|
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: 2864.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1 MGTTTMGVKLDDATRERIKMAASRIDRTPHWLIKQAIFSYLDKLENSDTLPELPALFAGAANESEEPVAPQDEPHQPFLE 80
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADTPAEEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 81 FAEQILPQSVSRAAITAAWRRPETDAVSMLMEQARLSPPVAEQAHKLAYQLAEKLRNQKSASGRAGMVQGLLQEFSLSSQ 160
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGRAGMVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEANLSRSLNRIIGKSG 240
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 241 EPLIRKGVDMAMRLMGEQFVTGETIAQALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGI 320
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGLNIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 401 FVIQAYQKRCPLVIDYLVELASRSRRRLMIRLVKGAYWDSEIKRAQMEGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLI 480
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 561 GANTSFVNRIADATLPLDELVADPVEAVEKLAQQEGQAGIPHPKIPLPRDLYGEGRINSAGLDLANEHRLASLSSALLSN 640
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLAS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 641 AMQKWQAKPVLEQPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQ 720
Cdd:PRK11809 641 AHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQ 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 721 MQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:PRK11809 721 MQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 801 AKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAQGRPIPL 880
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 881 IAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVI 960
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 961 DSEAKANIERHIQTMRAKGRPVFQAARENSDDaqeWQTGTFVMPTLIELENFAELEKEVFGPVLHVVRYNRNQLAELIEQ 1040
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSED---WQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQ 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLAHRPPNALNT 1120
Cdd:PRK11809 1038 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAV 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1121 TLTRQDARYPVDAQLKTTLLAPLTALTQWAADR-PALQTLCRQFADLAQAGTQRLLPGPTGERNTWTLLPRERVLCLADD 1199
Cdd:PRK11809 1118 TLARQDAEYPVDAQLRAALLAPLTALREWAAERePELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADT 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1200 EQDALTQLAAVLAVGSQALWSDDAFHRDLAKRLPAAVAARVQFAKAETLMAQPFDAVIFHGDSDKLRTVCEAVAAREGAI 1279
Cdd:PRK11809 1198 EQDALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPI 1277
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|.
gi 555258718 1280 VSVQGFARGESNMLLERLYIERSLSVNTAAAGGNASLMTIG 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: 2020.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 77 PFLEFAEQILPQSVSRAAITAAWRRPETDAVSMLMEQARLSPPVAEQAHKLAYQLAEKLRnqksASGRAGMVQGLLQEFS 156
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALR----AKRKGTGVEALLQEYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 157 LSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEANLSRSLNRII 236
Cdd:PRK11905 77 LSSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAQALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASN 316
Cdd:PRK11905 157 ARLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 317 GRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGLNIDAEEADRLEISLDLLEKLCFEPELAGW 396
Cdd:PRK11905 237 GRGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 397 NGIGFVIQAYQKRCPLVIDYLVELASRSRRRLMIRLVKGAYWDSEIKRAQMEGLEGYPVYTRKVYTDVSYLACAKKLLAV 476
Cdd:PRK11905 317 NGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 477 PNLIYPQFATHNAHTLAAIYHLAGQNYypgQYEFQCLHGMGEPLYEQVTGKvadGKLNRPCRIYAPVGTHETLLAYLVRR 556
Cdd:PRK11905 397 RDVIYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGK---EKLGRPCRIYAPVGTHETLLAYLVRR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 557 LLENGANTSFVNRIADATLPLDELVADPVEAVEKLAQQegqagiPHPKIPLPRDLYGEGRINSAGLDLANEHRLASLSSA 636
Cdd:PRK11905 471 LLENGANSSFVNRIVDENVPVEELIADPVEKVAAMGVA------PHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 637 LLSNAMQKWQAKPVLEQPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVL 716
Cdd:PRK11905 545 LNAFAAKTWHAAPLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADL 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 717 MEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAG 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 797 NSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqGR 876
Cdd:PRK11905 705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GP 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 877 PIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:PRK11905 782 PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDV 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 957 GPVIDSEAKANIERHIQTMRAKGRPVFQAARensddAQEWQTGTFVMPTLIELENFAELEKEVFGPVLHVVRYNRNQLAE 1036
Cdd:PRK11905 862 GPVIDAEAQANIEAHIEAMRAAGRLVHQLPL-----PAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDR 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1037 LIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLAHRPpn 1116
Cdd:PRK11905 937 VIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVREAP-- 1014
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1117 alnttltRQDARYPVDAQLKTTLLAPLTALTQWAADrpALQTLCRQFADLAQAGTQRLLPGPTGERNTWTLLPRERVLCL 1196
Cdd:PRK11905 1015 -------TPIPPAHESVDTDAAARDFLAWLDKEGKA--ALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCV 1085
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1197 ADDEQDALTQLAAVLAVGSQALWSDDAFHRDLAKRLPAAVAARVQFAKaETLMAQPFDAVIFHGDSDKLRTVCEAVAARE 1276
Cdd:PRK11905 1086 ADTEEALLRQLAAALATGNVAVVAADSGLAAALADLPGLVAARIDWTQ-DWEADDPFAGALLEGDAERARAVRQALAARP 1164
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 555258718 1277 GAIVSVQGfARGESNMLLERLYIERSLSVNTAAAGGNASLMTIG 1320
Cdd:PRK11905 1165 GAIVPLIA-AEPTDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
77-1317 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1554.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 77 PFLEFAEQILPQSVSRAAITAAWRRPETDAVSMLMEQARLSPPVAEQAHklayqlAEKLRNQKSASGRAGMVQGLLQEFS 156
Cdd:COG4230 2 PFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAA------AAALAARERVRARRGGGGGLLLLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 157 LSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEA--NLSRSLNR 234
Cdd:COG4230 76 LSSLSSEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESslSLASGLLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 235 IIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAQALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKA 314
Cdd:COG4230 156 LLGRLGRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 315 SNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGLNIDAEEADRLEISLDLLEKLCFEPELA 394
Cdd:COG4230 236 AGGGSGGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 395 GWNGIGFVIQAYQKRCPLVIDYLVELASRSRRRLMIRLVKGAYWDSEIKRAQmeGLEGYPVYTRKVYTDVSYLACAKKLL 474
Cdd:COG4230 316 GGLGGGGGVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREI--QRAQVLGYVVYPVTTRKVLYDAAALA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 475 AVPNLIYPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVTgkVADGKLNRPCRIYAPVGTHETLLAYLV 554
Cdd:COG4230 394 LALLLLAAQPAFAPQFATHAAATAAAAAAAGGGGEFEFQCLHGMGEYLYDQ--VGRGKLGRPCRIYAPVGSHEDLLAYLV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 555 RRLLENGANTSFVNRIADATLPLDELVADPVEAVEKLaqqegqAGIPHPKIPLPRDLYGEGRINSAGLDLANEHRLASLS 634
Cdd:COG4230 472 RRLLENGANSSFVNRIADEDVPVEELIADPVEKARAL------GGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 635 SALLSNAMQKWQAKPVLEQPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAA 714
Cdd:COG4230 546 AALAAAAEKQWQAAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAA 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 715 VLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAAL 793
Cdd:COG4230 626 DLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvLRGRGVFVCISPWNFPLAIFTGQVAAAL 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 794 AAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRlda 873
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR--- 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 874 QGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLT 953
Cdd:COG4230 783 DGPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLS 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 954 TDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARensddAQEWQTGTFVMPTLIELENFAELEKEVFGPVLHVVRYNRNQ 1033
Cdd:COG4230 863 TDVGPVIDAEARANLEAHIERMRAEGRLVHQLPL-----PEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADE 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1034 LAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLAHR 1113
Cdd:COG4230 938 LDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATER 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1114 PPnALNTTLTRQDarypvdaqlkttllAPLTALTQWAADRPALQTlcrqfadlaqagtqrlLPGPTGERNTWTLLPRERV 1193
Cdd:COG4230 1018 TV-TVNTTAAGGN--------------ASLLALGDWLASLLGALT----------------LPGPTGERNTLTLRPRGRV 1066
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1194 LCLADDEQDALTQLAAVLAVGSQALWSDDAfhrdLAKRLPAAVaarvqfakaetlmAQPFDAVIFHGDsdkLRTVCEAVA 1273
Cdd:COG4230 1067 LCLADSLEALLAQLAAALATGNRAVVAADL----ALAGLPAVL-------------LPPFDAVLFEGR---LRALRQALA 1126
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 555258718 1274 AREGAIVSVQGFArgesnMLLERLYIErslsvntaaAGGNASLM 1317
Cdd:COG4230 1127 ARDGAIVPVIDAG-----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: 1545.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 79 LEFAEQILPQSVSRAAITAAWRRPETDAVSMLMEQARLSPPVAEQAHKLAYQLAEKLRNQKsasGRAGMVQGLLQEFSLS 158
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKK---KKLGGIDAFLQEYSLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 159 SQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEA--NLSRSLNRII 236
Cdd:PRK11904 78 TEEGIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKLDKKAdgTPSGVLKRLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAQALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASN 316
Cdd:PRK11904 158 NRLGEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 317 GRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGLNIDAEEADRLEISLDLLEKLCFEPELAGW 396
Cdd:PRK11904 238 GADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 397 NGIGFVIQAYQKRCPLVIDYLVELASRSRRRLMIRLVKGAYWDSEIKRAQMEGLEGYPVYTRKVYTDVSYLACAKKLLAV 476
Cdd:PRK11904 318 GGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 477 PNLIYPQFATHNAHTLAAIYHLAGQnyypGQYEFQCLHGMGEPLYEQVTgkvadGKLNRPCRIYAPVGTHETLLAYLVRR 556
Cdd:PRK11904 398 RGAIYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 557 LLENGANTSFVNRIADATLPLDELVADPVEAVEKLAQqegqagIPHPKIPLPRDLYGEGRINSAGLDLANEHRLASLSSA 636
Cdd:PRK11904 469 LLENGANSSFVHRLVDPDVPIEELVADPVEKLRSFET------LPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 637 LLSNAMQKWQAKPVleqPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVL 716
Cdd:PRK11904 543 IAAFLEKQWQAGPI---INGEGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 717 MEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPlGPV--------------VCISPWNFPL 782
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLP-GPTgesnelrlhgrgvfVCISPWNFPL 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 783 AIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATL 862
Cdd:PRK11904 699 AIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARI 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 863 LQRNIATRldaQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMA 942
Cdd:PRK11904 779 INRTLAAR---DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMA 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 943 ECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARenSDDAQEwqtGTFVMPTLIELENFAELEKEVFGP 1022
Cdd:PRK11904 856 ELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPL--PAGTEN---GHFVAPTAFEIDSISQLEREVFGP 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1023 VLHVVRYNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGG 1102
Cdd:PRK11904 931 ILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGG 1010
|
1050
....*....|.
gi 555258718 1103 PLYLYRLLAHR 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: 806.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 610 DLYGEGRINSAGLDLANEHRLASLSSALLSNAMQKWQAKPVL-EQPVADGEMTPVINPAEPKDIVGWGREATESEVEQAL 688
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIgHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 689 QNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRP 768
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 769 LGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRV 848
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 849 RGVMFTGSTEVATLLQRNIATRLDAqgrPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDD 928
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDA---PVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 929 IAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSddaQEWQTGTFVMPTLIE 1008
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDS---RACQHGTFVAPTLFE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1009 LENFAELEKEVFGPVLHVVRYNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPF 1088
Cdd:TIGR01238 395 LDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPF 474
|
490 500
....*....|....*....|....*.
gi 555258718 1089 GGEGLSGTGPKAGGPLYLYRLLAHRP 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: 681.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 114 ARLSPPVAEQAHKLAYQLAEKLRNQksasgRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISngn 193
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAA-----PEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 194 wqshigRSPSLFVNAATWGLLFTgrlvsthneanlsrslnrIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAQALANAR 273
Cdd:COG0506 75 ------KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 274 KLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASngrgiYEGPGISIKLSALHPRYSRAQYDRVMEELYPRL 353
Cdd:COG0506 131 KLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 354 KSLTLLARQYDIGLNIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLVELASRSRRRLMIRLV 433
Cdd:COG0506 206 RPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 434 KGAYWDSEIKRAQMEGLeGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYHLAGQ-NYYPGQYEFQC 512
Cdd:COG0506 286 KGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 513 LHGMGEPLYEQVTgKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADATLPLDELVADPVEAVEKla 592
Cdd:COG0506 365 LYGMGEDLQRALA-AVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAAL-- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 593 qqegQAGIPHPKIPLPRDLYGEGRINSAGLDLANEHRLASLSSALLSNAMQKWQAKPVLEQPVADGEMTPVINPAEPKDI 672
Cdd:COG0506 442 ----AAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGAAAAAAAAAVAVVPAAAAAVV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 673 VGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHY 752
Cdd:COG0506 518 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAA 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 753 YAGQVRDDFDNETHRP--------LGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVP 824
Cdd:COG0506 598 AAAAAARAAAPPPPPPgglvallpLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLL 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 825 PGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVD 904
Cdd:COG0506 678 GGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVA 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 905 VLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQ 984
Cdd:COG0506 758 ASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLP 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 985 AAREnsddAQEWQTGTFVMPTLIELENFAELEKEVFGPVLHVVRYNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVT 1064
Cdd:COG0506 838 GGGP----LVPGLLTAPLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGR 913
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*....
gi 555258718 1065 GSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLAHRPPNALNTTLT 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: 670.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 643 QKWQAKPVL-EQPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQM 721
Cdd:cd07125 29 KEWEAIPIInGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 722 QQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFD-----------NETH-RPLGPVVCISPWNFPLAIFTGQI 789
Cdd:cd07125 109 GELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFVCISPWNFPLAIFTGQI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 790 AAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIAT 869
Cdd:cd07125 189 AAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 870 RldaQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNP 949
Cdd:cd07125 269 R---DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 950 GRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDdaqewqtGTFVMPTLIELENFAELEKEVFGPVLHVVRY 1029
Cdd:cd07125 346 WDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGN-------GYFVAPGIIEIVGIFDLTTEVFGPILHVIRF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1030 NRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRL 1109
Cdd:cd07125 419 KAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRF 498
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
643-1110 |
2.00e-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: 463.97 E-value: 2.00e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 643 QKWQAKP-VLEQPVAD-GEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQ 720
Cdd:cd07083 14 EFGRAYPlVIGGEWVDtKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 721 MQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRD------------DFDNET-HRPLGPVVCISPWNFPLAIFTG 787
Cdd:cd07083 94 RRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRlrypavevvpypGEDNESfYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 788 QIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNI 867
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 868 ATRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMG 947
Cdd:cd07083 254 ARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 948 NPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDdaqewqtGTFVMPTLIELENFAE--LEKEVFGPVLH 1025
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGE-------GYFVAPTVVEEVPPKAriAQEEIFGPVLS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1026 VVRYNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLY 1105
Cdd:cd07083 407 VIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHY 486
|
....*
gi 555258718 1106 LYRLL 1110
Cdd:cd07083 487 LRRFL 491
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
268-569 |
9.24e-147 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 446.17 E-value: 9.24e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 268 ALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVME 347
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 348 ELYPRLKSLTLLARQYDIGLNIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLVELASRSRRR 427
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 428 LMIRLVKGAYWDSEIKRAQmEGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYHLAGQ-NYYPG 506
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQ-QGGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555258718 507 QYEFQCLHGMGEPLYEQVtgkVADGklnRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNR 569
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFAL---VAAG---YRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
653-1107 |
6.90e-129 |
|
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: 406.99 E-value: 6.90e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREA 732
Cdd:cd07124 40 KEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 733 GKTFSNAIAEVREAVDFLHYYAGQV----------RDDFDNETH-RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07124 120 GKNWAEADADVAEAIDFLEYYAREMlrlrgfpvemVPGEDNRYVyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 802 KPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAQGRPIPLI 881
Cdd:cd07124 200 KPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 882 AETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVID 961
Cdd:cd07124 280 AEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVID 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 962 SEAKANIERHIQTMRAKGRPVFqaARENSDDAQEwqtGTFVMPTLIE-LENFAELEK-EVFGPVLHVVRYnrNQLAELIE 1039
Cdd:cd07124 360 KGARDRIRRYIEIGKSEGRLLL--GGEVLELAAE---GYFVQPTIFAdVPPDHRLAQeEIFGPVLAVIKA--KDFDEALE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1107
Cdd:cd07124 433 IANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLL 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
656-1102 |
1.81e-119 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 380.63 E-value: 1.81e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:COG1012 18 ASGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIAEVREAVDFLHYYAGQVR-----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:COG1012 97 LAEARGEVDRAADFLRYYAGEARrlygetipsdaPGTRAYVRRePLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 804 AEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAE 883
Cdd:COG1012 177 AEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVTLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 884 TGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSE 963
Cdd:COG1012 251 LGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 964 AKANIERHIQTMRAKG-RPVFQAARENSDDaqewqtGTFVMPTLIE-LENFAEL-EKEVFGPVLHVVRYNRnqLAELIEQ 1040
Cdd:COG1012 331 QLERVLAYIEDAVAEGaELLTGGRRPDGEG------GYFVEPTVLAdVTPDMRIaREEIFGPVLSVIPFDD--EEEAIAL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1102
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
656-1106 |
1.74e-116 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 371.86 E-value: 1.74e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAePKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:pfam00171 4 SESETIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIAEVREAVDFLHYYAGQVR----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:pfam00171 83 LAEARGEVDRAIDVLRYYAGLARrldgetlpsdPGRLAYTRRePLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 805 EQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAET 884
Cdd:pfam00171 163 ELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 885 GGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEA 964
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 965 KANIERHIQTMRAKGRPVFQAARENSDDaqewqtGTFVMPTLIE-LENFAELEK-EVFGPVLHVVRYnrNQLAELIEQIN 1042
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGGEAGLDN------GYFVEPTVLAnVTPDMRIAQeEIFGPVLSVIRF--KDEEEAIEIAN 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555258718 1043 ASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGpKAGGPLYL 1106
Cdd:pfam00171 389 DTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGL 450
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
663-1107 |
1.22e-107 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 350.00 E-value: 1.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAE 742
Cdd:PRK03137 54 SINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 743 VREAVDFLHYYAGQV-----------RDDFDNETH-RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLI 810
Cdd:PRK03137 134 TAEAIDFLEYYARQMlkladgkpvesRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 811 AAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAQGRPIPLIAETGGMNAM 890
Cdd:PRK03137 214 AAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 891 IVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRlTTDIGPVIDSEAKANIER 970
Cdd:PRK03137 294 VVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 971 HIQTMRAKGRPVFQAARENSddaqewqTGTFVMPTLI-ELENFAEL-EKEVFGPVLHVVRYnrNQLAELIEQINASGYGL 1048
Cdd:PRK03137 373 YIEIGKEEGRLVLGGEGDDS-------KGYFIQPTIFaDVDPKARImQEEIFGPVVAFIKA--KDFDHALEIANNTEYGL 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 555258718 1049 TLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1107
Cdd:PRK03137 444 TGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
654-1106 |
7.63e-107 |
|
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: 347.62 E-value: 7.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 654 PVADGEMTPV------INPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGL 727
Cdd:TIGR01237 35 LVINGERVETenkivsINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 728 LVREAGKTFSNAIAEVREAVDFLHYYA--------GQVRDDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAA 795
Cdd:TIGR01237 115 LVKEVGKPWNEADAEVAEAIDFMEYYArqmielakGKPVNSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 796 GNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAQG 875
Cdd:TIGR01237 195 GNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 876 RPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTD 955
Cdd:TIGR01237 275 HLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVY 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 956 IGPVIDSEAKANIERHIQTMRAKGRPVFQAArenSDDAQewqtGTFVMPTLI-ELENFAEL-EKEVFGPVLHVVRYNRNQ 1033
Cdd:TIGR01237 355 VGPVIDQKSFNKIMEYIEIGKAEGRLVSGGC---GDDSK----GYFIGPTIFaDVDRKARLaQEEIFGPVVAFIRASDFD 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555258718 1034 laELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1106
Cdd:TIGR01237 428 --EALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYL 498
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
685-1108 |
2.41e-105 |
|
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: 340.72 E-value: 2.41e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 685 EQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRD----- 759
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRlhgev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 760 ------DFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLP 832
Cdd:cd07078 81 ipspdpGELAIVrREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 833 GRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNiatrldAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDS 912
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRA------AAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 913 AGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGrpvfqAARENSDD 992
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEG-----AKLLCGGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 993 AQEWQTGTFVMPTLIE-LENFAEL-EKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVG 1070
Cdd:cd07078 310 RLEGGKGYFVPPTVLTdVDPDMPIaQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAG 387
|
410 420 430
....*....|....*....|....*....|....*...
gi 555258718 1071 NLYVNRNMVGAVVGvQPFGGEGLSGTGpKAGGPLYLYR 1108
Cdd:cd07078 388 TVWINDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEE 423
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
655-1103 |
4.55e-86 |
|
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: 288.76 E-value: 4.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 655 VADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGK 734
Cdd:cd07097 10 VAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 735 TFSNAIAEVREAVDFLHYYAGQ-----------VRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07097 90 TLPEARGEVTRAGQIFRYYAGEalrlsgetlpsTRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 803 PAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIATRLDAQGRPIPLia 882
Cdd:cd07097 170 PAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVG----RRIAAAAAARGARVQL-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 883 ETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDS 962
Cdd:cd07097 244 EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 963 EAKANIERHIQTMRAKG-RPVFQAARENSDDaqewqTGTFVMPTLIE-LENFAELEK-EVFGPVLHVVRYnrNQLAELIE 1039
Cdd:cd07097 324 RQLEKDLRYIEIARSEGaKLVYGGERLKRPD-----EGYYLAPALFAgVTNDMRIAReEIFGPVAAVIRV--RDYDEALA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555258718 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1103
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
698-1110 |
1.18e-82 |
|
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: 275.65 E-value: 1.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 698 WFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRD-----------DFDNET- 765
Cdd:cd06534 10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKlggpelpspdpGGEAYVr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTAD 845
Cdd:cd06534 90 REPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLSH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 846 TRVRGVMFTGSTEVATLLQRNiatrldAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCL 925
Cdd:cd06534 170 PRVDKISFTGSTAVGKAIMKA------AAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 926 QDDIAEhtlkmlrgamaecrmgnpgrlttdigpvidseakanierhiqTMRAKGRPVFQAARENSDDAQEwqtgtfvmpt 1005
Cdd:cd06534 244 HESIYD------------------------------------------EFVEKLVTVLVDVDPDMPIAQE---------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1006 lielenfaelekEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGv 1085
Cdd:cd06534 272 ------------EIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE- 336
|
410 420
....*....|....*....|....*
gi 555258718 1086 QPFGGEGLSGTGpKAGGPLYLYRLL 1110
Cdd:cd06534 337 APFGGVKNSGIG-REGGPYGLEEYT 360
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
654-1103 |
1.33e-82 |
|
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: 279.23 E-value: 1.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 654 PVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAG 733
Cdd:cd07131 9 DSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 734 KTFSNAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07131 89 KPLAEGRGDVQEAIDMAQYAAGEGRrlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 802 KPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRldaqGRPIPLi 881
Cdd:cd07131 169 KPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP----NKRVAL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 882 aETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVID 961
Cdd:cd07131 244 -EMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLIN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 962 SEAKANIERHIQTMRAKGRPVFQAARENSDDaqEWQTGTFVMPTLIELEN--FAELEKEVFGPVLHVVRYnrNQLAELIE 1039
Cdd:cd07131 323 EAQLEKVLNYNEIGKEEGATLLLGGERLTGG--GYEKGYFVEPTVFTDVTpdMRIAQEEIFGPVVALIEV--SSLEEAIE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555258718 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1103
Cdd:cd07131 399 IANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
656-1101 |
2.30e-82 |
|
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: 278.68 E-value: 2.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEPKDIVGWgREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:cd07086 10 SGGETFTSRNPANGEPIARV-FPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07086 89 LPEGLGEVQEMIDICDYAVGLSRmlygltipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 804 AEQTSLIAAQGIAILLEA----GVPPGVVQLLPGRGEtVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqGRPIp 879
Cdd:cd07086 169 SETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRVL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 880 liAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPV 959
Cdd:cd07086 244 --LELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 960 IDSEAKANIERHIQTMRAKGRPV-FQAARENSDDAqewqtGTFVMPTLIELEN--FAELEKEVFGPVLHVVRYnrNQLAE 1036
Cdd:cd07086 322 INQAAVEKYLNAIEIAKSQGGTVlTGGKRIDGGEP-----GNYVEPTIVTGVTddARIVQEETFAPILYVIKF--DSLEE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1037 LIEQINASGYGLTLGVHT---RIDETIAQVTGSaHVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAG 1101
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTedlREAFRWLGPKGS-DCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
663-1097 |
1.18e-79 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 270.07 E-value: 1.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAePKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAE 742
Cdd:cd07103 1 VINPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 743 VREAVDFLHYYAGQVR--------DDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLI 810
Cdd:cd07103 80 VDYAASFLEWFAEEARriygrtipSPAPGKrilvIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 811 AAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGmNA- 889
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGG-NAp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 890 MIVDSSALTEQVVVDVLASAFDSAGQRC-SALRVLClQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANI 968
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 969 ERHIQTMRAKG-RPVFQAARENSDdaqewqtGTFVMPTLI-----ELENFAElekEVFGPVLHVVRYnrNQLAELIEQIN 1042
Cdd:cd07103 312 EALVEDAVAKGaKVLTGGKRLGLG-------GYFYEPTVLtdvtdDMLIMNE---ETFGPVAPIIPF--DTEDEVIARAN 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 555258718 1043 ASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:cd07103 380 DTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
653-1108 |
1.74e-76 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 263.29 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVADGEMTPVINPAEPKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQM-QQLIGLLVRE 731
Cdd:cd07123 40 KEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYELNAATMLG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 732 AGKTFSNA-IAEVREAVDFLH---YYAGQVRDD---------FDNETHRPL-GPVVCISPWNFPlAIfTGQIAAALA-AG 796
Cdd:cd07123 120 QGKNVWQAeIDAACELIDFLRfnvKYAEELYAQqplsspagvWNRLEYRPLeGFVYAVSPFNFT-AI-GGNLAGAPAlMG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 797 NSVLAKPAEqTSLIAAQGI-AILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAQg 875
Cdd:cd07123 198 NVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRY- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 876 RPIP-LIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSAL-RV---LCLQDDIAEHTLKMLrgamAECRMGNPG 950
Cdd:cd07123 276 RTYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAAsRAyvpESLWPEVKERLLEEL----KEIKMGDPD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 951 RLTTDIGPVIDSEAKANIERHIQtmRAKGRPVFQ-AARENSDDAqewqTGTFVMPTLIELEN--FAELEKEVFGPVLHVV 1027
Cdd:cd07123 352 DFSNFMGAVIDEKAFDRIKGYID--HAKSDPEAEiIAGGKCDDS----VGYFVEPTVIETTDpkHKLMTEEIFGPVLTVY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1028 RYNRNQLAELIEQIN-ASGYGLTLGVHTRiDETIAQVTGSAH---VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGP 1103
Cdd:cd07123 426 VYPDSDFEETLELVDtTSPYALTGAIFAQ-DRKAIREATDALrnaAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSP 504
|
....*
gi 555258718 1104 LYLYR 1108
Cdd:cd07123 505 LNLLR 509
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
663-1101 |
2.00e-73 |
|
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: 252.47 E-value: 2.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPA--EPkdivgWGR--EATESEVEQALQNAvNQA---PVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:cd07114 1 SINPAtgEP-----WARvpEASAADVDRAVAAA-RAAfegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIAEVREAVDFLHYYAG-----------QVRDDFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07114 75 IRETRAQVRYLAEWYRYYAGladkiegavipVDKGDYLNFTrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 804 AEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAE 883
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 884 TGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSE 963
Cdd:cd07114 229 LGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 964 AKANIERHIQTMRAKG-RPVFQAARENSDDaqeWQTGTFVMPTLIE-LENFAEL-EKEVFGPVLHVVRYNRNqlAELIEQ 1040
Cdd:cd07114 309 QLEKVERYVARAREEGaRVLTGGERPSGAD---LGAGYFFEPTILAdVTNDMRIaQEEVFGPVLSVIPFDDE--EEAIAL 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1041 INASGYGLTLGVHTRiDETIA-QVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07114 384 ANDSEYGLAAGIWTR-DLARAhRVARAIEAGTVWV--NTYRALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
662-1097 |
1.04e-71 |
|
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: 247.65 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 662 PVINPAEPKdIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIA 741
Cdd:cd07145 2 EVRNPANGE-VIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 742 EVREAVDFLHYYAGQVR---------DDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07145 81 EVERTIRLFKLAAEEAKvlrgetipvDAYEYNERRiaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 806 QTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLlqrnIATRLDAQGRPIplIAETG 885
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLL----IASKAGGTGKKV--ALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 886 GMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAK 965
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 966 ANIERHIQTMRAKGRPVFQAAREnsddaqewQTGTFVMPTLIELENF--AELEKEVFGPVLHVVRYNRNQlaELIEQINA 1043
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKR--------DEGSFFPPTVLENDTPdmIVMKEEVFGPVLPIAKVKDDE--EAVEIANS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555258718 1044 SGYGLTLGVHTRiDETIAqvtgsahvgnLYVNRNM-VGAVV---------GVQPFGGEGLSGTG 1097
Cdd:cd07145 385 TEYGLQASVFTN-DINRA----------LKVARELeAGGVVindstrfrwDNLPFGGFKKSGIG 437
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
657-1097 |
3.72e-71 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 246.33 E-value: 3.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 657 DGEMTPVINPAEPKdIVGWGREATESEVEQALQNAVNQAPVWFAT-PPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:cd07082 14 SGKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIAEVREAVDFLHYYAGQVRD------DFDNETHR----------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07082 93 LKDALKEVDRTIDYIRDTIEELKRldgdslPGDWFPGTkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 800 LAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRniatrldaQGRPIP 879
Cdd:cd07082 173 VFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK--------QHPMKR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 880 LIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPV 959
Cdd:cd07082 245 LVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 960 IDSEAKANIERHIQTMRAKG-RPVFQAAREnsddaqewqTGTFVMPTLIELENfAELE---KEVFGPVLHVVRYnrNQLA 1035
Cdd:cd07082 325 IDPKSADFVEGLIDDAVAKGaTVLNGGGRE---------GGNLIYPTLLDPVT-PDMRlawEEPFGPVLPIIRV--NDIE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1036 ELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRnMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07082 393 EAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-KCQRGPDHFPFLGRKDSGIG 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
678-1097 |
2.86e-69 |
|
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: 240.54 E-value: 2.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 678 EATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIA-EVREAVDFLHYYAG- 755
Cdd:cd07093 15 EGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFADy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 756 ---------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPP 825
Cdd:cd07093 95 ilqldgesyPQDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 826 GVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDV 905
Cdd:cd07093 175 GVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPNIVFADADLDRAVDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 906 LASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVfqA 985
Cdd:cd07093 249 VRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEGATI--L 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 986 ARENSDDAQEWQTGTFVMPTLIE-LENFAELEK-EVFGPVLHVVRYNRNqlAELIEQINASGYGLTLGVHTRiDETIAQV 1063
Cdd:cd07093 327 TGGGRPELPDLEGGYFVEPTVITgLDNDSRVAQeEIFGPVVTVIPFDDE--EEAIELANDTPYGLAAYVWTR-DLGRAHR 403
|
410 420 430
....*....|....*....|....*....|....*
gi 555258718 1064 TGSA-HVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:cd07093 404 VARRlEAGTVWVNCWLVRDL--RTPFGGVKASGIG 436
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
683-1103 |
4.55e-69 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 238.97 E-value: 4.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 683 EVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVR---- 758
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRrpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 759 ----DDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIA-ILLEAGVPPGVVQ 829
Cdd:cd07104 81 eilpSDVPGKESMvrrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAeIFEEAGLPKGVLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 830 LLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIATrldAQGRPIPLIA-ETGGMNAMIVDSSALTEQVVVDVLAS 908
Cdd:cd07104 161 VVPGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIGE---LAGRHLKKVAlELGGNNPLIVLDDADLDLAVSAAAFG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 909 AFDSAGQRC-SALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGrpvfqaAR 987
Cdd:cd07104 234 AFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAG------AR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 988 ENsddAQEWQTGTFVMPTLI-----ELENFAElekEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQ 1062
Cdd:cd07104 307 LL---TGGTYEGLFYQPTVLsdvtpDMPIFRE---EIFGPVAPVIPF--DDDEEAVELANDTEYGLSAAVFTRDLERAMA 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 555258718 1063 VTGSAHVGNLYVNRNMV--GAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07104 379 FAERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
661-1097 |
6.87e-69 |
|
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: 239.42 E-value: 6.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 661 TPVINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAI 740
Cdd:cd07149 1 IEVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 741 AEVREAVDFLHYYA-------GQV---------RDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07149 80 KEVDRAIETLRLSAeeakrlaGETipfdaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 805 EQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRldaqgrpiPLIAET 884
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--------KVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 885 GGMNAMIVDSSALTEQVVVDVLASAFDSAGQRC-SALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSE 963
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 964 AKANIERHIQTMRAKG-RPVFQAAREnsddaqewqtGTFVMPTLieLENFAELEK----EVFGPVLHVVRYNRnqLAELI 1038
Cdd:cd07149 311 EAERIEEWVEEAVEGGaRLLTGGKRD----------GAILEPTV--LTDVPPDMKvvceEVFAPVVSLNPFDT--LDEAI 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555258718 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1097
Cdd:cd07149 377 AMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdsstfR------VDHMPYGGVKESGTG 434
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
679-1103 |
3.08e-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: 237.23 E-value: 3.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 679 ATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVR 758
Cdd:cd07150 18 GSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 759 ------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPG 826
Cdd:cd07150 98 rvrgetlpsdspGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 827 VVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIATRLDAQGRPIPLiaETGGMNAMIVDSSALTEQVVVDVL 906
Cdd:cd07150 178 VFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRHLKKITL--ELGGKNPLIVLADADLDYAVRAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 907 ASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAA 986
Cdd:cd07150 252 FGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVAKGAKLLTGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 987 RENsddaqewqtGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYNRNQlaELIEQINASGYGLTLGVHTR-IDETIAQV 1063
Cdd:cd07150 332 KYD---------GNFYQPTVLTdvTPDMRIFREETFGPVTSVIPAKDAE--EALELANDTEYGLSAAILTNdLQRAFKLA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 555258718 1064 ----TGSAHVGNLYVNRNmvgAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07150 401 erleSGMVHINDPTILDE---AHV---PFGGVKASGFG-REGGE 437
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
683-1095 |
2.20e-67 |
|
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: 234.09 E-value: 2.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 683 EVEQALQNAVNQAPVWFATPPQERAAILQRAAVLME---DQMQQLIGllvREAGKTFSNAIAEVRE-------AVDFLHY 752
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKankEELARLIS---RETGKPLWEAQTEVAAmagkidiSIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 753 YAGQVRDDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVV 828
Cdd:cd07095 78 RTGERATPMAQGravlRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 829 QLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLQRNIAtrldaqGRPIPLIA-ETGGMNAMIVDSSALTEQVVVDVLA 907
Cdd:cd07095 158 NLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 908 SAFDSAGQRCS-ALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKG-RPVFQA 985
Cdd:cd07095 231 SAFLTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGgEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 986 ARENSDDAqewqtgtFVMPTLIELENFAEL-EKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVT 1064
Cdd:cd07095 311 ERLVAGTA-------FLSPGIIDVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFL 381
|
410 420 430
....*....|....*....|....*....|.
gi 555258718 1065 GSAHVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:cd07095 382 ARIRAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
657-1097 |
1.38e-66 |
|
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: 233.56 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 657 DGEMTPVINPAePKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTF 736
Cdd:cd07085 14 TTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 737 SNAIAEVR---EAVDF--------LHYYAGQVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07085 93 ADARGDVLrglEVVEFacsiphllKGEYLENVARGIDTYSYRqPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 805 EQTSLiAAQGIAILL-EAGVPPGVVQLLPGRGETVGAQLTaDTRVRGVMFTGSTEVATLLQRNIAT---RLDAQGrpipl 880
Cdd:cd07085 173 ERVPG-AAMRLAELLqEAGLPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAAngkRVQALG----- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 881 iaetGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVI 960
Cdd:cd07085 246 ----GAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 961 DSEAKANIERHIQTMRAKGRPVFQAARENSddAQEWQTGTFVMPTLI-----ELENFAElekEVFGPVLHVVRYnrNQLA 1035
Cdd:cd07085 322 SPAAKERIEGLIESGVEEGAKLVLDGRGVK--VPGYENGNFVGPTILdnvtpDMKIYKE---EIFGPVLSIVRV--DTLD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555258718 1036 ELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmVGAVVGVQ--PFGGEGLSGTG 1097
Cdd:cd07085 395 EAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLAffSFGGWKGSFFG 455
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
654-1076 |
1.45e-66 |
|
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: 232.93 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 654 PVADGEMTPVINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAG 733
Cdd:cd07088 8 PSSSGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 734 KTFSNAIAEVREAVDFLHYYAGQVR--------DDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:cd07088 87 KTLSLARVEVEFTADYIDYMAEWARriegeiipSDRPNENififKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 802 KPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLI 881
Cdd:cd07088 167 KPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 882 AETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVID 961
Cdd:cd07088 241 LELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 962 SEAKANIERHIQTMRAKG-RPVFQAARENSDDaqewqtGTFVMPTLI-----ELENFAElekEVFGPVLHVVRYnrNQLA 1035
Cdd:cd07088 321 EAALDKVEEMVERAVEAGaTLLTGGKRPEGEK------GYFYEPTVLtnvrqDMEIVQE---EIFGPVLPVVKF--SSLD 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 555258718 1036 ELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR 1076
Cdd:cd07088 390 EAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
663-1097 |
1.80e-66 |
|
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: 232.51 E-value: 1.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEPKDIVGWGReATESEVEQALQNAVN-QAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIA 741
Cdd:cd07109 1 VFDPSTGEVFARIAR-GGAADVDRAVQAARRaFESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 742 EVREAVDFLHYYAGQVR----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLI 810
Cdd:cd07109 80 DVEAAARYFEYYGGAADklhgetiplgPGYFVYTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 811 AAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAM 890
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 891 IVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGnPGRLTTDIGPVIDSEAKANIER 970
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 971 HIQTMRAKGRPVFQAARENSDDAQEwqtGTFVMPTLI-ELENFAEL-EKEVFGPVLHVVRYnrNQLAELIEQINASGYGL 1048
Cdd:cd07109 313 FVARARARGARIVAGGRIAEGAPAG---GYFVAPTLLdDVPPDSRLaQEEIFGPVLAVMPF--DDEAEAIALANGTDYGL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 555258718 1049 TLGVHTRIDETIAQVTGSAHVGNLYVNRnmVGAVVGVQ-PFGGEGLSGTG 1097
Cdd:cd07109 388 VAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
658-1097 |
1.44e-65 |
|
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: 230.18 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 658 GEMTPVINPAEPKdIVGWGREATESEVEQALQNA--VNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:cd07112 1 GETFATINPATGR-VLAEVAACDAADVDRAVAAArrAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIA-EVREAVDFLHYYA-------GQV----RDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07112 80 ISDALAvDVPSAANTFRWYAeaidkvyGEVaptgPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 804 AEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIAtrlDAQGRPIPLiaE 883
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSG---QSNLKRVWL--E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 884 TGGMNAMIV-DSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDS 962
Cdd:cd07112 235 CGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 963 EAKANIERHIQTMRAKG-RPVFQAARENSDdaqewQTGTFVMPTLIE-LENFAEL-EKEVFGPVLHVVRYNRnqLAELIE 1039
Cdd:cd07112 315 AHFDKVLGYIESGKAEGaRLVAGGKRVLTE-----TGGFFVEPTVFDgVTPDMRIaREEIFGPVLSVITFDS--EEEAVA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07112 388 LANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
664-1097 |
3.09e-64 |
|
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: 225.95 E-value: 3.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 664 INPAEPKDiVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEV 743
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 744 REAVDFLHYYAGQVRDDFDNE---------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTS 808
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRkvptgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 809 LIAAQGIAILLEAGVPPGVVQLLPGRGETvGAQLtADTRVRGVMFTGSteVATllQRNIATRldAQGRPIPLIAETGGMN 888
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAAL-IDAGVDKVAFTGS--VAT--GRKVMAA--AAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 889 AMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANI 968
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 969 ERHIQTMRAKG-RPVFQAARENSDdaqewqtGTFVMPTLI--ELENFAELEKEVFGPVLHVVRYnrNQLAELIEQINASG 1045
Cdd:cd07099 312 RRHVDDAVAKGaKALTGGARSNGG-------GPFYEPTVLtdVPHDMDVMREETFGPVLPVMPV--ADEDEAIALANDSR 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1046 YGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07099 383 YGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
148-259 |
2.12e-63 |
|
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.
Pssm-ID: 434266 [Multi-domain] Cd Length: 112 Bit Score: 210.44 E-value: 2.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 148 VQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGRLVSTHNEAN 227
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 555258718 228 LSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQF 259
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
663-1097 |
2.45e-63 |
|
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: 223.17 E-value: 2.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEPkDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAE 742
Cdd:cd07106 1 VINPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 743 VREAVDFLHYYAGQVRDD---FDNET------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQ 813
Cdd:cd07106 80 VGGAVAWLRYTASLDLPDeviEDDDTrrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 814 GIAILLEAgVPPGVVQLLPGRGEtVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgRPIPLiaETGGMNAMIVD 893
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTL----KRVTL--ELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 894 SSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQ 973
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 974 TMRAKGRPVfqAARENSDDAQewqtGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLG 1051
Cdd:cd07106 312 DAKAKGAKV--LAGGEPLDGP----GYFIPPTIVDdpPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGAS 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 555258718 1052 VHTRiDETIAQVTGSA-HVGNLYVNRNmvGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07106 384 VWSS-DLERAEAVARRlEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
679-1097 |
1.13e-62 |
|
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: 221.54 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 679 ATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVR 758
Cdd:cd07094 18 DDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 759 ---------DDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAG 822
Cdd:cd07094 98 rirgeeiplDATQGSDNRlawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 823 VPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIatrldaqgrPIPLIA-ETGGMNAMIVDSSALTEQV 901
Cdd:cd07094 178 VPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANA---------GGKRIAlELGGNAPVIVDRDADLDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 902 VVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHI-QTMRAKGR 980
Cdd:cd07094 249 IEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVeEAVEAGAR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 981 PVFQAAREnsddaqewqtGTFVMPTLIE---LENFAELEkEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRiD 1057
Cdd:cd07094 329 LLCGGERD----------GALFKPTVLEdvpRDTKLSTE-ETFGPVVPIIRY--DDFEEAIRIANSTDYGLQAGIFTR-D 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 555258718 1058 ETIAqvtgsahvgnLYVNRNM-VGAVV---------GVQPFGGEGLSGTG 1097
Cdd:cd07094 395 LNVA----------FKAAEKLeVGGVMvndssafrtDWMPFGGVKESGVG 434
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
679-1103 |
2.70e-62 |
|
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: 219.86 E-value: 2.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 679 ATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYA---- 754
Cdd:cd07152 10 ADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAglpt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 755 ---GQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLE-AGVPPG 826
Cdd:cd07152 90 qpqGEILPSAPGRLslarRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLFEeAGLPAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 827 VVQLLPGRGEtVGAQLTADTRVRGVMFTGSTEVAtllqRNIAtrlDAQGRPIPLIA-ETGGMNAMIVDSSALTEQVVVDV 905
Cdd:cd07152 170 VLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVG----RKVG---EAAGRHLKKVSlELGGKNALIVLDDADLDLAASNG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 906 LASAFDSAGQRC-SALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQ 984
Cdd:cd07152 242 AWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 985 AARENsddaqewqtGTFVMPTLI-----ELENFAElekEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDET 1059
Cdd:cd07152 321 GGTYD---------GLFYRPTVLsgvkpGMPAFDE---EIFGPVAPVTVF--DSDEEAVALANDTEYGLSAGIISRDVGR 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 555258718 1060 IAQVTGSAHVGNLYVNRNMVGAVVgVQPFGGEGLSGTGPKAGGP 1103
Cdd:cd07152 387 AMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
663-1101 |
4.84e-62 |
|
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: 219.62 E-value: 4.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNA-IA 741
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 742 EVREAVDFLHYYAG----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLI 810
Cdd:cd07115 80 DVPRAADTFRYYAGwadkiegeviPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 811 AAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNiatrldAQGRPIPLIAETGGMNAM 890
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQG------AAGNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 891 IVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIER 970
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 971 HIQTMRAKGrpvfqaARENSDDAQEWQTGTFVMPTLielenFAELE-------KEVFGPVLHVVRYNRNQLAELIEqiNA 1043
Cdd:cd07115 314 YVDVGREEG------ARLLTGGKRPGARGFFVEPTI-----FAAVPpemriaqEEIFGPVVSVMRFRDEEEALRIA--NG 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1044 SGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07115 381 TEYGLAAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
657-1097 |
3.14e-61 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 218.41 E-value: 3.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 657 DGEMTPVINPAEPKDIVG---WGREATESeveqALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAG 733
Cdd:PLN02278 38 DGKTFPVYNPATGEVIANvpcMGRAETND----AIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 734 KTFSNAIAEVREAVDFLHYYAGQVRDDFDN------------ETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLA 801
Cdd:PLN02278 114 KPLKEAIGEVAYGASFLEYFAEEAKRVYGDiipspfpdrrllVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 802 KPAEQTSLI--AAQGIAilLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgRPIP 879
Cdd:PLN02278 194 KPSELTPLTalAAAELA--LQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV----KRVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 880 LiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRC-SALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGP 958
Cdd:PLN02278 268 L--ELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 959 VIDSEAKANIERHIQTMRAKGRPVFQAARENSDdaqewqTGTFVMPTLI-----ELENFAElekEVFGPVLHVVRYNRNq 1033
Cdd:PLN02278 345 LINEAAVQKVESHVQDAVSKGAKVLLGGKRHSL------GGTFYEPTVLgdvteDMLIFRE---EVFGPVAPLTRFKTE- 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555258718 1034 lAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1097
Cdd:PLN02278 415 -EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
663-1100 |
1.73e-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: 215.30 E-value: 1.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTF-SNAIA 741
Cdd:cd07108 1 VINPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 742 EVREAVDFLHYY---AGQVR--------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLi 810
Cdd:cd07108 80 EAAVLADLFRYFgglAGELKgetlpfgpDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 811 AAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAM 890
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 891 IVDSSALTEQVVVDVLASA-FDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIE 969
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 970 RHIQT-MRAKGRPVFQAARENSDDAQEwqTGTFVMPTLI-ELENFAEL-EKEVFGPVLHVVRYnrNQLAELIEQINASGY 1046
Cdd:cd07108 313 GYIDLgLSTSGATVLRGGPLPGEGPLA--DGFFVQPTIFsGVDNEWRLaREEIFGPVLCAIPW--KDEDEVIAMANDSHY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 555258718 1047 GLTLGVHTRiDETIAQVTGSA-HVGNLYVNRNmVGAVVGvQPFGGEGLSGTGPKA 1100
Cdd:cd07108 389 GLAAYVWTR-DLGRALRAAHAlEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
654-1101 |
3.49e-60 |
|
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: 214.77 E-value: 3.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 654 PVADGEMTPVINPAEPKDIVGWGrEATESEVEQALQNAVN--QAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVRE 731
Cdd:cd07091 14 DSVSGKTFPTINPATEEVICQVA-EADEEDVDAAVKAARAafETGWWRKMDPRERGRLLNKLADLIERDRDELAALESLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 732 AGKTFS-NAIAEVREAVDFLHYYAG----------QVRDDFDNETHR-PLGpvVC--ISPWNFPLAIFTGQIAAALAAGN 797
Cdd:cd07091 93 NGKPLEeSAKGDVALSIKCLRYYAGwadkiqgktiPIDGNFLAYTRRePIG--VCgqIIPWNFPLLMLAWKLAPALAAGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 798 SVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIA-TRLdaqgR 876
Cdd:cd07091 171 TVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAkSNL----K 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 877 PIPLiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:cd07091 247 KVTL--ELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 957 GPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDaqewqtGTFVMPTLielenFAELEK-------EVFGPVLHVVRY 1029
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSK------GYFIQPTV-----FTDVKDdmkiakeEIFGPVVTILKF 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555258718 1030 nrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07091 394 --KTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
653-1097 |
4.65e-60 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 214.29 E-value: 4.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVADGEMTPVINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREA 732
Cdd:cd07138 8 VAPAGTETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 733 G--KTFSNAiAEVREAVDFLHYYAGQVRDdFDNETHR--------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07138 87 GapITLARA-AQVGLGIGHLRAAADALKD-FEFEERRgnslvvrePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 803 PAEQTSLiAAQGIA-ILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLD--AQgrpip 879
Cdd:cd07138 165 PSEVAPL-SAIILAeILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKrvAL----- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 880 liaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSAL-RVLCLQDDIAEhTLKMLRGAMAECRMGNPGRLTTDIGP 958
Cdd:cd07138 239 ---ELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRMLVPRSRYAE-AEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 959 VIDSEAKANIERHIQTMRAKG---------RPvfqaarensddaQEWQTGTFVMPTLielenFAEL-------EKEVFGP 1022
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGarlvaggpgRP------------EGLERGYFVKPTV-----FADVtpdmtiaREEIFGP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 555258718 1023 VLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmvGAVVGVQ-PFGGEGLSGTG 1097
Cdd:cd07138 378 VLSIIPY--DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
663-1097 |
1.88e-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: 209.41 E-value: 1.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEpKDIVGWGREATESEVEQALQNAVNQAPVW-FATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIA 741
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 742 -EVREAVDFLHYYAGQVR-----DDFDNET-----------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07089 80 mQVDGPIGHLRYFADLADsfpweFDLPVPAlrggpgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 805 EQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgRPIPLiaET 884
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 885 GGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEA 964
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 965 KANIERHIQTMRAKG-RPVFQAARENSDDaqewqTGTFVMPTLI-ELENFAEL-EKEVFGPVLHVVRYnrNQLAELIEQI 1041
Cdd:cd07089 314 RDRVEGYIARGRDEGaRLVTGGGRPAGLD-----KGFYVEPTLFaDVDNDMRIaQEEIFGPVLVVIPY--DDDDEAVRIA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1042 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmvGAVVGV--QPFGGEGLSGTG 1097
Cdd:cd07089 387 NDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
672-1101 |
2.92e-58 |
|
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: 208.37 E-value: 2.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 672 IVGWGREATESEVEQALQNAVNQAPvwfATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLH 751
Cdd:cd07146 11 VVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 752 YYAGQV-RDD-----FDNETHR----------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGI 815
Cdd:cd07146 88 FAAAEAlRDDgesfsCDLTANGkarkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 816 AILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIAtrldAQGRPIPLIAETGGMNAMIVDSS 895
Cdd:cd07146 168 DLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVG----KAIA----ATAGYKRQLLELGGNDPLIVMDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 896 ALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHI-QT 974
Cdd:cd07146 240 ADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVeEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 975 MRAKGRPVFQAAREnsddaqewqtGTFVMPTLIE-LENFAEL-EKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGV 1052
Cdd:cd07146 320 IAQGARVLLGNQRQ----------GALYAPTVLDhVPPDAELvTEETFGPVAPVIRV--KDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 555258718 1053 HTRIDETIAQVTGSAHVGNLYVNrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
655-1115 |
5.27e-58 |
|
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: 208.79 E-value: 5.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 655 VADGEMTPVINPA--EPKDIVGwgrEATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREA 732
Cdd:cd07111 33 PENRKSFPTINPAtgEVLASVL---QAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 733 GKtfsnAIAEVRE-----AVDFLHYYAGQVR-DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQ 806
Cdd:cd07111 110 GK----PIRESRDcdiplVARHFYHHAGWAQlLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 807 TSLIAAQGIAILLEAGVPPGVVQLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLQRNIAtrldAQGRPIPLiaETGG 886
Cdd:cd07111 186 TPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA----GTGKKLSL--ELGG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 887 MNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKA 966
Cdd:cd07111 259 KSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 967 NIERHIQTMRAKGRPVFQAARENSDDaqewqtGTFVMPTLIELENFAE--LEKEVFGPVLHVVRYnRNqLAELIEQINAS 1044
Cdd:cd07111 339 RIRELVEEGRAEGADVFQPGADLPSK------GPFYPPTLFTNVPPASriAQEEIFGPVLVVLTF-RT-AKEAVALANNT 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1045 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGpKAGGPLYLYRLLahRPP 1115
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEYL--RPS 476
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
655-1102 |
1.29e-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: 207.44 E-value: 1.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 655 VADGEMTPVINPAEPKDIVGWgREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGK 734
Cdd:cd07130 8 GGGGGVVTSISPANGEPIARV-RQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 735 TFSNAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07130 87 ILPEGLGEVQEMIDICDFAVGLSRqlygltipserpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 803 PAEQTSL--IAAQGIA--ILLEAGVPPGVVQLLPGRGEtVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqGRpi 878
Cdd:cd07130 167 PSPTTPLtaIAVTKIVarVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---GR-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 879 pLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGP 958
Cdd:cd07130 241 -SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 959 VIDSEAKANIERHIQTMRAK-GRPVFQAARENSDdaqewqtGTFVMPTLIELENFAEL-EKEVFGPVLHVVRYnrNQLAE 1036
Cdd:cd07130 320 LHTKAAVDNYLAAIEEAKSQgGTVLFGGKVIDGP-------GNYVEPTIVEGLSDAPIvKEETFAPILYVLKF--DTLEE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555258718 1037 LIEQINASGYGLTLGVHTRIDETIAQ---VTGSaHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1102
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAFRwlgPKGS-DCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
656-1101 |
2.77e-57 |
|
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: 206.58 E-value: 2.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEPKDIVgwgrEATESEVE------QALQNAVNQAPvWFATPPQERAAILQRAAVLMEDQMQQLIGLLV 729
Cdd:cd07142 16 ASGKTFPTIDPRNGEVIA----HVAEGDAEdvdravKAARKAFDEGP-WPRMTGYERSRILLRFADLLEKHADELAALET 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 730 REAGKTFSNA-IAEVREAVDFLHYYAGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:cd07142 91 WDNGKPYEQArYAEVPLAARLFRYYAGWA-DKIHGMTlpadgphhvytlHEPIGVVGQIIPWNFPLLMFAWKVGPALACG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 797 NSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqrNIATRLDAQGR 876
Cdd:cd07142 170 NTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVG-----KIIMQLAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 877 PIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 957 GPVIDSEAKANIERHIQTMRAKGrpvfqaARENSDDAQEWQTGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnrNQL 1034
Cdd:cd07142 325 GPQVDKEQFEKILSYIEHGKEEG------ATLITGGDRIGSKGYYIQPTIFSdvKDDMKIARDEIFGPVQSILKF--KTV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1035 AELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
653-1097 |
2.95e-57 |
|
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: 206.00 E-value: 2.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVADGEMTPVINPAEPKDIVGWgREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREA 732
Cdd:cd07151 4 RDGTSERTIDVLNPYTGETLAEI-PAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 733 GKTFSNAIAEV-------REAVDFLHYYAGQ-VRDDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07151 83 GSTRIKANIEWgaamaitREAATFPLRMEGRiLPSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 801 AKPAEQTSLIAAQGIA-ILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIATrldAQGRPIP 879
Cdd:cd07151 163 LKPASDTPITGGLLLAkIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG----RHIGE---LAGRHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 880 LIA-ETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGP 958
Cdd:cd07151 236 KVAlELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 959 VIDSEAKANIERHIQTMRAKGrpvfqAARENSDDAQewqtGTFVMPT-LIELENFAELEK-EVFGPVLHVVRYNRNQlaE 1036
Cdd:cd07151 316 LINESQVDGLLDKIEQAVEEG-----ATLLVGGEAE----GNVLEPTvLSDVTNDMEIAReEIFGPVAPIIKADDEE--E 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1037 LIEQINASGYGLTLGVHTRIDETIAQV-----TGSAHVGNLYVNR--NMvgavvgvqPFGGEGLSGTG 1097
Cdd:cd07151 385 ALELANDTEYGLSGAVFTSDLERGVQFarridAGMTHINDQPVNDepHV--------PFGGEKNSGLG 444
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
657-1101 |
8.07e-57 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 205.07 E-value: 8.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 657 DGEMTPVINPAEPKDIVGWGrEATESEVEQALQNAVN--QAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGK 734
Cdd:cd07143 20 HGGTVKVYNPSTGKLITKIA-EATEADVDIAVEVAHAafETDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 735 TFSNAIA-EVREAVDFLHYYAGQVRDDFDN--ET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07143 99 TFGTAKRvDVQASADTFRYYGGWADKIHGQviETdikkltytrHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 803 PAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATrldAQGRPIPLia 882
Cdd:cd07143 179 PSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK---SNLKKVTL-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 883 ETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDS 962
Cdd:cd07143 254 ELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 963 EAKANIERHIQTMRAKGRPVFQAARENSDDaqewqtGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnrNQLAELIEQ 1040
Cdd:cd07143 334 IQYERIMSYIESGKAEGATVETGGKRHGNE------GYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKF--KTEEEAIKR 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07143 406 ANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
653-1097 |
8.33e-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: 205.24 E-value: 8.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVADGEMTPVINPAEpKDIVGWGREATESEVEQALQNAVN--QAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVR 730
Cdd:cd07119 7 VEAASGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRafDSGEWPHLPAQERAALLFRIADKIREDAEELARLETL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 731 EAGKTFSNAIAEVREAVDFLHYYAGQV--RDDFDNET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07119 86 NTGKTLRESEIDIDDVANCFRYYAGLAtkETGEVYDVpphvisrtvREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 800 LAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgRPIP 879
Cdd:cd07119 166 VIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNV----KKVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 880 LiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPV 959
Cdd:cd07119 242 L--ELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 960 IDSEAKANIERHIQTMRAKGRPVFQAARENSDDaqEWQTGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYNRNqlAEL 1037
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTGD--ELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERFDTE--EEA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1038 IEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1097
Cdd:cd07119 396 IRLANDTPYGLAGAVWTK-DIARANrVARRLRAGTVWINDYHPYFAEA--PWGGYKQSGIG 453
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
678-1101 |
1.03e-56 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 204.08 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 678 EATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQV 757
Cdd:cd07101 14 QSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 758 RDDFD--------------NETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGV 823
Cdd:cd07101 94 ERLLKprrrrgaipvltrtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 824 PPGVVQLLPGRGETVGAQLTAdtRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVV 903
Cdd:cd07101 174 PRDLWQVVTGPGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDADLDKAAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 904 DVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVF 983
Cdd:cd07101 246 GAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 984 QAARENSDdaqewqTGT-FVMPTLI-----ELENFAElekEVFGPVLHVVRYNRnqLAELIEQINASGYGLTLGVHTRID 1057
Cdd:cd07101 326 AGGRARPD------LGPyFYEPTVLtgvteDMELFAE---ETFGPVVSIYRVAD--DDEAIELANDTDYGLNASVWTRDG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 555258718 1058 ETIAQVTGSAHVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTGPKAG 1101
Cdd:cd07101 395 ARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
663-1097 |
1.93e-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: 203.30 E-value: 1.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEPKDIVGWgREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAE 742
Cdd:cd07090 1 VIEPATGEVLATV-HCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 743 VREAVDFLHYYAGQVRD------DFDNE----THR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIA 811
Cdd:cd07090 80 IDSSADCLEYYAGLAPTlsgehvPLPGGsfayTRRePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 812 AQGIAILLEAGVPPGVVQLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgRPIPLiaETGGMNAMI 891
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI----KHVTL--ELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 892 VDSSALTEQVVVDVLASAFDSAGQRCS-ALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIER 970
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 971 HIQTMRAKG--------RPVFQAARENsddaqewqtGTFVMPTLI-----ELENFAElekEVFGPVLHVVRYNRNQlaEL 1037
Cdd:cd07090 312 YIESAKQEGakvlcggeRVVPEDGLEN---------GFYVSPCVLtdctdDMTIVRE---EIFGPVMSILPFDTEE--EV 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1038 IEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07090 378 IRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
663-1097 |
3.91e-56 |
|
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: 202.58 E-value: 3.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAE 742
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 743 VREAVDFLHYYAGQVRD--------------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQT 807
Cdd:cd07110 80 VDDVAGCFEYYADLAEQldakaeravplpseDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 808 SLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIATRLDAQGRPIPLiaETGGM 887
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATG----SQVMQAAAQDIKPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 888 NAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKAN 967
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 968 IERHIQTMRAKG-RPVFQAARensddAQEWQTGTFVMPTLielenFAELEK-------EVFGPVLHVVRYNRNqlAELIE 1039
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRR-----PAHLEKGYFIAPTV-----FADVPTdsriwreEIFGPVLCVRSFATE--DEAIA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07110 382 LANDSEYGLAAAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
678-1101 |
4.13e-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: 202.18 E-value: 4.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 678 EATESEVEQALQ---NAVNQAPvWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYA 754
Cdd:cd07118 15 EGTVEDVDAAVAaarKAFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 755 GQVR----DDFDN--------ETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAG 822
Cdd:cd07118 94 SLARtlhgDSYNNlgddmlglVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 823 VPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAQGrpipliAETGGMNAMIVDSSALTEQVV 902
Cdd:cd07118 174 LPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQIVFADADLDAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 903 VDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPV 982
Cdd:cd07118 248 DAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 983 F----QAARENsddaqewqtGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRI 1056
Cdd:cd07118 328 LlggeRLASAA---------GLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 555258718 1057 DETIAQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTGPKAG 1101
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
653-1097 |
9.04e-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: 202.19 E-value: 9.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVADGEMTPVINPAEPKDIVGWGReATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREA 732
Cdd:cd07559 10 VAPSKGEYFDNYNPVNGKVLCEIPR-STAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 733 GKTFSNAI-AEVREAVDFLHYYAGQVR------DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07559 89 GKPIRETLaADIPLAIDHFRYFAGVIRaqegslSEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 801 AKPAEQTS---LIAAQGIAILLeagvPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrp 877
Cdd:cd07559 169 LKPASQTPlsiLVLMELIGDLL----PKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 878 IPLIAETGGMNAMIVDSSALTEQVVVD------VLASAFDSaGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGR 951
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 952 LTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDAQEwqTGTFVMPTLIELEN-----FAElekEVFGPVLHV 1026
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLD--KGYFYEPTLIKGGNndmriFQE---EIFGPVLAV 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1027 VRYNRNQlaELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07559 393 ITFKDEE--EAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
658-1095 |
1.92e-55 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 201.34 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 658 GEMTPVINPAEPKDIvgW-GREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTF 736
Cdd:PRK09457 14 GEAFESRNPVSGEVL--WqGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 737 SNAIAEVRE-------AVDFLHYYAGQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:PRK09457 92 WEAATEVTAminkiaiSIQAYHERTGEKRSEMADGAavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 806 QTSLIAAQGIAILLEAGVPPGVVQLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLQRNIAtrldaqGRPIPLIA-ET 884
Cdd:PRK09457 172 LTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFA------GQPEKILAlEM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 885 GGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCS-ALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTD-IGPVIDS 962
Cdd:PRK09457 245 GGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVGRWDAEPQPfMGAVISE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 963 E-AKANIERHIQTMRAKGRPVFQAARENSDDAqewqtgtFVMPTLIELENFAEL-EKEVFGPVLHVVRYNRnqLAELIEQ 1040
Cdd:PRK09457 325 QaAQGLVAAQAQLLALGGKSLLEMTQLQAGTG-------LLTPGIIDVTGVAELpDEEYFGPLLQVVRYDD--FDEAIRL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 555258718 1041 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:PRK09457 396 ANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
679-1097 |
1.66e-53 |
|
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: 194.77 E-value: 1.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 679 ATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVR 758
Cdd:cd07147 18 AGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEAT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 759 D------DFD----NETHR------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAG 822
Cdd:cd07147 98 RiygevlPLDisarGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 823 VPPGVVQLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLqRNIATRldaqgRPIPLiaETGGMNAMIVDSSALTEQVV 902
Cdd:cd07147 178 LPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-----KKVVL--ELGGNAAVIVDSDADLDFAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 903 VDVLASAFDSAGQRC-SALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRP 981
Cdd:cd07147 249 QRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 982 VFQAARENsddaqewqtGTFVMPTLieLENFAE----LEKEVFGPVLHVVRYNRnqLAELIEQINASGYGLTLGVHTRID 1057
Cdd:cd07147 328 LLTGGKRD---------GALLEPTI--LEDVPPdmevNCEEVFGPVVTVEPYDD--FDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 555258718 1058 ETIAQVTGSAHVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1097
Cdd:cd07147 395 EKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSGIG 433
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
677-1076 |
6.07e-53 |
|
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: 192.85 E-value: 6.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 677 REATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQ 756
Cdd:cd07102 13 PLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 757 VRDDFDNE------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVP 824
Cdd:cd07102 93 AEEALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 825 PGVVQLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLQRNiatrldAQGRPIPLIAETGGMNAMIVDSSALTEQVVVD 904
Cdd:cd07102 173 EGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRA------AAGRFIKVGLELGGKDPAYVRPDADLDAAAES 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 905 VLASAFDSAGQRCSAL-RVLC---LQDDIAEHTLKMLRGAmaecRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKG- 979
Cdd:cd07102 246 LVDGAFFNSGQSCCSIeRIYVhesIYDAFVEAFVAVVKGY----KLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGa 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 980 RPVFQAARENSDDAQewqtGTFVMPT-LIELENFAELEK-EVFGPVLHVVRYNRNqlAELIEQINASGYGLTLGVHTRID 1057
Cdd:cd07102 322 RALIDGALFPEDKAG----GAYLAPTvLTNVDHSMRVMReETFGPVVGIMKVKSD--AEAIALMNDSEYGLTASVWTKDI 395
|
410
....*....|....*....
gi 555258718 1058 ETIAQVTGSAHVGNLYVNR 1076
Cdd:cd07102 396 ARAEALGEQLETGTVFMNR 414
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
663-1097 |
6.15e-53 |
|
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: 192.98 E-value: 6.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAE 742
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 743 VREAVDFLHYYAGQVRD-----------DFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIA 811
Cdd:cd07107 80 VMVAAALLDYFAGLVTElkgetipvggrNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 812 AQgIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDaqgrpiPLIAETGGMNAMI 891
Cdd:cd07107 160 LR-LAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIK------HVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 892 VDSSALTEQVVVDVLASA-FDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIER 970
Cdd:cd07107 233 VFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 971 HIQTMRAKGRPVFQAARENSDDAQEwqTGTFVMPTLielenFAEL-------EKEVFGPVLHVVRYnrNQLAELIEQINA 1043
Cdd:cd07107 313 YIDSAKREGARLVTGGGRPEGPALE--GGFYVEPTV-----FADVtpgmriaREEIFGPVLSVLRW--RDEAEMVAQANG 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1044 SGYGLTLGVHTRiDETIAQVTGSA-HVGNLYVN---RNMVGAvvgvqPFGGEGLSGTG 1097
Cdd:cd07107 384 VEYGLTAAIWTN-DISQAHRTARRvEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
658-1101 |
6.60e-53 |
|
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: 193.72 E-value: 6.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 658 GEMTPVINPAEPKDIVGWgREATESEVEQALQ---NAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGK 734
Cdd:cd07141 21 GKTFPTINPATGEKICEV-QEGDKADVDKAVKaarAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 735 TFSNA-IAEVREAVDFLHYYAGQVrDDFDNET------------HRPLGpvVC--ISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07141 100 PFSKSyLVDLPGAIKVLRYYAGWA-DKIHGKTipmdgdfftytrHEPVG--VCgqIIPWNFPLLMAAWKLAPALACGNTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 800 LAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIA-TRLdaqgRPI 878
Cdd:cd07141 177 VLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGkSNL----KRV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 879 PLiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEhtlKMLRGAMAEC---RMGNPGRLTTD 955
Cdd:cd07141 253 TL--ELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYD---EFVKRSVERAkkrVVGNPFDPKTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 956 IGPVIDSEAKANIERHIQTMRAKGrpvfqaARENSDDAQEWQTGTFVMPTLielenFAEL-------EKEVFGPVLHVVR 1028
Cdd:cd07141 328 QGPQIDEEQFKKILELIESGKKEG------AKLECGGKRHGDKGYFIQPTV-----FSDVtddmriaKEEIFGPVQQIFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 555258718 1029 YnrNQLAELIEQINASGYGLTLGVHTR-IDETIAqVTGSAHVGNLYVNrnmVGAVVGVQ-PFGGEGLSGTGPKAG 1101
Cdd:cd07141 397 F--KTIDEVIERANNTTYGLAAAVFTKdIDKAIT-FSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
644-1095 |
2.98e-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: 191.85 E-value: 2.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 644 KWQAkpvleqpvADGEMTPVINPAEPKDIvgW-GREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQ 722
Cdd:TIGR03240 6 KWRA--------GQGESFASRNPATQEVL--WqGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 723 QLIGLLVREAGKTFSNAIAEVRE-------AVDFLHYYAGQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAA 791
Cdd:TIGR03240 76 ALARVIARETGKPLWETRTEVASmigkvaiSIKAYHERTGESENPMPDGRavlrHRPHGVVAVFGPYNFPGHLPNGHIVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 792 ALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLQRNIAtrl 871
Cdd:TIGR03240 156 ALIAGNTVVFKPSELTPWVAEETVKLWEKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFG--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 872 daqGRPIPLIA-ETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDiaEHTLKMLRGAMAECRMGNPG 950
Cdd:TIGR03240 232 ---GRPEKILAlEMGGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTCARRLLVPDG--AQGDAFLARLVEVAERLTVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 951 RLTTD----IGPVIDSEAKANIERHIQTMRAKG-RPVFQAARENSDDAqewqtgtFVMPTLIELENFAEL-EKEVFGPVL 1024
Cdd:TIGR03240 307 AWDAEpqpfMGAVISLRAAQRLLAAQAKLLALGgKSLLEMRQLDPGAA-------FLTPGIIDVTGVAELpDEEHFGPLL 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1025 HVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:TIGR03240 380 QVIRY--TDFDEAIAIANNTRFGLSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
684-1097 |
7.92e-52 |
|
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: 188.82 E-value: 7.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 684 VEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYA--------G 755
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenaeaflaD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 756 QVRDDFDNE---THRPLGPVVCISPWNFPLAiftgQI----AAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVV 828
Cdd:cd07100 81 EPIETDAGKayvRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 829 QLLPGRGETVgAQLTADTRVRGVMFTGST----EVATLLQRNIAtrldaqgrpiPLIAETGGMNAMIVDSSALTEQVVVD 904
Cdd:cd07100 157 QNLLIDSDQV-EAIIADPRVRGVTLTGSEragrAVAAEAGKNLK----------KSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 905 VLASAFDSAGQRC-SALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKG-RPV 982
Cdd:cd07100 226 AVKGRLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGaTLL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 983 FQAARENSDdaqewqtGTFVMPTL---IELEN--FAElekEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRID 1057
Cdd:cd07100 305 LGGKRPDGP-------GAFYPPTVltdVTPGMpaYDE---ELFGPVAAVIKV--KDEEEAIALANDSPFGLGGSVFTTDL 372
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 555258718 1058 ETIAQVTGSAHVGNLYVNRnMVGAVVGVqPFGGEGLSGTG 1097
Cdd:cd07100 373 ERAERVARRLEAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
656-1103 |
1.25e-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: 189.71 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEPKdIVGWGREATESEVEQAlqnaVNQA------PVWFATPPQERAAILQRAAVLMEDQMQQLIGLLV 729
Cdd:cd07139 11 SGSETIDVVSPATEE-VVGRVPEATPADVDAA----VAAArrafdnGPWPRLSPAERAAVLRRLADALEARADELARLWT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 730 REAGKTFS-NAIAEVREAVDFLHYYAGQVRDdFDNETHR-------------PLGPVVCISPWNFPLAIFTGQIAAALAA 795
Cdd:cd07139 86 AENGMPISwSRRAQGPGPAALLRYYAALARD-FPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 796 GNSVLAKPAEQTSLIA---AQGIAillEAGVPPGVVQLLPGrGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIATRLD 872
Cdd:cd07139 165 GCTVVLKPSPETPLDAyllAEAAE---EAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAG----RRIAAVCG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 873 AQGRPIPLiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSAL-RVLcLQDDIAEHTLKMLRGAMAECRMGNPGR 951
Cdd:cd07139 237 ERLARVTL--ELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 952 LTTDIGPVIDSEAKANIERHIQTMRAKG-RPVFQAARENSDDaqewqTGTFVMPTLI-ELENFAEL-EKEVFGPVLHVVR 1028
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGaRLVTGGGRPAGLD-----RGWFVEPTLFaDVDNDMRIaQEEIFGPVLSVIP 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 555258718 1029 YnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07139 389 Y--DDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA---PFGGFKQSGIG-REGGP 457
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
663-1097 |
3.97e-51 |
|
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: 187.53 E-value: 3.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEPKDIvGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIA- 741
Cdd:cd07092 1 VVDPATGEEI-ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 742 EVREAVDFLHYYAGQVRD-----------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSL 809
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTlegpaageylpGHTSMIRRePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 810 iAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIATRLDAQGRPIPLiaETGGMNA 889
Cdd:cd07092 160 -TTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTG----KKVARAAADTLKRVHL--ELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 890 MIVDSSALTEQVVVDVLASAFDSAGQRC-SALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANI 968
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 969 ERHIQTMRAKGRPVFQAARENSDdaqewqtGTFVMPTLI-ELENFAEL-EKEVFGPVLHVVRYNRNQlaELIEQINASGY 1046
Cdd:cd07092 312 AGFVERAPAHARVLTGGRRAEGP-------GYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPFDDED--EAIELANDVEY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1047 GLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1097
Cdd:cd07092 383 GLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
654-1097 |
1.38e-50 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 188.16 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 654 PVADGEMTPVINPA--EPkdiVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVRE 731
Cdd:PRK09407 27 DGAAGPTREVTAPFtgEP---LATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 732 AGKTFSNAIAEVREAVDFLHYYA-------------------GQVRddfdnETHRPLGPVVCISPWNFPLAIFTGQIAAA 792
Cdd:PRK09407 104 TGKARRHAFEEVLDVALTARYYArrapkllaprrragalpvlTKTT-----ELRQPKGVVGVISPWNYPLTLAVSDAIPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 793 LAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTAdtRVRGVMFTGSTevATllQRNIATRld 872
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD--NADYLMFTGST--AT--GRVLAEQ-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 873 AQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRL 952
Cdd:PRK09407 251 AGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 953 TTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDdaqewqTGT-FVMPTLI-----ELENFAElekEVFGPVLHV 1026
Cdd:PRK09407 331 SADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPD------LGPlFYEPTVLtgvtpDMELARE---ETFGPVVSV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1027 VRYNRnqLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTG 1097
Cdd:PRK09407 402 YPVAD--VDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
654-1101 |
2.53e-50 |
|
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: 186.07 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 654 PVADGEMTPVINPAEPKDIVGWgREATESEVEQALQNAVNQ-APVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREA 732
Cdd:cd07144 18 KSSDGETIKTVNPSTGEVIASV-YAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 733 GKTF-SNAIAEVREAVDFLHYYAGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07144 97 GKPYhSNALGDLDEIIAVIRYYAGWA-DKIQGKTiptspnklaytlHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 800 LAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAqgrpIP 879
Cdd:cd07144 176 VIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA----VT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 880 LiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAEC-RMGNPGRLTTDIGP 958
Cdd:cd07144 252 L--ECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 959 VIDSEAKANIERHIQTMRAKGRpvfQAARENSDDAQEWQTGTFVMPTLielenFAE-------LEKEVFGPVLHVVRYNR 1031
Cdd:cd07144 330 QVSKTQYDRVLSYIEKGKKEGA---KLVYGGEKAPEGLGKGYFIPPTI-----FTDvpqdmriVKEEIFGPVVVISKFKT 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1032 NQlaELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR-NMvgAVVGVqPFGGEGLSGTGPKAG 1101
Cdd:cd07144 402 YE--EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSsND--SDVGV-PFGGFKMSGIGRELG 467
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
664-1055 |
4.17e-50 |
|
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: 184.85 E-value: 4.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 664 INPAEPKdIVGWGREATESEVEQALQNAVN--QAPVWfATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIA 741
Cdd:cd07120 2 IDPATGE-VIGTYADGGVAEAEAAIAAARRafDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 742 EVREAVDFLHYYAGQVR-----------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLI 810
Cdd:cd07120 80 EISGAISELRYYAGLARteagrmiepepGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 811 AAQGIAILLEA-GVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAQGrpipliAETGGMNA 889
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 890 MIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIE 969
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 970 RHIQTMRAKG-RPVFQAARENSDDAQewqtGTFVMPTLIELENFAE--LEKEVFGPVLHVVRYNRNqlAELIEQINASGY 1046
Cdd:cd07120 314 RMVERAIAAGaEVVLRGGPVTEGLAK----GAFLRPTLLEVDDPDAdiVQEEIFGPVLTLETFDDE--AEAVALANDTDY 387
|
....*....
gi 555258718 1047 GLTLGVHTR 1055
Cdd:cd07120 388 GLAASVWTR 396
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
657-1106 |
6.64e-50 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 185.11 E-value: 6.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 657 DGEMTPVINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTF 736
Cdd:PRK11241 24 NGEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 737 SNAIAEVREAVDFLHYYAGQVRDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:PRK11241 103 AEAKGEISYAASFIEWFAEEGKRIYGDTIpghqadkrliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 805 EQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgRPIPLiaET 884
Cdd:PRK11241 183 SQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDI----KKVSL--EL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 885 GGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEA 964
Cdd:PRK11241 257 GGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 965 KANIERHIQTMRAKGRPVFQAARENSddaqewQTGTFVMPT-LIELENFAELEK-EVFGPVLHVVRYNRNqlAELIEQIN 1042
Cdd:PRK11241 337 VAKVEEHIADALEKGARVVCGGKAHE------LGGNFFQPTiLVDVPANAKVAKeETFGPLAPLFRFKDE--ADVIAQAN 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555258718 1043 ASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGvqPFGG---EGLSGTGPKAGGPLYL 1106
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
653-1097 |
1.08e-49 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 183.96 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVA-DGEMTPVINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVRE 731
Cdd:PRK13473 10 ELVAgEGEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 732 AGKTFSNAIA-EVREAVDFLHYYAGQVRD-----------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:PRK13473 89 CGKPLHLALNdEIPAIVDVFRFFAGAARClegkaageyleGHTSMIRRdPVGVVASIAPWNYPLMMAAWKLAPALAAGNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 799 VLAKPAEQTSLIA---AQGIAILLeagvPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqRNIATRLDAQG 875
Cdd:PRK13473 169 VVLKPSEITPLTAlklAELAADIL----PPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATG----KHVLSAAADSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 876 RPIPLiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTD 955
Cdd:PRK13473 241 KRTHL--ELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 956 IGPVIDSEAKANIERHIQtmRAKGRPVFQ--AARENSDDAqewqtGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnr 1031
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVE--RAKALGHIRvvTGGEAPDGK-----GYYYEPTLLAgaRQDDEIVQREVFGPVVSVTPF-- 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555258718 1032 NQLAELIEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1097
Cdd:PRK13473 390 DDEDQAVRWANDSDYGLASSVWTR-DVGRAHrVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
663-1097 |
8.64e-49 |
|
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: 181.49 E-value: 8.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEPKdIVGWGREATESEVEQALQNAVNQAPVWFA-TPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT--FSNA 739
Cdd:cd07113 19 ITNPATEQ-VIASVASATEADVDAAVASAWRAFVSAWAkTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSihLSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 740 IaEVREAVDFLHYYAGQVR----------------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07113 98 F-EVGQSANFLRYFAGWATkingetlapsipsmqgERYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 803 PAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGEtVGAQLTADTRVRGVMFTGSteVATllQRNIATRLDAQGRPIPLia 882
Cdd:cd07113 177 PSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGS--VAT--GKKIGRQAASDLTRVTL-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 883 ETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRC-SALRVLCLQDDIAEHTLKMlRGAMAECRMGNPGRLTTDIGPVID 961
Cdd:cd07113 250 ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCaAPERFYVHRSKFDELVTKL-KQALSSFQVGSPMDESVMFGPLAN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 962 SEAKANIERHIQTMRAKGRPVFQAARENSddaqewQTGTFVMPTLIELENFAE--LEKEVFGPVLHVVRYNRNQlaELIE 1039
Cdd:cd07113 329 QPHFDKVCSYLDDARAEGDEIVRGGEALA------GEGYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDEE--ELIQ 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 555258718 1040 QINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07113 401 LINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
656-1101 |
1.20e-47 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.87 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEPKDIVGWgREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:PLN02315 31 ANGPLVSSVNPANNQPIAEV-VEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:PLN02315 110 LAEGIGEVQEIIDMCDFAVGLSRqlngsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 804 AEQTSLIA---AQGIAILLEA-GVPPGVVQLLPGrGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqGRpip 879
Cdd:PLN02315 190 APTTPLITiamTKLVAEVLEKnNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GK--- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 880 LIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPV 959
Cdd:PLN02315 263 CLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 960 IDSEAKANIERHIQTMRAKGRPVFQAARENSDDaqewqtGTFVMPTLIELENFAELEK-EVFGPVLHVVRYnrNQLAELI 1038
Cdd:PLN02315 343 HTPESKKNFEKGIEIIKSQGGKILTGGSAIESE------GNFVQPTIVEISPDADVVKeELFGPVLYVMKF--KTLEEAI 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 555258718 1039 EQINASGYGLTLGVHTRIDETIAQVTG--SAHVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAG 1101
Cdd:PLN02315 415 EINNSVPQGLSSSIFTRNPETIFKWIGplGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
683-1097 |
2.04e-47 |
|
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: 176.23 E-value: 2.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 683 EVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQ------ 756
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLitqiig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 757 --VRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQL 830
Cdd:cd07105 81 gsIPSDKPGTLamvvKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 831 L---PGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLA 907
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHL------KPVLLELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 908 SAFDSAGQRC-SALRVLcLQDDIAEHTLKMLRGAMAECRMGNpgrltTDIGPVIDSEAKANIERHIQTMRAKG-RPVFQA 985
Cdd:cd07105 235 GAFLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGaKLVVGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 986 ARENSDDaqewqtGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRiDETIA-Q 1062
Cdd:cd07105 309 LADESPS------GTSMPPTILDnvTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR-DLARAlA 379
|
410 420 430
....*....|....*....|....*....|....*...
gi 555258718 1063 VTGSAHVGNLYVNrnmvGAVVGVQ---PFGGEGLSGTG 1097
Cdd:cd07105 380 VAKRIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
656-1097 |
4.66e-47 |
|
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: 176.49 E-value: 4.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEPKDIVGWGReATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:cd07117 13 SSGETIDSYNPANGETLSEITD-ATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIA-EVREAVDFLHYYAGQVR------DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07117 92 IRETRAvDIPLAADHFRYFAGVIRaeegsaNMIDEDTlsivlREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 804 AEQTSLIAAQgIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAE 883
Cdd:cd07117 172 SSTTSLSLLE-LAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------IPATLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 884 TGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSE 963
Cdd:cd07117 245 LGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 964 AKANIERHIQTMRAKGRPVFQAAR---ENSDDAqewqtGTFVMPTLIE-LENFAEL-EKEVFGPVLHVVRYNRNQlaELI 1038
Cdd:cd07117 325 QLDKILSYVDIAKEEGAKILTGGHrltENGLDK-----GFFIEPTLIVnVTNDMRVaQEEIFGPVATVIKFKTED--EVI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1039 EQINASGYGLTLGVHTRiDETIA-QVTGSAHVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07117 398 DMANDSEYGLGGGVFTK-DINRAlRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
653-1097 |
7.20e-46 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 173.14 E-value: 7.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVAD--GEMTPVINPA--EPKDIVgwgREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLL 728
Cdd:PRK13252 14 AYVEAtsGETFEVINPAtgEVLATV---QAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 729 VREAGKTFSNAI-AEVREAVDFLHYYAG----------QVRD-DFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:PRK13252 91 TLDTGKPIQETSvVDIVTGADVLEYYAGlapalegeqiPLRGgSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 797 NSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGEtVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDaqgr 876
Cdd:PRK13252 171 NAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 877 piPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCS-ALRVLcLQDDIAEHTLKMLRGAMAECRMGNPGRLTTD 955
Cdd:PRK13252 246 --EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 956 IGPVIDSEAKANIERHIQTMRAKG-RPVFQAARENSDDAQEwqtGTFVMPTLielenFAE-------LEKEVFGPVLHVV 1027
Cdd:PRK13252 323 FGPLVSFAHRDKVLGYIEKGKAEGaRLLCGGERLTEGGFAN---GAFVAPTV-----FTDctddmtiVREEIFGPVMSVL 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1028 RYNRNQlaELIEQINASGYGLTLGVHTRiDETIA-QVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:PRK13252 395 TFDDED--EVIARANDTEYGLAAGVFTA-DLSRAhRVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
644-1075 |
1.95e-45 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 172.22 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 644 KWQAkPVLeqpvadGEMTPVINPAEpKDIVGWGREATESEVEQALQNA-----VNQAPVWFATPPQERAAILQRAAVLME 718
Cdd:PLN02467 15 EWRE-PVL------GKRIPVVNPAT-EETIGDIPAATAEDVDAAVEAArkafkRNKGKDWARTTGAVRAKYLRAIAAKIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 719 DQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVR--------------DDFDNETHR-PLGPVVCISPWNFPLA 783
Cdd:PLN02467 87 ERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEaldakqkapvslpmETFKGYVLKePLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 784 IFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtll 863
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 864 qRNIATRLDAQGRPIPLiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAE 943
Cdd:PLN02467 244 -RKIMTAAAQMVKPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 944 CRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAArensDDAQEWQTGTFVMPTLI-----ELENFAElekE 1018
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGG----KRPEHLKKGFFIEPTIItdvttSMQIWRE---E 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 555258718 1019 VFGPVLHVVRYNRNqlAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:PLN02467 394 VFGPVLCVKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
656-1060 |
6.17e-45 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 170.71 E-value: 6.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEPKdiVGWGREA-TESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGK 734
Cdd:PLN00412 28 SSGKSVAITNPSTRK--TQYKVQAcTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 735 TFSNAIAEVREAVDFLHYYA---------GQ--VRDDF-DNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAA 795
Cdd:PLN00412 106 PAKDAVTEVVRSGDLISYTAeegvrilgeGKflVSDSFpGNERNKycltskiPLGVVLAIPPFNYPVNLAVSKIAPALIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 796 GNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGStevatllqrNIATRLDAQG 875
Cdd:PLN00412 186 GNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG---------DTGIAISKKA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 876 RPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRlTTD 955
Cdd:PLN00412 257 GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 956 IGPVIdSEAKAN-IERHIQTMRAKGrPVFqaarensddAQEWQ-TGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnr 1031
Cdd:PLN00412 336 ITPVV-SESSANfIEGLVMDAKEKG-ATF---------CQEWKrEGNLIWPLLLDnvRPDMRIAWEEPFGPVLPVIRI-- 402
|
410 420 430
....*....|....*....|....*....|
gi 555258718 1032 NQLAELIEQINASGYGLTLGVHTR-IDETI 1060
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRdINKAI 432
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
656-1075 |
7.00e-45 |
|
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: 170.06 E-value: 7.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKT 735
Cdd:TIGR01722 13 ASGTYIPVTNPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 736 FSNAIAEVREAVDFLHYYAG-----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:TIGR01722 92 HSDALGDVARGLEVVEHACGvnsllkgetstQVATRVDVYSIRqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 804 AEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGaQLTADTRVRGVMFTGSTEVAtllqRNIATRLDAQGRPIPliAE 883
Cdd:TIGR01722 172 SEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVD-RLLEHPDVKAVSFVGSTPIG----RYIHTTGSAHGKRVQ--AL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 884 TGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDiAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSE 963
Cdd:TIGR01722 245 GGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 964 AKANIERHIQTMRAKGRPVFQAARENSDDAQEwqTGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnrNQLAELIEQI 1041
Cdd:TIGR01722 324 AKDRVASLIAGGAAEGAEVLLDGRGYKVDGYE--EGNWVGPTLLErvPPTMKAYQEEIFGPVLCVLEA--DTLEEAIALI 399
|
410 420 430
....*....|....*....|....*....|....
gi 555258718 1042 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:TIGR01722 400 NASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN 433
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
678-1101 |
1.25e-44 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 170.00 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 678 EATESEVE---QALQNAVNQAPvWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFS-NAIAEVREAVDFLHYY 753
Cdd:PLN02766 54 EGDKEDVDlavKAAREAFDHGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAAAGLLRYY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 754 AGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEA 821
Cdd:PLN02766 133 AGAA-DKIHGETlkmsrqlqgytlKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 822 GVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATrldAQGRPIPLiaETGGMNAMIVDSSALTEQV 901
Cdd:PLN02766 212 GVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAT---SNLKQVSL--ELGGKSPLLIFDDADVDMA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 902 VVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRP 981
Cdd:PLN02766 287 VDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGAT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 982 VFQAARENSDDaqewqtGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDET 1059
Cdd:PLN02766 367 LLTGGKPCGDK------GYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAGIVTKDLDV 438
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 555258718 1060 IAQVTGSAHVGNLYVNRNMvgAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:PLN02766 439 ANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
653-1097 |
3.24e-44 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 168.01 E-value: 3.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVADGEMTPVINPAEPKDIVGWGReATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREA 732
Cdd:cd07116 10 VAPVKGEYFDNITPVTGKVFCEVPR-STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 733 GKTFSNAI-AEVREAVDFLHYYAGQVR------DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07116 89 GKPVRETLaADIPLAIDHFRYFAGCIRaqegsiSEIDENTvayhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 801 AKPAEQTSLiaaqGIAILLEA---GVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrp 877
Cdd:cd07116 169 LKPAEQTPA----SILVLMELigdLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 878 IPLIAETGGMNAMIVDSSALTEQvvvdvlASAFDSA-----------GQRCSALRVLCLQDDIAEHTLKMLRGAMAECRM 946
Cdd:cd07116 239 IPVTLELGGKSPNIFFADVMDAD------DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 947 GNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDAQEwqTGTFVMPTLIELENFAEL-EKEVFGPVLH 1025
Cdd:cd07116 313 GNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLL--GGGYYVPTTFKGGNKMRIfQEEIFGPVLA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1026 VVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07116 391 VTTF--KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
656-1101 |
4.01e-44 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 169.22 E-value: 4.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPaEPKDIVGWGREATESEVEQAL---QNAVNQAPvWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREA 732
Cdd:PLN02466 70 ASGKTFPTLDP-RTGEVIAHVAEGDAEDVNRAVaaaRKAFDEGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 733 GKTFSNAI-AEVREAVDFLHYYAG--------QVRDDFDNET---HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:PLN02466 148 GKPYEQSAkAELPMFARLFRYYAGwadkihglTVPADGPHHVqtlHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 801 AKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVAtllqrNIATRLDAQGRPIPL 880
Cdd:PLN02466 228 LKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTG-----KIVLELAAKSNLKPV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 881 IAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVI 960
Cdd:PLN02466 303 TLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQI 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 961 DSEAKANIERHIQTMRAKGrpvfqAARENSDDaQEWQTGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYnrNQLAELI 1038
Cdd:PLN02466 383 DSEQFEKILRYIKSGVESG-----ATLECGGD-RFGSKGYYIQPTVFSnvQDDMLIAQDEIFGPVQSILKF--KDLDEVI 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555258718 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG 515
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
702-1097 |
3.32e-43 |
|
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: 164.51 E-value: 3.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 702 PPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNE----------------T 765
Cdd:cd07148 42 PAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREipmgltpasagriaftT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGEtVGAQLTAD 845
Cdd:cd07148 122 REPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 846 TRVRGVMFTGSTEVATLLQRNIATrldaqGRPIPLiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCL 925
Cdd:cd07148 201 PRVAFFSFIGSARVGWMLRSKLAP-----GTRCAL--EHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 926 QDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDdaqewqtgTFVMPT 1005
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSD--------TTYAPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1006 -LIELENFAEL-EKEVFGPVlhVVRYNRNQLAELIEQINASGYGLTLGVHTR-ID---ETIAQVTGSAhvgnLYVNrNMV 1079
Cdd:cd07148 346 vLLDPPRDAKVsTQEIFGPV--VCVYSYDDLDEAIAQANSLPVAFQAAVFTKdLDvalKAVRRLDATA----VMVN-DHT 418
|
410
....*....|....*...
gi 555258718 1080 GAVVGVQPFGGEGLSGTG 1097
Cdd:cd07148 419 AFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
656-1101 |
1.74e-42 |
|
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: 163.05 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 656 ADGEMTPVINPAEPKDIVGWGReATESEVEQALQNAVN--QAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAG 733
Cdd:cd07140 18 EGGKTYNTINPTDGSVICKVSL-ATVEDVDRAVAAAKEafENGEWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 734 KTFSNAI-AEVREAVDFLHYYAG-------------QVRDDfDNET---HRPLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:cd07140 97 AVYTLALkTHVGMSIQTFRYFAGwcdkiqgktipinQARPN-RNLTltkREPIGVCGIVIPWNYPLMMLAWKMAACLAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 797 NSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATrldAQGR 876
Cdd:cd07140 176 NTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAV---SNLK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 877 PIPLiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:cd07140 253 KVSL--ELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 957 GPvidSEAKANIERHIQTMRakgRPVFQAARENSDDAQEWQTGTFVMPTL---IELENFAELEkEVFGPVLHVVRYNRNQ 1033
Cdd:cd07140 331 GP---QNHKAHLDKLVEYCE---RGVKEGATLVYGGKQVDRPGFFFEPTVftdVEDHMFIAKE-ESFGPIMIISKFDDGD 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1034 LAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN---RNMVGAvvgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07140 404 VDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynKTDVAA-----PFGGFKQSGFGKDLG 469
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
710-1084 |
2.61e-41 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 157.59 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 710 LQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVR--------DDFDNET----HRPLGPVVCISP 777
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegeiiqSDRPGENillfKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 778 WNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGST 857
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 858 EVAtllqrnIATRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKML 937
Cdd:PRK10090 161 SAG------EKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 938 RGAMAECRMGNP-GRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDaqewqtGTFVMPTLIE--LENFAE 1014
Cdd:PRK10090 235 GEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGK------GYYYPPTLLLdvRQEMSI 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1015 LEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVG 1084
Cdd:PRK10090 309 MHEETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQG 376
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
653-1097 |
1.93e-40 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 157.37 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 653 QPVADGEMTPVINPAEPKDIVGWGReATESEVEQALQNA--VNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVR 730
Cdd:PRK09847 29 TAAAENETFETVDPVTQAPLAKIAR-GKSVDIDRAVSAArgVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 731 EAGKTFSNAIAE-VREAVDFLHYYA-------GQVRDDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:PRK09847 108 DTGKPIRHSLRDdIPGAARAIRWYAeaidkvyGEVATTSSHElamiVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 799 VLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIAtrlDAQGRPI 878
Cdd:PRK09847 188 VILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG---DSNMKRV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 879 PLiaETGGMNAMIV--DSSALtEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDI 956
Cdd:PRK09847 265 WL--EAGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 957 GPVIDSEAKANIERHIQTMRAKGRpVFQAARENSDDAqewqtgtFVMPT-LIELENFAELEK-EVFGPVLHVVRYNRNQL 1034
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREGESKGQ-LLLDGRNAGLAA-------AIGPTiFVDVDPNASLSReEIFGPVLVVTRFTSEEQ 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555258718 1035 AELIEqiNASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:PRK09847 414 ALQLA--NDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
680-1101 |
4.74e-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: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 680 TESEVEQALQNAVNQAPVWFATPPQERAAILQraaVLME---DQMQQLIGLLVREAGKTFSNA-IAEVREAVDFLHY--- 752
Cdd:cd07098 16 TPEDVDEAIAAARAAQREWAKTSFAERRKVLR---SLLKyilENQEEICRVACRDTGKTMVDAsLGEILVTCEKIRWtlk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 753 -----YAGQVRDDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLE 820
Cdd:cd07098 93 hgekaLRPESRPGGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 821 A----GVPPGVVQLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSA 896
Cdd:cd07098 173 ClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLELGGKDPAIVLDDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 897 LTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMR 976
Cdd:cd07098 246 DLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 977 AKG-RPVFQAARENsddAQEWQTGTFVMPTLIE--LENFAELEKEVFGPVLHVVRYNRNqlAELIEQINASGYGLTLGVH 1053
Cdd:cd07098 326 EKGaRLLAGGKRYP---HPEYPQGHYFPPTLLVdvTPDMKIAQEEVFGPVMVVMKASDD--EEAVEIANSTEYGLGASVF 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 555258718 1054 TRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07098 401 GKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
679-1097 |
5.28e-36 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 143.34 E-value: 5.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 679 ATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYAGQVR 758
Cdd:PRK09406 20 LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 759 DDFDNET--------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE---QTSLIAAQGIAillEA 821
Cdd:PRK09406 100 ALLADEPadaaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASnvpQTALYLADLFR---RA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 822 GVPPGVVQ-LLPGRGeTVGAQLtADTRVRGVMFTGStEVATllqRNIATrldAQGRPI-PLIAETGGMNAMIVDSSALTE 899
Cdd:PRK09406 177 GFPDGCFQtLLVGSG-AVEAIL-RDPRVAAATLTGS-EPAG---RAVAA---IAGDEIkKTVLELGGSDPFIVMPSADLD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 900 QVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKG 979
Cdd:PRK09406 248 RAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 980 RPVFQAARENSDDaqewqtGTFVMPTLI-----ELENFAElekEVFGPVLHVvrYNRNQLAELIEQINASGYGLTLGVHT 1054
Cdd:PRK09406 328 ATILCGGKRPDGP------GWFYPPTVItditpDMRLYTE---EVFGPVASL--YRVADIDEAIEIANATTFGLGSNAWT 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 555258718 1055 RIDETIAQVTGSAHVGNLYVNrNMVGAVVGVqPFGGEGLSGTG 1097
Cdd:PRK09406 397 RDEAEQERFIDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSGYG 437
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
663-1047 |
8.12e-33 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 136.03 E-value: 8.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 663 VINPAEpKDIVGWGREATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAE 742
Cdd:PLN02419 133 VINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 743 VREAVDFLHYYAG-----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQ---T 807
Cdd:PLN02419 212 IFRGLEVVEHACGmatlqmgeylpNVSNGVDTYSIRePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKdpgA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 808 SLIAAQgiaILLEAGVPPGVVQLLPGRGETVGAqLTADTRVRGVMFTGSTEVATllqrNIATRLDAQGRPIPliAETGGM 887
Cdd:PLN02419 292 SVILAE---LAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGM----HIYARAAAKGKRIQ--SNMGAK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 888 NAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAeCRMGNPGRLTTDIGPVIDSEAKAN 967
Cdd:PLN02419 362 NHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKA-LKVTCGSEPDADLGPVISKQAKER 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 968 IERHIQTMRAKGRPVFQAARENSddAQEWQTGTFVMPTLI-----ELENFAElekEVFGPVLhvVRYNRNQLAELIEQIN 1042
Cdd:PLN02419 441 ICRLIQSGVDDGAKLLLDGRDIV--VPGYEKGNFIGPTILsgvtpDMECYKE---EIFGPVL--VCMQANSFDEAISIIN 513
|
....*
gi 555258718 1043 ASGYG 1047
Cdd:PLN02419 514 KNKYG 518
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
766-1097 |
1.02e-32 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 132.65 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQgIAILLEAGVPPGVVQLLPGrGETVGAQLTAd 845
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSAL-LAKLIPKYFDPEAVAVVEG-GVEVATALLA- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 846 TRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCL 925
Cdd:cd07087 175 EPFDHIFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 926 QDDIAEHTLKMLRGAMAEcRMGNPGRLTTDIGPVIDseakaniERHIQTMRA---KGRPVFQAARENSDDaqewqtgtFV 1002
Cdd:cd07087 249 HESIKDELIEELKKAIKE-FYGEDPKESPDYGRIIN-------ERHFDRLASlldDGKVVIGGQVDKEER--------YI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1003 MPTLIELENFAE--LEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVG 1080
Cdd:cd07087 313 APTILDDVSPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLH 390
|
330
....*....|....*..
gi 555258718 1081 AVVGVQPFGGEGLSGTG 1097
Cdd:cd07087 391 AAIPNLPFGGVGNSGMG 407
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
684-1114 |
1.28e-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: 129.67 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 684 VEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHY----YAGQVRD 759
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARafviYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 760 DFDNE--------THR---PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAG-VPPGV 827
Cdd:cd07084 81 EPGNHlgqglkqqSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 828 VQLLPGRGETvGAQLTADTRVRGVMFTGSTEVATLLqrniatRLDAqgRPIPLIAETGGMNAMIVDSSALTEQVVVD-VL 906
Cdd:cd07084 161 VTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKL------ALDA--KQARIYLELAGFNWKVLGPDAQAVDYVAWqCV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 907 ASAFDSAGQRCSALRVLCLQDDIAehTLKMLRGAMAECRMGNPGRLTtdIGPVIDSEAKANIErhiqTMRAKGRPV--FQ 984
Cdd:cd07084 232 QDMTACSGQKCTAQSMLFVPENWS--KTPLVEKLKALLARRKLEDLL--LGPVQTFTTLAMIA----HMENLLGSVllFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 985 AARENSDDAQEWqTGTFVMPTL---IELENFAEL--EKEVFGPVLHVVRYNRNQLAELIEQINASGYGLTLGVHTRIDET 1059
Cdd:cd07084 304 GKELKNHSIPSI-YGACVASALfvpIDEILKTYElvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIF 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555258718 1060 IAQVT------GSAHVGNLYVNRNMVGAVVGVQPFGGeglsGTGPKAGGPLYLYRllAHRP 1114
Cdd:cd07084 383 LQELIgnlwvaGRTYAILRGRTGVAPNQNHGGGPAAD----PRGAGIGGPEAIKL--VWRC 437
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
684-1059 |
2.18e-30 |
|
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: 126.50 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 684 VEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAG-----------------KTFSNAIAEvrea 746
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpearlqgelgrttgqlRLFADLVRE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 747 vdflHYYAGQVRDDFDNE-----------THRPLGPVVCISPWNFPLAIFT--GQIAAALAAGNSVLAK-----PAeqTS 808
Cdd:cd07129 77 ----GSWLDARIDPADPDrqplprpdlrrMLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahpahPG--TS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 809 LIAAQGI-AILLEAGVPPGVVQLLPGRGETVGAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDaqgrPIPLIAETGGM 887
Cdd:cd07129 151 ELVARAIrAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGSV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 888 NAMIVDSSALTEQvvVDVLASAFD-----SAGQRCSA--LrVLCLQDDIAEHTLKMLRGAMAECrmgNPGRLTTdigpvi 960
Cdd:cd07129 227 NPVFILPGALAER--GEAIAQGFVgsltlGAGQFCTNpgL-VLVPAGPAGDAFIAALAEALAAA---PAQTMLT------ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 961 dseakANIERHIQTMRA--KGRPVFQA-ARENSDDAQEWQTGTFVMPTLIELENFAELEKEVFGPVLHVVRY-NRNQLAE 1036
Cdd:cd07129 295 -----PGIAEAYRQGVEalAAAPGVRVlAGGAAAEGGNQAAPTLFKVDAAAFLADPALQEEVFGPASLVVRYdDAAELLA 369
|
410 420
....*....|....*....|...
gi 555258718 1037 LIEQINASgygLTLGVHTRIDET 1059
Cdd:cd07129 370 VAEALEGQ---LTATIHGEEDDL 389
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
766-1102 |
7.35e-30 |
|
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: 124.26 E-value: 7.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQgIAILLEAGVPPGVVQLLPGRGETVGAQLtaD 845
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAV-IAKIIREAFDEDEVAVFEGDAEVAQALL--E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 846 TRVRGVMFTGSTEVATLLQRNIATRLDaqgrPIPLiaETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCL 925
Cdd:cd07134 175 LPFDHIFFTGSPAVGKIVMAAAAKHLA----SVTL--ELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 926 QDDIAEHTLKMLRGAMAECRMGNPGRL-TTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAAreNSDDAQewqtgTFVMP 1004
Cdd:cd07134 249 HESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG--QFDAAQ-----RYIAP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1005 TLIE--LENFAELEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAV 1082
Cdd:cd07134 322 TVLTnvTPDMKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFL 399
|
330 340
....*....|....*....|
gi 555258718 1083 VGVQPFGGEGLSGTGpKAGG 1102
Cdd:cd07134 400 NPNLPFGGVNNSGIG-SYHG 418
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
664-1075 |
3.10e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 123.05 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 664 INPA--EPKDIVGWgreATESEVEQALQNAVNQAPVWFATPPQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIA 741
Cdd:PRK13968 12 VNPAtgEQLSVLPW---AGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 742 EVREAVDFLHYYAGQ-----------VRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTsLI 810
Cdd:PRK13968 89 EVAKSANLCDWYAEHgpamlkaeptlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV-MG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 811 AAQGIA-ILLEAGVPPGVVQLLPGRGETVgAQLTADTRVRGVMFTGSTEVATLLQRNIATRLDAqgrpipLIAETGGMNA 889
Cdd:PRK13968 168 CAQLIAqVFKDAGIPQGVYGWLNADNDGV-SQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 890 MIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIE 969
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 970 RHIQTMRAKGRPVFQAARENSDDaqewqtGTFVMPTLI-----ELENFAElekEVFGPVLHVVRYNRNQLAelIEQINAS 1044
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGA------GNYYAPTVLanvtpEMTAFRE---ELFGPVAAITVAKDAEHA--LELANDS 389
|
410 420 430
....*....|....*....|....*....|.
gi 555258718 1045 GYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1075
Cdd:PRK13968 390 EFGLSATIFTTDETQARQMAARLECGGVFIN 420
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
768-1148 |
4.00e-26 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 113.97 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEqTSLIAAQGIAILLEAGVPPGVVQLLPGrGETVGAQLTADtR 847
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSE-LSPHTSKLMAKLLTKYLDPSYVRVIEG-GVEVTTELLKE-P 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 848 VRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQD 927
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 928 DIAEHTLKMLRGAMAEcRMGNPGRLTTDIGPVIDSEAkanIERHIQTMRAKGRPVFQAAreNSDDAQEWqtgtfVMPTLI 1007
Cdd:PTZ00381 260 SIKDKFIEALKEAIKE-FFGEDPKKSEDYSRIVNEFH---TKRLAELIKDHGGKVVYGG--EVDIENKY-----VAPTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1008 ---ELENFAeLEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHT---RIDETIAQVTGSahvGNLYVNRNMVGA 1081
Cdd:PTZ00381 329 vnpDLDSPL-MQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGedkRHKELVLENTSS---GAVVINDCVFHL 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1082 VVGVQPFGGEGLSGTGPKAGgpLYLYRLLAHRPPNALNTTLTRQD--ARYP--VDAQLKT-TLLAPLTALTQ 1148
Cdd:PTZ00381 403 LNPNLPFGGVGNSGMGAYHG--KYGFDTFSHPKPVLNKSTGNSFDlsLRYPpyTSFKSWVlSFLLKLSIPVQ 472
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
765-1097 |
2.57e-25 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 110.65 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 765 THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQgIAILLEAGVPPGVVQLLPGRGEtVGAQLTA 844
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSAL-LAELLAEYFDEDEVAVVTGGAD-VAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 845 ---DTrvrgVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALR 921
Cdd:cd07133 176 lpfDH----LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 922 -VLCLQDDIAEHtLKMLRGAMAEC---RMGNPgrlttDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDAqewQ 997
Cdd:cd07133 246 yVLVPEDKLEEF-VAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDFA---A 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 998 TGTFVmPTLIelENFAE----LEKEVFGPVLHVVRYNRnqLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLY 1073
Cdd:cd07133 317 TRKLP-PTLV--LNVTDdmrvMQEEIFGPILPILTYDS--LDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVT 391
|
330 340
....*....|....*....|....
gi 555258718 1074 VNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07133 392 INDTLLHVAQDDLPFGGVGASGMG 415
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
766-1097 |
4.40e-25 |
|
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: 110.00 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLiAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLtaD 845
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPH-TAALLAELVPKYLDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 846 TRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALR-VLC 924
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIAEAAAKHL------TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDyVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 925 lQDDIAEHTLKMLRGAMAECRMGNPGRLtTDIGPVIDSEAKANIERHIQTmrAKGRPVFQaareNSDDAQEwqtgTFVMP 1004
Cdd:cd07135 257 -DPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLDT--TKGKVVIG----GEMDEAT----RFIPP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1005 TLIELENFAE--LEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAV 1082
Cdd:cd07135 325 TIVSDVSWDDslMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVG 402
|
330
....*....|....*
gi 555258718 1083 VGVQPFGGEGLSGTG 1097
Cdd:cd07135 403 VDNAPFGGVGDSGYG 417
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
704-1102 |
2.10e-22 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 102.73 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 704 QERAAILQR-AAVLMEDQmQQLIGLLVReAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPV---------- 772
Cdd:cd07128 59 HERAAMLKAlAKYLMERK-EDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVeplskdgtfv 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 773 ------------VCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGV-PPGVVQLLPGRGETVG 839
Cdd:cd07128 137 gqhiltprrgvaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 840 AQLTA-DTrvrgVMFTGSTEVATLLQRNIATrldaQGRPIPLIAETGGMNAMIV--DSSALTEQ---VVVDVLASAFDSA 913
Cdd:cd07128 217 DHLGEqDV----VAFTGSAATAAKLRAHPNI----VARSIRFNAEADSLNAAILgpDATPGTPEfdlFVKEVAREMTVKA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 914 GQRCSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDA 993
Cdd:cd07128 289 GQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 994 QEWQTGTFVMPTLI----ELENFAELEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQ-VTGSA- 1067
Cdd:cd07128 369 ADAEKGAFFPPTLLlcddPDAATAVHDVEAFGPVATLMPY--DSLAEAIELAARGRGSLVASVVTNDPAFARElVLGAAp 446
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 555258718 1068 HVGNLYV-NRNMVGAVVG---VQP---FGGEGLSGTGPKAGG 1102
Cdd:cd07128 447 YHGRLLVlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGG 488
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
709-1073 |
4.39e-22 |
|
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: 101.42 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 709 ILQRAAVLM-----EDQMQQLIGllvREAGKTFSNAIAEVREAVDFLHYYAG-QVR----------DDFDNETHR---PL 769
Cdd:cd07126 67 VSHRVAHELrkpevEDFFARLIQ---RVAPKSDAQALGEVVVTRKFLENFAGdQVRflarsfnvpgDHQGQQSSGyrwPY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 770 GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGVPPGVVQLLPGRGETVGaQLTADTRVR 849
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLEANPR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 850 GVMFTGSTEVATLLQRniatrlDAQGRpipLIAETGGMNAMIVDSSALTEQVVVDVL-ASAFDSAGQRCSALRVLCLQDD 928
Cdd:cd07126 223 MTLFTGSSKVAERLAL------ELHGK---VKLEDAGFDWKILGPDVSDVDYVAWQCdQDAYACSGQKCSAQSILFAHEN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 929 IAEHTLKMLRGAMAECRmgNPGRLTtdIGPVI--DSEA-KANIERHIQTMRAK----GRPVFQAARENSDDAQEwQTGTF 1001
Cdd:cd07126 294 WVQAGILDKLKALAEQR--KLEDLT--IGPVLtwTTERiLDHVDKLLAIPGAKvlfgGKPLTNHSIPSIYGAYE-PTAVF 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 555258718 1002 V-MPTLIELENFAELEKEVFGPVLHVVRYNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLY 1073
Cdd:cd07126 369 VpLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
706-1097 |
2.76e-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: 95.37 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 706 RAAILQRAAVLMEDQMQQLIGLLVREAGKT-FSNAIAEV-------REAVDFLHYYAG--QVRDDFDNET------HRPL 769
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPkFEAVLSEIllvkneiKYAISNLPEWMKpePVKKNLATLLddvyiyKEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 770 GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEqTSLIAAQGIAILLEAGVPPGVVQLLPGrgetvGAQLTA---DT 846
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSE-VSPATAKLLAELIPKYLDKECYPVVLG-----GVEETTellKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 847 RVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALR-VLCl 925
Cdd:cd07132 176 RFDYIFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDyVLC- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 926 QDDIAEHTLKMLRGAMAECrMGNPGRLTTDIGPVIDseakaniERHIQTMRA---KGRPVFQAareNSDDAQEwqtgtFV 1002
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIIN-------DRHFQRLKKllsGGKVAIGG---QTDEKER-----YI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1003 MPT-LIEL-ENFAELEKEVFGPVLHVVryNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVG 1080
Cdd:cd07132 313 APTvLTDVkPSDPVMQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMH 390
|
410
....*....|....*..
gi 555258718 1081 AVVGVQPFGGEGLSGTG 1097
Cdd:cd07132 391 YTLDSLPFGGVGNSGMG 407
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
768-1140 |
2.32e-18 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 89.79 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQtsliaAQGIAILLEAGVP----PGVVQLLPGrGETVGAQLT 843
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSEL-----APATSAFLAANIPkyldSKAVKVIEG-GPAVGEQLL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 844 aDTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVD--SSALTEQVVVD-VLASAFDS-AGQRCSA 919
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDslSSSRDTKVAVNrIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 920 LRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLttdigpviDSEAKANIERHIQtmRAKG---RPVFQAARENSDDAQEw 996
Cdd:PLN02203 255 IDYVLVEERFAPILIELLKSTIKKFFGENPRES--------KSMARILNKKHFQ--RLSNllkDPRVAASIVHGGSIDE- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 997 qTGTFVMPTLI---ELENfAELEKEVFGPVLHVVRYNRNQlaELIEQINASGYGLTLGVHTRiDETIAQ-VTGSAHVGNL 1072
Cdd:PLN02203 324 -KKLFIEPTILlnpPLDS-DIMTEEIFGPLLPIITVKKIE--DSIAFINSKPKPLAIYAFTN-NEKLKRrILSETSSGSV 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555258718 1073 YVNRNMVGAVVGVQPFGGEGLSGTGPKAGGplYLYRLLAHRPPNALNTTLTRQDARYPVDAQLKTTLL 1140
Cdd:PLN02203 399 TFNDAIIQYACDSLPFGGVGESGFGRYHGK--YSFDTFSHEKAVLRRSLLTEFEFRYPPWNDFKLGFL 464
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
768-1097 |
1.39e-17 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 87.08 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEqTSLIAAQGIAILLEAGVPPGVVQLLPGrGETVGAQLTaDTR 847
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSE-LAPATSALLAKLIPEYLDTKAIKVIEG-GVPETTALL-EQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 848 VRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDS-AGQRCSALRVLCLQ 926
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 927 DDIAEHTLKMLRGAMAECRMGNPgRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDdaqewqtgTFVMPTL 1006
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENP-KESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKN--------LYIEPTI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1007 I--ELENFAELEKEVFGPVLHVVRYNRNQlaELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVG 1084
Cdd:cd07137 323 LldPPLDSSIMTEEIFGPLLPIITVKKIE--ESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
330
....*....|...
gi 555258718 1085 VQPFGGEGLSGTG 1097
Cdd:cd07137 401 TLPFGGVGESGFG 413
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
89-136 |
2.90e-17 |
|
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain found in Proline utilization A (PutA) proteins. Proline utilization A (PutA) is a flavoprotein that has mutually exclusive roles as a transcriptional repressor of the put regulon and a membrane-associated enzyme that catalyzes the oxidation of proline to glutamate. The N-terminal region carries the flavoenzyme proline dehydrogenase (PRODH) domain which catalyzes the 2-electron oxidation of proline with the concomitant reduction of a flavin cofactor.
Pssm-ID: 465712 [Multi-domain] Cd Length: 48 Bit Score: 76.73 E-value: 2.90e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 555258718 89 SVSRAAITAAWRRPETDAVSMLMEQARLSPPVAEQAHKLAYQLAEKLR 136
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
768-1097 |
8.32e-16 |
|
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: 81.78 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE---QTSLIaaqgIAILLEAGVPPGVVQLLPGRGETVGAQLta 844
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSEltpNTSKV----IAKIIEETFDEEYVAVVEGGVEENQELL-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 845 DTRVRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLC 924
Cdd:cd07136 174 DQKFDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 925 LQDDIAEHTLKMLRGAMAEcRMGNPGRLTTDIGPVIDseakaniERH---IQTMRAKGRPVFQAareNSDDAQEWqtgtf 1001
Cdd:cd07136 248 VHESVKEKFIKELKEEIKK-FYGEDPLESPDYGRIIN-------EKHfdrLAGLLDNGKIVFGG---NTDRETLY----- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1002 VMPTLIELENF--AELEKEVFGPVLHVVRYnrNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGS------------A 1067
Cdd:cd07136 312 IEPTILDNVTWddPVMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENlsfgggcindtiM 389
|
330 340 350
....*....|....*....|....*....|
gi 555258718 1068 HVGNLYVnrnmvgavvgvqPFGGEGLSGTG 1097
Cdd:cd07136 390 HLANPYL------------PFGGVGNSGMG 407
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
705-1102 |
2.19e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 80.90 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 705 ERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIAEVREAVDFLHYYA------GQVRDDFDNETHR----------- 767
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalGDARLLRDGEAVQlgkdpafqgqh 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 768 ---PL-GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQGIAILLEAGV-PPGVVQLLPGRGETVGAQL 842
Cdd:PRK11903 144 vlvPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 843 TA-DTrvrgVMFTGSTEVATLLQRNIATrldAQgRPIPLIAETGGMNAMI-----VDSSALTEQVVVDVLASAFDSAGQR 916
Cdd:PRK11903 224 QPfDV----VSFTGSAETAAVLRSHPAV---VQ-RSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 917 CSALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRAKGRPVFQAARENSDDAQEw 996
Cdd:PRK11903 296 CTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVDADP- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 997 QTGTFVMPTLI----ELENFAELEKEVFGPVLHVVRYNRnqLAELIEQINASGYGLTLGVHTRIDETIAQVT-------G 1065
Cdd:PRK11903 375 AVAACVGPTLLgasdPDAATAVHDVEVFGPVATLLPYRD--AAHALALARRGQGSLVASVYSDDAAFLAAAAleladshG 452
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 555258718 1066 SAHVGNLYVNRNMVGAVVgVQP---FGGEGLSGTGPKAGG 1102
Cdd:PRK11903 453 RVHVISPDVAALHTGHGN-VMPqslHGGPGRAGGGEELGG 491
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
768-1143 |
8.96e-15 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 78.55 E-value: 8.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTSLIAAQgIAILLEAGVPPGVVQLLPGRGETVGAQLtaDTR 847
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAL-LAKLLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 848 VRGVMFTGSTEVATLLQRNIATRLdaqgrpIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFD-SAGQRCSALRVLCLQ 926
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 927 DDIAEHTLKMLRGAMAECRMGNPGRlTTDIGPVIDSEAKANIERHIQTMRAKGRPVF--QAARENSDdaqewqtgtfVMP 1004
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYggEKDRENLK----------IAP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 1005 TL---IELENFAeLEKEVFGPVLHVVryNRNQLAELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGA 1081
Cdd:PLN02174 332 TIlldVPLDSLI-MSEEIFGPLLPIL--TLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHL 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555258718 1082 VVGVQPFGGEGLSGTGPKAGGplYLYRLLAHRPPNALNTTLTRQDARYPVDAQLKTTLLAPL 1143
Cdd:PLN02174 409 ALHTLPFGGVGESGMGAYHGK--FSFDAFSHKKAVLYRSLFGDSAVRYPPYSRGKLRLLKAL 468
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-66 |
1.23e-13 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 66.77 E-value: 1.23e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555258718 2 GTTTMGVKLDDATRERIKMAASRIDRTPHWLIKQAIFSYLDKLENSDTLPE--LPALFAGAANESEE 66
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQegLAAADAGEFVSHEE 67
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
767-1082 |
2.86e-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: 67.89 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 767 RPLGPVVCISP---WNFPLAIFtgqiaAALAAGNSVLAKPAEQTSLIAAQGI----AILLEAGVPPGVVQLLP-GRGETV 838
Cdd:cd07127 194 RGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFDPNLVTLAAdTPEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 839 GAQLTADTRVRGVMFTGSTEVATLLQRNIatrldaqgRPIPLIAETGGMNAMIVDSsalTEQVVVDVLASAFDSA---GQ 915
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDWLEANA--------RQAQVYTEKAGVNTVVVDS---TDDLKAMLRNLAFSLSlysGQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 916 RCSALRVLCL-QDDIAEHTLKMLRGAMAEC-------RMGNPGRLTTDIGPVIDSEAKANIERHIQ------TMRAKGRP 981
Cdd:cd07127 338 MCTTPQNIYVpRDGIQTDDGRKSFDEVAADlaaaidgLLADPARAAALLGAIQSPDTLARIAEARQlgevllASEAVAHP 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 982 VFQAARENSddaqewqtgtfvmPTLIEL--ENFAELEKEVFGPVLHVVRYNR-NQLAELIEQINASGYGLTLGVHTRIDE 1058
Cdd:cd07127 418 EFPDARVRT-------------PLLLKLdaSDEAAYAEERFGPIAFVVATDStDHSIELARESVREHGAMTVGVYSTDPE 484
|
330 340
....*....|....*....|....
gi 555258718 1059 TIAQVTGSAHVGNLYVNRNMVGAV 1082
Cdd:cd07127 485 VVERVQEAALDAGVALSINLTGGV 508
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-46 |
2.94e-08 |
|
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: 50.83 E-value: 2.94e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 555258718 4 TTMGVKLDDATRERIKMAASRIDRTPHWLIKQAIFSYLDKLEN 46
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREEW 43
|
|
| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-45 |
3.74e-06 |
|
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: 44.81 E-value: 3.74e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 555258718 4 TTMGVKLDDATRERIKMAASRIDRTPHWLIKQAIFSYLDKLE 45
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLERLE 42
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|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
703-996 |
7.82e-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: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 703 PQERAAILQRAAVLMEDQMQQLIGLLVREAGKTFSNAIA-----------EVREAVDFLHYYAGQVR--------DDFDN 763
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIAnwiammgcsesKLYKNIDTERGITASVGhiqdvllpDNGET 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 764 ETHR-PLGPVVCISPWNFPLAIFTgQIAAALAAGNSVLAKPAEQTSlIAAQGIAILLEAGVPPG----VVQLLPGRGETV 838
Cdd:cd07077 95 YVRAfPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkiLVLYVPHPSDEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555258718 839 GAQLTADTRVRGVMFTGSTEVATLLQRNiatrldaqGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASA-FDSAGqrC 917
Cdd:cd07077 173 AEELLSHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA--C 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555258718 918 SALRVLCLQDDIAEHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMrakgrPVFQAARENSDDAQEW 996
Cdd:cd07077 243 ASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFDDEALESMTPLE-----CQFRVLDVISAVENAW 316
|
|
| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
1-45 |
2.36e-03 |
|
Predicted DNA-binding protein with an HTH domain [General function prediction only];
Pssm-ID: 443745 Cd Length: 76 Bit Score: 37.96 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 555258718 1 MGTTTmgVKLDDATRERIKMAASRIDRTPHWLIKQAIFSYLDKLE 45
Cdd:COG4710 1 MKMLS--IRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
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