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 744 REAVDFLHYYAGQVRDDFANE------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07102 80 RGMLERARYMISIAEEALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 812 AQGIAILLEAGVPPGVVQLLPGQGETvGAQLTGDDRVRGVMFTGSTEVATLLQRNiasrldAQGRPIPLIAETGGMNAMI 891
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRA------AAGRFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 892 VDSSALTEQVVIDVLASAFDSAGQRCSAL-RVLC---LQDEIADHTLKMLRGAmaecRMGNPGRLTTDIGPVIDSEAKVN 967
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIeRIYVhesIYDAFVEAFVAVVKGY----KLGDPLDPSTTLGPVVSARAADF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 968 IERHIQTMRSKG-RPVFQAVRENSEDArewqSGTFVAPT-LIELDDFAELQK-EVFGPVLHVVRYNRNQlpELIEQINAS 1044
Cdd:cd07102 309 VRAQIADAIAKGaRALIDGALFPEDKA----GGAYLAPTvLTNVDHSMRVMReETFGPVVGIMKVKSDA--EAIALMNDS 382
|
410 420 430
....*....|....*....|....*....|..
gi 157066218 1045 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR 1076
Cdd:cd07102 383 EYGLTASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
663-1097 |
1.08e-55 |
|
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: 201.06 E-value: 1.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE 742
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 743 VREAVDFLHYYAGQVRdDFANET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07107 80 VMVAAALLDYFAGLVT-ELKGETipvggrnlhytlREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQgIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDaqgrpiPLIAETGGMNAM 890
Cdd:cd07107 159 ALR-LAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 891 IVDSSALTEQVVIDVLASA-FDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIE 969
Cdd:cd07107 232 IVFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 970 RHIQTMRSKG-RPVFQAVRENSEDAREwqsGTFVAPTLielddFAEL-------QKEVFGPVLHVVRYNRNQlpELIEQI 1041
Cdd:cd07107 312 HYIDSAKREGaRLVTGGGRPEGPALEG---GFYVEPTV-----FADVtpgmriaREEIFGPVLSVLRWRDEA--EMVAQA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1042 NASGYGLTLGVHTRiDETIAQVTGSA-HVGNLYVN---RNMVGAvvgvqPFGGEGLSGTG 1097
Cdd:cd07107 382 NGVEYGLTAAIWTN-DISQAHRTARRvEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
658-1097 |
1.72e-55 |
|
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: 201.42 E-value: 1.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 658 GEMSPVINPAEPKDIVGFVReATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFS 737
Cdd:cd07559 15 GEYFDNYNPVNGKVLCEIPR-STAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 738 NAI-AEVREAVDFLHYYAGQVR-----------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07559 94 ETLaADIPLAIDHFRYFAGVIRaqegslseideDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 806 QTP---LIAAQGIAILLeagvPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIA 882
Cdd:cd07559 174 QTPlsiLVLMELIGDLL----PKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------IPVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 883 ETGGMNAMIVDSSALTEQVVID------VLASAFDSaGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:cd07559 244 ELGGKSPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 957 GPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEDAREwqSGTFVAPTLIEL--DDFAELQKEVFGPVLHVVRYNRNQl 1034
Cdd:cd07559 323 GAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLD--KGYFYEPTLIKGgnNDMRIFQEEIFGPVLAVITFKDEE- 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157066218 1035 pELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07559 400 -EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
657-1101 |
4.93e-55 |
|
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: 199.88 E-value: 4.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 657 AGEMSPVINPAEPKDIVGfVREATPREVEQALESAVN----NAPiWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:cd07141 20 SGKTFPTINPATGEKICE-VQEGDKADVDKAVKAARAafklGSP-WRTMDASERGRLLNKLADLIERDRAYLASLETLDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 GKTFSNA-IAEVREAVDFLHYYAGQVR-----------DDFANETHRPLGpvVC--ISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:cd07141 98 GKPFSKSyLVDLPGAIKVLRYYAGWADkihgktipmdgDFFTYTRHEPVG--VCgqIIPWNFPLLMAAWKLAPALACGNT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 799 VLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIA-SRLdaqgRP 877
Cdd:cd07141 176 VVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGkSNL----KR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 878 IPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADhtlKMLRGAMAEC---RMGNPGRLTT 954
Cdd:cd07141 252 VTL--ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYD---EFVKRSVERAkkrVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 955 DIGPVIDSEAKVNIERHIQTMRSKGrpvfqaVRENSEDAREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrN 1032
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEG------AKLECGGKRHGDKGYFIQPTVFSdvTDDMRIAKEEIFGPVQQIFKF--K 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157066218 1033 QLPELIEQINASGYGLTLGVHTR-IDETIAqVTGSAHVGNLYVNrnmVGAVVGVQ-PFGGEGLSGTGPKAG 1101
Cdd:cd07141 399 TIDEVIERANNTTYGLAAAVFTKdIDKAIT-FSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
663-1097 |
7.06e-55 |
|
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: 198.73 E-value: 7.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE 742
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 743 VREAVDFLHYYAGQVRD--------------DFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQT 807
Cdd:cd07110 80 VDDVAGCFEYYADLAEQldakaeravplpseDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 808 PLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDAQGRPIPLiaETGGM 887
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATG----SQVMQAAAQDIKPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 888 NAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVN 967
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 968 IERHIQTMRSKG-RPVFQAVRensedAREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRNQlpELIEQINAS 1044
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRR-----PAHLEKGYFIAPTVFAdvPTDSRIWREEIFGPVLCVRSFATED--EAIALANDS 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 157066218 1045 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07110 387 EYGLAAAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
684-1097 |
3.94e-53 |
|
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: 192.67 E-value: 3.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 684 VEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYA--------G 755
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenaeaflaD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 756 QVRDDFANE---THRPLGPVVCISPWNFPLAiftgQI----AAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVV 828
Cdd:cd07100 81 EPIETDAGKayvRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 829 QLLPGQGETVgAQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDAQGRPIPLiaETGGMNAMIVDSSALTEQVVIDVLAS 908
Cdd:cd07100 157 QNLLIDSDQV-EAIIADPRVRGVTLTGSERAG----RAVAAEAGKNLKKSVL--ELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 909 AFDSAGQRC-SALRVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKG-RPVFQAV 986
Cdd:cd07100 230 RLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 987 RENSEdarewqsGTFVAPTLIELDD-----FAElqkEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVHTRIDETIA 1061
Cdd:cd07100 309 RPDGP-------GAFYPPTVLTDVTpgmpaYDE---ELFGPVAAVIKVKDEE--EAIALANDSPFGLGGSVFTTDLERAE 376
|
410 420 430
....*....|....*....|....*....|....*.
gi 157066218 1062 QVTGSAHVGNLYVNRnMVGAVVGVqPFGGEGLSGTG 1097
Cdd:cd07100 377 RVARRLEAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
656-1097 |
1.36e-52 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 192.79 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKT 735
Cdd:PRK13252 19 TSGETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 736 FSNAI-AEVREAVDFLHYYAG----------QVRD-DFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:PRK13252 98 IQETSvVDIVTGADVLEYYAGlapalegeqiPLRGgSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 804 AEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGEtVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDaqgrpiPLIAE 883
Cdd:PRK13252 178 SEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK------EVTME 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 884 TGGMNAMIV-DSSALTEQVVIDVLASaFDSAGQRCS-ALRVLcLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVID 961
Cdd:PRK13252 251 LGGKSPLIVfDDADLDRAADIAMLAN-FYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 962 SEAKVNIERHIQTMRSKGRPVF---QAVRENsedarEWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRNQlpE 1036
Cdd:PRK13252 329 FAHRDKVLGYIEKGKAEGARLLcggERLTEG-----GFANGAFVAPTVFTdcTDDMTIVREEIFGPVMSVLTFDDED--E 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157066218 1037 LIEQINASGYGLTLGVHTRiDETIA-QVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTA-DLSRAhRVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
654-1101 |
2.49e-52 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 192.24 E-value: 2.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 654 PVAAGEMSPVINPAEPKDIVGFvREATPREVEQALESAVNN-APIWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:cd07144 18 KSSDGETIKTVNPSTGEVIASV-YAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 GKTF-SNAIAEVREAVDFLHYYAGQVrDDFANET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07144 97 GKPYhSNALGDLDEIIAVIRYYAGWA-DKIQGKTiptspnklaytlHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 800 LAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAqgrpIP 879
Cdd:cd07144 176 VIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA----VT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 880 LiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAEC-RMGNPGRLTTDIGP 958
Cdd:cd07144 252 L--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 959 VIDSEAKVNIERHIQTMRSKGRpvfQAVRENSEDAREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRNQlpE 1036
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGA---KLVYGGEKAPEGLGKGYFIPPTIFTdvPQDMRIVKEEIFGPVVVISKFKTYE--E 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157066218 1037 LIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMvgAVVGVqPFGGEGLSGTGPKAG 1101
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSsND--SDVGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
664-1055 |
3.78e-52 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 190.63 E-value: 3.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 664 INPAEPKDIVGFVrEATPREVEQALESAVN--NAPIWfATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIA 741
Cdd:cd07120 2 IDPATGEVIGTYA-DGGVAEAEAAIAAARRafDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 742 EVREAVDFLHYYAGQVR-----------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07120 80 EISGAISELRYYAGLARteagrmiepepGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQGIAILLEA-GVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGrpipliAETGGMNA 889
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 890 MIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIE 969
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 970 RHIQTMRSKGRPVFqaVRENSEDAReWQSGTFVAPTLIELDDFAE--LQKEVFGPVLHVVRYNRNQlpELIEQINASGYG 1047
Cdd:cd07120 314 RMVERAIAAGAEVV--LRGGPVTEG-LAKGAFLRPTLLEVDDPDAdiVQEEIFGPVLTLETFDDEA--EAVALANDTDYG 388
|
....*...
gi 157066218 1048 LTLGVHTR 1055
Cdd:cd07120 389 LAASVWTR 396
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
653-1097 |
4.70e-52 |
|
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: 191.12 E-value: 4.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 653 QPVAAG--EMSPVINPAEPKdIVGFVREATPREVEQALES---AVNNApiWFATPPVERAAILHRAAVLMESQMQQLIGI 727
Cdd:cd07113 7 RPVAGQseKRLDITNPATEQ-VIASVASATEADVDAAVASawrAFVSA--WAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 728 LVREAGKT--FSNAIaEVREAVDFLHYYAGQVrDDFANET------------------HRPLGPVVCISPWNFPLAIFTG 787
Cdd:cd07113 84 ETLCSGKSihLSRAF-EVGQSANFLRYFAGWA-TKINGETlapsipsmqgerytaftrREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 788 QIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGEtVGAQLTGDDRVRGVMFTGSteVATllQRNI 867
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGS--VAT--GKKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 868 ASRLDAQGRPIPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMG 947
Cdd:cd07113 237 GRQAASDLTRVTL--ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 948 NPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVfqaVRENSEDAREwqsGTFVAPTLIELD--DFAELQKEVFGPVLH 1025
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEI---VRGGEALAGE---GYFVQPTLVLARsaDSRLMREETFGPVVS 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157066218 1026 VVRYNRNQlpELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07113 389 FVPYEDEE--ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
653-1097 |
1.08e-51 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 190.12 E-value: 1.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 653 QPVA-AGEMSPVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVRE 731
Cdd:PRK13473 10 ELVAgEGEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 732 AGKTFSNAIA-EVREAVDFLHYYAGQVRD-----------DFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:PRK13473 89 CGKPLHLALNdEIPAIVDVFRFFAGAARClegkaageyleGHTSMIRRdPVGVVASIAPWNYPLMMAAWKLAPALAAGNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 799 VLAKPAEQTPLIA---AQGIAILLeagvPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDAQG 875
Cdd:PRK13473 169 VVLKPSEITPLTAlklAELAADIL----PPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATG----KHVLSAAADSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 876 RPIPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTD 955
Cdd:PRK13473 241 KRTHL--ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 956 IGPVIDSE--AKVN--IER-----HIQTMRSkGRPVFQAvrensedarewqsGTFVAPTLIE--LDDFAELQKEVFGPVL 1024
Cdd:PRK13473 319 LGPLISAAhrDRVAgfVERakalgHIRVVTG-GEAPDGK-------------GYYYEPTLLAgaRQDDEIVQREVFGPVV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157066218 1025 HVVRYnrNQLPELIEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1097
Cdd:PRK13473 385 SVTPF--DDEDQAVRWANDSDYGLASSVWTR-DVGRAHrVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
673-1097 |
3.10e-51 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 190.09 E-value: 3.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 673 VGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHY 752
Cdd:PRK09407 45 LATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 753 YAGQVRDDFA--------------NETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAIL 818
Cdd:PRK09407 125 YARRAPKLLAprrragalpvltktTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 819 LEAGVPPGVVQLLPGQGETVGAQLTgdDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALT 898
Cdd:PRK09407 205 YEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRL------IGFSLELGGKNPMIVLDDADL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 899 EQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSK 978
Cdd:PRK09407 277 DKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 979 GRPVFQAVRensedAREWQSGTFVAPT-LIELDDFAEL-QKEVFGPVLHVVRYNRnqLPELIEQINASGYGLTLGVHTRI 1056
Cdd:PRK09407 357 GATVLAGGK-----ARPDLGPLFYEPTvLTGVTPDMELaREETFGPVVSVYPVAD--VDEAVERANDTPYGLNASVWTGD 429
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 157066218 1057 DETIAQVTGSAHVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTG 1097
Cdd:PRK09407 430 TARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
644-1095 |
6.15e-51 |
|
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71), the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 274486 Cd Length: 484 Bit Score: 188.00 E-value: 6.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 644 KWQAlpmleqpvAAGEMSPVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQ 723
Cdd:TIGR03240 6 KWRA--------GQGESFASRNPAT-QEVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 724 LIGILVREAGKTFSNAIAEVRE-------AVDFLHYYAGQVRDDFANET----HRPLGPVVCISPWNFPLAIFTGQIAAA 792
Cdd:TIGR03240 77 LARVIARETGKPLWETRTEVASmigkvaiSIKAYHERTGESENPMPDGRavlrHRPHGVVAVFGPYNFPGHLPNGHIVPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 793 LAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETvGAQLTGDDRVRGVMFTGSTEVATLLQRNIAsrld 872
Cdd:TIGR03240 157 LIAGNTVVFKPSELTPWVAEETVKLWEKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFG---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 873 aqGRPIPLIA-ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCS-ALRVLCLQDEIADHTLKMLrgaMAECRMGNPG 950
Cdd:TIGR03240 232 --GRPEKILAlEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTcARRLLVPDGAQGDAFLARL---VEVAERLTVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 951 RLTTD----IGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEDArewqsgTFVAPTLIELDDFAEL-QKEVFGPVLH 1025
Cdd:TIGR03240 307 AWDAEpqpfMGAVISLRAAQRLLAAQAKLLALGGKSLLEMRQLDPGA------AFLTPGIIDVTGVAELpDEEHFGPLLQ 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1026 VVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:TIGR03240 381 VIRY--TDFDEAIAIANNTRFGLSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
658-1106 |
8.75e-51 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 187.42 E-value: 8.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 658 GEMSPVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFS 737
Cdd:PRK11241 25 GEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 738 NAIAEVREAVDFLHYYAGQVRDDFANET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:PRK11241 104 EAKGEISYAASFIEWFAEEGKRIYGDTIpghqadkrliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 806 QTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgRPIPLiaETG 885
Cdd:PRK11241 184 QTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI----KKVSL--ELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAK 965
Cdd:PRK11241 258 GNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 966 VNIERHIQTMRSKGRPVFQAVRENSedarewQSGTFVAPT-LIELDDFAELQK-EVFGPVLHVVRYNRNQlpELIEQINA 1043
Cdd:PRK11241 338 AKVEEHIADALEKGARVVCGGKAHE------LGGNFFQPTiLVDVPANAKVAKeETFGPLAPLFRFKDEA--DVIAQAND 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157066218 1044 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGG---EGLSGTGPKAGGPLYL 1106
Cdd:PRK11241 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
683-1097 |
5.29e-50 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 183.93 E-value: 5.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 683 EVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQV----- 757
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLItqiig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 758 -------RDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQL 830
Cdd:cd07105 81 gsipsdkPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 831 L---PGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLA 907
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHL------KPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 908 SAFDSAGQRC-SALRVLcLQDEIADHTLKMLRGAMAECRMGNpgrltTDIGPVIDSEAKVNIERHIQTMRSKGrpvfqAV 986
Cdd:cd07105 235 GAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKG-----AK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 987 RENSEDAREWQSGTFVAPTLIE-----LDDFAElqkEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVHTRiDETIA 1061
Cdd:cd07105 304 LVVGGLADESPSGTSMPPTILDnvtpdMDIYSE---ESFGPVVSIIRVKDEE--EAVRIANDSEYGLSAAVFTR-DLARA 377
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 157066218 1062 -QVTGSAHVGNLYVNrnmvGAVVGVQ---PFGGEGLSGTG 1097
Cdd:cd07105 378 lAVAKRIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
656-1101 |
1.11e-48 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 181.96 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPAEPKDIVGfVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKT 735
Cdd:PLN02315 31 ANGPLVSSVNPANNQPIAE-VVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 736 FSNAIAEVREAVDFLHYYAGQVR------------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:PLN02315 110 LAEGIGEVQEIIDMCDFAVGLSRqlngsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 804 AEQTPLIA---AQGIAILLEA-GVPPGVVQLLPGqGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqGRpip 879
Cdd:PLN02315 190 APTTPLITiamTKLVAEVLEKnNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GK--- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 880 LIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPV 959
Cdd:PLN02315 263 CLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 960 IDSEAKVNIERHIQTMRSKGRPVFQAVRENSEDarewqsGTFVAPTLIELDDFAELQK-EVFGPVLHVVRYnrNQLPELI 1038
Cdd:PLN02315 343 HTPESKKNFEKGIEIIKSQGGKILTGGSAIESE------GNFVQPTIVEISPDADVVKeELFGPVLYVMKF--KTLEEAI 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157066218 1039 EQINASGYGLTLGVHTRIDETIAQVTG--SAHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAG 1101
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIFKWIGplGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
658-1097 |
3.88e-48 |
|
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: 179.57 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 658 GEMSPVINPAEPKDIVGFVReATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFS 737
Cdd:cd07117 15 GETIDSYNPANGETLSEITD-ATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 738 NAIA-EVREAVDFLHYYAGQVR------DDFANET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07117 94 ETRAvDIPLAADHFRYFAGVIRaeegsaNMIDEDTlsivlREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 806 QTPLIAAQgIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETG 885
Cdd:cd07117 174 TTSLSLLE-LAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------IPATLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAK 965
Cdd:cd07117 247 GKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 966 VNIERHIQTMRSKGRPVF---QAVRENSEDArewqsGTFVAPTLIEL--DDFAELQKEVFGPVLHVVRYNRNQlpELIEQ 1040
Cdd:cd07117 327 DKILSYVDIAKEEGAKILtggHRLTENGLDK-----GFFIEPTLIVNvtNDMRVAQEEIFGPVATVIKFKTED--EVIDM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 157066218 1041 INASGYGLTLGVHTRiDETIA-QVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07117 400 ANDSEYGLGGGVFTK-DINRAlRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
656-1101 |
7.35e-48 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 180.39 E-value: 7.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPaEPKDIVGFVREATPREVEQALESA---VNNAPiWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:PLN02466 70 ASGKTFPTLDP-RTGEVIAHVAEGDAEDVNRAVAAArkaFDEGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 GKTFSNAI-AEVREAVDFLHYYAG--------QVRDD---FANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:PLN02466 148 GKPYEQSAkAELPMFARLFRYYAGwadkihglTVPADgphHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 801 AKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQrniasRLDAQGRPIPL 880
Cdd:PLN02466 228 LKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVL-----ELAAKSNLKPV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 881 IAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVI 960
Cdd:PLN02466 303 TLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQI 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 961 DSEAKVNIERHIQTMRSKGrpvfqAVRENSEDaREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPELI 1038
Cdd:PLN02466 383 DSEQFEKILRYIKSGVESG-----ATLECGGD-RFGSKGYYIQPTVFSnvQDDMLIAQDEIFGPVQSILKF--KDLDEVI 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157066218 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
656-1060 |
9.48e-48 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 178.80 E-value: 9.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPAEPKDIVGfVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKT 735
Cdd:PLN00412 28 SSGKSVAITNPSTRKTQYK-VQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 736 FSNAIAEVREAVDFLHYYA---------GQ--VRDDF-ANETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:PLN00412 107 AKDAVTEVVRSGDLISYTAeegvrilgeGKflVSDSFpGNERNKycltskiPLGVVLAIPPFNYPVNLAVSKIAPALIAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 797 NSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFT-GSTEVAtllqrniasrLDAQG 875
Cdd:PLN00412 187 NAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA----------ISKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 876 RPIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRlTTD 955
Cdd:PLN00412 257 GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 956 IGPVIdSEAKVN-IERHIQTMRSKGRPVFQAVRensedaREwqsGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRN 1032
Cdd:PLN00412 336 ITPVV-SESSANfIEGLVMDAKEKGATFCQEWK------RE---GNLIWPLLLDnvRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420
....*....|....*....|....*....
gi 157066218 1033 QlpELIEQINASGYGLTLGVHTR-IDETI 1060
Cdd:PLN00412 406 E--EGIHHCNASNFGLQGCVFTRdINKAI 432
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
671-1101 |
6.11e-47 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 176.55 E-value: 6.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 671 DIVGFVREATPREVEQALES---AVNNAPiWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFS-NAIAEVREA 746
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAareAFDHGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 747 VDFLHYYAGQVrDDFANET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQG 814
Cdd:PLN02766 126 AGLLRYYAGAA-DKIHGETlkmsrqlqgytlKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 815 IAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATL-LQRNIASRLdaqgRPIPLiaETGGMNAMIVD 893
Cdd:PLN02766 205 AHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKiMQAAATSNL----KQVSL--ELGGKSPLLIF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 894 SSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQ 973
Cdd:PLN02766 279 DDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 974 -------TMRSKGRPVFqavrensedarewQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPELIEQINAS 1044
Cdd:PLN02766 359 hgkregaTLLTGGKPCG-------------DKGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNT 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 157066218 1045 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMvgAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:PLN02766 424 KYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
656-1075 |
7.22e-47 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 175.84 E-value: 7.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKT 735
Cdd:TIGR01722 13 ASGTYIPVTNPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 736 FSNAIAEVREAVDFLHYYAG-----------QVRDDFANETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGvnsllkgetstQVATRVDVYSIRqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 804 AEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGaQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDAQGRPIPliAE 883
Cdd:TIGR01722 172 SEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIG----RYIHTTGSAHGKRVQ--AL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 884 TGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEiADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSE 963
Cdd:TIGR01722 245 GGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 964 AKVNIERHIQTMRSKGRPVFQAVRENSEDAREwqSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPELIEQI 1041
Cdd:TIGR01722 324 AKDRVASLIAGGAAEGAEVLLDGRGYKVDGYE--EGNWVGPTLLErvPPTMKAYQEEIFGPVLCVLEA--DTLEEAIALI 399
|
410 420 430
....*....|....*....|....*....|....
gi 157066218 1042 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN 433
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
663-1097 |
5.87e-45 |
|
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: 169.52 E-value: 5.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEPKDI--VGFVREAtprEVEQALESA------VNNapiWFatPPVERAAILHRAAVLMESQMQQLIGILVREAGK 734
Cdd:cd07148 3 VVNPFDLKPIgeVPTVDWA---AIDKALDTAhalfldRNN---WL--PAHERIAILERLADLMEERADELALLIAREGGK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 735 TFSNAIAEVREAVDFLHYYAGQVRDDFANE----------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:cd07148 75 PLVDAKVEVTRAIDGVELAADELGQLGGREipmgltpasagriaftTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 799 VLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGEtVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASrldaqGRPI 878
Cdd:cd07148 155 VIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLAP-----GTRC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 879 PLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGP 958
Cdd:cd07148 229 AL--EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 959 VIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEdarewqsgTFVAPTLIeLD---DFAELQKEVFGPVlhVVRYNRNQLP 1035
Cdd:cd07148 307 LIRPREVDRVEEWVNEAVAAGARLLCGGKRLSD--------TTYAPTVL-LDpprDAKVSTQEIFGPV--VCVYSYDDLD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157066218 1036 ELIEQINASGYGLTLGVHTR-ID---ETIAQVTGSAhvgnLYVNrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07148 376 EAIAQANSLPVAFQAAVFTKdLDvalKAVRRLDATA----VMVN-DHTAFRVDWMPFAGRRQSGYG 436
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
710-1084 |
4.37e-44 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 165.68 E-value: 4.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 710 LHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVR--------DDFANET----HRPLGPVVCISP 777
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegeiiqSDRPGENillfKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 778 WNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGST 857
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 858 EVAtllqrniASRLDAQGRPIPLIA-ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKM 936
Cdd:PRK10090 161 SAG-------EKIMAAAAKNITKVClELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 937 LRGAMAECRMGNP-GRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRensedaREWQSGTFVAPTLIeLD---DF 1012
Cdd:PRK10090 234 LGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGK------AVEGKGYYYPPTLL-LDvrqEM 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157066218 1013 AELQKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVG 1084
Cdd:PRK10090 307 SIMHEETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQG 376
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
656-1101 |
8.91e-44 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 166.90 E-value: 8.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 656 AAGEMSPVINPAEPKDIVGfVREATPREVEQALE---SAVNNAPiWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:cd07140 18 EGGKTYNTINPTDGSVICK-VSLATVEDVDRAVAaakEAFENGE-WGKMNARDRGRLMYRLADLMEEHQEELATIESLDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 GKTFSNAI-AEVREAVDFLHYYAG-----QVRDDFANETH----------RPLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:cd07140 96 GAVYTLALkTHVGMSIQTFRYFAGwcdkiQGKTIPINQARpnrnltltkrEPIGVCGIVIPWNYPLMMLAWKMAACLAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 797 NSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIAsrlDAQGR 876
Cdd:cd07140 176 NTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA---VSNLK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 877 PIPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:cd07140 253 KVSL--ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 957 GPvidseakvniERHIQTMRSKGRPVFQAVRENSE----DAREWQSGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYN 1030
Cdd:cd07140 331 GP----------QNHKAHLDKLVEYCERGVKEGATlvygGKQVDRPGFFFEPTVFTdvEDHMFIAKEESFGPIMIISKFD 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157066218 1031 RNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN---RNMVGAvvgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07140 401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynKTDVAA-----PFGGFKQSGFGKDLG 469
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
654-1075 |
1.42e-43 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 166.83 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 654 PVAAGEMsPVINPAEpKDIVGFVREATPREVEQALESA-----VNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGIL 728
Cdd:PLN02467 19 PVLGKRI-PVVNPAT-EETIGDIPAATAEDVDAAVEAArkafkRNKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 729 VREAGKTFSNAIAEVREAVDFLHYYAGQVR--------------DDFANETHR-PLGPVVCISPWNFPLAIFTGQIAAAL 793
Cdd:PLN02467 97 TLDCGKPLDEAAWDMDDVAGCFEYYADLAEaldakqkapvslpmETFKGYVLKePLGVVGLITPWNYPLLMATWKVAPAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 794 AAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVAtllqRNIASRLDA 873
Cdd:PLN02467 177 AAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG----RKIMTAAAQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 874 QGRPIPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLT 953
Cdd:PLN02467 253 MVKPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 954 TDIGPVIDSEAKVNIERHIQTMRSKGRPV-FQAVRenSEDAREwqsGTFVAPTLI-ELDDFAELQK-EVFGPVLHVVRYN 1030
Cdd:PLN02467 331 CRLGPVVSEGQYEKVLKFISTAKSEGATIlCGGKR--PEHLKK---GFFIEPTIItDVTTSMQIWReEVFGPVLCVKTFS 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 157066218 1031 RNqlPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:PLN02467 406 TE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
653-1097 |
4.63e-43 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 164.55 E-value: 4.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 653 QPVAAGEMSPVINPAEPKDIVGFVReATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREA 732
Cdd:cd07116 10 VAPVKGEYFDNITPVTGKVFCEVPR-STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 733 GKTFSNAI-AEVREAVDFLHYYAGQVR-----------DDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07116 89 GKPVRETLaADIPLAIDHFRYFAGCIRaqegsiseideNTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 801 AKPAEQTPLiaaqGIAILLEA---GVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrp 877
Cdd:cd07116 169 LKPAEQTPA----SILVLMELigdLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 878 IPLIAETGGMNAMIVDSSALTEQvvidvlASAFDSA-----------GQRCSALRVLCLQDEIADHTLKMLRGAMAECRM 946
Cdd:cd07116 239 IPVTLELGGKSPNIFFADVMDAD------DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 947 GNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEDAREwqSGTFVAPTLIEL-DDFAELQKEVFGPVLH 1025
Cdd:cd07116 313 GNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLL--GGGYYVPTTFKGgNKMRIFQEEIFGPVLA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157066218 1026 VVRYNRNQlpELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07116 391 VTTFKDEE--EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
626-1097 |
4.03e-42 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 162.37 E-value: 4.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 626 NEHRLASLSSALLNSALQKWQALPMLEQPVAAGEMSPVINPAEPKDIVGFVReATPREVEQALESA--VNNAPIWFATPP 703
Cdd:PRK09847 2 NFHHLAYWQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIAR-GKSVDIDRAVSAArgVFERGDWSLSSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 704 VERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE-VREAVDFLHYYA-------GQV----RDDFANETHRPLGP 771
Cdd:PRK09847 81 AKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDdIPGAARAIRWYAeaidkvyGEVattsSHELAMIVREPVGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 772 VVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGV 851
Cdd:PRK09847 161 IAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 852 MFTGSTEVATLLQRNIAsrlDAQGRPIPLiaETGGMNAMIV--DSSALtEQVVIDVLASAFDSAGQRCSALRVLCLQDEI 929
Cdd:PRK09847 241 AFTGSTRTGKQLLKDAG---DSNMKRVWL--EAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 930 ADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFqavrenseDAREWQSGTFVAPT-LIE 1008
Cdd:PRK09847 315 ADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLL--------DGRNAGLAAAIGPTiFVD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1009 LDDFAEL-QKEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVvgVQP 1087
Cdd:PRK09847 387 VDPNASLsREEIFGPVLVVTRFTSEE--QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVP 462
|
490
....*....|
gi 157066218 1088 FGGEGLSGTG 1097
Cdd:PRK09847 463 FGGYKQSGNG 472
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
674-1101 |
3.63e-38 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 149.76 E-value: 3.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 674 GFVREATPREVEQALESAVNNAPIWFATPPVERAAILHraaVLME---SQMQQLIGILVREAGKTFSNA-IAEVREAVDF 749
Cdd:cd07098 10 GSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLR---SLLKyilENQEEICRVACRDTGKTMVDAsLGEILVTCEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 750 LHY--------YAGQVRDDFANETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQG 814
Cdd:cd07098 87 IRWtlkhgekaLRPESRPGGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 815 IAILLEA----GVPPGVVQLLPGQGETvGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAM 890
Cdd:cd07098 167 LSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLELGGKDPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIER 970
Cdd:cd07098 240 IVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 971 HIQTMRSKG-RPVFQAVRENSEdarEWQSGTFVAPTLIeLD---DFAELQKEVFGPVLHVVRYNRNqlPELIEQINASGY 1046
Cdd:cd07098 320 LVADAVEKGaRLLAGGKRYPHP---EYPQGHYFPPTLL-VDvtpDMKIAQEEVFGPVMVVMKASDD--EEAVEIANSTEY 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 157066218 1047 GLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07098 394 GLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
664-1097 |
3.82e-37 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 146.42 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 664 INPAEPKDIVGFvREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEV 743
Cdd:PRK09406 6 INPATGETVKTF-TALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 744 REAVDFLHYYAGQVRDDFANET--------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPL 809
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLADEPadaaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 810 IAAQGIAILLEAGVPPGVVQ-LLPGQGEtVGAQLTgDDRVRGVMFTGStEVATllqRNIASrldAQGRPI-PLIAETGGM 887
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQtLLVGSGA-VEAILR-DPRVAAATLTGS-EPAG---RAVAA---IAGDEIkKTVLELGGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 888 NAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVN 967
Cdd:PRK09406 236 DPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 968 IERHIQTMRSKGRPVFQAVRensedaREWQSGTFVAPTLI-----ELDDFAElqkEVFGPVLHVvrYNRNQLPELIEQIN 1042
Cdd:PRK09406 316 VEKQVDDAVAAGATILCGGK------RPDGPGWFYPPTVItditpDMRLYTE---EVFGPVASL--YRVADIDEAIEIAN 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 157066218 1043 ASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrNMVGAVVGVqPFGGEGLSGTG 1097
Cdd:PRK09406 385 ATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSGYG 437
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
766-1097 |
7.07e-36 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 141.89 E-value: 7.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgIAILLEAGVPPGVVQLLPGQGEtVGAQLTgD 845
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSAL-LAKLIPKYFDPEAVAVVEGGVE-VATALL-A 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 846 DRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCL 925
Cdd:cd07087 175 EPFDHIFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 926 QDEIADHTLKMLRGAMAEcRMGNPGRLTTDIGPVIDseakvniERHIQTMRS---KGRPVFQAVRENSEDarewqsgtFV 1002
Cdd:cd07087 249 HESIKDELIEELKKAIKE-FYGEDPKESPDYGRIIN-------ERHFDRLASlldDGKVVIGGQVDKEER--------YI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1003 APTLIE---LDDfAELQKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMV 1079
Cdd:cd07087 313 APTILDdvsPDS-PLMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLL 389
|
330
....*....|....*...
gi 157066218 1080 GAVVGVQPFGGEGLSGTG 1097
Cdd:cd07087 390 HAAIPNLPFGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
663-1047 |
1.05e-34 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 141.81 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 663 VINPAEpKDIVGFVREATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAE 742
Cdd:PLN02419 133 VINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 743 VREAVDFLHYYAG----QVRDDFANETH--------RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:PLN02419 212 IFRGLEVVEHACGmatlQMGEYLPNVSNgvdtysirEPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 811 AAQGIAILLEAGVPPGVVQLLPGQGETVGAqLTGDDRVRGVMFTGSTEVATllqrNIASRLDAQGRPIPliAETGGMNAM 890
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGM----HIYARAAAKGKRIQ--SNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAeCRMGNPGRLTTDIGPVIDSEAKVNIER 970
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKA-LKVTCGSEPDADLGPVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 971 HIQTMRSKGRPVFQavrenseDARE-----WQSGTFVAPTLIE--LDDFAELQKEVFGPVLhvVRYNRNQLPELIEQINA 1043
Cdd:PLN02419 444 LIQSGVDDGAKLLL-------DGRDivvpgYEKGNFIGPTILSgvTPDMECYKEEIFGPVL--VCMQANSFDEAISIINK 514
|
....
gi 157066218 1044 SGYG 1047
Cdd:PLN02419 515 NKYG 518
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
684-1114 |
5.91e-33 |
|
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: 133.90 E-value: 5.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 684 VEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHY----YAGQVRD 759
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARafviYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 760 DFANE--------THR---PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAG-VPPGV 827
Cdd:cd07084 81 EPGNHlgqglkqqSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 828 VQLLPGQGETvGAQLTGDDRVRGVMFTGSTEVATLLqrniasRLDAqgRPIPLIAETGGMNAMIVDSSALTEQVVID-VL 906
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKL------ALDA--KQARIYLELAGFNWKVLGPDAQAVDYVAWqCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 907 ASAFDSAGQRCSALRVLCLQDeiADHTLKMLRGAMAECRMGNPGRLTtdIGPVIdseaKVNIERHIQTMRSKGRPV--FQ 984
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPE--NWSKTPLVEKLKALLARRKLEDLL--LGPVQ----TFTTLAMIAHMENLLGSVllFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 985 AVRENSEDAREWqSGTFVAPTL---IELDDFAEL--QKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDET 1059
Cdd:cd07084 304 GKELKNHSIPSI-YGACVASALfvpIDEILKTYElvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIF 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157066218 1060 IAQVT------GSAHVGNLYVNRNMVGAVVGVQPFGGeglsGTGPKAGGPLYLYRllANRP 1114
Cdd:cd07084 383 LQELIgnlwvaGRTYAILRGRTGVAPNQNHGGGPAAD----PRGAGIGGPEAIKL--VWRC 437
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
684-1054 |
5.92e-31 |
|
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: 128.04 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 684 VEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAG-----------------KTFSNAiaeVREA 746
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpearlqgelgrttgqlRLFADL---VREG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 747 vDFLhyyagQVRDDFANET------------HRPLGPVVCISPWNFPLAIFT--GQIAAALAAGNSVLAK-----PAeqT 807
Cdd:cd07129 78 -SWL-----DARIDPADPDrqplprpdlrrmLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahpahPG--T 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 808 PLIAAQGI-AILLEAGVPPGVVQLLPGQGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDaqgrPIPLIAETGG 886
Cdd:cd07129 150 SELVARAIrAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 887 MNAMIVDSSALTEQVviDVLASAFD-----SAGQRCSA--LrVLCLQDEIADHTLKMLRGAMAECrmgNPGRLTTDigpv 959
Cdd:cd07129 226 VNPVFILPGALAERG--EAIAQGFVgsltlGAGQFCTNpgL-VLVPAGPAGDAFIAALAEALAAA---PAQTMLTP---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 960 idseakvNIERHIQTMRS--KGRPVFQAVRENSEDAREWQsgtfVAPTL--IELDDFA---ELQKEVFGPVLHVVRY-NR 1031
Cdd:cd07129 296 -------GIAEAYRQGVEalAAAPGVRVLAGGAAAEGGNQ----AAPTLfkVDAAAFLadpALQEEVFGPASLVVRYdDA 364
|
410 420
....*....|....*....|...
gi 157066218 1032 NQLPELIEQINASgygLTLGVHT 1054
Cdd:cd07129 365 AELLAVAEALEGQ---LTATIHG 384
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
766-1102 |
1.42e-29 |
|
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: 123.49 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgIAILLEAGVPPGVVQLLPGQGETVGAQLtgD 845
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAV-IAKIIREAFDEDEVAVFEGDAEVAQALL--E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 846 DRVRGVMFTGSTEVATLLQ----RNIASrldaqgrpIPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALR 921
Cdd:cd07134 175 LPFDHIFFTGSPAVGKIVMaaaaKHLAS--------VTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 922 VLCLQDEIADHTLKMLRGAMAECRMGNPGRL-TTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEDarewqsgT 1000
Cdd:cd07134 245 YVFVHESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQ-------R 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1001 FVAPTLIE--LDDFAELQKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNM 1078
Cdd:cd07134 318 YIAPTVLTnvTPDMKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVV 395
|
330 340
....*....|....*....|....
gi 157066218 1079 VGAVVGVQPFGGEGLSGTGpKAGG 1102
Cdd:cd07134 396 LHFLNPNLPFGGVNNSGIG-SYHG 418
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
766-1097 |
9.39e-29 |
|
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: 121.17 E-value: 9.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLiAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLtgD 845
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPH-TAALLAELVPKYLDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 846 DRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALR-VLC 924
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIAEAAAKHL------TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDyVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 925 lQDEIADHTLKMLRGAMAECRMGNPGRLtTDIGPVIDSEAKVNIERHIQTmrSKGRPVFQAVRENSEdarewqsgTFVAP 1004
Cdd:cd07135 257 -DPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLDT--TKGKVVIGGEMDEAT--------RFIPP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1005 TLI---ELDDfAELQKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGA 1081
Cdd:cd07135 325 TIVsdvSWDD-SLMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHV 401
|
330
....*....|....*.
gi 157066218 1082 VVGVQPFGGEGLSGTG 1097
Cdd:cd07135 402 GVDNAPFGGVGDSGYG 417
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
679-1075 |
1.59e-28 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 120.74 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 679 ATPREVEQALESAVNNAPIWFATPPVERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQ-- 756
Cdd:PRK13968 26 AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHgp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 757 ---------VRDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTpLIAAQGIA-ILLEAGVPPG 826
Cdd:PRK13968 106 amlkaeptlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV-MGCAQLIAqVFKDAGIPQG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 827 VVQLLPGQGETVgAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAqgrpipLIAETGGMNAMIVDSSALTEQVVIDVL 906
Cdd:PRK13968 185 VYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDPFIVLNDADLELAVKAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 907 ASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAV 986
Cdd:PRK13968 258 AGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEGARLLLGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 987 RENSedarewQSGTFVAPTLI-----ELDDFAElqkEVFGPVLHV-VRYNRNQLPELieqINASGYGLTLGVHTRIDETI 1060
Cdd:PRK13968 338 EKIA------GAGNYYAPTVLanvtpEMTAFRE---ELFGPVAAItVAKDAEHALEL---ANDSEFGLSATIFTTDETQA 405
|
410
....*....|....*
gi 157066218 1061 AQVTGSAHVGNLYVN 1075
Cdd:PRK13968 406 RQMAARLECGGVFIN 420
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
768-1097 |
5.77e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 119.75 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIaAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTgdDR 847
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT-SKLMAKLLTKYLDPSYVRVIEGGVEVTTELLK--EP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 848 VRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQD 927
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 928 EIADHTLKMLRGAMAEcRMGNPGRLTTDIGPVIDSEAkvnIERHIQTMRSKGRPVFQAVRENSEDarewqsgTFVAPTLI 1007
Cdd:PTZ00381 260 SIKDKFIEALKEAIKE-FFGEDPKKSEDYSRIVNEFH---TKRLAELIKDHGGKVVYGGEVDIEN-------KYVAPTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1008 ---ELDDFAeLQKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHT---RIDETIAQVTGSahvGNLYVNRNMVGA 1081
Cdd:PTZ00381 329 vnpDLDSPL-MQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGedkRHKELVLENTSS---GAVVINDCVFHL 402
|
330
....*....|....*.
gi 157066218 1082 VVGVQPFGGEGLSGTG 1097
Cdd:PTZ00381 403 LNPNLPFGGVGNSGMG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
765-1097 |
1.86e-26 |
|
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: 114.12 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 765 THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgIAILLEAGVPPGVVQLLPGQGEtVGAQLTG 844
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSAL-LAELLAEYFDEDEVAVVTGGAD-VAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 845 ---DDrvrgVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALR 921
Cdd:cd07133 176 lpfDH----LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 922 -VLCLQDEIaDHTLKMLRGAMAEC---RMGNPgrlttDIGPVIDSEAKVNIERHIQTMRSKGRPVFQaVRENSEDArewQ 997
Cdd:cd07133 246 yVLVPEDKL-EEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIE-LNPAGEDF---A 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 998 SGTFVAPTLIE--LDDFAELQKEVFGPVLHVVRYNRnqLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:cd07133 316 ATRKLPPTLVLnvTDDMRVMQEEIFGPILPILTYDS--LDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN 393
|
330 340
....*....|....*....|..
gi 157066218 1076 RNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07133 394 DTLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
689-1097 |
9.91e-23 |
|
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: 103.07 E-value: 9.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 689 ESAVNNAPIWFA---TPPVE-RAAILHRAAVLMESQMQQLIGILVREAGKT-FSNAIAEV-------REAVDFLHYYAG- 755
Cdd:cd07132 1 AEAVRRAREAFSsgkTRPLEfRIQQLEALLRMLEENEDEIVEALAKDLRKPkFEAVLSEIllvkneiKYAISNLPEWMKp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 756 -QVRDDFANET------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPlIAAQGIAILLEAGVPPGVV 828
Cdd:cd07132 81 ePVKKNLATLLddvyiyKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP-ATAKLLAELIPKYLDKECY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 829 Q-LLPGQGETvgAQLTgDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLA 907
Cdd:cd07132 160 PvVLGGVEET--TELL-KQRFDYIFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 908 SAFDSAGQRCSALR-VLClQDEIADHTLKMLRGAMAECrMGNPGRLTTDIGPVIDseakvniERHIQTMR---SKGRPVF 983
Cdd:cd07132 231 GKFINAGQTCIAPDyVLC-TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIIN-------DRHFQRLKkllSGGKVAI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 984 QAvrenSEDAREwqsgTFVAPTLieLDDFAE----LQKEVFGPVLHVVryNRNQLPELIEQINASGYGLTLGVHTRIDET 1059
Cdd:cd07132 302 GG----QTDEKE----RYIAPTV--LTDVKPsdpvMQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVFSNNKKV 369
|
410 420 430
....*....|....*....|....*....|....*...
gi 157066218 1060 IAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07132 370 INKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMG 407
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
705-1102 |
3.14e-21 |
|
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: 99.27 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 705 ERAAILHR-AAVLMESQmQQLIGILVReAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRPLGPV----------- 772
Cdd:cd07128 60 ERAAMLKAlAKYLMERK-EDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVeplskdgtfvg 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 773 -----------VCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGV-PPGVVQLLPGQGETVGA 840
Cdd:cd07128 138 qhiltprrgvaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLD 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 841 QLTGDDRVrgvMFTGSTEVATLLQR--NIASRldaqgrPIPLIAETGGMNAMIV--DSSALTEQ---VVIDVLASAFDSA 913
Cdd:cd07128 218 HLGEQDVV---AFTGSAATAAKLRAhpNIVAR------SIRFNAEADSLNAAILgpDATPGTPEfdlFVKEVAREMTVKA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 914 GQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEDA 993
Cdd:cd07128 289 GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 994 REWQSGTFVAPTLIELDD----FAELQKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQ-VTGSA- 1067
Cdd:cd07128 369 ADAEKGAFFPPTLLLCDDpdaaTAVHDVEAFGPVATLMPY--DSLAEAIELAARGRGSLVASVVTNDPAFARElVLGAAp 446
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 157066218 1068 HVGNLYV-NRNMVGAVVG---VQP---FGGEGLSGTGPKAGG 1102
Cdd:cd07128 447 YHGRLLVlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGG 488
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
768-1097 |
1.16e-20 |
|
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: 96.33 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgIAILLEAGVPPGVVQLLPGqGETVGAQLTgDDR 847
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSAL-LAKLIPEYLDTKAIKVIEG-GVPETTALL-EQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 848 VRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDS-AGQRCSALRVLCLQ 926
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 927 DEIADHTLKMLRGAMAECRMGNPGRlttdigpvIDSEAKVNIERHIQtmRSKG---RPVFQA--VRENSEDAREwqsgTF 1001
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENPKE--------SKDLSRIVNSHHFQ--RLSRlldDPSVADkiVHGGERDEKN----LY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1002 VAPTLIeLD---DFAELQKEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNM 1078
Cdd:cd07137 318 IEPTIL-LDpplDSSIMTEEIFGPLLPIITVKKIE--ESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTV 394
|
330
....*....|....*....
gi 157066218 1079 VGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07137 395 VQYAIDTLPFGGVGESGFG 413
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
768-1097 |
1.30e-20 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 97.10 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAqgiaiLLEAGVP----PGVVQLLPGqGETVGAQLT 843
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPkyldSKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 844 gDDRVRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVD--SSALTEQVVID-VLASAFDS-AGQRCSA 919
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDslSSSRDTKVAVNrIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 920 LRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLttdigpviDSEAKVNIERHIQtmRSKG---RPVFQA--VRENSEDAR 994
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRES--------KSMARILNKKHFQ--RLSNllkDPRVAAsiVHGGSIDEK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 995 EwqsgTFVAPTLIeLD---DFAELQKEVFGPVLHVVRYNRNQlpELIEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVG 1070
Cdd:PLN02203 325 K----LFIEPTIL-LNpplDSDIMTEEIFGPLLPIITVKKIE--DSIAFINSKPKPLAIYAFTN-NEKLKRrILSETSSG 396
|
330 340
....*....|....*....|....*..
gi 157066218 1071 NLYVNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:PLN02203 397 SVTFNDAIIQYACDSLPFGGVGESGFG 423
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
709-1073 |
7.24e-19 |
|
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: 91.40 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 709 ILHRAAVLM-----ESQMQQLIGilvREAGKTFSNAIAEVREAVDFLHYYAG-QVR----------DDFANETHR---PL 769
Cdd:cd07126 67 VSHRVAHELrkpevEDFFARLIQ---RVAPKSDAQALGEVVVTRKFLENFAGdQVRflarsfnvpgDHQGQQSSGyrwPY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 770 GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGQGETVGAQLTgDDRVR 849
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILL-EANPR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 850 GVMFTGSTEVATLLQRniasrlDAQGRpipLIAETGGMNAMIVDSSALTEQVVIDVL-ASAFDSAGQRCSALRVLCLQDE 928
Cdd:cd07126 223 MTLFTGSSKVAERLAL------ELHGK---VKLEDAGFDWKILGPDVSDVDYVAWQCdQDAYACSGQKCSAQSILFAHEN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 929 IADHTLKMLRGAMAECRmgNPGRLTtdIGPVI--DSEAKVN-IERHIQTMRSK----GRPVFQAVRENSEDAREwQSGTF 1001
Cdd:cd07126 294 WVQAGILDKLKALAEQR--KLEDLT--IGPVLtwTTERILDhVDKLLAIPGAKvlfgGKPLTNHSIPSIYGAYE-PTAVF 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157066218 1002 VA-PTLIELDDFAELQKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLY 1073
Cdd:cd07126 369 VPlEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
768-1097 |
9.42e-19 |
|
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: 90.64 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgIAILLEAGVPPGVVQLLPGQGETVGAQLtgDDR 847
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKV-IAKIIEETFDEEYVAVVEGGVEENQELL--DQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 848 VRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRVLCLQD 927
Cdd:cd07136 177 FDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 928 EIADHTLKMLRGAMAEcRMGNPGRLTTDIGPVIDseakvniERH---IQTMRSKGRPVFQAvrENSEDARewqsgtFVAP 1004
Cdd:cd07136 251 SVKEKFIKELKEEIKK-FYGEDPLESPDYGRIIN-------EKHfdrLAGLLDNGKIVFGG--NTDRETL------YIEP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1005 TLIE---LDDfAELQKEVFGPVLHVVRYnrNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGS------------AHV 1069
Cdd:cd07136 315 TILDnvtWDD-PVMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENlsfgggcindtiMHL 391
|
330 340
....*....|....*....|....*...
gi 157066218 1070 GNLYVnrnmvgavvgvqPFGGEGLSGTG 1097
Cdd:cd07136 392 ANPYL------------PFGGVGNSGMG 407
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
89-136 |
1.46e-17 |
|
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: 77.50 E-value: 1.46e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 157066218 89 SVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLR 136
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
705-1029 |
4.47e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 82.83 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 705 ERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYA------GQVR------------DDFANETH 766
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalGDARllrdgeavqlgkDPAFQGQH 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 767 --RPL-GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGV-PPGVVQLLPGQGETVGAQL 842
Cdd:PRK11903 144 vlVPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 843 TGDDRVRgvmFTGSTEVATLLQRNIASrldAQgRPIPLIAETGGMNAMI-----VDSSALTEQVVIDVLASAFDSAGQRC 917
Cdd:PRK11903 224 QPFDVVS---FTGSAETAAVLRSHPAV---VQ-RSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQKC 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 918 SALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMRSKGRPVFQAVRENSEDArEWQ 997
Cdd:PRK11903 297 TAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVDA-DPA 375
|
330 340 350
....*....|....*....|....*....|....*.
gi 157066218 998 SGTFVAPTLIELDD--FAEL--QKEVFGPVLHVVRY 1029
Cdd:PRK11903 376 VAACVGPTLLGASDpdAATAvhDVEVFGPVATLLPY 411
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
768-1101 |
7.41e-16 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 82.02 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgIAILLEAGVPPGVVQLLPGQGETVGAQLtgDDR 847
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAL-LAKLLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 848 VRGVMFTGSTEVATLLQRNIASRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVIDVLASAFD-SAGQRCSALRVLCLQ 926
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 927 DEIADHTLKMLRGAMAECRMGNPGRlTTDIGPVIDSEAKVNIERHIQTMRSKGRPVF--QAVRENSEdarewqsgtfVAP 1004
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYggEKDRENLK----------IAP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 1005 TLIeLD---DFAELQKEVFGPVLHVVryNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGA 1081
Cdd:PLN02174 332 TIL-LDvplDSLIMSEEIFGPLLPIL--TLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHL 408
|
330 340
....*....|....*....|
gi 157066218 1082 VVGVQPFGGEGLSGTGPKAG 1101
Cdd:PLN02174 409 ALHTLPFGGVGESGMGAYHG 428
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-67 |
7.67e-15 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 70.24 E-value: 7.67e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157066218 2 GTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLENSDTLPE--LPALLSGAANESDEA 67
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQegLAAADAGEFVSHEEV 68
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
767-1113 |
3.79e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 64.04 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 767 RPLGPVVCISP---WNFPLAIFtgqiaAALAAGNSVLAKPAEQTPLIAAQGI----AILLEAGVPPGVVQLLPGQ-GETV 838
Cdd:cd07127 194 RGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFDPNLVTLAADTpEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 839 GAQLTGDDRVRGVMFTGSTEVATLLQRNIasrldaqgRPIPLIAETGGMNAMIVDSsalTEQVVIDVLASAFDSA---GQ 915
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDWLEANA--------RQAQVYTEKAGVNTVVVDS---TDDLKAMLRNLAFSLSlysGQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 916 RCSALRVLCLQ-------------DEIADHTLKMLRGAmaecrMGNPGRLTTDIGPVIDSEAKVNIErhiqtmrsKGRPV 982
Cdd:cd07127 338 MCTTPQNIYVPrdgiqtddgrksfDEVAADLAAAIDGL-----LADPARAAALLGAIQSPDTLARIA--------EARQL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 983 FQAVRENSEDAR-EWQSGTFVAPTLIELD--DFAELQKEVFGPVLHVVRYNR-NQLPELIEQINASGYGLTLGVHTRIDE 1058
Cdd:cd07127 405 GEVLLASEAVAHpEFPDARVRTPLLLKLDasDEAAYAEERFGPIAFVVATDStDHSIELARESVREHGAMTVGVYSTDPE 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 157066218 1059 TIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG--PKAGGPLYLYRLLANR 1113
Cdd:cd07127 485 VVERVQEAALDAGVALSINLTGGVFVNQSAAFSDFHGTGanPAANAALTDGAFVANR 541
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-46 |
1.01e-09 |
|
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar proteins; This family includes the N-terminal ribbon-helix-helix (RHH) domain of Shewanella oneidensis CopA(SO), a newly identified type II antitoxin, as well as the N-terminal RHH domain of Escherichia coli PutA flavoprotein, among other similar proteins, many of which are as yet uncharacterized. CopA(SO) is a typical RHH antitoxin that includes an ordered N-terminal domain (CopA(SO)-N) and a disordered C-terminal domain (CopA(SO)-C). Biophysical investigation indicates allosteric effects of CopA(SO)-N on CopA(SO)-C; DNA binding of CopA(SO)-N appears to induce CopA(SO)-C to fold and self-associate the C-terminal domain. The multifunctional E. coli proline utilization A (PutA) flavoprotein functions as a membrane-associated proline catabolic enzyme as well as a transcriptional repressor of the proline utilization genes putA and putP. The N-terminal domain of PutA is a transcriptional regulator with an RHH fold; structure studies show that it forms a homodimer to bind one DNA duplex. This family also includes orphan antitoxin ParD2, an antitoxin component of a non-functional type II toxin-antitoxin (TA system); it does not neutralize the effect of any of the RelE or ParE toxins.
Pssm-ID: 409023 Cd Length: 44 Bit Score: 55.07 E-value: 1.01e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 157066218 4 TTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLEN 46
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREEW 43
|
|
| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-45 |
4.60e-09 |
|
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription factor NikR, and similar proteins; This family includes the ribbon-helix-helix (RHH) domains of transcriptional repressor CopG, nickel-responsive transcription factor NikR, several antitoxins such as Shewanella oneidensis CopA(SO), Burkholderia pseudomallei HicB, and Caulobacter crescentus ParD, and similar proteins. CopG, a homodimeric RHH protein of around 45 residues, constitutes one of the smallest natural transcriptional repressors characterized and is the prototype of a series of repressor proteins encoded by plasmids that exhibit a similar genetic structure at their leading strand initiation and control regions. It is involved in the control of plasmid copy number. NikR, which consists of the N-terminal DNA-binding RHH domain and the C-terminal metal-binding domain (MBD) with four nickel ions, regulates several genes; in Helicobacter pylori, NikR regulates the urease enzyme under extreme acidic conditions, and is involved in the intracellular physiology of nickel. Protein HicB is part of the HicAB toxin-antitoxin (TA) system, where the toxins are RNases, found in many bacteria. In Burkholderia pseudomallei, the HicAB system may play a role in disease by regulating the frequency of persister cells, while in Yersinia pestis HicB acts as an autoregulatory protein that inhibits HicA, which acts as an mRNase. In Escherichia coli, an excess of HicA has been shown to de-repress a HicB-DNA complex and restore transcription of HicB. The CopG family RHH domain, represented by this model, forms a homodimer and binds DNA.
Pssm-ID: 409020 Cd Length: 42 Bit Score: 53.28 E-value: 4.60e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 157066218 4 TTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLE 45
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLERLE 42
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| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
768-996 |
4.37e-06 |
|
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: 50.68 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 768 PLGPVVCISPWNFPLAIFTgQIAAALAAGNSVLAKPAEQTPlIAAQGIAILLEAGVPPG----VVQLLPGQGETVGAQLT 843
Cdd:cd07077 100 PIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkiLVLYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157066218 844 GDDRVRGVMFTGSTEVATLLQRNiasrldaqGRPIPLIAETGGMNAMIVDSSALTEQVVIDVLASA-FDSAGqrCSALRV 922
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA--CASEQN 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157066218 923 LCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKVNIERHIQTMrskgrPVFQAVRENSEDAREW 996
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFDDEALESMTPLE-----CQFRVLDVISAVENAW 316
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|
| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
1-45 |
3.40e-03 |
|
Predicted DNA-binding protein with an HTH domain [General function prediction only];
Pssm-ID: 443745 Cd Length: 76 Bit Score: 37.57 E-value: 3.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 157066218 1 MGTTTmgVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLE 45
Cdd:COG4710 1 MKMLS--IRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
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