|
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: 2866.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1 MGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFNYLEKLENDETLPEIPALLAGAANESEEGALPTEEPHQPFLD 80
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADTPAEEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 81 FAEQILPQSVTRSAITAAWRRPETDAVPMLLEQARLPQPMADQAHKLAYQLAEKLRNQKNASGRAGMVQSLLQEFSLSSQ 160
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGRAGMVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 161 EGVALMCLAEALLRIPDKGTRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEANLSRSLNRIIGKSG 240
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGI 320
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 321 YEGPGISIKLSALHPRYSRAQYDRVMDELYPRLKSLTLLARSYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 401 FVIQAYQKRCPFVIDYLVDLAGRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAAPNLI 480
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 481 YPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYDQVVGKVSDGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 561 GANTSFVNRIADTSLPLDELVADPVCAVEELARQEGQPGLPHPKIPLPRELYGSGRVNSAGLDLANEHRLASLSSSLLTN 640
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLAS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 641 AQQQWRAKPVLEQPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQ 720
Cdd:PRK11809 641 AHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQ 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 721 MQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:PRK11809 721 MQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 801 AKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLDPQGRPTPL 880
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 881 IAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVI 960
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 961 DAEAKQNIDKHIQALRGKGRSVFQAVRENSEDrreWAQGTFVPPTLIELESFDELEKEVFGPVLHVVRYNRNKLGALVEQ 1040
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSED---WQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQ 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLYRLLASRPEDALLT 1120
Cdd:PRK11809 1038 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAV 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1121 TLNRQDAHYPVDSQLKSVLEQPLTALRAWAIKR-PALQALCDRYGELAQAGTQRVLPGPTGERNTWTLVPRERVLCLADN 1199
Cdd:PRK11809 1118 TLARQDAEYPVDAQLRAALLAPLTALREWAAERePELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADT 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1200 EEDALIQLAAATAAGCEVLWPEDGLQRGLAKQLPTAVSERIRFAGREQIASAQFDAVIYHGDSDQLRELCQQVAARDGAI 1279
Cdd:PRK11809 1198 EQDALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPI 1277
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|.
gi 689260967 1280 VSVQGFARGETNLLLERLYHERSLSVNTAAAGGNASLMTIG 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: 2032.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 77 PFLDFAEQILPQSVTRSAITAAWRRPETDAVPMLLEQARLPQPMADQAHKLAYQLAEKLRnqknASGRAGMVQSLLQEFS 156
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALR----AKRKGTGVEALLQEYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 157 LSSQEGVALMCLAEALLRIPDKGTRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEANLSRSLNRII 236
Cdd:PRK11905 77 LSSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASN 316
Cdd:PRK11905 157 ARLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 317 GRGIYEGPGISIKLSALHPRYSRAQYDRVMDELYPRLKSLTLLARSYDIGINIDAEEADRLEISLDLLEKLCFEPELAGW 396
Cdd:PRK11905 237 GRGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 397 NGIGFVIQAYQKRCPFVIDYLVDLAGRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAA 476
Cdd:PRK11905 317 NGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 477 PNLIYPQFATHNAHTLAAIYQLAGQNYypgQYEFQCLHGMGEPLYDQVVGKvsdGKLNRPCRIYAPVGTHETLLAYLVRR 556
Cdd:PRK11905 397 RDVIYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGK---EKLGRPCRIYAPVGTHETLLAYLVRR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 557 LLENGANTSFVNRIADTSLPLDELVADPVCAVEELarqegqPGLPHPKIPLPRELYGSGRVNSAGLDLANEHRLASLSSS 636
Cdd:PRK11905 471 LLENGANSSFVNRIVDENVPVEELIADPVEKVAAM------GVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 637 LLTNAQQQWRAKPVLEQPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAML 716
Cdd:PRK11905 545 LNAFAAKTWHAAPLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADL 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 717 MEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAG 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 797 NSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqGR 876
Cdd:PRK11905 705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GP 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 877 PTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDI 956
Cdd:PRK11905 782 PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDV 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 957 GPVIDAEAKQNIDKHIQALRGKGRSVFQAvrensEDRREWAQGTFVPPTLIELESFDELEKEVFGPVLHVVRYNRNKLGA 1036
Cdd:PRK11905 862 GPVIDAEAQANIEAHIEAMRAAGRLVHQL-----PLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDR 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1037 LVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLYRLLASRPED 1116
Cdd:PRK11905 937 VIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAPTP 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1117 ALlttlnrqDAHYPVDsqLKSVLEQPLTALRAWAikRPALQALCDRYGELAQAGTQRVLPGPTGERNTWTLVPRERVLCL 1196
Cdd:PRK11905 1017 IP-------PAHESVD--TDAAARDFLAWLDKEG--KAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCV 1085
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1197 ADNEEDALIQLAAATAAGCEVLWPEDGLQRGLAKQLPTAVSERIRFAgREQIASAQFDAVIYHGDSDQLRELCQQVAARD 1276
Cdd:PRK11905 1086 ADTEEALLRQLAAALATGNVAVVAADSGLAAALADLPGLVAARIDWT-QDWEADDPFAGALLEGDAERARAVRQALAARP 1164
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 689260967 1277 GAIVSVQGfARGETNLLLERLYHERSLSVNTAAAGGNASLMTIG 1320
Cdd:PRK11905 1165 GAIVPLIA-AEPTDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
82-1317 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1570.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 82 AEQILPQSVTRSAITAAWRRPETDAVPMLLEQARLPQPMADQAHKLAYQLAEKLRNQKNASGRAGMVQSLLQEFSLSSQE 161
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 162 GVALMCLAEALLRIPDKGTRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEA--NLSRSLNRIIGKS 239
Cdd:COG4230 81 SEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESslSLASGLLRLLGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 240 GEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRG 319
Cdd:COG4230 161 GRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 320 IYEGPGISIKLSALHPRYSRAQYDRVMDELYPRLKSLTLLARSYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGI 399
Cdd:COG4230 241 GGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 400 GFVI----QAYQKRCPFVIDYLVDLAGRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLA 475
Cdd:COG4230 321 GGGVgqavQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 476 APNLIYPQFATHNAHTLAAIYQLAGQnyypGQYEFQCLHGMGEPLYDQVVgkvsDGKLNRPCRIYAPVGTHETLLAYLVR 555
Cdd:COG4230 401 AQPAFAPQFATHAAATAAAAAAAGGG----GEFEFQCLHGMGEYLYDQVG----RGKLGRPCRIYAPVGSHEDLLAYLVR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 556 RLLENGANTSFVNRIADTSLPLDELVADPVCAVEELarqegqPGLPHPKIPLPRELYGSGRVNSAGLDLANEHRLASLSS 635
Cdd:COG4230 473 RLLENGANSSFVNRIADEDVPVEELIADPVEKARAL------GGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 636 SLLTNAQQQWRAKPVLEQPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAM 715
Cdd:COG4230 547 ALAAAAEKQWQAAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAAD 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 716 LMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRDDFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALA 794
Cdd:COG4230 627 LLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvLRGRGVFVCISPWNFPLAIFTGQVAAALA 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 795 AGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRldpQ 874
Cdd:COG4230 707 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR---D 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 875 GRPTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTT 954
Cdd:COG4230 784 GPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLST 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 955 DIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRensedRREWAQGTFVPPTLIELESFDELEKEVFGPVLHVVRYNRNKL 1034
Cdd:COG4230 864 DVGPVIDAEARANLEAHIERMRAEGRLVHQLPL-----PEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADEL 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1035 GALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLYRLLASRP 1114
Cdd:COG4230 939 DKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERT 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1115 EDALLTTLNRQDAhypvdsqlksvleqpLTALRAWaikrpalqalcdrygeLAQAGTQRVLPGPTGERNTWTLVPRERVL 1194
Cdd:COG4230 1019 VTVNTTAAGGNAS---------------LLALGDW----------------LASLLGALTLPGPTGERNTLTLRPRGRVL 1067
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1195 CLADNEEDALIQLAAATAAGCEVLWPEDGLQRGLAKQLptavserirfagreqiaSAQFDAVIYHGdsdQLRELCQQVAA 1274
Cdd:COG4230 1068 CLADSLEALLAQLAAALATGNRAVVAADLALAGLPAVL-----------------LPPFDAVLFEG---RLRALRQALAA 1127
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|...
gi 689260967 1275 RDGAIVSVQGFArgetnLLLERLYHErslsvntaaAGGNASLM 1317
Cdd:COG4230 1128 RDGAIVPVIDAG-----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: 1549.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 79 LDFAEQILPQSVTRSAITAAWRRPETDAVPMLLEQARLPQPMADQAHKLAYQLAEKLRNQKnasGRAGMVQSLLQEFSLS 158
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKK---KKLGGIDAFLQEYSLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 159 SQEGVALMCLAEALLRIPDKGTRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEA--NLSRSLNRII 236
Cdd:PRK11904 78 TEEGIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKAdgTPSGVLKRLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASN 316
Cdd:PRK11904 158 NRLGEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 317 GRGIYEGPGISIKLSALHPRYSRAQYDRVMDELYPRLKSLTLLARSYDIGINIDAEEADRLEISLDLLEKLCFEPELAGW 396
Cdd:PRK11904 238 GADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 397 NGIGFVIQAYQKRCPFVIDYLVDLAGRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAA 476
Cdd:PRK11904 318 GGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 477 PNLIYPQFATHNAHTLAAIYQLAGQnyypGQYEFQCLHGMGEPLYDQVVgkvsdGKLNRPCRIYAPVGTHETLLAYLVRR 556
Cdd:PRK11904 398 RGAIYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 557 LLENGANTSFVNRIADTSLPLDELVADPVCAVEELARqegqpgLPHPKIPLPRELYGSGRVNSAGLDLANEHRLASLSSS 636
Cdd:PRK11904 469 LLENGANSSFVHRLVDPDVPIEELVADPVEKLRSFET------LPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 637 LLTNAQQQWRAKPVleqPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAML 716
Cdd:PRK11904 543 IAAFLEKQWQAGPI---INGEGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 717 MEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRDDFDNETHRPlGPV--------------VCISPWNFPL 782
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLP-GPTgesnelrlhgrgvfVCISPWNFPL 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 783 AIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASL 862
Cdd:PRK11904 699 AIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARI 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 863 LQRNIASRldpQGRPTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMA 942
Cdd:PRK11904 779 INRTLAAR---DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMA 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 943 ECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAvrensEDRREWAQGTFVPPTLIELESFDELEKEVFGP 1022
Cdd:PRK11904 856 ELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQL-----PLPAGTENGHFVAPTAFEIDSISQLEREVFGP 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1023 VLHVVRYNRNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGG 1102
Cdd:PRK11904 931 ILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGG 1010
|
1050
....*....|.
gi 689260967 1103 PMYLYRLLASR 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: 816.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 610 ELYGSGRVNSAGLDLANEHRLASLSSSLLTNAQQQWRAKPVL-EQPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQAL 688
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIgHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 689 ENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRDDFDNETHRP 768
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 769 LGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRV 848
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 849 RGVMFTGSTEVASLLQRNIASRLDPQGrptPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDD 928
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDAPV---PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 929 IADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRENSedrREWAQGTFVPPTLIE 1008
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDS---RACQHGTFVAPTLFE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1009 LESFDELEKEVFGPVLHVVRYNRNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPF 1088
Cdd:TIGR01238 395 LDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPF 474
|
490 500
....*....|....*....|....*.
gi 689260967 1089 GGEGLSGTGPKAGGPMYLYRLLASRP 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: 694.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 114 ARLPQPMADQAHKLAYQLAEKLRNQknasgRAGMVQSLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKISngn 193
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAA-----PEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 194 wqshigRSPSLFVNAATWGLLFTgrlvsthneanlsrslnrIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANAR 273
Cdd:COG0506 75 ------KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 274 KLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASngrgiYEGPGISIKLSALHPRYSRAQYDRVMDELYPRL 353
Cdd:COG0506 131 KLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 354 KSLTLLARSYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLVDLAGRSRRRLMIRLV 433
Cdd:COG0506 206 RPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 434 KGAYWDSEIKRAQMDGLeGYPVYTRKVYTDVSYLACAKKLLAAPNLIYPQFATHNAHTLAAIYQLAGQ-NYYPGQYEFQC 512
Cdd:COG0506 286 KGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 513 LHGMGEPLYDQVVgKVSDGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVcaveelA 592
Cdd:COG0506 365 LYGMGEDLQRALA-AVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPR------F 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 593 RQEGQPGLPHPKIPLPRELYGSGRVNSAGLDLANEHRLASLSSSLLTNAQQQWRAKPVLEQPVDDGEMAPVVNPAEPKDI 672
Cdd:COG0506 438 LAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 673 VGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHY 752
Cdd:COG0506 518 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAA 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 753 YAGQVRDDFDNETHRP--------LGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVP 824
Cdd:COG0506 598 AAAAAARAAAPPPPPPgglvallpLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLL 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 825 PGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLDPQGRPTPLIAETGGMNAMIVDSSALTEQVVVD 904
Cdd:COG0506 678 GGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVA 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 905 VVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEakqnIDKHIQALRGKGRSVFQ 984
Cdd:COG0506 758 ASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAA----AAALLLALAALELGEEE 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 985 AVRENSEDRREWAQGTFVPPTLIELESFDELEKEVFGPVLHVVRYNRNKLGALVEQINASGYGLTLGVHTRIDETIAQVT 1064
Cdd:COG0506 834 LLLPGGGPLVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGR 913
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 689260967 1065 GSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLYRLLASRPEDALLTTLN 1123
Cdd:COG0506 914 VGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAA 972
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
643-1109 |
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: 678.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 643 QQWRAKPVL-EQPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQM 721
Cdd:cd07125 29 KEWEAIPIInGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 722 QQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRDDFD-----------NETH-RPLGPVVCISPWNFPLAIFTGQI 789
Cdd:cd07125 109 GELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFVCISPWNFPLAIFTGQI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 790 AAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIAS 869
Cdd:cd07125 189 AAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 870 RLDPQgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNP 949
Cdd:cd07125 269 RDGPI---LPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 950 GRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRENSedrrewaQGTFVPPTLIELESFDELEKEVFGPVLHVVRY 1029
Cdd:cd07125 346 WDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDG-------NGYFVAPGIIEIVGIFDLTTEVFGPILHVIRF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1030 NRNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLYRL 1109
Cdd:cd07125 419 KAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRF 498
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
643-1110 |
3.15e-150 |
|
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: 463.59 E-value: 3.15e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 643 QQWRAKP-VLEQP-VDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQ 720
Cdd:cd07083 14 EFGRAYPlVIGGEwVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 721 MQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRD------------DFDNET-HRPLGPVVCISPWNFPLAIFTG 787
Cdd:cd07083 94 RRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRlrypavevvpypGEDNESfYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 788 QIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNI 867
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 868 ASRLDPQGRPTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMG 947
Cdd:cd07083 254 ARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 948 NPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRENSEdrrewaqGTFVPPTLIELESFDE--LEKEVFGPVLH 1025
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGE-------GYFVAPTVVEEVPPKAriAQEEIFGPVLS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1026 VVRYNRNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMY 1105
Cdd:cd07083 407 VIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHY 486
|
....*
gi 689260967 1106 LYRLL 1110
Cdd:cd07083 487 LRRFL 491
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
268-569 |
5.75e-148 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 449.25 E-value: 5.75e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 268 ALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMD 347
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 348 ELYPRLKSLTLLARSYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLVDLAGRSRRR 427
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 428 LMIRLVKGAYWDSEIKRAQMdGLEGYPVYTRKVYTDVSYLACAKKLLAAPNLIYPQFATHNAHTLAAIYQLAGQ-NYYPG 506
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 689260967 507 QYEFQCLHGMGEPLYDQVVGKvsdgklNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNR 569
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAA------GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
653-1107 |
6.08e-135 |
|
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: 423.17 E-value: 6.08e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 653 QPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREA 732
Cdd:cd07124 40 KEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 733 GKTFANAIAEVREAVDFLHYYAGQV----------RDDFDNETH-RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07124 120 GKNWAEADADVAEAIDFLEYYAREMlrlrgfpvemVPGEDNRYVyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 802 KPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVA-SLLQRniASRLDP-QGRPTP 879
Cdd:cd07124 200 KPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGlRIYER--AAKVQPgQKWLKR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 880 LIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPV 959
Cdd:cd07124 278 VIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 960 IDAEAKQNIDKHIQALRGKGRsvfqaVRENSEDRREWAQGTFVPPTLIE-LESFDELEK-EVFGPVLHVVRYnRNKLGAL 1037
Cdd:cd07124 358 IDKGARDRIRRYIEIGKSEGR-----LLLGGEVLELAAEGYFVQPTIFAdVPPDHRLAQeEIFGPVLAVIKA-KDFDEAL 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1038 vEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLY 1107
Cdd:cd07124 432 -EIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLL 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
656-1102 |
2.44e-123 |
|
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: 391.03 E-value: 2.44e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 656 DDGEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKT 735
Cdd:COG1012 18 ASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 FANAIAEVREAVDFLHYYAGQVR-----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:COG1012 97 LAEARGEVDRAADFLRYYAGEARrlygetipsdaPGTRAYVRRePLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 804 AEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAE 883
Cdd:COG1012 177 AEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVTLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 884 TGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAE 963
Cdd:COG1012 251 LGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 964 AKQNIDKHIQALRGKGRSVfqaVRENseDRREWAQGTFVPPTLIE-----LESFDElekEVFGPVLHVVRYNRnkLGALV 1038
Cdd:COG1012 331 QLERVLAYIEDAVAEGAEL---LTGG--RRPDGEGGYFVEPTVLAdvtpdMRIARE---EIFGPVLSVIPFDD--EEEAI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1102
Cdd:COG1012 401 ALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
656-1106 |
3.08e-119 |
|
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: 379.18 E-value: 3.08e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 656 DDGEMAPVVNPAePKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKT 735
Cdd:pfam00171 4 SESETIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 FANAIAEVREAVDFLHYYAGQVR----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARrldgetlpsdPGRLAYTRRePLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 805 EQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAET 884
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 885 GGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEA 964
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 965 KQNIDKHIQALRGKGRSVFQAVRENSEDrrewaqGTFVPPTLI-----ELESFDElekEVFGPVLHVVRYnrNKLGALVE 1039
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGGEAGLDN------GYFVEPTVLanvtpDMRIAQE---EIFGPVLSVIRF--KDEEEAIE 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 689260967 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGpKAGGPMYL 1106
Cdd:pfam00171 386 IANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGL 450
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
653-1107 |
2.44e-112 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 362.72 E-value: 2.44e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 653 QPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREA 732
Cdd:PRK03137 44 ERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 733 GKTFANAIAEVREAVDFLHYYAGQV-----------RDDFDNETH-RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:PRK03137 124 GKPWAEADADTAEAIDFLEYYARQMlkladgkpvesRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 801 AKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVA-SLLQRniASRLDP-QGRPT 878
Cdd:PRK03137 204 LKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYER--AAKVQPgQIWLK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 879 PLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRmTTDIGP 958
Cdd:PRK03137 282 RVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 959 VIDAEAKQNIDKHIQALRGKGRSVFQAVRENSEdrrewaqGTFVPPTLI-ELESFDEL-EKEVFGPVLHVVRYnRNKLGA 1036
Cdd:PRK03137 361 VINQASFDKIMSYIEIGKEEGRLVLGGEGDDSK-------GYFIQPTIFaDVDPKARImQEEIFGPVVAFIKA-KDFDHA 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 689260967 1037 LvEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLY 1107
Cdd:PRK03137 433 L-EIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
685-1108 |
9.80e-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: 347.27 E-value: 9.80e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 685 EQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRD----- 759
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRlhgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 760 ------DFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLP 832
Cdd:cd07078 81 ipspdpGELAIVrREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 833 GRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDS 912
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 913 AGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGrsvfqAVRENSED 992
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEG-----AKLLCGGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 993 RREWAQGTFVPPTLIELESFDEL--EKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVG 1070
Cdd:cd07078 310 RLEGGKGYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAG 387
|
410 420 430
....*....|....*....|....*....|....*...
gi 689260967 1071 NLYVNRNMVGAVVGvQPFGGEGLSGTGpKAGGPMYLYR 1108
Cdd:cd07078 388 TVWINDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEE 423
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
664-1113 |
1.70e-106 |
|
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: 346.85 E-value: 1.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 664 VNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEV 743
Cdd:TIGR01237 51 INPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 744 REAVDFLHYYA--------GQVRDDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:TIGR01237 131 AEAIDFMEYYArqmielakGKPVNSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 812 AQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLDPQGRPTPLIAETGGMNAMI 891
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 892 VDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKH 971
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 972 IQALRGKGRSVFQAVRENSedrrewaQGTFVPPTLI-ELESFDEL-EKEVFGPVLHVVRYnRNKLGALvEQINASGYGLT 1049
Cdd:TIGR01237 371 IEIGKAEGRLVSGGCGDDS-------KGYFIGPTIFaDVDRKARLaQEEIFGPVVAFIRA-SDFDEAL-EIANNTEYGLT 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1050 LGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLYRLLASR 1113
Cdd:TIGR01237 442 GGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAK 505
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
655-1103 |
3.67e-88 |
|
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: 294.93 E-value: 3.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 655 VDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGK 734
Cdd:cd07097 10 VAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 735 TFANAIAEVREAVDFLHYYAGQ-----------VRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07097 90 TLPEARGEVTRAGQIFRYYAGEalrlsgetlpsTRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 803 PAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIA 882
Cdd:cd07097 170 PAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG------ARVQL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 883 ETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDA 962
Cdd:cd07097 244 EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 963 EAKQNIDKHIQALRGKGRS-VFQAVRENSEDRrewaqGTFVPPTLielesFDELEK-------EVFGPVLHVVRYnrNKL 1034
Cdd:cd07097 324 RQLEKDLRYIEIARSEGAKlVYGGERLKRPDE-----GYYLAPAL-----FAGVTNdmriareEIFGPVAAVIRV--RDY 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 689260967 1035 GALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1103
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
663-1097 |
6.60e-86 |
|
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: 287.79 E-value: 6.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAePKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:cd07103 1 VINPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAGQVR--------DDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07103 80 VDYAASFLEWFAEEARriygrtipSPAPGKrilvIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 811 AAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGmNA- 889
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGG-NAp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 890 MIVDSSALTEQVVVDVVASAFDSAGQRC-SALRILClQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNI 968
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 969 DKHIQALRGKGRSVfqavreNSEDRREWAQGTFVPPTLI-----ELESFDElekEVFGPVLHVVRYnrNKLGALVEQINA 1043
Cdd:cd07103 312 EALVEDAVAKGAKV------LTGGKRLGLGGYFYEPTVLtdvtdDMLIMNE---ETFGPVAPIIPF--DTEDEVIARAND 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1044 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:cd07103 381 TPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
664-1103 |
3.60e-83 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 280.77 E-value: 3.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 664 VNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEV 743
Cdd:cd07131 19 RNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 744 REAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07131 99 QEAIDMAQYAAGEGRrlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 812 AQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIAsrldpqgRPTPLIA-ETGGMNAM 890
Cdd:cd07131 179 LKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA-------RPNKRVAlEMGGKNPI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 891 IVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDK 970
Cdd:cd07131 252 IVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 971 HIQALRGKGRSVFQAvrENSEDRREWAQGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYnrNKLGALVEQINASGYGL 1048
Cdd:cd07131 332 YNEIGKEEGATLLLG--GERLTGGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEV--SSLEEAIEIANDTEYGL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 689260967 1049 TLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1103
Cdd:cd07131 408 SSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
691-1113 |
5.05e-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: 276.42 E-value: 5.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 691 AVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVRD----------- 759
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKlggpelpspdp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 760 DFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETV 838
Cdd:cd06534 83 GGEAYVrREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 839 GAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCS 918
Cdd:cd06534 163 GAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 919 ALRILCLQDDIADHTLKMLKGamaecrmgnpgrmttdigpvidaeakqnidkhiqalrgkgrsVFQAVRENSEDRREwaq 998
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVT------------------------------------------VLVDVDPDMPIAQE--- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 999 gtfvpptlielesfdelekEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNM 1078
Cdd:cd06534 272 -------------------EIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSS 330
|
410 420 430
....*....|....*....|....*....|....*
gi 689260967 1079 VGAVVGvQPFGGEGLSGTGpKAGGPMYLYRLLASR 1113
Cdd:cd06534 331 IGVGPE-APFGGVKNSGIG-REGGPYGLEEYTRTK 363
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
657-1101 |
5.14e-81 |
|
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: 274.83 E-value: 5.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEPKDIVGyVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTF 736
Cdd:cd07086 11 GGETFTSRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKIL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 737 ANAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07086 90 PEGLGEVQEMIDICDYAVGLSRmlygltipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 805 EQTPLIAAQGINILLEA----GVPPGVVQLLPGRGEtVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqGRPtpl 880
Cdd:cd07086 170 ETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRV--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 881 IAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVI 960
Cdd:cd07086 243 LLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 961 DAEAKQNIDKHIQALRGKGRSVfqAVRENSEDRREwaQGTFVPPTLIELESfDELE---KEVFGPVLHVVRYnrNKLGAL 1037
Cdd:cd07086 323 NQAAVEKYLNAIEIAKSQGGTV--LTGGKRIDGGE--PGNYVEPTIVTGVT-DDARivqEETFAPILYVIKF--DSLEEA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 689260967 1038 VEQINASGYGLTLGVHT---RIDETIAQVTGSaHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAG 1101
Cdd:cd07086 396 IAINNDVPQGLSSSIFTedlREAFRWLGPKGS-DCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
661-1097 |
4.24e-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: 268.83 E-value: 4.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 661 APVVNPAEPKdIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAI 740
Cdd:cd07145 1 IEVRNPANGE-VIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 741 AEVREAVDFLHYYAGQVR---------DDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKvlrgetipvDAYEYNERRiaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 805 EQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLlqrnIASRLDPQGRptPLIAET 884
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLL----IASKAGGTGK--KVALEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 885 GGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEA 964
Cdd:cd07145 234 GGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 965 KQNIDKHI-QALRGKGRSVFQAVREnsedrrewaQGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYNRNKlgALVEQI 1041
Cdd:cd07145 314 VERMENLVnDAVEKGGKILYGGKRD---------EGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKVKDDE--EAVEIA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 689260967 1042 NASGYGLTLGVHTRiDETIAqvtgsahvgnLYVNRNM-VGAVV---------GVQPFGGEGLSGTG 1097
Cdd:cd07145 383 NSTEYGLQASVFTN-DINRA----------LKVARELeAGGVVindstrfrwDNLPFGGFKKSGIG 437
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
653-1108 |
2.94e-74 |
|
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: 257.13 E-value: 2.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 653 QPVDDGEMAPVVNPAEPKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQM-QQLMGILVRE 731
Cdd:cd07123 40 KEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 732 AGKTFANA-IAEVREAVDFLH---YYAGQVRDD---------FDNETHRPL-GPVVCISPWNFPlAIfTGQIAAALA-AG 796
Cdd:cd07123 120 QGKNVWQAeIDAACELIDFLRfnvKYAEELYAQqplsspagvWNRLEYRPLeGFVYAVSPFNFT-AI-GGNLAGAPAlMG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 797 NSVLAKPAEqTPLIAAQGI-NILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLDpQG 875
Cdd:cd07123 198 NVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLD-RY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 876 RPTP-LIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTT 954
Cdd:cd07123 276 RTYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 955 DIGPVIDAEAKQNIDKHIQalRGKGRSVFQAVRENSEDRREwaqGTFVPPTLIELE--SFDELEKEVFGPVLHVVRYNRN 1032
Cdd:cd07123 356 FMGAVIDEKAFDRIKGYID--HAKSDPEAEIIAGGKCDDSV---GYFVEPTVIETTdpKHKLMTEEIFGPVLTVYVYPDS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1033 KLGALVEQIN-ASGYGLTLGVHTRiDETIAQVTGSAH---VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPMYLYR 1108
Cdd:cd07123 431 DFEETLELVDtTSPYALTGAIFAQ-DRKAIREATDALrnaAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLR 509
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
657-1097 |
1.01e-73 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 254.03 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEPKdIVGYVRDATENEVEQALENAVNSAPIWFAT-PPQERAAILERAAMLMEDQMQQLMGILVREAGKT 735
Cdd:cd07082 14 SGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 FANAIAEVREAVDFLHYYAGQVRD------DFDNETHR----------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07082 93 LKDALKEVDRTIDYIRDTIEELKRldgdslPGDWFPGTkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 800 LAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRnIASRLdpqgrptP 879
Cdd:cd07082 173 VFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK-QHPMK-------R 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 880 LIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPV 959
Cdd:cd07082 245 LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 960 IDAEAKQNIDKHIQ-ALRGKGRSVFQAVREnsedrrewaQGTFVPPTLIELESfDELE---KEVFGPVLHVVRYnrNKLG 1035
Cdd:cd07082 325 IDPKSADFVEGLIDdAVAKGATVLNGGGRE---------GGNLIYPTLLDPVT-PDMRlawEEPFGPVLPIIRV--NDIE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1036 ALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-KCQRGPDHFPFLGRKDSGIG 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
662-1097 |
4.28e-73 |
|
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: 251.36 E-value: 4.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 662 PVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIA 741
Cdd:cd07149 2 EVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EVREAVDFLHYYA-------GQV---------RDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07149 81 EVDRAIETLRLSAeeakrlaGETipfdaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 806 QTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRldpqgrptPLIAETG 885
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--------KVTLELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 886 GMNAMIVDSSALTEQVVVDVVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEA 964
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 965 KQNIDKHIQ-ALRGKGRSVFQAVRensedrrewaQGTFVPPTLieLESFDELEK----EVFGPVLHVVRYNRnkLGALVE 1039
Cdd:cd07149 312 AERIEEWVEeAVEGGARLLTGGKR----------DGAILEPTV--LTDVPPDMKvvceEVFAPVVSLNPFDT--LDEAIA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 689260967 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1097
Cdd:cd07149 378 MANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdsstfR------VDHMPYGGVKESGTG 434
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
683-1103 |
8.60e-72 |
|
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: 247.06 E-value: 8.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 683 EVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVR---- 758
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRrpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 759 ----DDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP-----LIAaqgiNILLEAGVPP 825
Cdd:cd07104 81 eilpSDVPGKESMvrrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA----EIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 826 GVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVAsllqRNIASRldpQGRPTPLIA-ETGGMNAMIVDSSALTEQVVVD 904
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIGEL---AGRHLKKVAlELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 905 VVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVF 983
Cdd:cd07104 230 AAFGAFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 984 QavrensedrREWAQGTFVPPTLI-----ELESFDElekEVFGPVLHVVRYnRNKLGAlVEQINASGYGLTLGVHTRIDE 1058
Cdd:cd07104 309 T---------GGTYEGLFYQPTVLsdvtpDMPIFRE---EIFGPVAPVIPF-DDDEEA-VELANDTEYGLSAAVFTRDLE 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 689260967 1059 TIAQVTGSAHVGNLYVNRNMV--GAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07104 375 RAMAFAERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
663-1101 |
9.47e-72 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 247.85 E-value: 9.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPKdIVGYVRDATENEVEQALENAVN--SAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAI 740
Cdd:cd07114 1 SINPATGE-PWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 741 AEVREAVDFLHYYAG-----------QVRDDFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07114 80 AQVRYLAEWYRYYAGladkiegavipVDKGDYLNFTrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 809 LIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMN 888
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 889 AMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNI 968
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 969 DKHIQALRGKG-RSVFQAVRENSEDrreWAQGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYNRNKlgALVEQINASG 1045
Cdd:cd07114 314 ERYVARAREEGaRVLTGGERPSGAD---LGAGYFFEPTILADVTNDMriAQEEVFGPVLSVIPFDDEE--EAIALANDSE 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 689260967 1046 YGLTLGVHTRiDETIA-QVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07114 389 YGLAAGIWTR-DLARAhRVARAIEAGTVWV--NTYRALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
657-1076 |
1.50e-71 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 247.56 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTF 736
Cdd:cd07088 11 SGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 737 ANAIAEVREAVDFLHYYAGQVR--------DDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07088 90 SLARVEVEFTADYIDYMAEWARriegeiipSDRPNENififKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 805 EQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAET 884
Cdd:cd07088 170 EETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVSLEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 885 GGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEA 964
Cdd:cd07088 244 GGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 965 KQNIDKHIQALRGKGRSVfqavrENSEDRREWAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYnrNKLGALVEQIN 1042
Cdd:cd07088 324 LDKVEEMVERAVEAGATL-----LTGGKRPEGEKGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELAN 396
|
410 420 430
....*....|....*....|....*....|....
gi 689260967 1043 ASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR 1076
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
663-1097 |
4.37e-71 |
|
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: 245.55 E-value: 4.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIA- 741
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EVREAVDFLHYYAG----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07093 80 DIPRAAANFRFFADyilqldgesyPQDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 811 AAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAM 890
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 891 IVDSSALTEQVVVDVVASAFDSAGQRCSA-LRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNID 969
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAgSRIL-VQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 970 KHIQALRGKGRSVFQAVRENSEDRREwaQGTFVPPTLIELESfDELE---KEVFGPVLHVVRYNRNKLGalVEQINASGY 1046
Cdd:cd07093 313 GYVELARAEGATILTGGGRPELPDLE--GGYFVEPTVITGLD-NDSRvaqEEIFGPVVTVIPFDDEEEA--IELANDTPY 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1047 GLTLGVHTRiDETIAQVTGSA-HVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:cd07093 388 GLAAYVWTR-DLGRAHRVARRlEAGTVWVNCWLVRDL--RTPFGGVKASGIG 436
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
683-1095 |
9.99e-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: 243.72 E-value: 9.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 683 EVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVRE-------AVDFLHYYAG 755
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAmagkidiSIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 756 QVRDDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLL 831
Cdd:cd07095 81 ERATPMAQGravlRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 832 PGRGETvGAQLTGDDRVRGVMFTGSTEVASLLQRNIAsrldpqGRPTPLIA-ETGGMNAMIVDSSALTEQVVVDVVASAF 910
Cdd:cd07095 161 QGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 911 DSAGQRCS-ALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRen 989
Cdd:cd07095 234 LTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAME-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 990 sedRREwAQGTFVPPTLIELESFDEL-EKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAH 1068
Cdd:cd07095 312 ---RLV-AGTAFLSPGIIDVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420
....*....|....*....|....*..
gi 689260967 1069 VGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:cd07095 386 AGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
665-1103 |
1.45e-68 |
|
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: 238.38 E-value: 1.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 665 NPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVR 744
Cdd:cd07150 5 NPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 745 EAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAA 812
Cdd:cd07150 84 FTPELLRAAAGECRrvrgetlpsdspGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 813 QGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVAsllqRNIASRLDPQGRPTPLiaETGGMNAMIV 892
Cdd:cd07150 164 KIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRHLKKITL--ELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 893 DSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHI 972
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 973 QALRGKGRSVFQAvrensedrrEWAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYnRNKLGALvEQINASGYGLTL 1050
Cdd:cd07150 318 EDAVAKGAKLLTG---------GKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPA-KDAEEAL-ELANDTEYGLSA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 689260967 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 ... |
656-1097 |
1.88e-68 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 238.96 E-value: 1.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 656 DDGEMAPVVNPAePKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKT 735
Cdd:cd07085 13 KTTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 FANAIAEVR---EAVDF--------LHYYAGQVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07085 92 LADARGDVLrglEVVEFacsiphllKGEYLENVARGIDTYSYRqPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 804 AEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTgDDRVRGVMFTGSTEVASLLQRNIASRldpqGRPtpLIAE 883
Cdd:cd07085 172 SERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAAN----GKR--VQAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 884 TGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAE 963
Cdd:cd07085 245 GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 964 AKQNIDKHIQalrgkgrsvfQAVRENSE---DRRE-----WAQGTFVPPTLI-----ELESFDElekEVFGPVLHVVRYn 1030
Cdd:cd07085 325 AKERIEGLIE----------SGVEEGAKlvlDGRGvkvpgYENGNFVGPTILdnvtpDMKIYKE---EIFGPVLSIVRV- 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 689260967 1031 rNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmVGAVVGVQ--PFGGEGLSGTG 1097
Cdd:cd07085 391 -DTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLAffSFGGWKGSFFG 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
663-1097 |
4.94e-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: 234.05 E-value: 4.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPKDIvGYVRDATENEVEQALENAVNSAPI-WFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIA 741
Cdd:cd07109 1 VFDPSTGEVF-ARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EVREAVDFLHYYAGQVR----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07109 80 DVEAAARYFEYYGGAADklhgetiplgPGYFVYTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 811 AAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAM 890
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 891 IVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGnPGRMTTDIGPVIDAEAKQNIDK 970
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 971 HIQALRGKG-RSVFQAVRENSEDRRewaqGTFVPPTLI-ELESFDEL-EKEVFGPVLHVVRYnrnklGALVEQI---NAS 1044
Cdd:cd07109 313 FVARARARGaRIVAGGRIAEGAPAG----GYFVAPTLLdDVPPDSRLaQEEIFGPVLAVMPF-----DDEAEAIalaNGT 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1045 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnmVGAVVGVQ-PFGGEGLSGTG 1097
Cdd:cd07109 384 DYGLVAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
663-1097 |
7.59e-67 |
|
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: 233.48 E-value: 7.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPKdIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:cd07094 3 VHNPYDGE-VIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAGQVR---------DDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQ 806
Cdd:cd07094 82 VDRAIDTLRLAAEEAErirgeeiplDATQGSDNRlawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 807 TPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASrldpqgrpTPLIAETGG 886
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------KRIALELGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 887 MNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQ 966
Cdd:cd07094 234 NAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 967 NIDKHI-QALRGKGRSVFQAVREnsedrrewaqGTFVPPTLIELESFDEL--EKEVFGPVLHVVRYNRNKLGalVEQINA 1043
Cdd:cd07094 314 RVERWVeEAVEAGARLLCGGERD----------GALFKPTVLEDVPRDTKlsTEETFGPVVPIIRYDDFEEA--IRIANS 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1044 SGYGLTLGVHTRiDETIAqvtgsahvgnLYVNRNM-VGAVV---------GVQPFGGEGLSGTG 1097
Cdd:cd07094 382 TDYGLQAGIFTR-DLNVA----------FKAAEKLeVGGVMvndssafrtDWMPFGGVKESGVG 434
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
663-1097 |
1.36e-66 |
|
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: 232.42 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPkDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:cd07106 1 VINPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAGQVRDD---FDNET------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQ 813
Cdd:cd07106 80 VGGAVAWLRYTASLDLPDeviEDDDTrrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 814 GINILLEAgVPPGVVQLLPGRGEtVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVD 893
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTL------KRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 894 SSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVidaeakQNidkhiq 973
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPV------QN------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 974 alrgkgRSVFQAVRENSED-RREWAQ-----------GTFVPPTLIE--LESFDELEKEVFGPVLHVVRYnrNKLGALVE 1039
Cdd:cd07106 300 ------KMQYDKVKELVEDaKAKGAKvlaggepldgpGYFIPPTIVDdpPEGSRIVDEEQFGPVLPVLKY--SDEDEVIA 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 689260967 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 |
6.99e-66 |
|
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: 230.79 E-value: 6.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANA-IA 741
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EVREAVDFLHYYAG----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07115 80 DVPRAADTFRYYAGwadkiegeviPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 811 AAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAM 890
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNL------KRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 891 IVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDK 970
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 971 HIQALRGKGRSVFQAvrenseDRREWAQGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYNRNKLGALVEqiNASGYGL 1048
Cdd:cd07115 314 YVDVGREEGARLLTG------GKRPGARGFFVEPTIFAAVPPEMriAQEEIFGPVVSVMRFRDEEEALRIA--NGTEYGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 689260967 1049 TLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07115 386 AAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
658-1097 |
8.94e-64 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 224.79 E-value: 8.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 658 GEMAPVVNPAEPKdIVGYVRDATENEVEQALENA--VNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKT 735
Cdd:cd07112 1 GETFATINPATGR-VLAEVAACDAADVDRAVAAArrAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 FANAIA-EVREAVDFLHYYA-------GQV----RDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07112 80 ISDALAvDVPSAANTFRWYAeaidkvyGEVaptgPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 804 AEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIA-SRLdpqgrpTPLIA 882
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGqSNL------KRVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 883 ETGGMNAMIV-DSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVID 961
Cdd:cd07112 234 ECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 962 AEAKQNIDKHIQALRGKG-RSVFQAVRENSEdrrewAQGTFVPPTLielesFDELE-------KEVFGPVLHVVRYNRNK 1033
Cdd:cd07112 314 EAHFDKVLGYIESGKAEGaRLVAGGKRVLTE-----TGGFFVEPTV-----FDGVTpdmriarEEIFGPVLSVITFDSEE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1034 LGalVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07112 384 EA--VALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
656-1097 |
2.32e-63 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 224.95 E-value: 2.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 656 DDGEMAPVVNPAEPKDIVGyVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKT 735
Cdd:PLN02278 37 YDGKTFPVYNPATGEVIAN-VPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 FANAIAEVREAVDFLHYYAGQVRDDFDN------------ETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:PLN02278 116 LKEAIGEVAYGASFLEYFAEEAKRVYGDiipspfpdrrllVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 804 AEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgRPTPLiaE 883
Cdd:PLN02278 196 SELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV----KRVSL--E 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 884 TGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDA 962
Cdd:PLN02278 270 LGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 963 EAKQNIDKHIQALRGKGRSVFQAvrenseDRREWAQGTFVPPTLIELESFDEL--EKEVFGPVLHVVRYNRNKlgalvEQ 1040
Cdd:PLN02278 349 AAVQKVESHVQDAVSKGAKVLLG------GKRHSLGGTFYEPTVLGDVTEDMLifREEVFGPVAPLTRFKTEE-----EA 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1041 I---NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1097
Cdd:PLN02278 418 IaiaNDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
148-259 |
3.91e-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: 209.67 E-value: 3.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 148 VQSLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEAN 227
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 689260967 228 LSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQF 259
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
679-1103 |
4.93e-63 |
|
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: 222.17 E-value: 4.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 679 ATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYA---- 754
Cdd:cd07152 10 ADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAglpt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 755 ---GQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP----LIAAQginILLEAGV 823
Cdd:cd07152 90 qpqGEILPSAPGRLslarRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsggVVIAR---LFEEAGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 824 PPGVVQLLPGRGEtVGAQLTGDDRVRGVMFTGSTEVAsllqRNIASRLDPQGRPTPLiaETGGMNAMIVDSSALTEQVVV 903
Cdd:cd07152 167 PAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVG----RKVGEAAGRHLKKVSL--ELGGKNALIVLDDADLDLAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 904 DVVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSV 982
Cdd:cd07152 240 NGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 983 FQAVRensedrrewAQGTFVPPTLI-----ELESFDElekEVFGPVLHVVRYNRNKlgALVEQINASGYGLTLGVHTRID 1057
Cdd:cd07152 319 EAGGT---------YDGLFYRPTVLsgvkpGMPAFDE---EIFGPVAPVTVFDSDE--EAVALANDTEYGLSAGIISRDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 689260967 1058 ETIAQVTGSAHVGNLYVNRNMVGAVVgVQPFGGEGLSGTGPKAGGP 1103
Cdd:cd07152 385 GRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
664-1097 |
5.03e-63 |
|
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: 222.48 E-value: 5.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 664 VNPAEPKDiVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEV 743
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 744 REAVDFLHYYAGQVRDDFDNE---------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRkvptgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 809 LIAAQGINILLEAGVPPGVVQLLPGRGETvGAQLTgDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMN 888
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALI-DAGVDKVAFTGSVATGRKVMAAAAERL------IPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 889 AMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNI 968
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 969 DKHIQ-ALRGKGRSVFQAVRENSedrrewaQGTFVPPTLI--ELESFDELEKEVFGPVLHVVRYnrNKLGALVEQINASG 1045
Cdd:cd07099 312 RRHVDdAVAKGAKALTGGARSNG-------GGPFYEPTVLtdVPHDMDVMREETFGPVLPVMPV--ADEDEAIALANDSR 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1046 YGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07099 383 YGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
663-1101 |
2.30e-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: 217.61 E-value: 2.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPKdIVGYVRDATENEVEQALENAVNSAPiwfATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:cd07146 3 VRNPYTGE-VVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAGQV-RDD-----FDNETHR----------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQ 806
Cdd:cd07146 79 VGRAADVLRFAAAEAlRDDgesfsCDLTANGkarkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 807 TPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRldpqgrptPLIAETGG 886
Cdd:cd07146 159 TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--------RQLLELGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 887 MNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQ 966
Cdd:cd07146 231 NDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 967 NIDKHI-QALRGKGRSVFQAVRensedrrewaQGTFVPPTLIELESFD-EL-EKEVFGPVLHVVRYnrNKLGALVEQINA 1043
Cdd:cd07146 311 QIENRVeEAIAQGARVLLGNQR----------QGALYAPTVLDHVPPDaELvTEETFGPVAPVIRV--KDLDEAIAISNS 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 689260967 1044 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07146 379 TAYGLSSGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
657-1101 |
6.87e-61 |
|
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: 216.69 E-value: 6.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEPKDIvGYVRDATENEVEQALENAVNSAPI--WFATPPQERAAILERAAMLMEDQMQQLMGILVREAGK 734
Cdd:cd07091 17 SGKTFPTINPATEEVI-CQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 735 TF-ANAIAEVREAVDFLHYYAG----------QVRDDFDNETHR-PLGpvVC--ISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07091 96 PLeESAKGDVALSIKCLRYYAGwadkiqgktiPIDGNFLAYTRRePIG--VCgqIIPWNFPLLMLAWKLAPALAAGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 801 AKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIA-SRLdpqgRPTP 879
Cdd:cd07091 174 LKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAkSNL----KKVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 880 LiaETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPV 959
Cdd:cd07091 250 L--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 960 IDAEAKQNIDKHIQalrgkgrsvfQAVRENSE----DRREWAQGTFVPPTLielesFDELEK-------EVFGPVLHVVR 1028
Cdd:cd07091 328 VSKAQFDKILSYIE----------SGKKEGATlltgGERHGSKGYFIQPTV-----FTDVKDdmkiakeEIFGPVVTILK 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1029 YnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07091 393 F--KTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
653-1097 |
9.59e-61 |
|
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: 216.21 E-value: 9.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 653 QPVDDGEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREA 732
Cdd:cd07138 8 VAPAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 733 G--KTFANAiAEVREAVDFLHYYAGQVRDdFDNETHR--------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07138 87 GapITLARA-AQVGLGIGHLRAAADALKD-FEFEERRgnslvvrePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 803 PAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLDpqgRPTpliA 882
Cdd:cd07138 165 PSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK---RVA---L 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 883 ETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSAL-RILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVID 961
Cdd:cd07138 239 ELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLAS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 962 AEAKQNIDKHIQalrgkgrsvfQAVRENS------EDRRE-WAQGTFVPPTL---------IELEsfdelekEVFGPVLH 1025
Cdd:cd07138 318 AAQFDRVQGYIQ----------KGIEEGArlvaggPGRPEgLERGYFVKPTVfadvtpdmtIARE-------EIFGPVLS 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 689260967 1026 VVRYnRNKLGAlVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmvGAVVGVQ-PFGGEGLSGTG 1097
Cdd:cd07138 381 IIPY-DDEDEA-IAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
655-1110 |
2.47e-60 |
|
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: 215.34 E-value: 2.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 655 VDDGEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGK 734
Cdd:cd07111 33 PENRKSFPTINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 735 tfanAIAEVRE-----AVDFLHYYAGQVR-DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07111 112 ----PIRESRDcdiplVARHFYHHAGWAQlLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 809 LIAAQGINILLEAGVPPGVVQLLPGRGETvGAQLTGDDRVRGVMFTGSTEVASLLQRNIAsrldpqGRPTPLIAETGGMN 888
Cdd:cd07111 188 LTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA------GTGKKLSLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 889 AMIVDSSALTEQVVVDVVASAFDSAGQRCSA-LRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQN 967
Cdd:cd07111 261 PFIVFDDADLDSAVEGIVDAIWFNQGQVCCAgSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 968 IDKHIQALRGKGRSVFQAVRENSEDrrewaqGTFVPPTLIE-LESFDEL-EKEVFGPVLHVVRYnRNKLGAlVEQINASG 1045
Cdd:cd07111 340 IRELVEEGRAEGADVFQPGADLPSK------GPFYPPTLFTnVPPASRIaQEEIFGPVLVVLTF-RTAKEA-VALANNTP 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 689260967 1046 YGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGpKAGGPMYLYRLL 1110
Cdd:cd07111 412 YGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEYL 473
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
663-1100 |
3.34e-60 |
|
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: 214.15 E-value: 3.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTF-ANAIA 741
Cdd:cd07108 1 VINPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EVREAVDFLHYY---AGQVR--------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLi 810
Cdd:cd07108 80 EAAVLADLFRYFgglAGELKgetlpfgpDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 811 AAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAM 890
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 891 IVDSSALTEQVVVDVVASA-FDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNID 969
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 970 KHIQAlrGKGRSVFQAVReNSEDRRE--WAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYNRNKlgALVEQINASG 1045
Cdd:cd07108 313 GYIDL--GLSTSGATVLR-GGPLPGEgpLADGFFVQPTIFSgvDNEWRLAREEIFGPVLCAIPWKDED--EVIAMANDSH 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 689260967 1046 YGLTLGVHTRiDETIAQVTGSA-HVGNLYVNRNmVGAVVGvQPFGGEGLSGTGPKA 1100
Cdd:cd07108 388 YGLAAYVWTR-DLGRALRAAHAlEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
684-1097 |
5.33e-58 |
|
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: 206.93 E-value: 5.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 684 VEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYA--------G 755
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenaeaflaD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 756 QVRDDFDNE---THRPLGPVVCISPWNFPLAiftgQI----AAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVV 828
Cdd:cd07100 81 EPIETDAGKayvRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 829 QLLPGRGETVgAQLTGDDRVRGVMFTGST----EVASLLQRNIasrldpqgRPTPLiaETGGMNAMIVDSSALTEQVVVD 904
Cdd:cd07100 157 QNLLIDSDQV-EAIIADPRVRGVTLTGSEragrAVAAEAGKNL--------KKSVL--ELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 905 VVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVf 983
Cdd:cd07100 226 AVKGRLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATL- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 984 qaVRENSEDRREwaqGTFVPPTLI-----ELESFDElekEVFGPVLHVVRYNRNKlgALVEQINASGYGLTLGVHTRIDE 1058
Cdd:cd07100 304 --LLGGKRPDGP---GAFYPPTVLtdvtpGMPAYDE---ELFGPVAAVIKVKDEE--EAIALANDSPFGLGGSVFTTDLE 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 689260967 1059 TIAQVTGSAHVGNLYVNRnMVGAVVGVqPFGGEGLSGTG 1097
Cdd:cd07100 374 RAERVARRLEAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
662-1097 |
6.77e-58 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 207.93 E-value: 6.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 662 PVVNPAEPKDIVGyVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIA 741
Cdd:cd07151 13 DVLNPYTGETLAE-IPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EV-------REAVDFLHYYAGQ-VRDDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP- 808
Cdd:cd07151 92 EWgaamaitREAATFPLRMEGRiLPSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPi 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 809 ----LIAaqgiNILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVAsllqRNIASRldpQGRPTPLIA-E 883
Cdd:cd07151 172 tgglLLA----KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG----RHIGEL---AGRHLKKVAlE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 884 TGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSAL-RILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDa 962
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAInRII-VHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLIN- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 963 eakqniDKHIQALRGKgrsVFQAVRENSEDRREW-AQGTFVPPT-LIELESFDELEK-EVFGPVLHVVRYnRNKLGAlVE 1039
Cdd:cd07151 319 ------ESQVDGLLDK---IEQAVEEGATLLVGGeAEGNVLEPTvLSDVTNDMEIAReEIFGPVAPIIKA-DDEEEA-LE 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 689260967 1040 QINASGYGLTLGVHTRIDETIAQV-----TGSAHVGNLYVNR--NMvgavvgvqPFGGEGLSGTG 1097
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFarridAGMTHINDQPVNDepHV--------PFGGEKNSGLG 444
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
663-1097 |
7.69e-58 |
|
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: 207.48 E-value: 7.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIW-FATPPQERAAILERAAMLMEDQMQQLMGILVREAGKT------ 735
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmtara 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 --FANAIAEVREAVDFLHYYAGQVRDDFDNET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07089 80 mqVDGPIGHLRYFADLADSFPWEFDLPVPALRggpgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 805 EQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgRPTPLiaET 884
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 885 GGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSAL-RILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAE 963
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTtRLL-VPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 964 AKQNIDKHIQALRGKG-RSVFQAVRENSEDRrewaqGTFVPPTLielesFDELE-------KEVFGPVLHVVRYnRNKLG 1035
Cdd:cd07089 313 QRDRVEGYIARGRDEGaRLVTGGGRPAGLDK-----GFYVEPTL-----FADVDndmriaqEEIFGPVLVVIPY-DDDDE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1036 AlVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmvGAVVGV--QPFGGEGLSGTG 1097
Cdd:cd07089 382 A-VRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
658-1102 |
5.70e-57 |
|
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: 205.52 E-value: 5.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 658 GEMAPVVNPAEPKDIVGyVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFA 737
Cdd:cd07130 11 GGVVTSISPANGEPIAR-VRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 738 NAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07130 90 EGLGEVQEMIDICDFAVGLSRqlygltipserpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 806 QTPL--IAAQGI--NILLEAGVPPGVVQLLPGRGEtVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqGRptpLI 881
Cdd:cd07130 170 TTPLtaIAVTKIvaRVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---GR---SL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 882 AETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVID 961
Cdd:cd07130 243 LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 962 AEAKQNIDKHIQALRGKGRSVFqavrenSEDRREWAQGTFVPPTLIELESFDELEK-EVFGPVLHVVRYnrNKLGALVEQ 1040
Cdd:cd07130 323 KAAVDNYLAAIEEAKSQGGTVL------FGGKVIDGPGNYVEPTIVEGLSDAPIVKeETFAPILYVLKF--DTLEEAIAW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 689260967 1041 INASGYGLTLGVHTRIDETIAQ---VTGSaHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1102
Cdd:cd07130 395 NNEVPQGLSSSIFTTDLRNAFRwlgPKGS-DCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
653-1097 |
6.39e-57 |
|
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: 205.62 E-value: 6.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 653 QPVDDGEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNS--APIWFATPPQERAAILERAAMLMEDQMQQLMGILVR 730
Cdd:cd07119 7 VEAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 731 EAGKTFANAIAEVREAVDFLHYYAGQV--RDDFDNET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07119 86 NTGKTLRESEIDIDDVANCFRYYAGLAtkETGEVYDVpphvisrtvREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 800 LAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTP 879
Cdd:cd07119 166 VIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV------KK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 880 LIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPV 959
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 960 IDAEAKQNIDKHIQALRGKGRSVfqAVRENSEDRREWAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYnRNKLGAl 1037
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARL--VCGGKRPTGDELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERF-DTEEEA- 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 689260967 1038 VEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1097
Cdd:cd07119 396 IRLANDTPYGLAGAVWTK-DIARANrVARRLRAGTVWINDYHPYFAEA--PWGGYKQSGIG 453
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
657-1101 |
1.30e-56 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 204.68 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEPKdIVGYVRDATENEVEQALENAVNS--APIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGK 734
Cdd:cd07143 20 HGGTVKVYNPSTGK-LITKIAEATEADVDIAVEVAHAAfeTDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 735 TFANAIA-EVREAVDFLHYYAGQVRDDFDN--ET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07143 99 TFGTAKRvDVQASADTFRYYGGWADKIHGQviETdikkltytrHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 803 PAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASrldpqGRPTPLIA 882
Cdd:cd07143 179 PSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK-----SNLKKVTL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 883 ETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDA 962
Cdd:cd07143 254 ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 963 EAKQNIDKHIQALRGKGRSVfqavreNSEDRREWAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYNRNKlgALVEQ 1040
Cdd:cd07143 334 IQYERIMSYIESGKAEGATV------ETGGKRHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKFKTEE--EAIKR 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07143 406 ANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
666-1101 |
1.41e-56 |
|
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: 203.72 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 666 PAEPKDIVGYVRdATENEVEQALE---NAVNSAPiWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:cd07118 4 PAHGVVVARYAE-GTVEDVDAAVAaarKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAGQVR----DDFDN--------ETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07118 82 IEGAADLWRYAASLARtlhgDSYNNlgddmlglVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 811 AAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLDPQGrptpliAETGGMNAM 890
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 891 IVDSSALTEQVVVDVVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNID 969
Cdd:cd07118 236 IVFADADLDAAADAVVFGVYFNAGECCnSGSRLL-VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 970 KHIQALRGKGRSVFQAvrensEDRREWAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYnrNKLGALVEQINASGYG 1047
Cdd:cd07118 315 DYVDAGRAEGATLLLG-----GERLASAAGLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1048 LTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTGPKAG 1101
Cdd:cd07118 388 LSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
677-1095 |
3.21e-56 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 203.65 E-value: 3.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 677 RDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVRE-------AVDF 749
Cdd:PRK09457 32 NDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiaiSIQA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 750 LHYYAGQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPP 825
Cdd:PRK09457 112 YHERTGEKRSEMADGAavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 826 GVVQLLPGRGETvGAQLTGDDRVRGVMFTGSTEVASLLQRNIAsrldpqGRPTPLIA-ETGGMNAMIVDSSALTEQVVVD 904
Cdd:PRK09457 192 GVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFA------GQPEKILAlEMGGNNPLVIDEVADIDAAVHL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 905 VVASAFDSAGQRCS-ALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTD-IGPVIDAEAKQNIDKHIQALRGKGRSV 982
Cdd:PRK09457 265 IIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 983 FQAVRensedRREwAQGTFVPPTLIELESFDEL-EKEVFGPVLHVVRYNRnkLGALVEQINASGYGLTLGVHTRIDETIA 1061
Cdd:PRK09457 345 LLEMT-----QLQ-AGTGLLTPGIIDVTGVAELpDEEYFGPLLQVVRYDD--FDEAIRLANNTRFGLSAGLLSDDREDYD 416
|
410 420 430
....*....|....*....|....*....|....
gi 689260967 1062 QVTGSAHVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:PRK09457 417 QFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
657-1097 |
3.85e-56 |
|
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: 202.96 E-value: 3.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEPKdIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGK-- 734
Cdd:cd07559 14 KGEYFDNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKpi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 735 --TFAnaiAEVREAVDFLHYYAGQVR------DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07559 93 reTLA---ADIPLAIDHFRYFAGVIRaqegslSEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 802 KPAEQTP---LIAAQGINILLeagvPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpT 878
Cdd:cd07559 170 KPASQTPlsiLVLMELIGDLL----PKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------I 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 879 PLIAETGGMNAMIVDSSALTEQVVVD------VVASAFDSaGQRCSA-LRILcLQDDIADHTLKMLKGAMAECRMGNPGR 951
Cdd:cd07559 240 PVTLELGGKSPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCpSRAL-VQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 952 MTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRENSEDrrEWAQGTFVPPTLIE-----LESFDElekEVFGPVLHV 1026
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLG--GLDKGYFYEPTLIKggnndMRIFQE---EIFGPVLAV 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1027 VRYNRNKlgALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07559 393 ITFKDEE--EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
663-1138 |
9.17e-56 |
|
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: 201.38 E-value: 9.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPKdIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAGQVRD------DFDNE----THR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07090 80 IDSSADCLEYYAGLAPTlsgehvPLPGGsfayTRRePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 812 AQGINILLEAGVPPGVVQLLPGRGETvGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMI 891
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI------KHVTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 892 VDSSALTEQVVVDVVASAFDSAGQRCS-ALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDK 970
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 971 HIQA--------LRGKGRSVFQAVRENsedrrewaqGTFVPPTLIElESFDELE---KEVFGPVLHVVRYNRNKlgALVE 1039
Cdd:cd07090 312 YIESakqegakvLCGGERVVPEDGLEN---------GFYVSPCVLT-DCTDDMTivrEEIFGPVMSILPFDTEE--EVIR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTGPKAGgpmylyrllasrpedal 1118
Cdd:cd07090 380 RANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFGRENG----------------- 439
|
490 500
....*....|....*....|
gi 689260967 1119 LTTLNrqdaHYpvdSQLKSV 1138
Cdd:cd07090 440 TAALE----HY---TQLKTV 452
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
662-1097 |
1.19e-55 |
|
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: 200.93 E-value: 1.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 662 PVVNPAEPKdIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIA 741
Cdd:cd07147 2 EVTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EVREAVDFLHYYAGQVRD------DFD----NETHR------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07147 81 EVARAIDTFRIAAEEATRiygevlPLDisarGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 806 QTPLIAAQGINILLEAGVPPGVVQLLPGRGETvGAQLTGDDRVRGVMFTGSTEVASLLqRNIASRldpqgrpTPLIAETG 885
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-------KKVVLELG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 886 GMNAMIVDSSALTEQVVVDVVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEA 964
Cdd:cd07147 232 GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 965 KQNIDKHIQalrgkgrsvfQAVRENSE----DRREwaqGTFVPPTLIE-LESFDELE-KEVFGPVLHVVRYNRNKlgALV 1038
Cdd:cd07147 311 AERVEGWVN----------EAVDAGAKlltgGKRD---GALLEPTILEdVPPDMEVNcEEVFGPVVTVEPYDDFD--EAL 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1097
Cdd:cd07147 376 AAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSGIG 433
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
663-1097 |
1.98e-55 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 200.25 E-value: 1.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPKDIvGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIA- 741
Cdd:cd07092 1 VVDPATGEEI-ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EVREAVDFLHYYAGQVRD-----------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPL 809
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTlegpaageylpGHTSMIRRePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 810 iAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNA 889
Cdd:cd07092 160 -TTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTL------KRVHLELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 890 MIVDSSALTEQVVVDVVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNI 968
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 969 DKHIQALRGKGRSVfqavrenSEDRREWAQGTFVPPTLI-ELESFDEL-EKEVFGPVLHVVRYnrNKLGALVEQINASGY 1046
Cdd:cd07092 312 AGFVERAPAHARVL-------TGGRRAEGPGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPF--DDEDEAIELANDVEY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 689260967 1047 GLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1097
Cdd:cd07092 383 GLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
673-1101 |
5.02e-55 |
|
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: 199.07 E-value: 5.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 673 VGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHY 752
Cdd:cd07101 9 LGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 753 YAGQVRDDFD--------------NETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINIL 818
Cdd:cd07101 89 YARRAERLLKprrrrgaipvltrtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 819 LEAGVPPGVVQLLPGRGETVGAQLTgdDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALT 898
Cdd:cd07101 169 IEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 899 EQVVVDVVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRG 977
Cdd:cd07101 241 DKAAAGAVRACFSNAGQLCvSIERIY-VHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 978 KGRSVFQAVRensedRREWAQGTFVPPTLI-----ELESFDElekEVFGPVLHVVRYNRnkLGALVEQINASGYGLTLGV 1052
Cdd:cd07101 320 KGATVLAGGR-----ARPDLGPYFYEPTVLtgvteDMELFAE---ETFGPVVSIYRVAD--DDEAIELANDTDYGLNASV 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 689260967 1053 HTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTGPKAG 1101
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
663-1097 |
5.52e-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: 199.11 E-value: 5.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAGQVRD--------------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQT 807
Cdd:cd07110 80 VDDVAGCFEYYADLAEQldakaeravplpseDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 808 PLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgRPTPLiaETGGM 887
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDI----KPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 888 NAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQN 967
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 968 IDKHI-QALRGKGRSVFQAVRensedRREWAQGTFVPPTLI-ELESFDEL-EKEVFGPVLHVVRYNRNKlgALVEQINAS 1044
Cdd:cd07110 314 VLSFIaRGKEEGARLLCGGRR-----PAHLEKGYFIAPTVFaDVPTDSRIwREEIFGPVLCVRSFATED--EAIALANDS 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 689260967 1045 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07110 387 EYGLAAAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
663-1097 |
1.47e-54 |
|
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: 197.98 E-value: 1.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAGQVRD-----------DFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07107 80 VMVAAALLDYFAGLVTElkgetipvggrNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 812 AQGINILLEAgVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMI 891
Cdd:cd07107 160 LRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGI------KHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 892 VDSSALTEQVVVDVVASA-FDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDK 970
Cdd:cd07107 233 VFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 971 HIQALRGKG-RSVFQAVRENSEdrrEWAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYnrNKLGALVEQINASGYG 1047
Cdd:cd07107 313 YIDSAKREGaRLVTGGGRPEGP---ALEGGFYVEPTVFAdvTPGMRIAREEIFGPVLSVLRW--RDEAEMVAQANGVEYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1048 LTLGVHTRiDETIAQVTGSA-HVGNLYVN---RNMVGAvvgvqPFGGEGLSGTG 1097
Cdd:cd07107 388 LTAAIWTN-DISQAHRTARRvEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
658-1101 |
2.26e-53 |
|
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: 195.02 E-value: 2.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 658 GEMAPVVNPaEPKDIVGYVRDATENEVEQALE---NAVNSAPiWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGK 734
Cdd:cd07142 18 GKTFPTIDP-RNGEVIAHVAEGDAEDVDRAVKaarKAFDEGP-WPRMTGYERSRILLRFADLLEKHADELAALETWDNGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 735 TFANA-IAEVREAVDFLHYYAGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07142 96 PYEQArYAEVPLAARLFRYYAGWA-DKIHGMTlpadgphhvytlHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 802 KPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIAsrldpQGRPTPLI 881
Cdd:cd07142 175 KPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA-----KSNLKPVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 882 AETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVID 961
Cdd:cd07142 250 LELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 962 AEAKQNIDKHIQalRGKGrsvfQAVRENSEDRREWAQGTFVPPTLIELESFDEL--EKEVFGPVLHVVRYnrNKLGALVE 1039
Cdd:cd07142 330 KEQFEKILSYIE--HGKE----EGATLITGGDRIGSKGYYIQPTIFSDVKDDMKiaRDEIFGPVQSILKF--KTVDEVIK 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 689260967 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
664-1055 |
5.38e-53 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 193.33 E-value: 5.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 664 VNPAEPKdIVGYVRDATENEVEQALENAVNS--APIWfATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIA 741
Cdd:cd07120 2 IDPATGE-VIGTYADGGVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 742 EVREAVDFLHYYAGQVR-----------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07120 80 EISGAISELRYYAGLARteagrmiepepGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 811 AAQGINILLEA-GVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLDPQGrptpliAETGGMNA 889
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 890 MIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNID 969
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 970 KHIQALRGKGRSVFqaVRENSEDRReWAQGTFVPPTLIELE--SFDELEKEVFGPVLHVVRYNRNKLGalVEQINASGYG 1047
Cdd:cd07120 314 RMVERAIAAGAEVV--LRGGPVTEG-LAKGAFLRPTLLEVDdpDADIVQEEIFGPVLTLETFDDEAEA--VALANDTDYG 388
|
....*...
gi 689260967 1048 LTLGVHTR 1055
Cdd:cd07120 389 LAASVWTR 396
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
657-1101 |
1.60e-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: 192.62 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNS-APIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKT 735
Cdd:cd07144 21 DGETIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 F-ANAIAEVREAVDFLHYYAGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07144 100 YhSNALGDLDEIIAVIRYYAGWA-DKIQGKTiptspnklaytlHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 803 PAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIA 882
Cdd:cd07144 179 PAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNL------KAVTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 883 ETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSAL-RILcLQDDIADHTLKMLKGAMAEC-RMGNPGRMTTDIGPVI 960
Cdd:cd07144 253 ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATsRIY-VQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGPQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 961 DAEAKQNIDKHIQALRGKGRSVfqaVRENSEDRREWAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYNRNKlgALV 1038
Cdd:cd07144 332 SKTQYDRVLSYIEKGKKEGAKL---VYGGEKAPEGLGKGYFIPPTIFTdvPQDMRIVKEEIFGPVVVISKFKTYE--EAI 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMvgAVVGVqPFGGEGLSGTGPKAG 1101
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSsND--SDVGV-PFGGFKMSGIGRELG 467
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
653-1097 |
1.72e-52 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 192.43 E-value: 1.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 653 QPVD-DGEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVRE 731
Cdd:PRK13473 10 ELVAgEGEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 732 AGKTFANAIA-EVREAVDFLHYYAGQVRD-----------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:PRK13473 89 CGKPLHLALNdEIPAIVDVFRFFAGAARClegkaageyleGHTSMIRRdPVGVVASIAPWNYPLMMAAWKLAPALAAGNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 799 VLAKPAEQTPLIAAQGINILLEAgVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVAsllqRNIASRLDPQGRPT 878
Cdd:PRK13473 169 VVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATG----KHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 879 PLiaETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCS-ALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIG 957
Cdd:PRK13473 244 HL--ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTaACRIY-AQRGIYDDLVAKLAAAVATLKVGDPDDEDTELG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 958 PVIDAEAKQNID---------KHIQALRGkGRSVFQAvrensedrrewaqGTFVPPTLIE--LESFDELEKEVFGPVLHV 1026
Cdd:PRK13473 321 PLISAAHRDRVAgfverakalGHIRVVTG-GEAPDGK-------------GYYYEPTLLAgaRQDDEIVQREVFGPVVSV 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1027 VRYnrNKLGALVEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1097
Cdd:PRK13473 387 TPF--DDEDQAVRWANDSDYGLASSVWTR-DVGRAHrVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
679-1076 |
2.71e-52 |
|
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: 190.92 E-value: 2.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 679 ATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVR 758
Cdd:cd07102 15 ASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 759 DDFDNE------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPG 826
Cdd:cd07102 95 EALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 827 VVQLLPGRGETvGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVV 906
Cdd:cd07102 175 VFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRF------IKVGLELGGKDPAYVRPDADLDAAAESLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 907 ASAFDSAGQRCSAL-RILC---LQDDIADHTLKMLKGAmaecRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSV 982
Cdd:cd07102 248 DGAFFNSGQSCCSIeRIYVhesIYDAFVEAFVAVVKGY----KLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 983 fqAVRENSEDRREwAQGTFVPPT-LIELE-SFDELEKEVFGPVLHVVRYnRNKLGAlVEQINASGYGLTLGVHTRIDETI 1060
Cdd:cd07102 324 --LIDGALFPEDK-AGGAYLAPTvLTNVDhSMRVMREETFGPVVGIMKV-KSDAEA-IALMNDSEYGLTASVWTKDIARA 398
|
410
....*....|....*.
gi 689260967 1061 AQVTGSAHVGNLYVNR 1076
Cdd:cd07102 399 EALGEQLETGTVFMNR 414
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
677-1095 |
4.06e-52 |
|
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: 191.47 E-value: 4.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 677 RDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTF-------ANAIAEVREAVDF 749
Cdd:TIGR03240 30 AAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVIARETGKPLwetrtevASMIGKVAISIKA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 750 LHYYAGQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPP 825
Cdd:TIGR03240 110 YHERTGESENPMPDGRavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPSELTPWVAEETVKLWEKAGLPA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 826 GVVQLLPGRGETvGAQLTGDDRVRGVMFTGSTEVASLLQRNIAsrldpqGRPTPLIA-ETGGMNAMIVDSSALTEQVVVD 904
Cdd:TIGR03240 190 GVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFG------GRPEKILAlEMGGNNPLIVDEVADIDAAVHH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 905 VVASAFDSAGQRCS-ALRILCLQDDIADHTLKMLKGAMAECRmgnPGRMTTD----IGPVIDAEAKQNIDKHIQALRGKG 979
Cdd:TIGR03240 263 IIQSAFISAGQRCTcARRLLVPDGAQGDAFLARLVEVAERLT---VGAWDAEpqpfMGAVISLRAAQRLLAAQAKLLALG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 980 RSVFQAVRensedRREwAQGTFVPPTLIELESFDEL-EKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDE 1058
Cdd:TIGR03240 340 GKSLLEMR-----QLD-PGAAFLTPGIIDVTGVAELpDEEHFGPLLQVIRY--TDFDEAIAIANNTRFGLSAGLLSDDRE 411
|
410 420 430
....*....|....*....|....*....|....*..
gi 689260967 1059 TIAQVTGSAHVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:TIGR03240 412 LYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
658-1101 |
1.46e-51 |
|
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: 189.87 E-value: 1.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 658 GEMAPVVNPAEPKDIVGyVRDATENEVEQALENAVNS----APiWFATPPQERAAILERAAMLMEDQMQQLMGILVREAG 733
Cdd:cd07141 21 GKTFPTINPATGEKICE-VQEGDKADVDKAVKAARAAfklgSP-WRTMDASERGRLLNKLADLIERDRAYLASLETLDNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 734 KTFANA-IAEVREAVDFLHYYAGQVrDDFDNET------------HRPLGpvVC--ISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:cd07141 99 KPFSKSyLVDLPGAIKVLRYYAGWA-DKIHGKTipmdgdfftytrHEPVG--VCgqIIPWNFPLLMAAWKLAPALACGNT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 799 VLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIA-SRLDpqgRP 877
Cdd:cd07141 176 VVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGkSNLK---RV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 878 TpliAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADhtlKMLKGAMAEC---RMGNPGRMTT 954
Cdd:cd07141 253 T---LELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYD---EFVKRSVERAkkrVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 955 DIGPVIDAEAKQNIDKHIQALRGKGrsvfqAVRENSEDRREwAQGTFVPPTLIElESFDEL---EKEVFGPVLHVVRYnr 1031
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEG-----AKLECGGKRHG-DKGYFIQPTVFS-DVTDDMriaKEEIFGPVQQIFKF-- 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1032 NKLGALVEQINASGYGLTLGVHTR-IDETIAqVTGSAHVGNLYVNrnmVGAVVGVQ-PFGGEGLSGTGPKAG 1101
Cdd:cd07141 398 KTIDEVIERANNTTYGLAAAVFTKdIDKAIT-FSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
644-1103 |
2.24e-51 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 188.94 E-value: 2.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 644 QWRAKpvleqpvDDGEMAPVVNPAEPKdIVGYVRDATENEVEQALENAVNS--APIWFATPPQERAAILERAAMLMEDQM 721
Cdd:cd07139 6 RWVAP-------SGSETIDVVSPATEE-VVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 722 QQLMGILVREAGKTFA-NAIAEVREAVDFLHYYAGQVRDdFDNETHR-------------PLGPVVCISPWNFPLAIFTG 787
Cdd:cd07139 78 DELARLWTAENGMPISwSRRAQGPGPAALLRYYAALARD-FPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 788 QIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGrGETVGAQLTGDDRVRGVMFTGSTEVAsllqRNI 867
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAG----RRI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 868 ASRLDPQGRPTPLiaETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSAL-RILcLQDDIADHTLKMLKGAMAECRM 946
Cdd:cd07139 232 AAVCGERLARVTL--ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVEALAAAVAALKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 947 GNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKG-RSVFQAVRENSEDRrewaqGTFVPPTLielesFDELE-------KE 1018
Cdd:cd07139 309 GDPLDPATQIGPLASARQRERVEGYIAKGRAEGaRLVTGGGRPAGLDR-----GWFVEPTL-----FADVDndmriaqEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1019 VFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVgvqPFGGEGLSGTGp 1098
Cdd:cd07139 379 IFGPVLSVIPY--DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA---PFGGFKQSGIG- 452
|
....*
gi 689260967 1099 KAGGP 1103
Cdd:cd07139 453 REGGP 457
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
683-1097 |
4.20e-51 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 187.01 E-value: 4.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 683 EVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQ------ 756
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLitqiig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 757 --VRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQL 830
Cdd:cd07105 81 gsIPSDKPGTLamvvKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 831 L---PGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVA 907
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHL------KPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 908 SAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNpgrmtTDIGPVIDAEAKQNIDKHI-QALRGKGRSVFQA 985
Cdd:cd07105 235 GAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVdDALSKGAKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 986 VRENSEDrrewaqGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYNrNKLGAlVEQINASGYGLTLGVHTRiDETIA-Q 1062
Cdd:cd07105 309 LADESPS------GTSMPPTILDnvTPDMDIYSEESFGPVVSIIRVK-DEEEA-VRIANDSEYGLSAAVFTR-DLARAlA 379
|
410 420 430
....*....|....*....|....*....|....*...
gi 689260967 1063 VTGSAHVGNLYVNrnmvGAVVGVQ---PFGGEGLSGTG 1097
Cdd:cd07105 380 VAKRIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
673-1097 |
7.14e-51 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 188.93 E-value: 7.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 673 VGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHY 752
Cdd:PRK09407 45 LATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 753 YA-------------------GQVRddfdnETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQ 813
Cdd:PRK09407 125 YArrapkllaprrragalpvlTKTT-----ELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 814 GINILLEAGVPPGVVQLLPGRGETVGAQLTgdDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVD 893
Cdd:PRK09407 200 AVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRL------IGFSLELGGKNPMIVL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 894 SSALTEQVVVDVVASAFDSAGQRC-SALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHI 972
Cdd:PRK09407 272 DDADLDKAAAGAVRACFSNAGQLCiSIERIY-VHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 973 QALRGKGRSVFQAVRensedRREWAQGTFVPPTLI-----ELESFDElekEVFGPVLHVVRYNRnkLGALVEQINASGYG 1047
Cdd:PRK09407 351 DDAVAKGATVLAGGK-----ARPDLGPLFYEPTVLtgvtpDMELARE---ETFGPVVSVYPVAD--VDEAVERANDTPYG 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 689260967 1048 LTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTG 1097
Cdd:PRK09407 421 LNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
663-1097 |
3.51e-50 |
|
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: 185.72 E-value: 3.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPKdIVGYVRDATENEVEQALEN---AVNSApiWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANA 739
Cdd:cd07113 19 ITNPATEQ-VIASVASATEADVDAAVASawrAFVSA--WAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 740 IA-EVREAVDFLHYYAGQVR----------------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07113 96 RAfEVGQSANFLRYFAGWATkingetlapsipsmqgERYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 802 KPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGEtVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLI 881
Cdd:cd07113 176 KPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDL------TRVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 882 AETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVID 961
Cdd:cd07113 249 LELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLAN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 962 AEAKQNIDKHIQALRGKGRSVFQAVRENSEDrrewaqGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYNRNKlgALVE 1039
Cdd:cd07113 329 QPHFDKVCSYLDDARAEGDEIVRGGEALAGE------GYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDEE--ELIQ 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 689260967 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07113 401 LINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
656-1106 |
1.52e-49 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 183.95 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 656 DDGEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKT 735
Cdd:PRK11241 23 NNGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 736 FANAIAEVREAVDFLHYYAGQVRDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:PRK11241 102 LAEAKGEISYAASFIEWFAEEGKRIYGDTIpghqadkrliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 804 AEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAE 883
Cdd:PRK11241 182 ASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI------KKVSLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 884 TGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAE 963
Cdd:PRK11241 256 LGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 964 AKQNIDKHIQALRGKGRSVFQAVRENSedrrewAQGTFVPPT-LIELESFDELEK-EVFGPVLHVVRYNRNklGALVEQI 1041
Cdd:PRK11241 336 AVAKVEEHIADALEKGARVVCGGKAHE------LGGNFFQPTiLVDVPANAKVAKeETFGPLAPLFRFKDE--ADVIAQA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 689260967 1042 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGG---EGLSGTGPKAGGPMYL 1106
Cdd:PRK11241 408 NDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
657-1097 |
8.45e-49 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 181.50 E-value: 8.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEPKdIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTF 736
Cdd:cd07117 14 SGETIDSYNPANGE-TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 737 ANAIA-EVREAVDFLHYYAGQVR------DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07117 93 RETRAvDIPLAADHFRYFAGVIRaeegsaNMIDEDTlsivlREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 805 EQTPLIAAQGINILLEAgVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAET 884
Cdd:cd07117 173 STTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------IPATLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 885 GGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEA 964
Cdd:cd07117 246 GGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 965 KQNIDKHIQALRGKGRSVFQAVRENSEDrrEWAQGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYNRNKlgALVEQIN 1042
Cdd:cd07117 326 LDKILSYVDIAKEEGAKILTGGHRLTEN--GLDKGFFIEPTLIVNVTNDMrvAQEEIFGPVATVIKFKTED--EVIDMAN 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 689260967 1043 ASGYGLTLGVHTRiDETIA-QVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07117 402 DSEYGLGGGVFTK-DINRAlRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
653-1139 |
8.40e-48 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 178.92 E-value: 8.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 653 QPVDD--GEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVR 730
Cdd:PRK13252 14 AYVEAtsGETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 731 EAGKTFANAI-AEVREAVDFLHYYAG----------QVRD-DFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:PRK13252 93 DTGKPIQETSvVDIVTGADVLEYYAGlapalegeqiPLRGgSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 799 VLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGEtVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpT 878
Cdd:PRK13252 173 MIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASL------K 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 879 PLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCS-ALRILcLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIG 957
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 958 PVIDAEAKQNIDKHIQALRGKGRSVF---QAVRENsedrrEWAQGTFVPPTLielesF----DELE---KEVFGPVLHVV 1027
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGARLLcggERLTEG-----GFANGAFVAPTV-----FtdctDDMTivrEEIFGPVMSVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1028 RYNRNKlgALVEQINASGYGLTLGVHTRiDETIA-QVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAGgpmyl 1106
Cdd:PRK13252 395 TFDDED--EVIARANDTEYGLAAGVFTA-DLSRAhRVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIGRENG----- 464
|
490 500 510
....*....|....*....|....*....|...
gi 689260967 1107 yrllasrpedalLTTLNrqdaHYpvdSQLKSVL 1139
Cdd:PRK13252 465 ------------IATLE----HY---TQIKSVQ 478
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
658-1101 |
4.59e-46 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 174.25 E-value: 4.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 658 GEMAPVVNPAEPKDIvGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFA 737
Cdd:PLN02315 33 GPLVSSVNPANNQPI-AEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 738 NAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:PLN02315 112 EGIGEVQEIIDMCDFAVGLSRqlngsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 806 QTPLIAAQGINILLEA----GVPPGVVQLLPGrGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqGRptpLI 881
Cdd:PLN02315 192 TTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GK---CL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 882 AETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVID 961
Cdd:PLN02315 265 LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 962 AEAKQNIDKHIQALRGKGRSVFQAVRENSEDrrewaqGTFVPPTLIELE-SFDELEKEVFGPVLHVVRYnrNKLGALVEQ 1040
Cdd:PLN02315 345 PESKKNFEKGIEIIKSQGGKILTGGSAIESE------GNFVQPTIVEISpDADVVKEELFGPVLYVMKF--KTLEEAIEI 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 689260967 1041 INASGYGLTLGVHTRIDETIAQVTG--SAHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAG 1101
Cdd:PLN02315 417 NNSVPQGLSSSIFTRNPETIFKWIGplGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
707-1106 |
5.60e-46 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 171.46 E-value: 5.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 707 AAILERAAMLMEdqmqqlmgILVREAGKTFANAIAEVREAVDFLHYYAGQVR--------DDFDNET----HRPLGPVVC 774
Cdd:PRK10090 6 AGIRERASEISA--------LIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegeiiqSDRPGENillfKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 775 ISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFT 854
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 855 GSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTL 934
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 935 KMLKGAMAECRMGNP-GRMTTDIGPVIDAEAKQNIDKHIQalrgkgRSVFQAVRENSEDRREWAQGTFVPPTLIE--LES 1011
Cdd:PRK10090 232 NRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVA------RAVEEGARVALGGKAVEGKGYYYPPTLLLdvRQE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1012 FDELEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQP-FGG 1090
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAgWRK 383
|
410
....*....|....*.
gi 689260967 1091 EGLSGTGPKAGGPMYL 1106
Cdd:PRK10090 384 SGIGGADGKHGLHEYL 399
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
658-1060 |
6.96e-45 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 170.32 E-value: 6.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 658 GEMAPVVNPAEPKDIVGyVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFA 737
Cdd:PLN00412 30 GKSVAITNPSTRKTQYK-VQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 738 NAIAEVREAVDFLHYYA---------GQ--VRDDF-DNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:PLN00412 109 DAVTEVVRSGDLISYTAeegvrilgeGKflVSDSFpGNERNKycltskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 799 VLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRniasrldpqGRPT 878
Cdd:PLN00412 189 VVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKK---------AGMV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 879 PLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPgRMTTDIGP 958
Cdd:PLN00412 260 PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPP-EDDCDITP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 959 VIDAEAKQNIDKHIQALRGKGRSVFQavrensEDRREwaqGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYNRNKLGa 1036
Cdd:PLN00412 339 VVSESSANFIEGLVMDAKEKGATFCQ------EWKRE---GNLIWPLLLDNVRPDMriAWEEPFGPVLPVIRINSVEEG- 408
|
410 420
....*....|....*....|....*
gi 689260967 1037 lVEQINASGYGLTLGVHTR-IDETI 1060
Cdd:PLN00412 409 -IHHCNASNFGLQGCVFTRdINKAI 432
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
656-1101 |
2.49e-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: 168.44 E-value: 2.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 656 DDGEMAPVVNPAEPKDIVGyVRDATENEVEQALE---NAVNSAPiWFATPPQERAAILERAAMLMEDQMQQLMGILVREA 732
Cdd:cd07140 18 EGGKTYNTINPTDGSVICK-VSLATVEDVDRAVAaakEAFENGE-WGKMNARDRGRLMYRLADLMEEHQEELATIESLDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 733 GKTFANAI-AEVREAVDFLHYYAG-------------QVRDDfDNET---HRPLGPVVCISPWNFPLAIFTGQIAAALAA 795
Cdd:cd07140 96 GAVYTLALkTHVGMSIQTFRYFAGwcdkiqgktipinQARPN-RNLTltkREPIGVCGIVIPWNYPLMMLAWKMAACLAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 796 GNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIAsrlDPQG 875
Cdd:cd07140 175 GNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA---VSNL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 876 RPTPLiaETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTD 955
Cdd:cd07140 252 KKVSL--ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 956 IGPvidaeakQNIDKHIQALRgkgRSVFQAVRENSE----DRREWAQGTFVPPTL---IELESFDELEkEVFGPVLHVVR 1028
Cdd:cd07140 330 HGP-------QNHKAHLDKLV---EYCERGVKEGATlvygGKQVDRPGFFFEPTVftdVEDHMFIAKE-ESFGPIMIISK 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 689260967 1029 YNRNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN---RNMVGAvvgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07140 399 FDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynKTDVAA-----PFGGFKQSGFGKDLG 469
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
671-1101 |
2.84e-44 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 168.85 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 671 DIVGYVRDATENEVEQALE---NAVNSAPiWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFA-NAIAEVREA 746
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKaarEAFDHGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 747 VDFLHYYAGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQG 814
Cdd:PLN02766 126 AGLLRYYAGAA-DKIHGETlkmsrqlqgytlKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 815 INILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASL-LQRNIASRLdpqgrpTPLIAETGGMNAMIVD 893
Cdd:PLN02766 205 AHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKiMQAAATSNL------KQVSLELGGKSPLLIF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 894 SSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQ 973
Cdd:PLN02766 279 DDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 974 ALRGKGRSVFQAVRENSEdrrewaQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLG 1051
Cdd:PLN02766 359 HGKREGATLLTGGKPCGD------KGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAG 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 689260967 1052 VHTRIDETIAQVTGSAHVGNLYVNRNMvgAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:PLN02766 431 IVTKDLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
658-1101 |
3.01e-44 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 169.60 E-value: 3.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 658 GEMAPVVNPaEPKDIVGYVRDATENEVEQAL---ENAVNSAPiWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGK 734
Cdd:PLN02466 72 GKTFPTLDP-RTGEVIAHVAEGDAEDVNRAVaaaRKAFDEGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 735 TFANAI-AEVREAVDFLHYYAG--------QVRDDFDNET---HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:PLN02466 150 PYEQSAkAELPMFARLFRYYAGwadkihglTVPADGPHHVqtlHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 803 PAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQrNIASRLDPQgrptPLIA 882
Cdd:PLN02466 230 TAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVL-ELAAKSNLK----PVTL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 883 ETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDA 962
Cdd:PLN02466 305 ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDS 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 963 EAKQNIDKHIQALRGKGrsvfqAVRENSEDRREwAQGTFVPPTLIELESFDEL--EKEVFGPVLHVVRYnrNKLGALVEQ 1040
Cdd:PLN02466 385 EQFEKILRYIKSGVESG-----ATLECGGDRFG-SKGYYIQPTVFSNVQDDMLiaQDEIFGPVQSILKF--KDLDEVIRR 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:PLN02466 457 ANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
644-1075 |
1.05e-43 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 167.22 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 644 QWRAkPVLeqpvddGEMAPVVNPAEpKDIVGYVRDATENEVEQALENA-----VNSAPIWFATPPQERAAILERAAMLME 718
Cdd:PLN02467 15 EWRE-PVL------GKRIPVVNPAT-EETIGDIPAATAEDVDAAVEAArkafkRNKGKDWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 719 DQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYAGQVR--------------DDFDNETHR-PLGPVVCISPWNFPLA 783
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEaldakqkapvslpmETFKGYVLKePLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 784 IFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVAsll 863
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 864 qRNIASRLDPQGRPTPLiaETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAE 943
Cdd:PLN02467 244 -RKIMTAAAQMVKPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 944 CRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGrsvfqAVRENSEDRRE-WAQGTFVPPTLI-----ELESFDElek 1017
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEG-----ATILCGGKRPEhLKKGFFIEPTIItdvttSMQIWRE--- 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 689260967 1018 EVFGPVLHVVRYNRNKlgALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:PLN02467 393 EVFGPVLCVKTFSTED--EAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
644-1097 |
7.32e-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: 164.16 E-value: 7.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 644 QWRAkpvleqPVDdGEMAPVVNPAEPKDIVGYVRdATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQ 723
Cdd:cd07116 8 EWVA------PVK-GEYFDNITPVTGKVFCEVPR-STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 724 LMGILVREAGKTFANAI-AEVREAVDFLHYYAGQVR------DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAA 791
Cdd:cd07116 80 LAVAETWDNGKPVRETLaADIPLAIDHFRYFAGCIRaqegsiSEIDENTvayhfHEPLGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 792 ALAAGNSVLAKPAEQTPLiaaqGINILLEA---GVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIA 868
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPA----SILVLMELigdLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 869 SRLdpqgrpTPLIAETGGMNAMIVDSSALTEQ------VVVDVVASAFDSaGQRCSALRILCLQDDIADHTLKMLKGAMA 942
Cdd:cd07116 236 ENI------IPVTLELGGKSPNIFFADVMDADdaffdkALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 943 ECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRENSEDrREWAQGTFVPPTLIELESFDELEKEVFGP 1022
Cdd:cd07116 309 AIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELG-GLLGGGYYVPTTFKGGNKMRIFQEEIFGP 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 689260967 1023 VLHVVRYNRNKlgALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07116 388 VLAVTTFKDEE--EALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
658-1075 |
9.69e-42 |
|
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: 160.82 E-value: 9.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 658 GEMAPVVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFA 737
Cdd:TIGR01722 15 GTYIPVTNPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 738 NAIAEVREAVDFLHYYAG-----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:TIGR01722 94 DALGDVARGLEVVEHACGvnsllkgetstQVATRVDVYSIRqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 806 QTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGaQLTGDDRVRGVMFTGSTEVAsllqRNIASRLDPQGRPTPliAETG 885
Cdd:TIGR01722 174 KVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIG----RYIHTTGSAHGKRVQ--ALGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 886 GMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDiADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAK 965
Cdd:TIGR01722 247 AKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 966 QNIDKHIQALRGKGRSVFQAVRENSEDRREwaQGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYnrNKLGALVEQINA 1043
Cdd:TIGR01722 326 DRVASLIAGGAAEGAEVLLDGRGYKVDGYE--EGNWVGPTLLERVPPTMkaYQEEIFGPVLCVLEA--DTLEEAIALINA 401
|
410 420 430
....*....|....*....|....*....|..
gi 689260967 1044 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:TIGR01722 402 SPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN 433
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
663-1097 |
1.47e-41 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 159.51 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEPKDIvGYVRDATENEVEQALENA------VNSapiWFatPPQERAAILERAAMLMEDQMQQLMGILVREAGKTF 736
Cdd:cd07148 3 VVNPFDLKPI-GEVPTVDWAAIDKALDTAhalfldRNN---WL--PAHERIAILERLADLMEERADELALLIAREGGKPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 737 ANAIAEVREAVDFLHYYAGQVRDDFDNE----------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07148 77 VDAKVEVTRAIDGVELAADELGQLGGREipmgltpasagriaftTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 801 AKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGEtVGAQLTGDDRVRGVMFTGSTEVASLLQrniaSRLDPQGRptpl 880
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLR----SKLAPGTR---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 881 IA-ETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPV 959
Cdd:cd07148 228 CAlEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 960 IDAEAKQNIDKHIQALRGKGRSVFQAVRENSEDrrewaqgTFVPPTLIE-LESFDELEKEVFGPVlhVVRYNRNKLGALV 1038
Cdd:cd07148 308 IRPREVDRVEEWVNEAVAAGARLLCGGKRLSDT-------TYAPTVLLDpPRDAKVSTQEIFGPV--VCVYSYDDLDEAI 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 689260967 1039 EQINASGYGLTLGVHTR-ID---ETIAQVTGSAhvgnLYVNrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07148 379 AQANSLPVAFQAAVFTKdLDvalKAVRRLDATA----VMVN-DHTAFRVDWMPFAGRRQSGYG 436
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
664-1097 |
1.20e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 156.82 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 664 VNPAEPKDIVGYvRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEV 743
Cdd:PRK09406 6 INPATGETVKTF-TALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 744 REAVDFLHYYAGQVRDDFDNET--------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPL 809
Cdd:PRK09406 85 LKCAKGFRYYAEHAEALLADEPadaaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 810 IAAQGINILLEAGVPPGVVQ-LLPGRGEtVGAQLTgDDRVRGVMFTGStEVASllqRNIASRLDPQGRPTPLiaETGGMN 888
Cdd:PRK09406 165 TALYLADLFRRAGFPDGCFQtLLVGSGA-VEAILR-DPRVAAATLTGS-EPAG---RAVAAIAGDEIKKTVL--ELGGSD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 889 AMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNI 968
Cdd:PRK09406 237 PFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 969 DKHIQALRGKGRSVFQAVRenSEDRREWaqgtFVPPTLI-----ELESFDElekEVFGPVLHVvrYNRNKLGALVEQINA 1043
Cdd:PRK09406 317 EKQVDDAVAAGATILCGGK--RPDGPGW----FYPPTVItditpDMRLYTE---EVFGPVASL--YRVADIDEAIEIANA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1044 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrNMVGAVVGVqPFGGEGLSGTG 1097
Cdd:PRK09406 386 TTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSGYG 437
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
657-1097 |
9.32e-39 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 152.36 E-value: 9.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 657 DGEMAPVVNPAEPKDIVGYVRdATENEVEQALENA--VNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGK 734
Cdd:PRK09847 33 ENETFETVDPVTQAPLAKIAR-GKSVDIDRAVSAArgVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 735 TF-----------ANAIAEVREAVDFLHyyaGQVRDDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:PRK09847 112 PIrhslrddipgaARAIRWYAEAIDKVY---GEVATTSSHElamiVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 800 LAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIAsrldpQGRPTP 879
Cdd:PRK09847 189 ILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG-----DSNMKR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 880 LIAETGGMNAMIV--DSSALtEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIG 957
Cdd:PRK09847 264 VWLEAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 958 PVIDAEAKQNIDKHIQALRGKGRSVFqavrenseDRREWAQGTFVPPT-LIELESFDELEK-EVFGPVLHVVRYNRNKLG 1035
Cdd:PRK09847 343 TLIDCAHADSVHSFIREGESKGQLLL--------DGRNAGLAAAIGPTiFVDVDPNASLSReEIFGPVLVVTRFTSEEQA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 689260967 1036 ALVEqiNASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:PRK09847 415 LQLA--NDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
766-1097 |
3.34e-36 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 143.05 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgINILLEAGVPPGVVQLLPGrGETVGAQLTgD 845
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSAL-LAKLIPKYFDPEAVAVVEG-GVEVATALL-A 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 846 DRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCL 925
Cdd:cd07087 175 EPFDHIFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 926 QDDIADHTLKMLKGAMAEcRMGNPGRMTTDIGPVIDaeakqniDKHIQALRG--KGRSVFQAVRENSEDRrewaqgtFVP 1003
Cdd:cd07087 249 HESIKDELIEELKKAIKE-FYGEDPKESPDYGRIIN-------ERHFDRLASllDDGKVVIGGQVDKEER-------YIA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1004 PTLIELESFDE--LEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGA 1081
Cdd:cd07087 314 PTILDDVSPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHA 391
|
330
....*....|....*.
gi 689260967 1082 VVGVQPFGGEGLSGTG 1097
Cdd:cd07087 392 AIPNLPFGGVGNSGMG 407
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
674-1101 |
4.48e-36 |
|
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: 143.59 E-value: 4.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 674 GYVRDATENEVEQALENAVNSAPIWFATPPQERAAILeraAMLME---DQMQQLMGILVREAGKTFANA-IAEVREAVDF 749
Cdd:cd07098 10 GSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVL---RSLLKyilENQEEICRVACRDTGKTMVDAsLGEILVTCEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 750 LHY--------YAGQVRDDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQG 814
Cdd:cd07098 87 IRWtlkhgekaLRPESRPGGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 815 INILLEA----GVPPGVVQLLPGRGETvGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAM 890
Cdd:cd07098 167 LSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLELGGKDPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 891 IVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVI-DAEAKQNID 969
Cdd:cd07098 240 IVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMIsPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 970 KHIQALRGKGRSVFQAVRENsedRREWAQGTFVPPTLIE--LESFDELEKEVFGPVLHVVRYNRNKlgALVEQINASGYG 1047
Cdd:cd07098 320 LVADAVEKGARLLAGGKRYP---HPEYPQGHYFPPTLLVdvTPDMKIAQEEVFGPVMVVMKASDDE--EAVEIANSTEYG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1048 LTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
663-1047 |
2.38e-32 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 134.49 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 663 VVNPAEpKDIVGYVRDATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAE 742
Cdd:PLN02419 133 VINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 743 VREAVDFLHYYAG-----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:PLN02419 212 IFRGLEVVEHACGmatlqmgeylpNVSNGVDTYSIRePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 811 AAQGINILLEAGVPPGVVQLLPGRGETVGAqLTGDDRVRGVMFTGSTEVAsllqRNIASRLDPQGRptPLIAETGGMNAM 890
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAG----MHIYARAAAKGK--RIQSNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 891 IVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAeCRMGNPGRMTTDIGPVIDAEAKQNIDK 970
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKA-LKVTCGSEPDADLGPVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 971 HIQALRGKGRSVFQAVRENSEDRREwaQGTFVPPTLI-----ELESFDElekEVFGPVLhvVRYNRNKLGALVEQINASG 1045
Cdd:PLN02419 444 LIQSGVDDGAKLLLDGRDIVVPGYE--KGNFIGPTILsgvtpDMECYKE---EIFGPVL--VCMQANSFDEAISIINKNK 516
|
..
gi 689260967 1046 YG 1047
Cdd:PLN02419 517 YG 518
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
664-1075 |
7.91e-32 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 130.75 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 664 VNPAEPKDIVGYVRdATENEVEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEV 743
Cdd:PRK13968 12 VNPATGEQLSVLPW-AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 744 REAVDFLHYYAGQ-----------VRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAA 812
Cdd:PRK13968 91 AKSANLCDWYAEHgpamlkaeptlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 813 QGINILLEAGVPPGVVQLLPGRGETVgAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIV 892
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAAL------KKCVLELGGSDPFIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 893 DSSALTEQVVVDVVASAFDSAGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHI 972
Cdd:PRK13968 244 LNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 973 QALRGKGRSVFQAVRENSedrrewAQGTFVPPTLI-----ELESFDElekEVFGPVLhVVRYNRNKLGALvEQINASGYG 1047
Cdd:PRK13968 324 EATLAEGARLLLGGEKIA------GAGNYYAPTVLanvtpEMTAFRE---ELFGPVA-AITVAKDAEHAL-ELANDSEFG 392
|
410 420
....*....|....*....|....*...
gi 689260967 1048 LTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:PRK13968 393 LSATIFTTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
684-1117 |
7.63e-31 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 127.35 E-value: 7.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 684 VEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHY----YAGQVRD 759
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARafviYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 760 DFDNE--------THR---PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAG-VPPGV 827
Cdd:cd07084 81 EPGNHlgqglkqqSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 828 VQLLPGRGETvGAQLTGDDRVRGVMFTGSTEVASLLqrniasRLDPqgRPTPLIAETGGMNAMIVDSSALTEQVVVD-VV 906
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKL------ALDA--KQARIYLELAGFNWKVLGPDAQAVDYVAWqCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 907 ASAFDSAGQRCSALRILCLQDDiaDHTLKMLKGAMAECRMGNPGrmTTDIGPVIdaeaKQNIDKHIQALRGKGRSV--FQ 984
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPEN--WSKTPLVEKLKALLARRKLE--DLLLGPVQ----TFTTLAMIAHMENLLGSVllFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 985 AVRENSEDRREWAQGTFVPPTLIELESFDEL----EKEVFGPVLHVVRYNRNKLGALVEQINASGYGLTLGVHTRIDETI 1060
Cdd:cd07084 304 GKELKNHSIPSIYGACVASALFVPIDEILKTyelvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFL 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 689260967 1061 AQVT------GSAHVGNLYVNRNMVGAVVGVQPFGGeglsGTGPKAGGPMYLYRLLASRPEDA 1117
Cdd:cd07084 384 QELIgnlwvaGRTYAILRGRTGVAPNQNHGGGPAAD----PRGAGIGGPEAIKLVWRCHAEQA 442
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
766-1102 |
7.95e-31 |
|
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: 127.34 E-value: 7.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAgVPPGVVQLLPGRGETVGAQLtgD 845
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVAQALL--E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 846 DRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCL 925
Cdd:cd07134 175 LPFDHIFFTGSPAVGKIVMAAAAKHL------ASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 926 QDDIADHTLKMLKGAMAECRMGNPGRM-TTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRENSEDRrewaqgtFVPP 1004
Cdd:cd07134 249 HESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR-------YIAP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1005 TLIE--LESFDELEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAV 1082
Cdd:cd07134 322 TVLTnvTPDMKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFL 399
|
330 340
....*....|....*....|
gi 689260967 1083 VGVQPFGGEGLSGTGpKAGG 1102
Cdd:cd07134 400 NPNLPFGGVNNSGIG-SYHG 418
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
766-1097 |
3.30e-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: 122.33 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLiAAQGINILLEAGVPPGVVQLLPGRGETVGAQLtgD 845
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPH-TAALLAELVPKYLDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 846 DRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCL 925
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIAEAAAKHL------TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 926 QDDIADHTLKMLKGAMAEcRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKgrsVFQAVRENSEDRrewaqgtFVPPT 1005
Cdd:cd07135 257 DPSVYDEFVEELKKVLDE-FYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGK---VVIGGEMDEATR-------FIPPT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1006 LIELESFDE--LEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVV 1083
Cdd:cd07135 326 IVSDVSWDDslMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGV 403
|
330
....*....|....
gi 689260967 1084 GVQPFGGEGLSGTG 1097
Cdd:cd07135 404 DNAPFGGVGDSGYG 417
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
684-1054 |
8.03e-28 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 118.41 E-value: 8.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 684 VEQALENAVNSAPIWFATPPQERAAILERAAMLMEDQMQQLMGILVREAG-----------------KTFANAIAEvrea 746
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpearlqgelgrttgqlRLFADLVRE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 747 vdflHYYAGQVRDDFDNE-----------THRPLGPVVCISPWNFPLAIFT--GQIAAALAAGNSVLAK-----PAeqTP 808
Cdd:cd07129 77 ----GSWLDARIDPADPDrqplprpdlrrMLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahpahPG--TS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 809 LIAAQGI-NILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVASLLQRNIASRLDpqgrPTPLIAETGGM 887
Cdd:cd07129 151 ELVARAIrAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGSV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 888 NAMIVDSSALTE---QVVVDVVASAFDSAGQRCSALRILCLQDDIADHTL-KMLKGAMAECrmgNPGRMTTdigPVIdAE 963
Cdd:cd07129 227 NPVFILPGALAErgeAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAGDAFiAALAEALAAA---PAQTMLT---PGI-AE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 964 AKQNIDKHIQALRGkgrsVFQAVRENSEDRREWAQGTFVPPTLIELESFDELEKEVFGPVLHVVRY-NRNKLGALVEQIN 1042
Cdd:cd07129 300 AYRQGVEALAAAPG----VRVLAGGAAAEGGNQAAPTLFKVDAAAFLADPALQEEVFGPASLVVRYdDAAELLAVAEALE 375
|
410
....*....|..
gi 689260967 1043 ASgygLTLGVHT 1054
Cdd:cd07129 376 GQ---LTATIHG 384
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
768-1097 |
2.89e-27 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 117.44 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIaAQGINILLEAGVPPGVVQLLPGrGETVGAQLTgDDR 847
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT-SKLMAKLLTKYLDPSYVRVIEG-GVEVTTELL-KEP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 848 VRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRILCLQD 927
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 928 DIADHTLKMLKGAMAEcRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKgrsVFQAVRENSEDRrewaqgtFVPPTLI 1007
Cdd:PTZ00381 260 SIKDKFIEALKEAIKE-FFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGK---VVYGGEVDIENK-------YVAPTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1008 ELESFDE--LEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHT---RIDETIAQVTGSahvGNLYVNRNMVGAV 1082
Cdd:PTZ00381 329 VNPDLDSplMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGedkRHKELVLENTSS---GAVVINDCVFHLL 403
|
330
....*....|....*
gi 689260967 1083 VGVQPFGGEGLSGTG 1097
Cdd:PTZ00381 404 NPNLPFGGVGNSGMG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
765-1097 |
1.36e-24 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 108.34 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 765 THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINiLLEAGVPPGVVQLLPGRGEtVGAQLTG 844
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAE-LLAEYFDEDEVAVVTGGAD-VAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 845 ---DDrvrgVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALR 921
Cdd:cd07133 176 lpfDH----LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 922 ILCLQDDIADHTLKMLKGAMAEC---RMGNPgrmttDIGPVIDAEAKQNIDKHIQALRGKGRSVFQaVRENSEDRrewAQ 998
Cdd:cd07133 246 YVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIE-LNPAGEDF---AA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 999 GTFVPPTLIeLESFDE---LEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:cd07133 317 TRKLPPTLV-LNVTDDmrvMQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN 393
|
330 340
....*....|....*....|..
gi 689260967 1076 RNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07133 394 DTLLHVAQDDLPFGGVGASGMG 415
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
768-1097 |
1.43e-21 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 99.80 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAqginiLLEAGVP----PGVVQLLPGrGETVGAQLT 843
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPkyldSKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 844 gDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVD--SSALTEQVVVD-VVASAFDS-AGQRCSA 919
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDslSSSRDTKVAVNrIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 920 LRILCLQDDIADHTLKMLKgAMAECRMGNPGRMTTDIGPVIDAeakqnidKHIQALRG--KGRSVfQA--VRENSEDrre 995
Cdd:PLN02203 255 IDYVLVEERFAPILIELLK-STIKKFFGENPRESKSMARILNK-------KHFQRLSNllKDPRV-AAsiVHGGSID--- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 996 wAQGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRiDET----IAQVTGSahv 1069
Cdd:PLN02203 323 -EKKLFIEPTILLNPPLDSdiMTEEIFGPLLPIITV--KKIEDSIAFINSKPKPLAIYAFTN-NEKlkrrILSETSS--- 395
|
330 340
....*....|....*....|....*...
gi 689260967 1070 GNLYVNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:PLN02203 396 GSVTFNDAIIQYACDSLPFGGVGESGFG 423
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
704-1102 |
2.11e-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: 99.65 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 704 QERAAILER-AAMLMEDQmQQLMGILVReAGKTFANAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPV---------- 772
Cdd:cd07128 59 HERAAMLKAlAKYLMERK-EDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVeplskdgtfv 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 773 ------------VCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGV-PPGVVQLLPGRGETVG 839
Cdd:cd07128 137 gqhiltprrgvaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 840 AQLTGDDRVrgvMFTGSTEVASLLQR--NIASRldpqgrPTPLIAETGGMNAMIV--DSSALTEQ---VVVDVVASAFDS 912
Cdd:cd07128 217 DHLGEQDVV---AFTGSAATAAKLRAhpNIVAR------SIRFNAEADSLNAAILgpDATPGTPEfdlFVKEVAREMTVK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 913 AGQRCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRENSED 992
Cdd:cd07128 288 AGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 993 RREWAQGTFVPPTLIELESFDEL----EKEVFGPVLHVVRY-NRNKLGALVeqinASGYG-LTLGVHTRIDETIAQ-VTG 1065
Cdd:cd07128 368 GADAEKGAFFPPTLLLCDDPDAAtavhDVEAFGPVATLMPYdSLAEAIELA----ARGRGsLVASVVTNDPAFARElVLG 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 689260967 1066 SA-HVGNLYV-NRNMVGAVVG---VQP---FGGEGLSGTGPKAGG 1102
Cdd:cd07128 444 AApYHGRLLVlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGG 488
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
706-1097 |
6.50e-20 |
|
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: 94.21 E-value: 6.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 706 RAAILERAAMLMEDQMQQLMGILVREAGKT-FANAIAEV-------REAVDFLHYYAG--QVRDDFDNET------HRPL 769
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPkFEAVLSEIllvkneiKYAISNLPEWMKpePVKKNLATLLddvyiyKEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 770 GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPlIAAQGINILLEAGVPPGVVQLLPGrgetvGAQLTG---DD 846
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP-ATAKLLAELIPKYLDKECYPVVLG-----GVEETTellKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 847 RVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALR-ILCl 925
Cdd:cd07132 176 RFDYIFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDyVLC- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 926 QDDIADHTLKMLKGAMAECrMGNPGRMTTDIGPVIDaeakqniDKHIQALRG--KGRSVFQAVRENSEDRrewaqgtFVP 1003
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIIN-------DRHFQRLKKllSGGKVAIGGQTDEKER-------YIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1004 PT-LIELESFDEL-EKEVFGPVLHVVryNRNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGA 1081
Cdd:cd07132 314 PTvLTDVKPSDPVmQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHY 391
|
410
....*....|....*.
gi 689260967 1082 VVGVQPFGGEGLSGTG 1097
Cdd:cd07132 392 TLDSLPFGGVGNSGMG 407
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
768-1097 |
1.58e-19 |
|
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: 92.86 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgINILLEAGVPPGVVQLLPGrGETVGAQLTgDDR 847
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSAL-LAKLIPEYLDTKAIKVIEG-GVPETTALL-EQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 848 VRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDS-AGQRCSALRILCLQ 926
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 927 DDIADHTLKMLKGAMAECRMGNPgRMTTDIGPVIDAeakqnidKHIQALRG--KGRSVFQAV---RENSEDRrewaqgTF 1001
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENP-KESKDLSRIVNS-------HHFQRLSRllDDPSVADKIvhgGERDEKN------LY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1002 VPPTLIELESFDEL--EKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMV 1079
Cdd:cd07137 318 IEPTILLDPPLDSSimTEEIFGPLLPIITV--KKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVV 395
|
330
....*....|....*...
gi 689260967 1080 GAVVGVQPFGGEGLSGTG 1097
Cdd:cd07137 396 QYAIDTLPFGGVGESGFG 413
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
713-1073 |
3.93e-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: 92.56 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 713 AAMLMEDQMQQLMGILV-REAGKTFANAIAEVREAVDFLHYYAG-QVR----------DDFDNETHR---PLGPVVCISP 777
Cdd:cd07126 72 AHELRKPEVEDFFARLIqRVAPKSDAQALGEVVVTRKFLENFAGdQVRflarsfnvpgDHQGQQSSGyrwPYGPVAIITP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 778 WNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGVPPGVVQLLPGRGETVGAQLTgDDRVRGVMFTGST 857
Cdd:cd07126 152 FNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILL-EANPRMTLFTGSS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 858 EVASLLQRNIASRLDpqgrptpliAETGGMNAMIVDSSALTeqvvVDVVA-----SAFDSAGQRCSALRILCLQDDIADH 932
Cdd:cd07126 231 KVAERLALELHGKVK---------LEDAGFDWKILGPDVSD----VDYVAwqcdqDAYACSGQKCSAQSILFAHENWVQA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 933 TLKMLKGAMAECRmgNPGRMTtdIGPVI--DAEAKQNIDKHIQALRGkGRSVF--QAVRENSEDRREWA---QGTFVP-P 1004
Cdd:cd07126 298 GILDKLKALAEQR--KLEDLT--IGPVLtwTTERILDHVDKLLAIPG-AKVLFggKPLTNHSIPSIYGAyepTAVFVPlE 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 689260967 1005 TLIELESFDELEKEVFGPVLHVVRYNRNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLY 1073
Cdd:cd07126 373 EIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
705-1130 |
5.11e-19 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 92.46 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 705 ERAAILERAAMLMEDQMQQLMGILVREAGKTFANAIAEVREAVDFLHYYA------GQVRDDFDNETHR----------- 767
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalGDARLLRDGEAVQlgkdpafqgqh 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 768 ---PL-GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGINILLEAGV-PPGVVQLLPGRGETVGAQL 842
Cdd:PRK11903 144 vlvPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 843 TGDDRVRgvmFTGSTEVASLLqrniasRLDPQ--GRPTPLIAETGGMNAMI-----VDSSALTEQVVVDVVASAFDSAGQ 915
Cdd:PRK11903 224 QPFDVVS---FTGSAETAAVL------RSHPAvvQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 916 RCSALRILCLQDDIADHTLKMLKGAMAECRMGNPGRMTTDIGPVIDAEAKQNIDKHIQALRGKGRSVFQAVRENSEDrRE 995
Cdd:PRK11903 295 KCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVD-AD 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 996 WAQGTFVPPTLIELESFDEL----EKEVFGPVLHVVRYN---------RNKLGALVeqinASGYGLTLGVHTRIDETIAQ 1062
Cdd:PRK11903 374 PAVAACVGPTLLGASDPDAAtavhDVEVFGPVATLLPYRdaahalalaRRGQGSLV----ASVYSDDAAFLAAAALELAD 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 689260967 1063 VTGSAHVGNLYVNRNMVGAVVgVQP---FGGEGLSGTGPKAGG--PMYLY-RLLASRPEDALLTTLnRQDAHYP 1130
Cdd:PRK11903 450 SHGRVHVISPDVAALHTGHGN-VMPqslHGGPGRAGGGEELGGlrALAFYhRRSAVQASPAVLDAL-TQAAAAP 521
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
89-136 |
6.46e-18 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 78.27 E-value: 6.46e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 689260967 89 SVTRSAITAAWRRPETDAVPMLLEQARLPQPMADQAHKLAYQLAEKLR 136
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
768-1097 |
8.66e-18 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 87.94 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP----LIAAqginiLLEAGVPPGVVQLLPGRGETVGAQLt 843
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPntskVIAK-----IIEETFDEEYVAVVEGGVEENQELL- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 844 gDDRVRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFDSAGQRCSALRIL 923
Cdd:cd07136 174 -DQKFDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 924 CLQDDIADHTLKMLKGAMAEcRMGNPGRMTTDIGPVIDaeakqniDKHIQALRG--KGRSVFQAVRENSEDRrewaqgtF 1001
Cdd:cd07136 247 LVHESVKEKFIKELKEEIKK-FYGEDPLESPDYGRIIN-------EKHFDRLAGllDNGKIVFGGNTDRETL-------Y 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1002 VPPTLIELESFDE--LEKEVFGPVLHVVRYnrNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGS------------A 1067
Cdd:cd07136 312 IEPTILDNVTWDDpvMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENlsfgggcindtiM 389
|
330 340 350
....*....|....*....|....*....|
gi 689260967 1068 HVGNLYVnrnmvgavvgvqPFGGEGLSGTG 1097
Cdd:cd07136 390 HLANPYL------------PFGGVGNSGMG 407
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
768-1101 |
3.57e-15 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 80.09 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgINILLEAGVPPGVVQLLPGRGETVGAQLtgDDR 847
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAL-LAKLLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 848 VRGVMFTGSTEVASLLQRNIASRLdpqgrpTPLIAETGGMNAMIVDSSALTEQVVVDVVASAFD-SAGQRCSALRILCLQ 926
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 927 DDIADHTLKMLKGAMAECRMGNPGRmTTDIGPVIDAEAKQNIDKHIQAlrgkgRSVFQAVRENSEDRREWAQgtfVPPTL 1006
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDE-----KEVSDKIVYGGEKDRENLK---IAPTI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 1007 IELESFDEL--EKEVFGPVLHVVryNRNKLGALVEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVG 1084
Cdd:PLN02174 334 LLDVPLDSLimSEEIFGPLLPIL--TLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALH 411
|
330
....*....|....*..
gi 689260967 1085 VQPFGGEGLSGTGPKAG 1101
Cdd:PLN02174 412 TLPFGGVGESGMGAYHG 428
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-66 |
4.95e-15 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 71.01 E-value: 4.95e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 689260967 2 GTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFNYLEKLENDETLPE--IPALLAGAANESEE 66
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQegLAAADAGEFVSHEE 67
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
767-1082 |
8.70e-11 |
|
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: 66.35 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 767 RPLGPVVCISP---WNFPLAIFtgqiaAALAAGNSVLAKPAEQTPLIAAQGINI----LLEAGVPPGVVQLLP-GRGETV 838
Cdd:cd07127 194 RGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVQVarevLAEAGFDPNLVTLAAdTPEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 839 GAQLTGDDRVRGVMFTGSTEVASLLQRNIasrldpqgRPTPLIAETGGMNAMIVDSsalTEQVVVDVVASAFDSA---GQ 915
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDWLEANA--------RQAQVYTEKAGVNTVVVDS---TDDLKAMLRNLAFSLSlysGQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 916 RCSALR-ILCLQDDIADHTLKMLKGAMAEC-------RMGNPGRMTTDIGPVIDAEAKQNIDKhiqALRGKGRSVFQAVR 987
Cdd:cd07127 338 MCTTPQnIYVPRDGIQTDDGRKSFDEVAADlaaaidgLLADPARAAALLGAIQSPDTLARIAE---ARQLGEVLLASEAV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 988 ENSedrrEWAQGTFVPPTLIELESFDE--LEKEVFGPVLHVVRYNRNKLGALVEQINASGYG-LTLGVHTRIDETIAQVT 1064
Cdd:cd07127 415 AHP----EFPDARVRTPLLLKLDASDEaaYAEERFGPIAFVVATDSTDHSIELARESVREHGaMTVGVYSTDPEVVERVQ 490
|
330
....*....|....*...
gi 689260967 1065 GSAHVGNLYVNRNMVGAV 1082
Cdd:cd07127 491 EAALDAGVALSINLTGGV 508
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-46 |
2.72e-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: 53.91 E-value: 2.72e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 689260967 4 TTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFNYLEKLEN 46
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREEW 43
|
|
| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-45 |
2.78e-08 |
|
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: 50.97 E-value: 2.78e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 689260967 4 TTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFNYLEKLE 45
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLERLE 42
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
768-943 |
8.38e-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: 49.91 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 768 PLGPVVCISPWNFPLAIFTgQIAAALAAGNSVLAKPAEQTPlIAAQGINILLEAGVPPG----VVQLLPGRGETVGAQLT 843
Cdd:cd07077 100 PIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkiLVLYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 844 GDDRVRGVMFTGSTEVASLLQRNiasrldpqGRPTPLIAETGGMNAMIVDSSALTEQVVVDVVASA-FDSAGqrCSALRI 922
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA--CASEQN 247
|
170 180
....*....|....*....|.
gi 689260967 923 LCLQDDIADHTLKMLKGAMAE 943
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLKLVV 268
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
327-588 |
2.41e-05 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 48.54 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 327 SIKLSALH-PRYS--------RAQYDRVMDELYPRLKSLTLLARSYDIGINIDAEEA------DRleISLDLLEKLCFEP 391
Cdd:PLN02681 187 SFPLFADSsPLYHatsepeplTAEEERLLELAHERLQKLCERAAQLGVPLLIDAEYTslqpaiDY--ITYDLAREFNKGK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 392 ELAgwngIGFV-IQAYQKRCPfviDYLVDLAGRSRRR---LMIRLVKGAYWDSEIKRAQMDGLEGyPVYTRKVYTDVSYL 467
Cdd:PLN02681 265 DRP----IVYGtYQAYLKDAR---ERLRLDLERSEREgvpLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYN 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 689260967 468 ACAKKLL--AAPNLIYPQFATHNAHTL-AAIYQLAGQNYYPG--QYEFQCLHGMGEPLydqvvgkvSDGKLNRPCRI--Y 540
Cdd:PLN02681 337 RCAEFLLekASNGDGEVMLATHNVESGeLAAAKMNELGLHKGdpRVQFAQLLGMSDNL--------SFGLGNAGFRVskY 408
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 689260967 541 APVGTHETLLAYLVRRLLENGANTSfvNRIADTSLPLDELVADPVCAV 588
Cdd:PLN02681 409 LPYGPVEEVIPYLLRRAEENRGLLS--GSAIDRQLLRKELKRRLKAAV 454
|
|
| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
1-45 |
3.71e-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: 3.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 689260967 1 MGTTTmgVKLDDATRERIKSAATRIDRTPHWLIKQAIFNYLEKLE 45
Cdd:COG4710 1 MKMLS--IRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
|
|
| |
