|
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: 2853.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1 MGTTTMGVKLDDATRERIKFAASRIDRTPHWLIKQAIFNYLEKLENDETLPELPALLAGAANESDDVSSPVDEPWQPFLE 80
Cdd:PRK11809 1 MATTTMGVKLDDATRERIKSAAQRIDRTPHWLIKQAIFNYLEKLENGDTLPELPALLSGAANESEEADTPAEEPHQPFLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 81 FAEQILPQSVTRASITAAYRRAETDAVPMLLEQARLPQPLAEQAHKLAYQLAEKLRNQKTASGRAGMVQSLLQEFSLSSQ 160
Cdd:PRK11809 81 FAEQILPQSVLRAAITAAYRRPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGGRAGMVQGLLQEFSLSSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNETSLSRSLNRIIGKSG 240
Cdd:PRK11809 161 EGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHLGRSPSLFVNAATWGLLFTGKLVSTHNEASLSSSLNRIIGKSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGI 320
Cdd:PRK11809 241 EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 321 YEGPGISIKLSALHPRYSRAQYDRVMDELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
Cdd:PRK11809 321 YEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 401 FVIQAYQKRCPFVIDSLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPSLI 480
Cdd:PRK11809 401 FVIQAYQKRCPFVIDYLIDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLAVPNLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 481 YPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
Cdd:PRK11809 481 YPQFATHNAHTLAAIYHLAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 561 GANTSFVNRIADTTLPLDELVADPVSAVEKLARQEGQAGLPHPKIPLPRDLYGKGRSNSAGLDLANEHRLASLSSSLLNS 640
Cdd:PRK11809 561 GANTSFVNRIADTSLPLDELVADPVEAVEKLAQQEGQLGLPHPKIPLPRDLYGKGRANSAGLDLANEHRLASLSSALLAS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 641 ALHKWQALPALEHPVMAGELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQ 720
Cdd:PRK11809 641 AHQKWQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQ 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 721 MQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:PRK11809 721 MQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 801 AKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAQGRPTPL 880
Cdd:PRK11809 801 AKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDPQGRPIPL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 881 IAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVI 960
Cdd:PRK11809 881 IAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 961 DAEAKENIERHIQSLRAKGRTVFQAVRENSEDareWQSGTFIPPTLIELESFDELKKEVFGPVLHVVRYNRNELDQLVEQ 1040
Cdd:PRK11809 961 DAEAKANIERHIQAMRAKGRPVFQAARENSED---WQSGTFVPPTLIELDSFDELKREVFGPVLHVVRYNRNQLDELIEQ 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1041 INASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSRPQNAVGT 1120
Cdd:PRK11809 1038 INASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLATRPEDALAV 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1121 TLARQDAERPLDAQLKTLLEKPLNALQQWAAGR-PELQALCQQYRELAQAGTQRLLPGPTGERNTLTFIPRDRVLCVADN 1199
Cdd:PRK11809 1118 TLARQDAEYPVDAQLRAALLAPLTALREWAAERePELAALCDQYAELAQAGTTRLLPGPTGERNTYTLLPRERVLCLADT 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1200 EQDALIQLAAVTAVGCEILWPESALHRELAKKLPREVSERLHFAKPEMLTAQAFDAVIYHGDSDQLRELCEQVAARDGAI 1279
Cdd:PRK11809 1198 EQDALTQLAAVLAVGSQALWPDDALHRALVAALPAAVQARIQLAKDWQLADQPFDAVLFHGDSDQLRALCEQVAQRDGPI 1277
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|.
gi 1588278917 1280 ISVQGFARGESNLLLERLYIERSLSVNTAAAGGNASLMTIG 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: 2028.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 77 PFLEFAEQILPQSVTRASITAAYRRAETDAVPMLLEQARLPQPLAEQAHKLAYQLAEKLRnqktASGRAGMVQSLLQEFS 156
Cdd:PRK11905 1 MFQMFAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALR----AKRKGTGVEALLQEYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 157 LSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNETSLSRSLNRII 236
Cdd:PRK11905 77 LSSQEGVALMCLAEALLRIPDTATRDALIRDKIAPGDWKSHLGGSKSLFVNAATWGLMLTGKLLSTVNDRGLSAALTRLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASN 316
Cdd:PRK11905 157 ARLGEPVIRKAVDMAMRMMGEQFVTGETIEEALKRARELEARGYRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 317 GRGIYEGPGISIKLSALHPRYSRAQYDRVMDELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGW 396
Cdd:PRK11905 237 GRGVYDGPGISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 397 NGIGFVIQAYQKRCPFVIDSLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAV 476
Cdd:PRK11905 317 NGIGFVVQAYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 477 PSLIYPQFATHNAHTLAAIYQLAGQNYypgQYEFQCLHGMGEPLYEQVVGKvadGKLNRPCRIYAPVGTHETLLAYLVRR 556
Cdd:PRK11905 397 RDVIYPQFATHNAQTLAAIYELAGGKG---DFEFQCLHGMGEPLYDQVVGK---EKLGRPCRIYAPVGTHETLLAYLVRR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 557 LLENGANTSFVNRIADTTLPLDELVADPVSAVEKLarqegqAGLPHPKIPLPRDLYGKGRSNSAGLDLANEHRLASLSSS 636
Cdd:PRK11905 471 LLENGANSSFVNRIVDENVPVEELIADPVEKVAAM------GVAPHPQIPLPRDLYGPERRNSKGLDLSDEATLAALDEA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 637 LLNSALHKWQALPALEHPVMAGELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVL 716
Cdd:PRK11905 545 LNAFAAKTWHAAPLLAGGDVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADL 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 717 MEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAG 796
Cdd:PRK11905 625 MEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAG 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 797 NSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqGR 876
Cdd:PRK11905 705 NTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRS---GP 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 877 PTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDI 956
Cdd:PRK11905 782 PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDV 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 957 GPVIDAEAKENIERHIQSLRAKGRTVFQAvrensEDAREWQSGTFIPPTLIELESFDELKKEVFGPVLHVVRYNRNELDQ 1036
Cdd:PRK11905 862 GPVIDAEAQANIEAHIEAMRAAGRLVHQL-----PLPAETEKGTFVAPTLIEIDSISDLEREVFGPVLHVVRFKADELDR 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1037 LVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLsSRPQN 1116
Cdd:PRK11905 937 VIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLV-REAPT 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1117 AVGTTLARQDAErPLDAQLKTLLEKplnalqqwaAGRPELQALCQQYRELAQAGTQRLLPGPTGERNTLTFIPRDRVLCV 1196
Cdd:PRK11905 1016 PIPPAHESVDTD-AAARDFLAWLDK---------EGKAALAAAARDARARSALGLEQELPGPTGESNLLSLHPRGRVLCV 1085
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1197 ADNEQDALIQLAAVTAVGCEILWPESALHRELAKKLPREVSERLHFAkPEMLTAQAFDAVIYHGDSDQLRELCEQVAARD 1276
Cdd:PRK11905 1086 ADTEEALLRQLAAALATGNVAVVAADSGLAAALADLPGLVAARIDWT-QDWEADDPFAGALLEGDAERARAVRQALAARP 1164
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 1588278917 1277 GAIISVQGfARGESNLLLERLYIERSLSVNTAAAGGNASLMTIG 1320
Cdd:PRK11905 1165 GAIVPLIA-AEPTDAYDLARLVEERSVSINTTAAGGNASLMALG 1207
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
82-1317 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1567.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 82 AEQILPQSVTRASITAAYRRAETDAVPMLLEQARLPQPLAEQAHKLAYQLAEKLRNQKTASGRAGMVQSLLQEFSLSSQE 161
Cdd:COG4230 1 APFALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 162 GVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNE--TSLSRSLNRIIGKS 239
Cdd:COG4230 81 SEALALLLLALLLLALAATRDAAARDDDDKGDGASHLGSSSSSSSSAAAATLLLLGLLLLTALEssLSLASGLLRLLGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 240 GEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRG 319
Cdd:COG4230 161 GRPGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARKREYYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 320 IYEGPGISIKLSALHPRYSRAQYDRVMDELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGI 399
Cdd:COG4230 241 GGPGPSISSSLSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 400 GFVI----QAYQKRCPFVIDSLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLA 475
Cdd:COG4230 321 GGGVgqavQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 476 VPSLIYPQFATHNAHTLAAIyqlagqNYYPGQYEFQCLHGMGEPLYEQVVgkVADGKLNRPCRIYAPVGTHETLLAYLVR 555
Cdd:COG4230 401 AQPAFAPQFATHAAATAAAA------AAAGGGGEFEFQCLHGMGEYLYDQ--VGRGKLGRPCRIYAPVGSHEDLLAYLVR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 556 RLLENGANTSFVNRIADTTLPLDELVADPVSAVEKLarqegqAGLPHPKIPLPRDLYGKGRSNSAGLDLANEHRLASLSS 635
Cdd:COG4230 473 RLLENGANSSFVNRIADEDVPVEELIADPVEKARAL------GGAPHPRIPLPRDLYGPERRNSAGLDLSDEAVLAALSA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 636 SLLNSALHKWQALPALEHPVMAGELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAV 715
Cdd:COG4230 547 ALAAAAEKQWQAAPLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAAD 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 716 LMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALA 794
Cdd:COG4230 627 LLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTvLRGRGVFVCISPWNFPLAIFTGQVAAALA 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 795 AGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRldaQ 874
Cdd:COG4230 707 AGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR---D 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 875 GRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTT 954
Cdd:COG4230 784 GPIVPLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLST 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 955 DIGPVIDAEAKENIERHIQSLRAKGRTVFQAVRensedAREWQSGTFIPPTLIELESFDELKKEVFGPVLHVVRYNRNEL 1034
Cdd:COG4230 864 DVGPVIDAEARANLEAHIERMRAEGRLVHQLPL-----PEECANGTFVAPTLIEIDSISDLEREVFGPVLHVVRYKADEL 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1035 DQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSRP 1114
Cdd:COG4230 939 DKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERT 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1115 qNAVGTTLARQDAerpldaqlktllekPLNALQQWaagrpelqalcqqyreLAQAGTQRLLPGPTGERNTLTFIPRDRVL 1194
Cdd:COG4230 1019 -VTVNTTAAGGNA--------------SLLALGDW----------------LASLLGALTLPGPTGERNTLTLRPRGRVL 1067
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1195 CVADNEQDALIQLAAVTAVGCEILWPESALHRELAKKLprevserlhfakpemltAQAFDAVIYHGdsdQLRELCEQVAA 1274
Cdd:COG4230 1068 CLADSLEALLAQLAAALATGNRAVVAADLALAGLPAVL-----------------LPPFDAVLFEG---RLRALRQALAA 1127
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|...
gi 1588278917 1275 RDGAIISVQGFArgesnLLLERLYIErslsvntaaAGGNASLM 1317
Cdd:COG4230 1128 RDGAIVPVIDAG-----YDLERLLEE---------AGGNASLM 1156
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
79-1113 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1548.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 79 LEFAEQILPQSVTRASITAAYRRAETDAVPMLLEQARLPQPLAEQAHKLAYQLAEKLRNQKtasGRAGMVQSLLQEFSLS 158
Cdd:PRK11904 1 LLGIYILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKK---KKLGGIDAFLQEYSLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 159 SQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVS--THNETSLSRSLNRII 236
Cdd:PRK11904 78 TEEGIALMCLAEALLRIPDAATADALIRDKLSGADWKKHLGRSDSLFVNASTWGLMLTGKVVKldKKADGTPSGVLKRLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 237 GKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASN 316
Cdd:PRK11904 158 NRLGEPVIRKAMRQAMKIMGKQFVLGRTIEEALKRARSARNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 317 GRGIYEGPGISIKLSALHPRYSRAQYDRVMDELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGW 396
Cdd:PRK11904 238 GADLPARPGISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 397 NGIGFVIQAYQKRCPFVIDSLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAV 476
Cdd:PRK11904 318 GGFGLAVQAYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 477 PSLIYPQFATHNAHTLAAIYQLAGQnyypGQYEFQCLHGMGEPLYEQVVgkvadGKLNRPCRIYAPVGTHETLLAYLVRR 556
Cdd:PRK11904 398 RGAIYPQFATHNAHTVAAILEMAGH----RGFEFQRLHGMGEALYDALL-----DAPGIPCRIYAPVGSHKDLLPYLVRR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 557 LLENGANTSFVNRIADTTLPLDELVADPVSAVEKLARqegqagLPHPKIPLPRDLYGKGRSNSAGLDLANEHRLASLSSS 636
Cdd:PRK11904 469 LLENGANSSFVHRLVDPDVPIEELVADPVEKLRSFET------LPNPKIPLPRDIFGPERKNSKGLNLNDRSELEPLAAA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 637 LLNSALHKWQALPaleHPVMAGELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVL 716
Cdd:PRK11904 543 IAAFLEKQWQAGP---IINGEGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADL 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 717 MEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPlGPV--------------VCISPWNFPL 782
Cdd:PRK11904 620 LEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLP-GPTgesnelrlhgrgvfVCISPWNFPL 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 783 AIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATL 862
Cdd:PRK11904 699 AIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARI 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 863 LQRNIASRldaQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMG 942
Cdd:PRK11904 779 INRTLAAR---DGPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMA 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 943 ECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAvrensEDAREWQSGTFIPPTLIELESFDELKKEVFGP 1022
Cdd:PRK11904 856 ELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQL-----PLPAGTENGHFVAPTAFEIDSISQLEREVFGP 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1023 VLHVVRYNRNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGG 1102
Cdd:PRK11904 931 ILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGG 1010
|
1050
....*....|.
gi 1588278917 1103 PLYLYRLLSSR 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: 841.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 610 DLYGKGRSNSAGLDLANEHRLASLSSSLLNSALHKWQALPALEH-PVMAGELQAVINPAEPKDIVGHVREAHPEEIELAL 688
Cdd:TIGR01238 1 DLYGEGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHsYKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 689 TSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRP 768
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 769 LGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERV 848
Cdd:TIGR01238 161 RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 849 RGVMFTGSTEVATLLQRNIASRLDAQGrptPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEE 928
Cdd:TIGR01238 241 AGVAFTGSTEVAQLINQTLAQREDAPV---PLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 929 IADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAVRENSedaREWQSGTFIPPTLIE 1008
Cdd:TIGR01238 318 VADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDS---RACQHGTFVAPTLFE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1009 LESFDELKKEVFGPVLHVVRYNRNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPF 1088
Cdd:TIGR01238 395 LDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPF 474
|
490 500
....*....|....*....|....*.
gi 1588278917 1089 GGEGLSGTGPKAGGPLYLYRLLSSRP 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: 688.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 114 ARLPQPLAEQAHKLAYQLAEKLRNQktasgRAGMVQSLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISngn 193
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIRAA-----PEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 194 wqshigRSPSLFVNAATWGLLFTgklvsthnetslsrslnrIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANAR 273
Cdd:COG0506 75 ------KSPSFLVNASTWGLMLT------------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAAR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 274 KLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASngrgiYEGPGISIKLSALHPRYSRAQYDRVMDELYPRL 353
Cdd:COG0506 131 KLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALEAIGAAG-----VDRPGVSVKLSALGPRYSPAQRERVVEELLERL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 354 KSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDSLIDLATRSRRRLMIRLV 433
Cdd:COG0506 206 RPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 434 KGAYWDSEIKRAQMDGLeGYPVYTRKVYTDVSYLACAKKLLAVPSLIYPQFATHNAHTLAAIYQLAGQ-NYYPGQYEFQC 512
Cdd:COG0506 286 KGAYWDPEIVRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAGDAIYPQFATHNARTIAAALALAGErGRPPDRFEFQM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 513 LHGMGEPLYEQVVgKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTTLPLDELVADPVsaveklA 592
Cdd:COG0506 365 LYGMGEDLQRALA-AVDGGRLLLYCPVVAPVGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPR------F 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 593 RQEGQAGLPHPKIPLPRDLYGKGRSNSAGLDLANEHRLASLSSSLLNSALHKWQALPALEhPVMAGELQAVINPAEPKDI 672
Cdd:COG0506 438 LAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAALAAAAAAAAALAAAAAGA-AAAAAAAAVAVVPAAAAAV 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 673 VGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHY 752
Cdd:COG0506 517 VAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAA 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 753 YAGQVRDDFDNETHRP---------LGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGV 823
Cdd:COG0506 597 AAAAAAARAAAPPPPPpgglvallpLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLL 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 824 PPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAQGRPTPLIAETGGMNAMIVDSSALTEQVVI 903
Cdd:COG0506 677 LGGAGGGVLVLGAGGGAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAV 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 904 DVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVF 983
Cdd:COG0506 757 AASAAASASASASLLSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLL 836
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 984 QAVRENSEDAREWqsgtFIPPTLIELESFDELKKEVFGPVLHVVRYNRNELDQLVEQINASGYGLTLGVHTRIDETIAQV 1063
Cdd:COG0506 837 PGGGPLVPGLLTA----PLLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGG 912
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1064 TGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSRPQNAVGTTLA 1123
Cdd:COG0506 913 RVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAA 972
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
643-1128 |
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: 671.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 643 HKWQALPAL-EHPVMAGELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQM 721
Cdd:cd07125 29 KEWEAIPIInGEETETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 722 QTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFD-----------NETH-RPLGPVVCISPWNFPLAIFTGQI 789
Cdd:cd07125 109 GELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSdpelpgptgelNGLElHGRGVFVCISPWNFPLAIFTGQI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 790 AAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIAS 869
Cdd:cd07125 189 AAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 870 RldaQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNP 949
Cdd:cd07125 269 R---DGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 950 GRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAVRENSEdarewqsGTFIPPTLIELESFDELKKEVFGPVLHVVRY 1029
Cdd:cd07125 346 WDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGN-------GYFVAPGIIEIVGIFDLTTEVFGPILHVIRF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1030 NRNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRL 1109
Cdd:cd07125 419 KAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRF 498
|
490
....*....|....*....
gi 1588278917 1110 LSSRpQNAVGTTLARQDAE 1128
Cdd:cd07125 499 GNEK-TVSLNTTAAGGNPS 516
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
644-1111 |
3.79e-148 |
|
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: 457.81 E-value: 3.79e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 644 KWQALPAL--EHPVMAGELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQM 721
Cdd:cd07083 15 FGRAYPLVigGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 722 QTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRD------------DFDNET-HRPLGPVVCISPWNFPLAIFTGQ 788
Cdd:cd07083 95 RELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRlrypavevvpypGEDNESfYVGLGAGVVISPWNFPVAIFTGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 789 IAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIA 868
Cdd:cd07083 175 IVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 869 SRLDAQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGN 948
Cdd:cd07083 255 RLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 949 PGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAVRENSEdarewqsGTFIPPTLIELESFDE--LKKEVFGPVLHV 1026
Cdd:cd07083 335 PEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGE-------GYFVAPTVVEEVPPKAriAQEEIFGPVLSV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1027 VRYNRNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYL 1106
Cdd:cd07083 408 IRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYL 487
|
....*
gi 1588278917 1107 YRLLS 1111
Cdd:cd07083 488 RRFLE 492
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
268-569 |
3.51e-147 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 447.32 E-value: 3.51e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 268 ALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMD 347
Cdd:pfam01619 1 ALKTIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 348 ELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDSLIDLATRSRRR 427
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 428 LMIRLVKGAYWDSEIKRAQMdGLEGYPVYTRKVYTDVSYLACAKKLLAVPSLIYPQFATHNAHTLAAIYQLAGQ-NYYPG 506
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLENHDRIYPQFATHNARSVAAALALAEElGIPPR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588278917 507 QYEFQCLHGMGEPLYEQVVGKvadgklNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNR 569
Cdd:pfam01619 240 RFEFQQLYGMGDNLSFALVAA------GYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
654-1116 |
2.17e-131 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 413.93 E-value: 2.17e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 654 PVMAGELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAG 733
Cdd:cd07124 41 EVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 734 KTFSNAIAEVREAVDFLHYYAGQV----------RDDFDNETH-RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07124 121 KNWAEADADVAEAIDFLEYYAREMlrlrgfpvemVPGEDNRYVyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 803 PAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAQGRPTPLIA 882
Cdd:cd07124 201 PAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 883 ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDA 962
Cdd:cd07124 281 EMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 963 EAKENIERHIQSLRAKGRtvfqaVRENSEDAREWQSGTFIPPTLIE-LESFDEL-KKEVFGPVLHVVRYnrNELDQLVEQ 1040
Cdd:cd07124 361 GARDRIRRYIEIGKSEGR-----LLLGGEVLELAAEGYFVQPTIFAdVPPDHRLaQEEIFGPVLAVIKA--KDFDEALEI 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1588278917 1041 INASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLyrLLSSRPQN 1116
Cdd:cd07124 434 ANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYL--LQFMQPKT 507
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
657-1102 |
4.07e-126 |
|
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: 398.34 E-value: 4.07e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:COG1012 19 SGETFDVINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVREAVDFLHYYAGQVR-----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:COG1012 98 AEARGEVDRAADFLRYYAGEARrlygetipsdaPGTRAYVRRePLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAET 884
Cdd:COG1012 178 EQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL------KRVTLEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEA 964
Cdd:COG1012 252 GGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 965 KENIERHIQSLRAKGRTVfqaVRENseDAREWQSGTFIPPTLIE-----LESFDElkkEVFGPVLHVVRYnrNELDQLVE 1039
Cdd:COG1012 332 LERVLAYIEDAVAEGAEL---LTGG--RRPDGEGGYFVEPTVLAdvtpdMRIARE---EIFGPVLSVIPF--DDEEEAIA 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588278917 1040 QINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1102
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGR 463
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
657-1106 |
2.94e-118 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 376.87 E-value: 2.94e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAePKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:pfam00171 5 ESETIEVINPA-TGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVREAVDFLHYYAGQVR----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:pfam00171 84 AEARGEVDRAIDVLRYYAGLARrldgetlpsdPGRLAYTRRePLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 806 QTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETG 885
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAK 965
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 966 ENIERHIQSLRAKGRTVFQAVRENSEDarewqsGTFIPPTLIE-LESFDEL-KKEVFGPVLHVVRYnrNELDQLVEQINA 1043
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAGLDN------GYFVEPTVLAnVTPDMRIaQEEIFGPVLSVIRF--KDEEEAIEIAND 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588278917 1044 SGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVqPFGGEGLSGTGpKAGGPLYL 1106
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL-PFGGFKQSGFG-REGGPYGL 450
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
687-1108 |
1.16e-109 |
|
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: 352.28 E-value: 1.16e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 687 ALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRD------- 759
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRlhgevip 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 760 ----DFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGR 834
Cdd:cd07078 83 spdpGELAIVrREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 835 GETVGAALTTDERVRGVMFTGSTEVATLLQRNiasrldAQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAG 914
Cdd:cd07078 163 GDEVGAALASHPRVDKISFTGSTAVGKAIMRA------AAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 915 QRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVfqaVRENSEDAR 994
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKL---LCGGKRLEG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 995 EwqSGTFIPPTLIELESFDEL--KKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNL 1072
Cdd:cd07078 314 G--KGYFVPPTVLTDVDPDMPiaQEEIFGPVLPVIPF--KDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTV 389
|
410 420 430
....*....|....*....|....*....|....*.
gi 1588278917 1073 YVNRNMVGAVVGvQPFGGEGLSGTGpKAGGPLYLYR 1108
Cdd:cd07078 390 WINDYSVGAEPS-APFGGVKQSGIG-REGGPYGLEE 423
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
663-1107 |
1.62e-109 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 355.01 E-value: 1.62e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:PRK03137 54 SINPANKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAGQV-----------RDDFDNETH-RPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:PRK03137 134 TAEAIDFLEYYARQMlkladgkpvesRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAQGRPTPLIAETGGMNAM 890
Cdd:PRK03137 214 AAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRlTTDIGPVIDAEAKENIER 970
Cdd:PRK03137 294 VVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKGRTVFQAVRENSEdarewqsGTFIPPTLI-ELESFDEL-KKEVFGPVLHVVRYnrNELDQLVEQINASGYGL 1048
Cdd:PRK03137 373 YIEIGKEEGRLVLGGEGDDSK-------GYFIQPTIFaDVDPKARImQEEIFGPVVAFIKA--KDFDHALEIANNTEYGL 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1588278917 1049 TLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLY 1107
Cdd:PRK03137 444 TGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSGTDSKAGGPDYLL 502
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
664-1113 |
5.75e-106 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 345.31 E-value: 5.75e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 664 INPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEV 743
Cdd:TIGR01237 51 INPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 744 REAVDFLHYYA--------GQVRDDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:TIGR01237 131 AEAIDFMEYYArqmielakGKPVNSREGETNQyvytPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 812 AQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAQGRPTPLIAETGGMNAMI 891
Cdd:TIGR01237 211 AKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 892 VDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERH 971
Cdd:TIGR01237 291 VDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEY 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 972 IQSLRAKGRTVFQAVRENSEdarewqsGTFIPPTLI-ELESFDEL-KKEVFGPVLHVVRYnrNELDQLVEQINASGYGLT 1049
Cdd:TIGR01237 371 IEIGKAEGRLVSGGCGDDSK-------GYFIGPTIFaDVDRKARLaQEEIFGPVVAFIRA--SDFDEALEIANNTEYGLT 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1588278917 1050 LGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSR 1113
Cdd:TIGR01237 442 GGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAK 505
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
655-1103 |
1.22e-89 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 298.78 E-value: 1.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 655 VMAGELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGK 734
Cdd:cd07097 10 VAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 735 TFSNAIAEVREAVDFLHYYAGQ-----------VRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAK 802
Cdd:cd07097 90 TLPEARGEVTRAGQIFRYYAGEalrlsgetlpsTRPGVEVETTRePLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 803 PAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASRLDAQGRPTPLia 882
Cdd:cd07097 170 PAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVG----RRIAAAAAARGARVQL-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 883 ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDA 962
Cdd:cd07097 244 EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 963 EAKENIERHIQSLRAKG-RTVFQAVRENSEDarewqSGTFIPPTLielesFDEL-------KKEVFGPVLHVVRYnrNEL 1034
Cdd:cd07097 324 RQLEKDLRYIEIARSEGaKLVYGGERLKRPD-----EGYYLAPAL-----FAGVtndmriaREEIFGPVAAVIRV--RDY 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1588278917 1035 DQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1103
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-PFGGRKGSSYGPREQGE 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
663-1097 |
3.14e-87 |
|
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: 291.26 E-value: 3.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAePKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:cd07103 1 VINPA-TGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAGQVR--------DDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07103 80 VDYAASFLEWFAEEARriygrtipSPAPGKrilvIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGmNA- 889
Cdd:cd07103 160 ALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTV------KRVSLELGG-NAp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 890 MIVDSSALTEQVVIDVLASAFDSAGQRC-SALRILClQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENI 968
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCvCANRIYV-HESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 969 ERHIQSLRAKGRTVfqavreNSEDAREWQSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGY 1046
Cdd:cd07103 312 EALVEDAVAKGAKV------LTGGKRLGLGGYFYEPTVLTdvTDDMLIMNEETFGPVAPIIPF--DTEDEVIARANDTPY 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1047 GLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:cd07103 384 GLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKESGLG 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
696-1113 |
8.81e-87 |
|
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: 287.20 E-value: 8.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 696 PIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRD-----------DFDNE 764
Cdd:cd06534 8 KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKlggpelpspdpGGEAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 765 T-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALT 843
Cdd:cd06534 88 VrREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 844 TDERVRGVMFTGSTEVATLLQRNiasrldAQGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRIL 923
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKA------AAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 924 CLQEEIADhtltmlrgamgecrmgnpgrlttdigPVIDaeakenierhiqslraKGRTVFQAVRENSEDAREwqsgtfip 1003
Cdd:cd06534 242 LVHESIYD--------------------------EFVE----------------KLVTVLVDVDPDMPIAQE-------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1004 ptlielesfdelkkEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVV 1083
Cdd:cd06534 272 --------------EIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP 335
|
410 420 430
....*....|....*....|....*....|
gi 1588278917 1084 GvQPFGGEGLSGTGpKAGGPLYLYRLLSSR 1113
Cdd:cd06534 336 E-APFGGVKNSGIG-REGGPYGLEEYTRTK 363
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
662-1097 |
1.58e-85 |
|
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: 286.94 E-value: 1.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 662 AVINPAEPKdIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIA 741
Cdd:cd07145 2 EVRNPANGE-VIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYYAGQVR---------DDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07145 81 EVERTIRLFKLAAEEAKvlrgetipvDAYEYNERRiaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 806 QTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLlqrnIASRldAQGRPTPLIAETG 885
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLL----IASK--AGGTGKKVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAK 965
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 966 ENIERHI-QSLRAKGRTVFQAVRensedarewQSGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYnrNELDQLVEQIN 1042
Cdd:cd07145 315 ERMENLVnDAVEKGGKILYGGKR---------DEGSFFPPTVLENDTPDMivMKEEVFGPVLPIAKV--KDDEEAVEIAN 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1588278917 1043 ASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNR-------NMvgavvgvqPFGGEGLSGTG 1097
Cdd:cd07145 384 STEYGLQASVFTNDINRALKVARELEAGGVVINDstrfrwdNL--------PFGGFKKSGIG 437
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
664-1103 |
8.91e-84 |
|
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: 282.70 E-value: 8.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 664 INPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEV 743
Cdd:cd07131 19 RNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 744 REAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07131 99 QEAIDMAQYAAGEGRrlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 812 AQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRniasrldAQGRPTPLIA-ETGGMNAM 890
Cdd:cd07131 179 LKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE-------TCARPNKRVAlEMGGKNPI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIER 970
Cdd:cd07131 252 IVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKGRTVFQAvrENSEDAREWQSGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYnrNELDQLVEQINASGYGL 1048
Cdd:cd07131 332 YNEIGKEEGATLLLG--GERLTGGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEV--SSLEEAIEIANDTEYGL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1588278917 1049 TLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAGGP 1103
Cdd:cd07131 408 SSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVHL-PFGGVKKSGNGHREAGT 461
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
657-1101 |
6.36e-83 |
|
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: 280.22 E-value: 6.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAEPKDIVGhVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:cd07086 11 GGETFTSRNPANGEPIAR-VFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKIL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07086 90 PEGLGEVQEMIDICDYAVGLSRmlygltipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLIAAQGVAILLEA----GVPPGVIQLLPGRGEtVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqGRPtpl 880
Cdd:cd07086 170 ETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF---GRV--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 881 IAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVI 960
Cdd:cd07086 243 LLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 961 DAEAKENIERHIQSLRAKGRTVF--QAVRENSEDarewqsGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYnrNELDQ 1036
Cdd:cd07086 323 NQAAVEKYLNAIEIAKSQGGTVLtgGKRIDGGEP------GNYVEPTIVTGVTDDAriVQEETFAPILYVIKF--DSLEE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1588278917 1037 LVEQINASGYGLTLGVHT---RIDETIAQVTGSaKVGNLYVNRNMVGAVVGVqPFGGEGLSGTGPKAG 1101
Cdd:cd07086 395 AIAINNDVPQGLSSSIFTedlREAFRWLGPKGS-DCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESG 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
663-1101 |
8.68e-77 |
|
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: 262.10 E-value: 8.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKdIVGHVREAHPEEIELALTSAVN--NAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAI 740
Cdd:cd07114 1 SINPATGE-PWARVPEASAADVDRAVAAARAafEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 741 AEVREAVDFLHYYAG-----------QVRDDFDNET-HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07114 80 AQVRYLAEWYRYYAGladkiegavipVDKGDYLNFTrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 809 LIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMN 888
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENL------APVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 889 AMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENI 968
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 969 ERHIQSLRAKGRTVfqAVRENSEDAREWQSGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYnRNElDQLVEQINASGY 1046
Cdd:cd07114 314 ERYVARAREEGARV--LTGGERPSGADLGAGYFFEPTILADVTNDMriAQEEVFGPVLSVIPF-DDE-EEAIALANDSEY 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1588278917 1047 GLTLGVHTRiDETIA-QVTGSAKVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07114 390 GLAAGIWTR-DLARAhRVARAIEAGTVWV--NTYRALSPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
658-1097 |
7.34e-76 |
|
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: 259.81 E-value: 7.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKdIVGHVREAHPEEIELALTSAVNNAPIWFAT-PPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:cd07082 15 GKTIEVYSPIDGE-VIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVREAVDFLHYYAGQVRD------DFDNETHR----------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07082 94 KDALKEVDRTIDYIRDTIEELKRldgdslPGDWFPGTkgkiaqvrrePLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 801 AKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRnIASRLdaqgrptPL 880
Cdd:cd07082 174 FKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK-QHPMK-------RL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 881 IAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVI 960
Cdd:cd07082 246 VLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 961 DAEAKENIERHIQSLRAKGRTVFQavrensEDAREwqSGTFIPPTLIELESfDELK---KEVFGPVLHVVRYnrNELDQL 1037
Cdd:cd07082 326 DPKSADFVEGLIDDAVAKGATVLN------GGGRE--GGNLIYPTLLDPVT-PDMRlawEEPFGPVLPIIRV--NDIEEA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1038 VEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRnMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07082 395 IELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-KCQRGPDHFPFLGRKDSGIG 453
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
658-1113 |
1.96e-75 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 260.21 E-value: 1.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQ------MQTLIGilvre 731
Cdd:cd07123 45 GNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKyryelnAATMLG----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 732 AGKTFSNA-IAEVREAVDFLH---YYAGQVRDD---------FDNETHRPL-GPVVCISPWNFPlAIfTGQIAAALA-AG 796
Cdd:cd07123 120 QGKNVWQAeIDAACELIDFLRfnvKYAEELYAQqplsspagvWNRLEYRPLeGFVYAVSPFNFT-AI-GGNLAGAPAlMG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 797 NSVLAKPAEqTPLIAAQGV-AILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAQg 875
Cdd:cd07123 198 NVVLWKPSD-TAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRY- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 876 RPTP-LIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTT 954
Cdd:cd07123 276 RTYPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 955 DIGPVIDAEAKENIERHIQslRAKGRTVFQAVRENSEDAREwqsGTFIPPTLIELE--SFDELKKEVFGPVLHVVRYNRN 1032
Cdd:cd07123 356 FMGAVIDEKAFDRIKGYID--HAKSDPEAEIIAGGKCDDSV---GYFVEPTVIETTdpKHKLMTEEIFGPVLTVYVYPDS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1033 ELDQLVEQIN-ASGYGLTLGVHTRIDETIAQVTGSAK--VGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRL 1109
Cdd:cd07123 431 DFEETLELVDtTSPYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGSPLNLLRW 510
|
....
gi 1588278917 1110 LSSR 1113
Cdd:cd07123 511 VSPR 514
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
661-1097 |
2.69e-75 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 257.52 E-value: 2.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 661 QAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAI 740
Cdd:cd07149 1 IEVISPYD-GEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 741 AEVREAVDFLHYYA-------GQV---------RDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07149 80 KEVDRAIETLRLSAeeakrlaGETipfdaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRldaqgrptPLIAET 884
Cdd:cd07149 160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--------KVTLEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAE 963
Cdd:cd07149 232 GSNAAVIVDADADLEKAVERCVSGAFANAGQVCiSVQRIF-VHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 964 AKENIERHIQSLRAKGRTVFQAVRENsedarewqsGTFIPPTLieLESFDE----LKKEVFGPVLHVVRYnrNELDQLVE 1039
Cdd:cd07149 311 EAERIEEWVEEAVEGGARLLTGGKRD---------GAILEPTV--LTDVPPdmkvVCEEVFAPVVSLNPF--DTLDEAIA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588278917 1040 QINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1097
Cdd:cd07149 378 MANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINdsstfR------VDHMPYGGVKESGTG 434
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
663-1097 |
2.30e-73 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 252.10 E-value: 2.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIA- 741
Cdd:cd07093 1 NFNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYYAG----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07093 80 DIPRAAANFRFFADyilqldgesyPQDGGALNYVLRqPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAM 890
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNL------KPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASAFDSAGQRCSA-LRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIE 969
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAgSRIL-VQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 970 RHIQSLRAKGRTVfqAVRENSEDAREWQSGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYnrNELDQLVEQINASGYG 1047
Cdd:cd07093 313 GYVELARAEGATI--LTGGGRPELPDLEGGYFVEPTVITGLDNDSrvAQEEIFGPVVTVIPF--DDEEEAIELANDTPYG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1048 LTLGVHTRiDETIAQVTGSA-KVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:cd07093 389 LAAYVWTR-DLGRAHRVARRlEAGTVWVNCWLVRDL--RTPFGGVKASGIG 436
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
657-1076 |
4.08e-73 |
|
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: 251.80 E-value: 4.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:cd07088 11 SGETIDVLNPAT-GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVREAVDFLHYYAGQVR--------DDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07088 90 SLARVEVEFTADYIDYMAEWARriegeiipSDRPNENififKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAET 884
Cdd:cd07088 170 EETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI------TKVSLEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEA 964
Cdd:cd07088 244 GGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 965 KENIERHIQSLRAKGRTVfqaVRENSEDAREwqSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQIN 1042
Cdd:cd07088 324 LDKVEEMVERAVEAGATL---LTGGKRPEGE--KGYFYEPTVLTnvRQDMEIVQEEIFGPVLPVVKF--SSLDEAIELAN 396
|
410 420 430
....*....|....*....|....*....|....
gi 1588278917 1043 ASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNR 1076
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNELEFGETYINR 430
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
683-1095 |
5.10e-72 |
|
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: 247.57 E-value: 5.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 683 EIELALTSAVNNAPIWFATPPQERAAILERAAVLME---DQMQTLIGilvREAGKTFSNAIAEVRE-------AVDFLHY 752
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKankEELARLIS---RETGKPLWEAQTEVAAmagkidiSIKAYHE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 753 YAGQVRDDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVI 828
Cdd:cd07095 78 RTGERATPMAQGravlRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 829 QLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLQRNIAsrldaqGRPTPLIA-ETGGMNAMIVDSSALTEQVVIDVLA 907
Cdd:cd07095 158 NLVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFA------GRPGKILAlEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 908 SAFDSAGQRCS-ALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAV 986
Cdd:cd07095 231 SAFLTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 987 RensedaREWQSGTFIPPTLIELESFDEL-KKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTG 1065
Cdd:cd07095 311 E------RLVAGTAFLSPGIIDVTDAADVpDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLA 382
|
410 420 430
....*....|....*....|....*....|
gi 1588278917 1066 SAKVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:cd07095 383 RIRAGIVNWNRPTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
683-1103 |
1.48e-71 |
|
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: 246.29 E-value: 1.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 683 EIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVR---- 758
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRrpeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 759 ----DDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP----LIAAQgvaILLEAGVPPG 826
Cdd:cd07104 81 eilpSDVPGKESMvrrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtggLLIAE---IFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 827 VIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASrldAQGRPTPLIA-ETGGMNAMIVDSSALTEQVVIDV 905
Cdd:cd07104 158 VLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIGE---LAGRHLKKVAlELGGNNPLIVLDDADLDLAVSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 906 LASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFq 984
Cdd:cd07104 231 AFGAFLHQGQICmAAGRIL-VHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLL- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 985 avrensedAREWQSGTFIPPTLI-----ELESFDElkkEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDET 1059
Cdd:cd07104 309 --------TGGTYEGLFYQPTVLsdvtpDMPIFRE---EIFGPVAPVIPF--DDDEEAVELANDTEYGLSAAVFTRDLER 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1588278917 1060 IAQVTGSAKVGNLYVNRNMV--GAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07104 376 AMAFAERLETGMVHINDQTVndEPHV---PFGGVKASGGG-RFGGP 417
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
662-1097 |
2.25e-70 |
|
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: 243.49 E-value: 2.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 662 AVINPAEPKdIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIA 741
Cdd:cd07094 2 DVHNPYDGE-VIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYYAGQVR---------DDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07094 81 EVDRAIDTLRLAAEEAErirgeeiplDATQGSDNRlawtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 806 QTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASrldaqgrpTPLIAETG 885
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--------KRIALELG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAK 965
Cdd:cd07094 233 GNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 966 ENIERHI-QSLRAKGRTVFQAVREnsedarewqsGTFIPPTLIELESFDEL--KKEVFGPVLHVVRYnrNELDQLVEQIN 1042
Cdd:cd07094 313 ERVERWVeEAVEAGARLLCGGERD----------GALFKPTVLEDVPRDTKlsTEETFGPVVPIIRY--DDFEEAIRIAN 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1588278917 1043 ASGYGLTLGVHTRiDETIAqvtgsakvgnLYVNRNM-VGAVV---------GVQPFGGEGLSGTG 1097
Cdd:cd07094 381 STDYGLQAGIFTR-DLNVA----------FKAAEKLeVGGVMvndssafrtDWMPFGGVKESGVG 434
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
657-1097 |
9.47e-70 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 242.81 E-value: 9.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAePKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:cd07085 14 TTEWLDVYNPA-TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVR---EAVDF--------LHYYAGQVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07085 93 ADARGDVLrglEVVEFacsiphllKGEYLENVARGIDTYSYRqPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAaLTTDERVRGVMFTGSTEVATLLQRNIAS---RLDAQGrptpli 881
Cdd:cd07085 173 ERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNA-LLDHPDIKAVSFVGSTPVGEYIYERAAAngkRVQALG------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 882 aetGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVID 961
Cdd:cd07085 246 ---GAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVIS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 962 AEAKENIERHIQSlrakgrtvfqAVRENSE---DARE-----WQSGTFIPPTLI-----ELESFDElkkEVFGPVLHVVR 1028
Cdd:cd07085 323 PAAKERIEGLIES----------GVEEGAKlvlDGRGvkvpgYENGNFVGPTILdnvtpDMKIYKE---EIFGPVLSIVR 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1029 YnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNrnmVG-AV-VGVQPFGGEGLSGTG 1097
Cdd:cd07085 390 V--DTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPiPVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
664-1097 |
1.51e-69 |
|
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: 241.36 E-value: 1.51e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 664 INPAEPKDiVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEV 743
Cdd:cd07099 1 RNPATGEV-LGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 744 REAVDFLHYYAGQVRDDFDNE---------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAPRkvptgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 809 LIAAQGVAILLEAGVPPGVIQLLPGRGETvGAALtTDERVRGVMFTGSteVATllQRNIASRldAQGRPTPLIAETGGMN 888
Cdd:cd07099 160 LVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAAL-IDAGVDKVAFTGS--VAT--GRKVMAA--AAERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 889 AMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENI 968
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 969 ERHIQSLRAKGRTVFqavrenSEDAREWQSGTFIPPTLI--ELESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGY 1046
Cdd:cd07099 312 RRHVDDAVAKGAKAL------TGGARSNGGGPFYEPTVLtdVPHDMDVMREETFGPVLPVMPV--ADEDEAIALANDSRY 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1047 GLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07099 384 GLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGG 434
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
658-1097 |
3.41e-69 |
|
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: 240.58 E-value: 3.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKdIVGHVREAHPEEIELALTSA--VNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKT 735
Cdd:cd07112 1 GETFATINPATGR-VLAEVAACDAADVDRAVAAArrAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 736 FSNAIA-EVREAVDFLHYYA-------GQV----RDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07112 80 ISDALAvDVPSAANTFRWYAeaidkvyGEVaptgPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 804 AEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQrniasRLDAQGRPTPLIAE 883
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFL-----EYSGQSNLKRVWLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 884 TGGMNAMIV-DSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDA 962
Cdd:cd07112 235 CGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 963 EAKENIERHIQSLRAKGrtvfQAVRENSEDAREWQSGTFIPPTLielesFDEL-------KKEVFGPVLHVVRYNRneLD 1035
Cdd:cd07112 315 AHFDKVLGYIESGKAEG----ARLVAGGKRVLTETGGFFVEPTV-----FDGVtpdmriaREEIFGPVLSVITFDS--EE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1588278917 1036 QLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07112 384 EAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV--NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
663-1097 |
2.17e-68 |
|
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: 237.81 E-value: 2.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPkDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:cd07106 1 VINPATG-EVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAGQVRDD---FDNET------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQ 813
Cdd:cd07106 80 VGGAVAWLRYTASLDLPDeviEDDDTrrvelrRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 814 GVAILLEAgVPPGVIQLLPGRGEtVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVD 893
Cdd:cd07106 160 LGELAQEV-LPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTL------KRVTLELGGNDAAIVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 894 SSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQ 973
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 974 SLRAKGRTVfqAVRENSEDArewqSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLG 1051
Cdd:cd07106 312 DAKAKGAKV--LAGGEPLDG----PGYFIPPTIVDdpPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGAS 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1588278917 1052 VHTRiDETIAQVTGSA-KVGNLYVNRNmvGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07106 384 VWSS-DLERAEAVARRlEAGTVWINTH--GALDPDAPFGGHKQSGIG 427
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
663-1097 |
2.72e-68 |
|
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: 237.52 E-value: 2.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKDIvGHVREAHPEEIELALTSAVNNAPI-WFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIA 741
Cdd:cd07109 1 VFDPSTGEVF-ARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYYAGQVR----------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07109 80 DVEAAARYFEYYGGAADklhgetiplgPGYFVYTVRePHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAM 890
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENV------VPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGnPGRLTTDIGPVIDAEAKENIER 970
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKG-RTVFQAVREnsEDAREwqSGTFIPPTLI-ELESFDEL-KKEVFGPVLHVVRYnrNELDQLVEQINASGYG 1047
Cdd:cd07109 313 FVARARARGaRIVAGGRIA--EGAPA--GGYFVAPTLLdDVPPDSRLaQEEIFGPVLAVMPF--DDEAEAIALANGTDYG 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1048 LTLGVHTRIDETIAQVTGSAKVGNLYVNRnmVGAVVGVQ-PFGGEGLSGTG 1097
Cdd:cd07109 387 LVAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
665-1103 |
1.56e-67 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 235.30 E-value: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 665 NPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVR 744
Cdd:cd07150 5 NPAD-GSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 745 EAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAA 812
Cdd:cd07150 84 FTPELLRAAAGECRrvrgetlpsdspGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 813 QGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASRLDAQGRPTPLiaETGGMNAMIV 892
Cdd:cd07150 164 KIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVG----REIAEKAGRHLKKITL--ELGGKNPLIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 893 DSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHI 972
Cdd:cd07150 238 LADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 973 QSLRAKGRTVFqavrensedAREWQSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTL 1050
Cdd:cd07150 318 EDAVAKGAKLL---------TGGKYDGNFYQPTVLTdvTPDMRIFREETFGPVTSVIPA--KDAEEALELANDTEYGLSA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1588278917 1051 GVHTRiDETIA-QVTGSAKVGNLYVNRNMV--GAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07150 387 AILTN-DLQRAfKLAERLESGMVHINDPTIldEAHV---PFGGVKASGFG-REGGE 437
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
663-1101 |
1.63e-67 |
|
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: 235.41 E-value: 1.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNA-IA 741
Cdd:cd07115 1 TLNPAT-GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYYAG----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07115 80 DVPRAADTFRYYAGwadkiegeviPVRGPFLNYTVRePVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNiasrldAQGRPTPLIAETGGMNAM 890
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQG------AAGNLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIER 970
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKGRTVFQAvrenseDAREWQSGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYNRNEldQLVEQINASGYGL 1048
Cdd:cd07115 314 YVDVGREEGARLLTG------GKRPGARGFFVEPTIFAAVPPEMriAQEEIFGPVVSVMRFRDEE--EALRIANGTEYGL 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1588278917 1049 TLGVHTRIDETIAQVTGSAKVGNLYVnrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07115 386 AAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGSPFGGYKQSGFGREMG 436
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
663-1101 |
1.70e-66 |
|
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: 233.26 E-value: 1.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKDIvGHVREAHPEEIELALTSAVNNAPI--WFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFS-NA 739
Cdd:cd07091 23 TINPATEEVI-CQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEeSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 740 IAEVREAVDFLHYYAG----------QVRDDFDNETHR-PLGpvVC--ISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQ 806
Cdd:cd07091 102 KGDVALSIKCLRYYAGwadkiqgktiPIDGNFLAYTRRePIG--VCgqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 807 TPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIA-SRLdaqgRPTPLiaETG 885
Cdd:cd07091 180 TPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAkSNL----KKVTL--ELG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAK 965
Cdd:cd07091 254 GKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 966 ENIERHIQSLRAKGRTVFQAvrensedAREWQS-GTFIPPTLielesFDELKK-------EVFGPVLHVVRYnrNELDQL 1037
Cdd:cd07091 334 DKILSYIESGKKEGATLLTG-------GERHGSkGYFIQPTV-----FTDVKDdmkiakeEIFGPVVTILKF--KTEDEV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1588278917 1038 VEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNR-NMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQSGFGRELG 461
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
671-1103 |
2.65e-65 |
|
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: 228.72 E-value: 2.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 671 DIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFL 750
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 751 HYYA-------GQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILL 819
Cdd:cd07152 82 HEAAglptqpqGEILPSAPGRLslarRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 820 E-AGVPPGVIQLLPGRGEtVGAALTTDERVRGVMFTGSTEVAtllqRNIASrldAQGRPTPLIA-ETGGMNAMIVDSSAL 897
Cdd:cd07152 162 EeAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVG----RKVGE---AAGRHLKKVSlELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 898 TEQVVIDVLASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLR 976
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICmAAGRHL-VHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 977 AKGRTVFQAVRENsedarewqsGTFIPPTLI-----ELESFDElkkEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLG 1051
Cdd:cd07152 313 AAGARLEAGGTYD---------GLFYRPTVLsgvkpGMPAFDE---EIFGPVAPVTVF--DSDEEAVALANDTEYGLSAG 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1588278917 1052 VHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVgVQPFGGEGLSGTGPKAGGP 1103
Cdd:cd07152 379 IISRDVGRAMALADRLRTGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
657-1097 |
7.49e-64 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 225.65 E-value: 7.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAEpKDIVGHVREAHPEEIELALTSAVN--NAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGK 734
Cdd:cd07119 11 SGKTRDIINPAN-GEVIATVPEGTAEDAKRAIAAARRafDSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 735 TFSNAIAEVREAVDFLHYYAGQV--RDDFDNET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07119 90 TLRESEIDIDDVANCFRYYAGLAtkETGEVYDVpphvisrtvREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 804 AEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNiasrldAQGRPTPLIAE 883
Cdd:cd07119 170 SEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRA------AAGNVKKVALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 884 TGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAE 963
Cdd:cd07119 244 LGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 964 AKENIERHIQSLRAKGRTVFQAVRENSEDarEWQSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnRNElDQLVEQI 1041
Cdd:cd07119 324 HREKVLSYIQLGKEEGARLVCGGKRPTGD--ELAKGYFVEPTIFDdvDRTMRIVQEEIFGPVLTVERF-DTE-EEAIRLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1588278917 1042 NASGYGLTLGVHTRiDETIAQ-VTGSAKVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1097
Cdd:cd07119 400 NDTPYGLAGAVWTK-DIARANrVARRLRAGTVWINDYHPYFAEA--PWGGYKQSGIG 453
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
658-1097 |
1.69e-63 |
|
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: 224.30 E-value: 1.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAG--KT 735
Cdd:cd07138 13 TETIDVINPAT-EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGapIT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 736 FSNAiAEVREAVDFLHYYAGQVRDdFDNETHR--------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQT 807
Cdd:cd07138 92 LARA-AQVGLGIGHLRAAADALKD-FEFEERRgnslvvrePIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 808 PLiAAQGVA-ILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLD--AQgrptpliaET 884
Cdd:cd07138 170 PL-SAIILAeILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKrvAL--------EL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSAL-RILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAE 963
Cdd:cd07138 241 GGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPtRML-VPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 964 AKENIERHIQS-------LRAKGR--------------TVFQAVRENSEDAREwqsgtfipptlielesfdelkkEVFGP 1022
Cdd:cd07138 320 QFDRVQGYIQKgieegarLVAGGPgrpeglergyfvkpTVFADVTPDMTIARE----------------------EIFGP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1588278917 1023 VLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNrnmvGAVVGVQ-PFGGEGLSGTG 1097
Cdd:cd07138 378 VLSIIPY--DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
663-1100 |
1.75e-63 |
|
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: 223.78 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF-SNAIA 741
Cdd:cd07108 1 VINPAT-GQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYY---AGQVR--------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLi 810
Cdd:cd07108 80 EAAVLADLFRYFgglAGELKgetlpfgpDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAM 890
Cdd:cd07108 159 AVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRL------IPVSLELGGKSPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASA-FDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIE 969
Cdd:cd07108 233 IVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 970 RHIQS-LRAKGRTVFQAVRENSEDAREwqSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGY 1046
Cdd:cd07108 313 GYIDLgLSTSGATVLRGGPLPGEGPLA--DGFFVQPTIFSgvDNEWRLAREEIFGPVLCAIPW--KDEDEVIAMANDSHY 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1588278917 1047 GLTLGVHTRiDETIAQVTGSA-KVGNLYVNRNmVGAVVGvQPFGGEGLSGTGPKA 1100
Cdd:cd07108 389 GLAAYVWTR-DLGRALRAAHAlEAGWVQVNQG-GGQQPG-QSYGGFKQSGLGREA 440
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
148-259 |
2.43e-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: 2.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 148 VQSLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNETS 227
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKSHLGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 1588278917 228 LSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQF 259
Cdd:pfam14850 81 LAGALKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
657-1097 |
5.26e-63 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 223.80 E-value: 5.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAEPkDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:PLN02278 38 DGKTFPVYNPATG-EVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVREAVDFLHYYAGQVRDDFDN------------ETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:PLN02278 117 KEAIGEVAYGASFLEYFAEEAKRVYGDiipspfpdrrllVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLI--AAQGVAilLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgRPTPLia 882
Cdd:PLN02278 197 ELTPLTalAAAELA--LQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATV----KRVSL-- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 883 ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVID 961
Cdd:PLN02278 269 ELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCvCANRIL-VQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLIN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 962 AEAKENIERHIQSLRAKGRTVFQAvrenseDAREWQSGTFIPPTLIELESFDEL--KKEVFGPVLHVVRYNRNEldQLVE 1039
Cdd:PLN02278 348 EAAVQKVESHVQDAVSKGAKVLLG------GKRHSLGGTFYEPTVLGDVTEDMLifREEVFGPVAPLTRFKTEE--EAIA 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1588278917 1040 QINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGvqPFGGEGLSGTG 1097
Cdd:PLN02278 420 IANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGLG 475
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
672-1101 |
3.61e-61 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 216.84 E-value: 3.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 672 IVGHVREAHPEEIELALTSAVNNAPiwfATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLH 751
Cdd:cd07146 11 VVGTVPAGTEEALREALALAASYRS---TLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 752 YYAGQV-RDD-----FDNETHR----------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGV 815
Cdd:cd07146 88 FAAAEAlRDDgesfsCDLTANGkarkiftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 816 AILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASRldAQGRPTPLiaETGGMNAMIVDSS 895
Cdd:cd07146 168 DLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVG----KAIAAT--AGYKRQLL--ELGGNDPLIVMDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 896 ALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHI-QS 974
Cdd:cd07146 240 ADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVeEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 975 LRAKGRTVFQAVREnsedarewqsGTFIPPTLIELESFD-EL-KKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGV 1052
Cdd:cd07146 320 IAQGARVLLGNQRQ----------GALYAPTVLDHVPPDaELvTEETFGPVAPVIRV--KDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1588278917 1053 HTRIDETIAQVTGSAKVGNLYVNrNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
671-1101 |
1.83e-60 |
|
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: 215.82 E-value: 1.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 671 DIVGHVREAHPEEIELALTSA---VNNAPiWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNA-IAEVREA 746
Cdd:cd07142 30 EVIAHVAEGDAEDVDRAVKAArkaFDEGP-WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 747 VDFLHYYAGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQG 814
Cdd:cd07142 109 ARLFRYYAGWA-DKIHGMTlpadgphhvytlHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 815 VAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqrNIASRLDAQGRPTPLIAETGGMNAMIVDS 894
Cdd:cd07142 188 AKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVG-----KIIMQLAAKSNLKPVTLELGGKSPFIVCE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 895 SALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQS 974
Cdd:cd07142 263 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEH 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 975 LRAKGRTVfqavreNSEDAREWQSGTFIPPTLIElESFDELK---KEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLG 1051
Cdd:cd07142 343 GKEEGATL------ITGGDRIGSKGYYIQPTIFS-DVKDDMKiarDEIFGPVQSILKF--KTVDEVIKRANNSKYGLAAG 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1052 VHTRIDETIAQVTGSAKVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07142 414 VFSKNIDTANTLSRALKAGTVWVNcYDVFDASI---PFGGYKMSGIGREKG 461
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
663-1097 |
2.32e-60 |
|
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: 214.80 E-value: 2.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIW-FATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIA 741
Cdd:cd07089 1 VINPAT-EEVIGTAPDAGAADVDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 -EVREAVDFLHYYAGQVR-----DDFDNET-----------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:cd07089 80 mQVDGPIGHLRYFADLADsfpweFDLPVPAlrggpgrrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgRPTPLiaET 884
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATL----KRVLL--EL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSAL-RILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAE 963
Cdd:cd07089 234 GGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTtRLL-VPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 964 AKENIERHIQSLRAKGRTVFQAVRENSEDARewqsGTFIPPTLielesFDELK-------KEVFGPVLHVVRYnrNELDQ 1036
Cdd:cd07089 313 QRDRVEGYIARGRDEGARLVTGGGRPAGLDK----GFYVEPTL-----FADVDndmriaqEEIFGPVLVVIPY--DDDDE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588278917 1037 LVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNrnmvGAVVGV--QPFGGEGLSGTG 1097
Cdd:cd07089 382 AVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
663-1101 |
3.06e-60 |
|
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: 215.09 E-value: 3.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKdIVGHVREAHPEEIELALTSAVN--NAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAI 740
Cdd:cd07143 26 VYNPSTGK-LITKIAEATEADVDIAVEVAHAafETDWGLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 741 A-EVREAVDFLHYYAGQVRDDFDN--ET---------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:cd07143 105 RvDVQASADTFRYYGGWADKIHGQviETdikkltytrHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 809 LIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVA-TLLQRNIASRLDAqgrptpLIAETGGM 887
Cdd:cd07143 185 LSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGrKVMEAAAKSNLKK------VTLELGGK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 888 NAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKEN 967
Cdd:cd07143 259 SPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYER 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 968 IERHIQSLRAKGRTVFQAVRensedaREWQSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYNRNEldQLVEQINASG 1045
Cdd:cd07143 339 IMSYIESGKAEGATVETGGK------RHGNEGYFIEPTIFTdvTEDMKIVKEEIFGPVVAVIKFKTEE--EAIKRANDST 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1588278917 1046 YGLTLGVHTRIDETIAQVTGSAKVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07143 411 YGLAAAVFTNNINNAIRVANALKAGTVWVNcYNLLHHQV---PFGGYKQSGIGRELG 464
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
678-1101 |
1.55e-59 |
|
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: 212.20 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 678 EAHPEEIELALTSA---VNNAPiWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYA 754
Cdd:cd07118 15 EGTVEDVDAAVAAArkaFDKGP-WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 755 GQVR----DDFDN--------ETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAG 822
Cdd:cd07118 94 SLARtlhgDSYNNlgddmlglVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 823 VPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAQGrptpliAETGGMNAMIVDSSALTEQVV 902
Cdd:cd07118 174 LPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVS------LELGGKNPQIVFADADLDAAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 903 IDVLASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRT 981
Cdd:cd07118 248 DAVVFGVYFNAGECCnSGSRLL-VHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 982 VfqAVRENSEDAREwqsGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDET 1059
Cdd:cd07118 327 L--LLGGERLASAA---GLFYQPTIFTdvTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1588278917 1060 IAQVTGSAKVGNLYVNRNMVGAVvgVQPFGGEGLSGTGPKAG 1101
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
663-1110 |
2.89e-59 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 212.26 E-value: 2.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKtfsnAIAE 742
Cdd:cd07111 41 TINPAT-GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGK----PIRE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VRE-----AVDFLHYYAGQVR-DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVA 816
Cdd:cd07111 116 SRDcdiplVARHFYHHAGWAQlLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 817 ILLEAGVPPGVIQLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLQRNIAsrldaqGRPTPLIAETGGMNAMIVDSSA 896
Cdd:cd07111 196 ICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA------GTGKKLSLELGGKSPFIVFDDA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 897 LTEQVVIDVLASAFDSAGQRCSA-LRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSL 975
Cdd:cd07111 269 DLDSAVEGIVDAIWFNQGQVCCAgSRLL-VQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 976 RAKGRTVFQAVRENSEDarewqsGTFIPPTLIE-LESFDEL-KKEVFGPVLHVVRYnRNeLDQLVEQINASGYGLTLGVH 1053
Cdd:cd07111 348 RAEGADVFQPGADLPSK------GPFYPPTLFTnVPPASRIaQEEIFGPVLVVLTF-RT-AKEAVALANNTPYGLAASVW 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1588278917 1054 TRIDETIAQVTGSAKVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGpKAGGPLYLYRLL 1110
Cdd:cd07111 420 SENLSLALEVALSLKAGVVWINgHNLFDAAA---GFGGYRESGFG-REGGKEGLYEYL 473
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
673-1101 |
3.13e-59 |
|
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: 211.40 E-value: 3.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 673 VGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHY 752
Cdd:cd07101 9 LGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 753 YAGQVRDDFD--------------NETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAIL 818
Cdd:cd07101 89 YARRAERLLKprrrrgaipvltrtTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 819 LEAGVPPGVIQLLPGRGETVGAALTtdERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALT 898
Cdd:cd07101 169 IEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRL------IGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 899 EQVVIDVLASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRA 977
Cdd:cd07101 241 DKAAAGAVRACFSNAGQLCvSIERIY-VHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 978 KGRTVFQAVRensedAREWQSGTFIPPTLI-----ELESFDElkkEVFGPVLHVVRYNRneLDQLVEQINASGYGLTLGV 1052
Cdd:cd07101 320 KGATVLAGGR-----ARPDLGPYFYEPTVLtgvteDMELFAE---ETFGPVVSIYRVAD--DDEAIELANDTDYGLNASV 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1053 HTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTGPKAG 1101
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNEGYAAAWASIDaPMGGMKDSGLGRRHG 439
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
663-1097 |
5.00e-59 |
|
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: 210.65 E-value: 5.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKDIvGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIA- 741
Cdd:cd07092 1 VVDPATGEEI-ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYYAGQVRD-----------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPL 809
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTlegpaageylpGHTSMIRRePIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 810 iAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASRLDAQGRPTPLiaETGGMNA 889
Cdd:cd07092 160 -TTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTG----KKVARAAADTLKRVHL--ELGGKAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 890 MIVDSSALTEQVVIDVLASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENI 968
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCtAACRVY-VHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 969 ERHIQSLRAKGRTVfqavrenSEDAREWQSGTFIPPTLI-ELESFDEL-KKEVFGPVLHVVRYnrNELDQLVEQINASGY 1046
Cdd:cd07092 312 AGFVERAPAHARVL-------TGGRRAEGPGYFYEPTVVaGVAQDDEIvQEEIFGPVVTVQPF--DDEDEAIELANDVEY 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1047 GLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1097
Cdd:cd07092 383 GLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
658-1102 |
7.82e-59 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 210.91 E-value: 7.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKDIVgHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILER-AAVLMEDQmqTLIGILVR-EAGKT 735
Cdd:cd07130 11 GGVVTSISPANGEPIA-RVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQiGDALRKKK--EALGKLVSlEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 736 FSNAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07130 88 LPEGLGEVQEMIDICDFAVGLSRqlygltipserpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 804 AEQTPLIAAQGVAILLEA----GVPPGVIQLLPGRGEtVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqGRptp 879
Cdd:cd07130 168 SPTTPLTAIAVTKIVARVleknGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF---GR--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 880 LIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPV 959
Cdd:cd07130 241 SLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 960 IDAEAKENIERHIQSLRAKGRTVFqavrenSEDAREWQSGTFIPPTLIELESFDEL-KKEVFGPVLHVVRYnrNELDQLV 1038
Cdd:cd07130 321 HTKAAVDNYLAAIEEAKSQGGTVL------FGGKVIDGPGNYVEPTIVEGLSDAPIvKEETFAPILYVLKF--DTLEEAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1588278917 1039 EQINASGYGLTLGVHTRIDETIAQ---VTGSaKVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAGG 1102
Cdd:cd07130 393 AWNNEVPQGLSSSIFTTDLRNAFRwlgPKGS-DCGIVNVNIGTSGAEIG-GAFGGEKETGGGRESGS 457
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
663-1097 |
9.04e-59 |
|
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: 209.79 E-value: 9.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKdIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:cd07147 3 VTNPYTGE-VVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAGQVRD------DFD----NETHR------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQ 806
Cdd:cd07147 82 VARAIDTFRIAAEEATRiygevlPLDisarGEGRQglvrrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 807 TPLIAAQGVAILLEAGVPPGVIQLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLqRNIASRldaqgrpTPLIAETGG 886
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDL-KARAGK-------KKVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 887 MNAMIVDSSALTEQVVIDVLASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAK 965
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCiSVQRVL-VHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 966 ENIERHIQSLRAKGRTVFQAVRENsedarewqsGTFIPPTLIE-LESFDEL-KKEVFGPVLHVVRYNRneLDQLVEQINA 1043
Cdd:cd07147 312 ERVEGWVNEAVDAGAKLLTGGKRD---------GALLEPTILEdVPPDMEVnCEEVFGPVVTVEPYDD--FDEALAAVND 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1588278917 1044 SGYGLTLGVHTRIDETIAQVTGSAKVGNLYVN-----RnmvgavVGVQPFGGEGLSGTG 1097
Cdd:cd07147 381 SKFGLQAGVFTRDLEKALRAWDELEVGGVVINdvptfR------VDHMPYGGVKDSGIG 433
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
663-1097 |
1.55e-58 |
|
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: 209.47 E-value: 1.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKdIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:cd07090 1 VIEPATGE-VLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAGQVRD------DFDNE----THR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07090 80 IDSSADCLEYYAGLAPTlsgehvPLPGGsfayTRRePLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 812 AQGVAILLEAGVPPGVIQLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMI 891
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGI------KHVTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 892 VDSSALTEQVVIDVLASAFDSAGQRCS-ALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIER 970
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSnGTRVF-VQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKGRTVFQ-AVRENSEDAREwqSGTFIPPTLIElESFDEL---KKEVFGPVLHVVRYNRNEldQLVEQINASGY 1046
Cdd:cd07090 312 YIESAKQEGAKVLCgGERVVPEDGLE--NGFYVSPCVLT-DCTDDMtivREEIFGPVMSILPFDTEE--EVIRRANDTTY 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1588278917 1047 GLTLGVHTRIDETIAQVTGSAKVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07090 387 GLAAGVFTRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
644-1095 |
2.00e-58 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 210.20 E-value: 2.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 644 KWQAlpalehpvMAGELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLME---DQ 720
Cdd:PRK09457 8 DWIA--------GQGEAFESRNPVS-GEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEenkEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 721 MQTLIGilvREAGKTFSNAIAEVRE-------AVDFLHYYAGQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQI 789
Cdd:PRK09457 79 LAEVIA---RETGKPLWEAATEVTAminkiaiSIQAYHERTGEKRSEMADGAavlrHRPHGVVAVFGPYNFPGHLPNGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 790 AAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLQRNIAs 869
Cdd:PRK09457 156 VPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTGYLLHRQFA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 870 rldaqGRPTPLIA-ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCS-ALRILCLQEEIADHTLTMLRGAMGECRMG 947
Cdd:PRK09457 234 -----GQPEKILAlEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTcARRLLVPQGAQGDAFLARLVAVAKRLTVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 948 NPGRLTTD-IGPVIDAEAKENIERHIQSLRAKGRTVFQAVRENSEDArewqsgTFIPPTLIELESFDEL-KKEVFGPVLH 1025
Cdd:PRK09457 309 RWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGT------GLLTPGIIDVTGVAELpDEEYFGPLLQ 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1026 VVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:PRK09457 383 VVRY--DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGA-SSAAPFGGVGASG 449
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
663-1097 |
2.87e-57 |
|
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: 205.69 E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:cd07107 1 VINPAT-GQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAGQVRD-----------DFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07107 80 VMVAAALLDYFAGLVTElkgetipvggrNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 812 AQgVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMI 891
Cdd:cd07107 160 LR-LAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGI------KHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 892 VDSSALTEQVVIDVLASA-FDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIER 970
Cdd:cd07107 233 VFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKG-RTVFQAVRENSEDAREwqsGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYG 1047
Cdd:cd07107 313 YIDSAKREGaRLVTGGGRPEGPALEG---GFYVEPTVFAdvTPGMRIAREEIFGPVLSVLRW--RDEAEMVAQANGVEYG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1588278917 1048 LTLGVHTRiDETIAQVTGSA-KVGNLYVN---RNMVGAvvgvqPFGGEGLSGTG 1097
Cdd:cd07107 388 LTAAIWTN-DISQAHRTARRvEAGYVWINgssRHFLGA-----PFGGVKNSGIG 435
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
653-1101 |
1.19e-56 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 204.50 E-value: 1.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 653 HPVMAGELQAVINPAEPKDIVgHVREAHPEEIELALTSAVN----NAPiWFATPPQERAAILERAAVLMEDQMQTLIGIL 728
Cdd:cd07141 16 HDSVSGKTFPTINPATGEKIC-EVQEGDKADVDKAVKAARAafklGSP-WRTMDASERGRLLNKLADLIERDRAYLASLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 729 VREAGKTFSNA-IAEVREAVDFLHYYAGQVrDDFDNET------------HRPLGpvVC--ISPWNFPLAIFTGQIAAAL 793
Cdd:cd07141 94 TLDNGKPFSKSyLVDLPGAIKVLRYYAGWA-DKIHGKTipmdgdfftytrHEPVG--VCgqIIPWNFPLLMAAWKLAPAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 794 AAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIA-SRLD 872
Cdd:cd07141 171 ACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGkSNLK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 873 aqgRPTpliAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHtltMLRGAMGEC---RMGNP 949
Cdd:cd07141 251 ---RVT---LELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDE---FVKRSVERAkkrVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 950 GRLTTDIGPVIDAEAKENIERHIQSLRAKGrtvfqaVRENSEDAREWQSGTFIPPTLIElESFDEL---KKEVFGPVLHV 1026
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEG------AKLECGGKRHGDKGYFIQPTVFS-DVTDDMriaKEEIFGPVQQI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1588278917 1027 VRYnrNELDQLVEQINASGYGLTLGVHTR-IDETIAqVTGSAKVGNLYVNrnmVGAVVGVQ-PFGGEGLSGTGPKAG 1101
Cdd:cd07141 395 FKF--KTIDEVIERANNTTYGLAAAVFTKdIDKAIT-FSNALRAGTVWVN---CYNVVSPQaPFGGYKMSGNGRELG 465
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
658-1097 |
4.01e-56 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 202.83 E-value: 4.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFS 737
Cdd:PRK13473 16 GEKQPVYNPAT-GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 738 NAIA-EVREAVDFLHYYAGQVRD-----------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:PRK13473 95 LALNdEIPAIVDVFRFFAGAARClegkaageyleGHTSMIRRdPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLIAAQGVAILLEAgVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASRLDAQGRPTPLiaET 884
Cdd:PRK13473 175 EITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATG----KHVLSAAADSVKRTHL--EL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCS-ALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAE 963
Cdd:PRK13473 248 GGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTaACRIY-AQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 964 AKENIERHIQslRAKGRTVFQAVRENsedAREWQSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQI 1041
Cdd:PRK13473 327 HRDRVAGFVE--RAKALGHIRVVTGG---EAPDGKGYYYEPTLLAgaRQDDEIVQREVFGPVVSVTPF--DDEDQAVRWA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1588278917 1042 NASGYGLTLGVHTRiDETIAQ-VTGSAKVGNLYVNRNMVgaVVGVQPFGGEGLSGTG 1097
Cdd:PRK13473 400 NDSDYGLASSVWTR-DVGRAHrVSARLQYGCTWVNTHFM--LVSEMPHGGQKQSGYG 453
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
684-1097 |
5.78e-56 |
|
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: 201.15 E-value: 5.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 684 IELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYA--------G 755
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAenaeaflaD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 756 QVRDDFDNE---THRPLGPVVCISPWNFPLAiftgQI----AAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVI 828
Cdd:cd07100 81 EPIETDAGKayvRYEPLGVVLGIMPWNFPFW----QVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 829 QLLPGRGETVgAALTTDERVRGVMFTGSTEVAtllqRNIASRLDAQGRPTPLiaETGGMNAMIVDSSALTEQVVIDVLAS 908
Cdd:cd07100 157 QNLLIDSDQV-EAIIADPRVRGVTLTGSERAG----RAVAAEAGKNLKKSVL--ELGGSDPFIVLDDADLDKAVKTAVKG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 909 AFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVfqaVR 987
Cdd:cd07100 230 RLQNAGQSCiAAKRFI-VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATL---LL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 988 ENSEDAREwqsGTFIPPTLI-----ELESFDElkkEVFGPVLHVVRYnRNElDQLVEQINASGYGLTLGVHTRIDETIAQ 1062
Cdd:cd07100 306 GGKRPDGP---GAFYPPTVLtdvtpGMPAYDE---ELFGPVAAVIKV-KDE-EEAIALANDSPFGLGGSVFTTDLERAER 377
|
410 420 430
....*....|....*....|....*....|....*
gi 1588278917 1063 VTGSAKVGNLYVNRnMVGAVVGVqPFGGEGLSGTG 1097
Cdd:cd07100 378 VARRLEAGMVFING-MVKSDPRL-PFGGVKRSGYG 410
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
658-1097 |
1.06e-55 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 201.80 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKdIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFS 737
Cdd:cd07559 15 GEYFDNYNPVNGK-VLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 738 NAI-AEVREAVDFLHYYAGQVR------DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07559 94 ETLaADIPLAIDHFRYFAGVIRaqegslSEIDEDTlsyhfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 806 QTP---LIAAQGVAILLeagvPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIA 882
Cdd:cd07559 174 QTPlsiLVLMELIGDLL----PKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL------IPVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 883 ETGGMNAMIVDSSALTEQVVID------VLASAFDSaGQRCSA-LRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTD 955
Cdd:cd07559 244 ELGGKSPNIFFDDAMDADDDFDdkaeegQLGFAFNQ-GEVCTCpSRAL-VQESIYDEFIERAVERFEAIKVGNPLDPETM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 956 IGPVIDAEAKENIERHIQSLRAKGRTVFQAVRENSEDAREwqSGTFIPPTLIE-----LESFDElkkEVFGPVLHVVRYn 1030
Cdd:cd07559 322 MGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLD--KGYFYEPTLIKggnndMRIFQE---EIFGPVLAVITF- 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1588278917 1031 RNElDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07559 396 KDE-EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcYHQYPAHA---PFGGYKKSGIG 459
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
663-1097 |
1.86e-55 |
|
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: 200.61 E-value: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKDIVgHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:cd07151 14 VLNPYTGETLA-EIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 V-------REAVDFLHYYAGQ-VRDDFDNETHR----PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07151 93 WgaamaitREAATFPLRMEGRiLPSDVPGKENRvyrePLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPIT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVA-ILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASrldAQGRPTPLIA-ETGGMN 888
Cdd:cd07151 173 GGLLLAkIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVG----RHIGE---LAGRHLKKVAlELGGNN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 889 AMIVDSSALTEQVVIDVLASAFDSAGQRCSAL-RILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKEN 967
Cdd:cd07151 246 PFVVLEDADIDAAVNAAVFGKFLHQGQICMAInRII-VHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 968 IERHIQSLRAKGRTVfqaVRENSEDarewqsGTFIPPT-LIELESFDEL-KKEVFGPVLHVVRYnRNElDQLVEQINASG 1045
Cdd:cd07151 325 LLDKIEQAVEEGATL---LVGGEAE------GNVLEPTvLSDVTNDMEIaREEIFGPVAPIIKA-DDE-EEALELANDTE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1588278917 1046 YGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVqPFGGEGLSGTG 1097
Cdd:cd07151 394 YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLG 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
663-1097 |
2.49e-55 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 199.88 E-value: 2.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:cd07110 1 VINPAT-EATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAGQVRD--------------DFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQT 807
Cdd:cd07110 80 VDDVAGCFEYYADLAEQldakaeravplpseDFKARVRRePVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 808 PLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASRLDAQGRPTPLiaETGGM 887
Cdd:cd07110 160 SLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATG----SQVMQAAAQDIKPVSL--ELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 888 NAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKEN 967
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 968 IERHIQSLRAKG-RTVFQAVRensedAREWQSGTFIPPTLI-ELESFDEL-KKEVFGPVLhVVRYNRNElDQLVEQINAS 1044
Cdd:cd07110 314 VLSFIARGKEEGaRLLCGGRR-----PAHLEKGYFIAPTVFaDVPTDSRIwREEIFGPVL-CVRSFATE-DEAIALANDS 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1588278917 1045 GYGLTLGVHTRIDETIAQVTGSAKVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07110 387 EYGLAAAVISRDAERCDRVAEALEAGIVWI--NCSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
658-1103 |
3.39e-55 |
|
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: 200.11 E-value: 3.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKdIVGHVREAHPEEIELAL---TSAVNNAPiWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGK 734
Cdd:cd07139 13 SETIDVVSPATEE-VVGRVPEATPADVDAAVaaaRRAFDNGP-WPRLSPAERAAVLRRLADALEARADELARLWTAENGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 735 TFS-NAIAEVREAVDFLHYYAGQVRDdFDNETHR-------------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07139 91 PISwSRRAQGPGPAALLRYYAALARD-FPFEERRpgsggghvlvrrePVGVVAAIVPWNAPLFLAALKIAPALAAGCTVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 801 AKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGrGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASRldAQGRPTPL 880
Cdd:cd07139 170 LKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAG----RRIAAV--CGERLARV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 881 IAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSAL-RILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPV 959
Cdd:cd07139 243 TLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALtRIL-VPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 960 IDAEAKENIERHIQSLRAKGRTVFQAVRENSEDAREWqsgtFIPPTLI-ELESFDEL-KKEVFGPVLHVVRYnrNELDQL 1037
Cdd:cd07139 322 ASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGW----FVEPTLFaDVDNDMRIaQEEIFGPVLSVIPY--DDEDDA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1588278917 1038 VEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVgvqPFGGEGLSGTGpKAGGP 1103
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFGA---PFGGFKQSGIG-REGGP 457
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
653-1101 |
4.43e-55 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 200.33 E-value: 4.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 653 HPVMAGELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNN-APIWFATPPQERAAILERAAVLMEDQMQTLIGILVRE 731
Cdd:cd07144 17 VKSSDGETIKTVNPST-GEVIASVYAAGEEDVDKAVKAARKAfESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 732 AGKTF-SNAIAEVREAVDFLHYYAGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNS 798
Cdd:cd07144 96 SGKPYhSNALGDLDEIIAVIRYYAGWA-DKIQGKTiptspnklaytlHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 799 VLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAqgrpt 878
Cdd:cd07144 175 VVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKA----- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 879 pLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSAL-RILcLQEEIADHTLTMLRGAMGEC-RMGNPGRLTTDI 956
Cdd:cd07144 250 -VTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATsRIY-VQESIYDKFVEKFVEHVKQNyKVGSPFDDDTVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 957 GPVIDAEAKENIERHIQSLRAKGRTVfqaVRENSEDAREWQSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYNRNel 1034
Cdd:cd07144 328 GPQVSKTQYDRVLSYIEKGKKEGAKL---VYGGEKAPEGLGKGYFIPPTIFTdvPQDMRIVKEEIFGPVVVISKFKTY-- 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1588278917 1035 DQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNR-NMvgAVVGVqPFGGEGLSGTGPKAG 1101
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSsND--SDVGV-PFGGFKMSGIGRELG 467
|
|
| arg_catab_astD |
TIGR03240 |
succinylglutamate-semialdehyde dehydrogenase; Members of this protein family are ... |
657-1095 |
3.42e-54 |
|
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: 197.63 E-value: 3.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:TIGR03240 11 QGESFASRNPAT-QEVLWQGAAASADQVEAAVAAARAAFPAWARLSLEERIAVVQRFAALLEERKEALARVIARETGKPL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVRE-------AVDFLHYYAGQVRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:TIGR03240 90 WETRTEVASmigkvaiSIKAYHERTGESENPMPDGRavlrHRPHGVVAVFGPYNFPGHLPNGHIVPALIAGNTVVFKPSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 806 QTPLIAAQGVAILLEAGVPPGVIQLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLQRNIAsrldaqGRPTPLIA-ET 884
Cdd:TIGR03240 170 LTPWVAEETVKLWEKAGLPAGVLNLVQGARET-GVALAAHPQIDGLLFTGSSNTGTLLHRQFG------GRPEKILAlEM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 885 GGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCS-ALRILCLQEEIADHTLTMLRGAMGECRmgnPGRLTTD----IGPV 959
Cdd:TIGR03240 243 GGNNPLIVDEVADIDAAVHHIIQSAFISAGQRCTcARRLLVPDGAQGDAFLARLVEVAERLT---VGAWDAEpqpfMGAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 960 IDAEAKENIERHIQSLRAKGRTVFQAVRENSEDArewqsgTFIPPTLIELESFDEL-KKEVFGPVLHVVRYnrNELDQLV 1038
Cdd:TIGR03240 320 ISLRAAQRLLAAQAKLLALGGKSLLEMRQLDPGA------AFLTPGIIDVTGVAELpDEEHFGPLLQVIRY--TDFDEAI 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1588278917 1039 EQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAvVGVQPFGGEGLSG 1095
Cdd:TIGR03240 392 AIANNTRFGLSAGLLSDDRELYDRFLLEIRAGIVNWNKPLTGA-SSAAPFGGIGASG 447
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
673-1097 |
4.03e-54 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 198.56 E-value: 4.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 673 VGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHY 752
Cdd:PRK09407 45 LATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 753 YA-------------------GQVRddfdnETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQ 813
Cdd:PRK09407 125 YArrapkllaprrragalpvlTKTT-----ELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 814 GVAILLEAGVPPGVIQLLPGRGETVGAALTtdERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVD 893
Cdd:PRK09407 200 AVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRL------IGFSLELGGKNPMIVL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 894 SSALTEQVVIDVLASAFDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHI 972
Cdd:PRK09407 272 DDADLDKAAAGAVRACFSNAGQLCiSIERIY-VHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 973 QSLRAKGRTVFQAVRensedAREWQSGTFIPPTLI-----ELESFDElkkEVFGPVLHVVRYNRneLDQLVEQINASGYG 1047
Cdd:PRK09407 351 DDAVAKGATVLAGGK-----ARPDLGPLFYEPTVLtgvtpDMELARE---ETFGPVVSVYPVAD--VDEAVERANDTPYG 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1048 LTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQ-PFGGEGLSGTG 1097
Cdd:PRK09407 421 LNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
662-1097 |
3.81e-53 |
|
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: 194.20 E-value: 3.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 662 AVINPAEPKdIVGHVREAHPEEIELALTS---AVNNApiWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKT--F 736
Cdd:cd07113 18 DITNPATEQ-VIASVASATEADVDAAVASawrAFVSA--WAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSihL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIaEVREAVDFLHYYAGQVR----------------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSV 799
Cdd:cd07113 95 SRAF-EVGQSANFLRYFAGWATkingetlapsipsmqgERYTAFTRRePVGVVAGIVPWNFSVMIAVWKIGAALATGCTI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 800 LAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGEtVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTP 879
Cdd:cd07113 174 VIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQAASDL------TR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 880 LIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPV 959
Cdd:cd07113 247 VTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 960 IDAEAKENIERHIQSLRAKGRTVfqaVRENSEDAREwqsGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYNRNEldQL 1037
Cdd:cd07113 327 ANQPHFDKVCSYLDDARAEGDEI---VRGGEALAGE---GYFVQPTLVLARSADSrlMREETFGPVVSFVPYEDEE--EL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1588278917 1038 VEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVN-RNMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
664-1076 |
3.57e-52 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 190.53 E-value: 3.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 664 INPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEV 743
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 744 REAVDFLHYYAGQVRDDFDNE------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIA 811
Cdd:cd07102 80 RGMLERARYMISIAEEALADIrvpekdgferyiRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 812 AQGVAILLEAGVPPGVIQLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLQRNiasrldAQGRPTPLIAETGGMNAMI 891
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRA------AAGRFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 892 VDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERH 971
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 972 IQSLRAKGRTVfqAVRENSEDAREwQSGTFIPPT-LIELE-SFDELKKEVFGPVLHVVRYNRNEldQLVEQINASGYGLT 1049
Cdd:cd07102 313 IADAIAKGARA--LIDGALFPEDK-AGGAYLAPTvLTNVDhSMRVMREETFGPVVGIMKVKSDA--EAIALMNDSEYGLT 387
|
410 420
....*....|....*....|....*..
gi 1588278917 1050 LGVHTRIDETIAQVTGSAKVGNLYVNR 1076
Cdd:cd07102 388 ASVWTKDIARAEALGEQLETGTVFMNR 414
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
664-1055 |
5.27e-52 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 190.25 E-value: 5.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 664 INPAEPKdIVGHVREAHPEEIELALTSAVN--NAPIWfATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIA 741
Cdd:cd07120 2 IDPATGE-VIGTYADGGVAEAEAAIAAARRafDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYYAGQVR-----------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:cd07120 80 EISGAISELRYYAGLARteagrmiepepGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEA-GVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAQGrptpliAETGGMNA 889
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLG------LELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 890 MIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIE 969
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 970 RHIQSLRAKGRTVFqaVRENSEDAReWQSGTFIPPTLIELE--SFDELKKEVFGPVLHVVRYNrNElDQLVEQINASGYG 1047
Cdd:cd07120 314 RMVERAIAAGAEVV--LRGGPVTEG-LAKGAFLRPTLLEVDdpDADIVQEEIFGPVLTLETFD-DE-AEAVALANDTDYG 388
|
....*...
gi 1588278917 1048 LTLGVHTR 1055
Cdd:cd07120 389 LAASVWTR 396
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
671-1122 |
3.04e-51 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 190.40 E-value: 3.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 671 DIVGHVREAHPEEIELALTSA---VNNAPiWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAI-AEVREA 746
Cdd:PLN02466 84 EVIAHVAEGDAEDVNRAVAAArkaFDEGP-WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAkAELPMF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 747 VDFLHYYAG--------QVRDDFDNET---HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGV 815
Cdd:PLN02466 163 ARLFRYYAGwadkihglTVPADGPHHVqtlHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 816 AILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQrniasRLDAQGRPTPLIAETGGMNAMIVDSS 895
Cdd:PLN02466 243 KLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVL-----ELAAKSNLKPVTLELGGKSPFIVCED 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 896 ALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSL 975
Cdd:PLN02466 318 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 976 RAKGRTVfqavrENSEDaREWQSGTFIPPTLIELESFDEL--KKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVH 1053
Cdd:PLN02466 398 VESGATL-----ECGGD-RFGSKGYYIQPTVFSNVQDDMLiaQDEIFGPVQSILKF--KDLDEVIRRANNTRYGLAAGVF 469
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1054 TRIDETIAQVTGSAKVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAGgplyLYRLLSSRPQNAVGTTL 1122
Cdd:PLN02466 470 TQNLDTANTLSRALRVGTVWVNcFDVFDAAI---PFGGYKMSGIGREKG----IYSLNNYLQVKAVVTPL 532
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
671-1101 |
8.09e-51 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 188.11 E-value: 8.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 671 DIVGHVREAHPEEIELALTS---AVNNAPiWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFS-NAIAEVREA 746
Cdd:PLN02766 47 EVIARIAEGDKEDVDLAVKAareAFDHGP-WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFAlGKAVDIPAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 747 VDFLHYYAGQVrDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQG 814
Cdd:PLN02766 126 AGLLRYYAGAA-DKIHGETlkmsrqlqgytlKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 815 VAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATL-LQRNIASRLdaqgrpTPLIAETGGMNAMIVD 893
Cdd:PLN02766 205 AHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKiMQAAATSNL------KQVSLELGGKSPLLIF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 894 SSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQ 973
Cdd:PLN02766 279 DDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 974 SLRAKGRTVFQAVRENSEdarewqSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLG 1051
Cdd:PLN02766 359 HGKREGATLLTGGKPCGD------KGYYIEPTIFTdvTEDMKIAQDEIFGPVMSLMKF--KTVEEAIKKANNTKYGLAAG 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1052 VHTRIDETIAQVTGSAKVGNLYVNRNMvgAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:PLN02766 431 IVTKDLDVANTVSRSIRAGTIWVNCYF--AFDPDCPFGGYKMSGFGRDQG 478
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
657-1097 |
1.51e-50 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 187.01 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:PRK13252 20 SGETFEVINPAT-GEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAI-AEVREAVDFLHYYAG----------QVRD-DFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPA 804
Cdd:PRK13252 99 QETSvVDIVTGADVLEYYAGlapalegeqiPLRGgSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 805 EQTPLIAAQGVAILLEAGVPPGVIQLLPGRGEtVGAALTTDERVRGVMFTGstEVATllQRNIASrlDAQGRPTPLIAET 884
Cdd:PRK13252 179 EVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTG--GVPT--GKKVMA--AAAASLKEVTMEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 885 GGMNAMIV-DSSALTEQVVIDVLASaFDSAGQRCS-ALRILcLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDA 962
Cdd:PRK13252 252 GGKSPLIVfDDADLDRAADIAMLAN-FYSSGQVCTnGTRVF-VQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 963 EAKENIERHIQSLRAKGRTVF---QAVRENsedarEWQSGTFIPPTLielesF----DEL---KKEVFGPVLHVVRYnRN 1032
Cdd:PRK13252 330 AHRDKVLGYIEKGKAEGARLLcggERLTEG-----GFANGAFVAPTV-----FtdctDDMtivREEIFGPVMSVLTF-DD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1588278917 1033 ElDQLVEQINASGYGLTLGVHTRiDETIA-QVTGSAKVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:PRK13252 399 E-DEVIARANDTEYGLAAGVFTA-DLSRAhRVIHQLEAGICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
689-1097 |
3.69e-50 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 184.32 E-value: 3.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 689 TSAVNNA----PIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQ-------- 756
Cdd:cd07105 3 DQAVEAAaaafPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLitqiiggs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 757 VRDDFDNET----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLL- 831
Cdd:cd07105 83 IPSDKPGTLamvvKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 832 --PGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASA 909
Cdd:cd07105 163 hsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHL------KPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 910 FDSAGQRC-SALRILcLQEEIADHTLTMLRGAMGECRMGNpgrltTDIGPVIDAEAKENIERHIQSLRAKG-RTVFQAVR 987
Cdd:cd07105 237 FLNSGQICmSTERII-VHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGaKLVVGGLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 988 ENSEDarewqsGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRiDETIA-QVT 1064
Cdd:cd07105 311 DESPS------GTSMPPTILDnvTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTR-DLARAlAVA 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 1588278917 1065 GSAKVGNLYVNrnmvGAVVGVQ---PFGGEGLSGTG 1097
Cdd:cd07105 382 KRIESGAVHIN----GMTVHDEptlPHGGVKSSGYG 413
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
707-1084 |
1.63e-49 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 181.86 E-value: 1.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 707 AAILERAAVLMEdqmqtligILVREAGKTFSNAIAEVREAVDFLHYYAGQVR--------DDFDNET----HRPLGPVVC 774
Cdd:PRK10090 6 AGIRERASEISA--------LIVEEGGKIQQLAEVEVAFTADYIDYMAEWARryegeiiqSDRPGENillfKRALGVTTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 775 ISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFT 854
Cdd:PRK10090 78 ILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 855 GSTE----VATLLQRNIasrldaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIA 930
Cdd:PRK10090 158 GSVSagekIMAAAAKNI----------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 931 DHTLTMLRGAMGECRMGNP-GRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAVRensedaREWQSGTFIPPTLIE- 1008
Cdd:PRK10090 228 DQFVNRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGK------AVEGKGYYYPPTLLLd 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1588278917 1009 -LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVG 1084
Cdd:PRK10090 302 vRQEMSIMHEETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQG 376
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
658-1101 |
3.41e-49 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 183.50 E-value: 3.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKDIvGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFS 737
Cdd:PLN02315 33 GPLVSSVNPANNQPI-AEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 738 NAIAEVREAVDFLHYYAGQVR------------DDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:PLN02315 112 EGIGEVQEIIDMCDFAVGLSRqlngsiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 806 QTPLIA---AQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqGRptpLIA 882
Cdd:PLN02315 192 TTPLITiamTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARF---GK---CLL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 883 ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDA 962
Cdd:PLN02315 266 ELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 963 EAKENIERHIQSLRAKGRTVFQAVRENSEDarewqsGTFIPPTLIELE-SFDELKKEVFGPVLHVVRYnrNELDQLVEQI 1041
Cdd:PLN02315 346 ESKKNFEKGIEIIKSQGGKILTGGSAIESE------GNFVQPTIVEISpDADVVKEELFGPVLYVMKF--KTLEEAIEIN 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1588278917 1042 NASGYGLTLGVHTRIDETIAQVTG--SAKVGNLYVNRNMVGAVVGvQPFGGEGLSGTGPKAG 1101
Cdd:PLN02315 418 NSVPQGLSSSIFTRNPETIFKWIGplGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAG 478
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
658-1106 |
1.95e-48 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 180.49 E-value: 1.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFS 737
Cdd:PRK11241 25 GEVIDVTNPAN-GDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 738 NAIAEVREAVDFLHYYAGQVRDDFDNET------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:PRK11241 104 EAKGEISYAASFIEWFAEEGKRIYGDTIpghqadkrliviKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPAS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 806 QTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDAqgrptpLIAETG 885
Cdd:PRK11241 184 QTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK------VSLELG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAK 965
Cdd:PRK11241 258 GNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 966 ENIERHIQSLRAKGRTVFQAVRENSedarewQSGTFIPPTLIELESFDEL--KKEVFGPVLHVVRYnRNELDqLVEQINA 1043
Cdd:PRK11241 338 AKVEEHIADALEKGARVVCGGKAHE------LGGNFFQPTILVDVPANAKvaKEETFGPLAPLFRF-KDEAD-VIAQAND 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1588278917 1044 SGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGvqPFGG---EGLSGTGPKAGGPLYL 1106
Cdd:PRK11241 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGikaSGLGREGSKYGIEDYL 473
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
663-1097 |
7.85e-47 |
|
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: 175.30 E-value: 7.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEPKDIvGHVREAHPEEIELALTSA------VNNapiWFatPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:cd07148 3 VVNPFDLKPI-GEVPTVDWAAIDKALDTAhalfldRNN---WL--PAHERIAILERLADLMEERADELALLIAREGGKPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVREAVDFLHYYAGQVRDDFDNE----------------THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVL 800
Cdd:cd07148 77 VDAKVEVTRAIDGVELAADELGQLGGREipmgltpasagriaftTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 801 AKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGEtVGAALTTDERVRGVMFTGSTEVATLLQRNIAsrldaqgrPTPL 880
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENA-VAEKLVTDPRVAFFSFIGSARVGWMLRSKLA--------PGTR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 881 IA-ETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPV 959
Cdd:cd07148 228 CAlEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 960 IDAEAKENIERHIQSLRAKGRTVFQAVRENSEdarewqsgTFIPPTLIeLESFDELK---KEVFGPVlhVVRYNRNELDQ 1036
Cdd:cd07148 308 IRPREVDRVEEWVNEAVAAGARLLCGGKRLSD--------TTYAPTVL-LDPPRDAKvstQEIFGPV--VCVYSYDDLDE 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1588278917 1037 LVEQINASGYGLTLGVHTR-ID---ETIAQVTGSAkvgnLYVNrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07148 377 AIAQANSLPVAFQAAVFTKdLDvalKAVRRLDATA----VMVN-DHTAFRVDWMPFAGRRQSGYG 436
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
658-1097 |
5.53e-46 |
|
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: 173.02 E-value: 5.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKdIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFS 737
Cdd:cd07117 15 GETIDSYNPANGE-TLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 738 NAIA-EVREAVDFLHYYAGQVR------DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAE 805
Cdd:cd07117 94 ETRAvDIPLAADHFRYFAGVIRaeegsaNMIDEDTlsivlREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 806 QTPLIAAQgVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETG 885
Cdd:cd07117 174 TTSLSLLE-LAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL------IPATLELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 886 GMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAK 965
Cdd:cd07117 247 GKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 966 ENIERHIQSLRAKGRTVF---QAVRENSEDArewqsGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYnRNElDQLVEQ 1040
Cdd:cd07117 327 DKILSYVDIAKEEGAKILtggHRLTENGLDK-----GFFIEPTLIVNVTNDMrvAQEEIFGPVATVIKF-KTE-DEVIDM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1588278917 1041 INASGYGLTLGVHTRiDETIA-QVTGSAKVGNLYVNR-NMVGAVVgvqPFGGEGLSGTG 1097
Cdd:cd07117 400 ANDSEYGLGGGVFTK-DINRAlRVARAVETGRVWVNTyNQIPAGA---PFGGYKKSGIG 454
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
657-1069 |
1.46e-45 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 172.63 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 657 AGELQAVINPAEPKDIVGhVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTF 736
Cdd:PLN00412 29 SGKSVAITNPSTRKTQYK-VQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 737 SNAIAEVREAVDFLHYYA---------GQ--VRDDF-DNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGN 797
Cdd:PLN00412 108 KDAVTEVVRSGDLISYTAeegvrilgeGKflVSDSFpGNERNKycltskiPLGVVLAIPPFNYPVNLAVSKIAPALIAGN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 798 SVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFT-GSTEVAtllqrniasrLDAQGR 876
Cdd:PLN00412 188 AVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTgGDTGIA----------ISKKAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 877 PTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRlTTDI 956
Cdd:PLN00412 258 MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED-DCDI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 957 GPVIDAEAKENIERHIQSLRAKGRTVFQAVRensedaREwqsGTFIPPTLIElESFDELK---KEVFGPVLHVVRYNRNE 1033
Cdd:PLN00412 337 TPVVSESSANFIEGLVMDAKEKGATFCQEWK------RE---GNLIWPLLLD-NVRPDMRiawEEPFGPVLPVIRINSVE 406
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1588278917 1034 ldQLVEQINASGYGLTLGVHTR-IDETI----AQVTGSAKV 1069
Cdd:PLN00412 407 --EGIHHCNASNFGLQGCVFTRdINKAIlisdAMETGTVQI 445
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
682-1097 |
4.56e-45 |
|
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: 170.71 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 682 EEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAI-AEVREAVDFLHYYAGQVR-- 758
Cdd:cd07116 38 EDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLaADIPLAIDHFRYFAGCIRaq 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 759 ----DDFDNET-----HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLiaaqGVAILLEA---GVPPG 826
Cdd:cd07116 118 egsiSEIDENTvayhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPA----SILVLMELigdLLPPG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 827 VIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQvvidvl 906
Cdd:cd07116 194 VVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI------IPVTLELGGKSPNIFFADVMDAD------ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 907 ASAFDSA-----------GQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSL 975
Cdd:cd07116 262 DAFFDKAlegfvmfalnqGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 976 RAKGRTVFQAVRENSEDArEWQSGTFIPPTLIELESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTR 1055
Cdd:cd07116 342 KEEGAEVLTGGERNELGG-LLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTTF--KDEEEALEIANDTLYGLGAGVWTR 418
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1588278917 1056 IDETIAQVTGSAKVGNLYVnrNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07116 419 DGNTAYRMGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
654-1075 |
1.84e-44 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 169.53 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 654 PVMAGELqAVINPAEpKDIVGHVREAHPEEIELALTSA-----VNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGIL 728
Cdd:PLN02467 19 PVLGKRI-PVVNPAT-EETIGDIPAATAEDVDAAVEAArkafkRNKGKDWARTTGAVRAKYLRAIAAKITERKSELAKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 729 VREAGKTFSNAIAEVREAVDFLHYYAGQVR--------------DDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAAL 793
Cdd:PLN02467 97 TLDCGKPLDEAAWDMDDVAGCFEYYADLAEaldakqkapvslpmETFKGYVLKePLGVVGLITPWNYPLLMATWKVAPAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 794 AAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVAtllqRNIASRLDA 873
Cdd:PLN02467 177 AAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG----RKIMTAAAQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 874 QGRPTPLiaETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLT 953
Cdd:PLN02467 253 MVKPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 954 TDIGPVIDAEAKENIERHIQSLRAKGRTV-FQAVRenSEDAREwqsGTFIPPTLIE--LESFDELKKEVFGPVLhVVRYN 1030
Cdd:PLN02467 331 CRLGPVVSEGQYEKVLKFISTAKSEGATIlCGGKR--PEHLKK---GFFIEPTIITdvTTSMQIWREEVFGPVL-CVKTF 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1588278917 1031 RNElDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVN 1075
Cdd:PLN02467 405 STE-DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN 448
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
663-1075 |
2.20e-44 |
|
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: 168.52 E-value: 2.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:TIGR01722 20 VTNPAT-NEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAG-----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:TIGR01722 99 VARGLEVVEHACGvnsllkgetstQVATRVDVYSIRqPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDErVRGVMFTGSTEVAtllqRNIASRLDAQGRPTPliAETGGMNAM 890
Cdd:TIGR01722 179 AVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPD-VKAVSFVGSTPIG----RYIHTTGSAHGKRVQ--ALGGAKNHM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEiADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIER 970
Cdd:TIGR01722 252 VVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEMGPLITPQAKDRVAS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKGRTVFQAVRENSEDAREwqSGTFIPPTLIELESFDE--LKKEVFGPVLHVVRYnrNELDQLVEQINASGYGL 1048
Cdd:TIGR01722 331 LIAGGAAEGAEVLLDGRGYKVDGYE--EGNWVGPTLLERVPPTMkaYQEEIFGPVLCVLEA--DTLEEAIALINASPYGN 406
|
410 420
....*....|....*....|....*..
gi 1588278917 1049 TLGVHTRIDETIAQVTGSAKVGNLYVN 1075
Cdd:TIGR01722 407 GTAIFTRDGAAARRFQHEIEVGQVGVN 433
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
664-1101 |
2.42e-44 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 168.44 E-value: 2.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 664 INPAEPKdIVGHVREAHPEEIELALT---SAVNNAPiWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAI 740
Cdd:cd07140 26 INPTDGS-VICKVSLATVEDVDRAVAaakEAFENGE-WGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 741 -AEVREAVDFLHYYAG-------------QVRDDfDNET---HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:cd07140 104 kTHVGMSIQTFRYFAGwcdkiqgktipinQARPN-RNLTltkREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 804 AEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIAsrlDAQGRPTPLiaE 883
Cdd:cd07140 183 AQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA---VSNLKKVSL--E 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 884 TGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPvidae 963
Cdd:cd07140 258 LGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP----- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 964 akENIERHIQSLRakgRTVFQAVRENSE----DAREWQSGTFIPPTL---IELESFDElKKEVFGPVLHVVRYNRNELDQ 1036
Cdd:cd07140 333 --QNHKAHLDKLV---EYCERGVKEGATlvygGKQVDRPGFFFEPTVftdVEDHMFIA-KEESFGPIMIISKFDDGDVDG 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1588278917 1037 LVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVN---RNMVGAvvgvqPFGGEGLSGTGPKAG 1101
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNtynKTDVAA-----PFGGFKQSGFGKDLG 469
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
658-1097 |
6.49e-42 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 161.60 E-value: 6.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 658 GELQAVINPAEPKDIvGHVREAHPEEIELALTSA--VNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKT 735
Cdd:PRK09847 34 NETFETVDPVTQAPL-AKIARGKSVDIDRAVSAArgVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 736 FSNAIAE-VREAVDFLHYYA-------GQVRDDFDNE----THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKP 803
Cdd:PRK09847 113 IRHSLRDdIPGAARAIRWYAeaidkvyGEVATTSSHElamiVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 804 AEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIAsrlDAQGRPTPLiaE 883
Cdd:PRK09847 193 SEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG---DSNMKRVWL--E 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 884 TGGMNAMIV--DSSALtEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVID 961
Cdd:PRK09847 268 AGGKSANIVfaDCPDL-QQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLID 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 962 AEAKENIERHIQSLRAKGRTVFqavrenseDAREWQSGTFIPPT-LIELESFDEL-KKEVFGPVLHVVRYNRNEldQLVE 1039
Cdd:PRK09847 347 CAHADSVHSFIREGESKGQLLL--------DGRNAGLAAAIGPTiFVDVDPNASLsREEIFGPVLVVTRFTSEE--QALQ 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1588278917 1040 QINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1097
Cdd:PRK09847 417 LANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDM--TVPFGGYKQSGNG 472
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
674-1101 |
1.25e-40 |
|
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: 157.08 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 674 GHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILeraAVLME---DQMQTLIGILVREAGKTFSNA-IAEVREAVDF 749
Cdd:cd07098 10 GSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVL---RSLLKyilENQEEICRVACRDTGKTMVDAsLGEILVTCEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 750 LHY--------YAGQVRDDFDNETHR-------PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQG 814
Cdd:cd07098 87 IRWtlkhgekaLRPESRPGGLLMFYKrarveyePLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 815 VAILLEA----GVPPGVIQLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAM 890
Cdd:cd07098 167 LSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESL------TPVVLELGGKDPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIER 970
Cdd:cd07098 240 IVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKG-RTVFQAVRENSEdarEWQSGTFIPPTLIE--LESFDELKKEVFGPVLHVVRYNRNEldQLVEQINASGYG 1047
Cdd:cd07098 320 LVADAVEKGaRLLAGGKRYPHP---EYPQGHYFPPTLLVdvTPDMKIAQEEVFGPVMVVMKASDDE--EAVEIANSTEYG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1588278917 1048 LTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAG 1101
Cdd:cd07098 395 LGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG 448
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
662-1097 |
4.11e-39 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 152.58 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 662 AVINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIA 741
Cdd:PRK09406 4 ATINPAT-GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 742 EVREAVDFLHYYAGQVRDDFDNET--------------HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQT 807
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLADEPadaaavgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 808 PLIAAQGVAILLEAGVPPGVIQ-LLPGRGETvgAALTTDERVRGVMFTGStEVATllqRNIASRLDAQGRPTPLiaETGG 886
Cdd:PRK09406 163 PQTALYLADLFRRAGFPDGCFQtLLVGSGAV--EAILRDPRVAAATLTGS-EPAG---RAVAAIAGDEIKKTVL--ELGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 887 MNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKE 966
Cdd:PRK09406 235 SDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 967 NIERHIQSLRAKGRTVFQAVRensedaREWQSGTFIPPTLI-----ELESFDElkkEVFGPVLHVvrYNRNELDQLVEQI 1041
Cdd:PRK09406 315 EVEKQVDDAVAAGATILCGGK------RPDGPGWFYPPTVItditpDMRLYTE---EVFGPVASL--YRVADIDEAIEIA 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1588278917 1042 NASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNrNMVGAVVGVqPFGGEGLSGTG 1097
Cdd:PRK09406 384 NATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMTVSYPEL-PFGGVKRSGYG 437
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
766-1097 |
3.44e-36 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 143.05 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgVAILLEAGVPPGVIQLLPGrGETVGAALtTD 845
Cdd:cd07087 98 PEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSAL-LAKLIPKYFDPEAVAVVEG-GVEVATAL-LA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 846 ERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCL 925
Cdd:cd07087 175 EPFDHIFFTGSPAVGKIVMEAAAKHL------TPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 926 QEEIADHTLTMLRGAMGEcRMGNPGRLTTDIGPVIDaeakeniERH---IQSLRAKGRTVFQAVRENSEDarewqsgtFI 1002
Cdd:cd07087 249 HESIKDELIEELKKAIKE-FYGEDPKESPDYGRIIN-------ERHfdrLASLLDDGKVVIGGQVDKEER--------YI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1003 PPTLIELESFDE--LKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVG 1080
Cdd:cd07087 313 APTILDDVSPDSplMQEEIFGPILPILTY--DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLH 390
|
330
....*....|....*..
gi 1588278917 1081 AVVGVQPFGGEGLSGTG 1097
Cdd:cd07087 391 AAIPNLPFGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
663-1047 |
2.53e-35 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 143.73 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 663 VINPAEpKDIVGHVREAHPEEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAE 742
Cdd:PLN02419 133 VINPAT-QEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 743 VREAVDFLHYYAG-----------QVRDDFDNETHR-PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLI 810
Cdd:PLN02419 212 IFRGLEVVEHACGmatlqmgeylpNVSNGVDTYSIRePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 811 AAQGVAILLEAGVPPGVIQLLPGRGETVGaALTTDERVRGVMFTGSTEVATllqrNIASRLDAQGRptPLIAETGGMNAM 890
Cdd:PLN02419 292 SVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGM----HIYARAAAKGK--RIQSNMGAKNHG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 891 IVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGeCRMGNPGRLTTDIGPVIDAEAKENIER 970
Cdd:PLN02419 365 LVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKA-LKVTCGSEPDADLGPVISKQAKERICR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 971 HIQSLRAKGRTVFQavrenseDARE-----WQSGTFIPPTLI-----ELESFdelKKEVFGPVLhvVRYNRNELDQLVEQ 1040
Cdd:PLN02419 444 LIQSGVDDGAKLLL-------DGRDivvpgYEKGNFIGPTILsgvtpDMECY---KEEIFGPVL--VCMQANSFDEAISI 511
|
....*..
gi 1588278917 1041 INASGYG 1047
Cdd:PLN02419 512 INKNKYG 518
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
766-1097 |
3.74e-32 |
|
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: 131.19 E-value: 3.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLiAAQGVAILLEAGVPPGVIQLLPGRGETVGAALttD 845
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPH-TAALLAELVPKYLDPDAFQVVQGGVPETTALL--E 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 846 ERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCL 925
Cdd:cd07135 183 QKFDKIFYTGSGRVGRIIAEAAAKHL------TPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 926 QEEIADHTLTMLRGAMGECRMGNPGRLtTDIGPVIDAEAKENIERHIQslRAKGRTVFQAVRENSEdarewqsgTFIPPT 1005
Cdd:cd07135 257 DPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNPRHFNRLKSLLD--TTKGKVVIGGEMDEAT--------RFIPPT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1006 LIELESFDE--LKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVV 1083
Cdd:cd07135 326 IVSDVSWDDslMSEELFGPVLPIIKV--DDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGV 403
|
330
....*....|....
gi 1588278917 1084 GVQPFGGEGLSGTG 1097
Cdd:cd07135 404 DNAPFGGVGDSGYG 417
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
685-1113 |
1.52e-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: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 685 ELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHY----YAGQVRDD 760
Cdd:cd07084 2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARafviYSYRIPHE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 761 FDNE--------THR---PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAG-VPPGVI 828
Cdd:cd07084 82 PGNHlgqglkqqSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 829 QLLPGRGETvGAALTTDERVRGVMFTGSTEVATLLqrniasRLDAqgRPTPLIAETGGMNAMIVDSSALTEQVVID-VLA 907
Cdd:cd07084 162 TLINGDGKT-MQALLLHPNPKMVLFTGSSRVAEKL------ALDA--KQARIYLELAGFNWKVLGPDAQAVDYVAWqCVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 908 SAFDSAGQRCSALRILCLQEeiADHTLTMLRGAMGECRMGNPGRLTtdIGPVIdaeaKENIERHIQSLRAKGRTV--FQA 985
Cdd:cd07084 233 DMTACSGQKCTAQSMLFVPE--NWSKTPLVEKLKALLARRKLEDLL--LGPVQ----TFTTLAMIAHMENLLGSVllFSG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 986 VRENSEDAREWQSGTFIPPTLIELESFDEL----KKEVFGPVLHVVRYNRNELDQLVEQINASGYGLTLGVHTRIDETIA 1061
Cdd:cd07084 305 KELKNHSIPSIYGACVASALFVPIDEILKTyelvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQ 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1588278917 1062 QVTG-SAKVGNLY-VNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSR 1113
Cdd:cd07084 385 ELIGnLWVAGRTYaILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCH 438
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
766-1102 |
4.64e-31 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 127.73 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 766 HRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAgVPPGVIQLLPGRGETVGAALttD 845
Cdd:cd07134 98 YEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVFEGDAEVAQALL--E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 846 ERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCL 925
Cdd:cd07134 175 LPFDHIFFTGSPAVGKIVMAAAAKHL------ASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 926 QEEIADHTLTMLRGAMGECRMGNPGRL-TTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAVRENSEDarewqsgTFIPP 1004
Cdd:cd07134 249 HESVKDAFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQ-------RYIAP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1005 TLIE--LESFDELKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAV 1082
Cdd:cd07134 322 TVLTnvTPDMKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFL 399
|
330 340
....*....|....*....|
gi 1588278917 1083 VGVQPFGGEGLSGTGpKAGG 1102
Cdd:cd07134 400 NPNLPFGGVNNSGIG-SYHG 418
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
664-1075 |
2.19e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 123.43 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 664 INPAEpkdivGHVREAHP----EEIELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAGKTFSNA 739
Cdd:PRK13968 12 VNPAT-----GEQLSVLPwagaDDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 740 IAEVREAVDFLHYYAGQ-----------VRDDFDNETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTP 808
Cdd:PRK13968 87 RAEVAKSANLCDWYAEHgpamlkaeptlVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 809 LIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTtDERVRGVMFTGSTEVATLLQRNIASRLDAqgrptpLIAETGGMN 888
Cdd:PRK13968 167 GCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIGAQAGAALKK------CVLELGGSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 889 AMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENI 968
Cdd:PRK13968 240 PFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 969 ERHIQSLRAKGRTVFQAVRENSedarewQSGTFIPPTLI-----ELESFdelKKEVFGPV--LHVVRynrnELDQLVEQI 1041
Cdd:PRK13968 320 HHQVEATLAEGARLLLGGEKIA------GAGNYYAPTVLanvtpEMTAF---REELFGPVaaITVAK----DAEHALELA 386
|
410 420 430
....*....|....*....|....*....|....
gi 1588278917 1042 NASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVN 1075
Cdd:PRK13968 387 NDSEFGLSATIFTTDETQARQMAARLECGGVFIN 420
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
765-1097 |
4.18e-28 |
|
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: 119.13 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 765 THRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgVAILLEAGVPPGVIQLLPGRGEtVGAALTT 844
Cdd:cd07133 98 EYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSAL-LAELLAEYFDEDEVAVVTGGAD-VAAAFSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 845 ---DErvrgVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALR 921
Cdd:cd07133 176 lpfDH----LLFTGSTAVGRHVMRAAAENL------TPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 922 ILCLQEEIADHTLTMLRGAMGEC---RMGNPgrlttDIGPVIDAEAKENIERHIQSLRAKGRTVFQaVRENSEDArewQS 998
Cdd:cd07133 246 YVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIE-LNPAGEDF---AA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 999 GTFIPPTLIeLESFDELK---KEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVN 1075
Cdd:cd07133 317 TRKLPPTLV-LNVTDDMRvmqEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIN 393
|
330 340
....*....|....*....|..
gi 1588278917 1076 RNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:cd07133 394 DTLLHVAQDDLPFGGVGASGMG 415
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
768-1097 |
5.99e-28 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 119.75 E-value: 5.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIaAQGVAILLEAGVPPGVIQLLPGrGETVGAALTTdER 847
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT-SKLMAKLLTKYLDPSYVRVIEG-GVEVTTELLK-EP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 848 VRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQE 927
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENL------TPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 928 EIADHTLTMLRGAMGEcRMGNPGRLTTDIGPVIDAEAKENIERHIQSlrAKGRTVFQAvrENSEDARewqsgtFIPPTLI 1007
Cdd:PTZ00381 260 SIKDKFIEALKEAIKE-FFGEDPKKSEDYSRIVNEFHTKRLAELIKD--HGGKVVYGG--EVDIENK------YVAPTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1008 ELESFDE--LKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHT---RIDETIAQVTGSakvGNLYVNRNMVGAV 1082
Cdd:PTZ00381 329 VNPDLDSplMQEEIFGPILPILTY--ENIDEVLEFINSRPKPLALYYFGedkRHKELVLENTSS---GAVVINDCVFHLL 403
|
330
....*....|....*
gi 1588278917 1083 VGVQPFGGEGLSGTG 1097
Cdd:PTZ00381 404 NPNLPFGGVGNSGMG 418
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
684-1075 |
7.66e-27 |
|
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: 115.72 E-value: 7.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 684 IELALTSAVNNAPIWFATPPQERAAILERAAVLMEDQMQTLIGILVREAG-----------------KTFSNAIAEvrea 746
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpearlqgelgrttgqlRLFADLVRE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 747 vdflHYYAGQVRDDFDNE-----------THRPLGPVVCISPWNFPLAIFT--GQIAAALAAGNSVLAK--PA--EQTPL 809
Cdd:cd07129 77 ----GSWLDARIDPADPDrqplprpdlrrMLVPLGPVAVFGASNFPLAFSVagGDTASALAAGCPVVVKahPAhpGTSEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 810 IAAQGVAILLEAGVPPGVIQLLPGRGETVGAALTTDERVRGVMFTGSTEVATLLQRNIASRLDaqgrPTPLIAETGGMNA 889
Cdd:cd07129 153 VARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPE----PIPFYAELGSVNP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 890 MIVDSSALTEQVviDVLASAFD-----SAGQRCSA--LrILCLQEEIADHTLTMLRGAMGECrmgNPGRLTTdigpvida 962
Cdd:cd07129 229 VFILPGALAERG--EAIAQGFVgsltlGAGQFCTNpgL-VLVPAGPAGDAFIAALAEALAAA---PAQTMLT-------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 963 eakENIERHIQSLRA--KGRTVFQAVRENSEDAREWQSgtfiPPTL--IELESF---DELKKEVFGPVLHVVRYnrNELD 1035
Cdd:cd07129 295 ---PGIAEAYRQGVEalAAAPGVRVLAGGAAAEGGNQA----APTLfkVDAAAFladPALQEEVFGPASLVVRY--DDAA 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1588278917 1036 QLVEQINASGYGLTLGVH--TRIDETIAQVTG--SAKVGNLYVN 1075
Cdd:cd07129 366 ELLAVAEALEGQLTATIHgeEDDLALARELLPvlERKAGRLLFN 409
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
706-1097 |
2.80e-23 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 104.61 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 706 RAAILERAAVLMEDQMQTLIGILVREAGKT-FSNAIAEV-------REAVDFLHYYAG--QVRDDFDNET------HRPL 769
Cdd:cd07132 22 RIQQLEALLRMLEENEDEIVEALAKDLRKPkFEAVLSEIllvkneiKYAISNLPEWMKpePVKKNLATLLddvyiyKEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 770 GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPlIAAQGVAILLEAGVPPGVIQLLPGrgetvGAALTT---DE 846
Cdd:cd07132 102 GVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP-ATAKLLAELIPKYLDKECYPVVLG-----GVEETTellKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 847 RVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALR-ILCl 925
Cdd:cd07132 176 RFDYIFYTGSTSVGKIVMQAAAKHL------TPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDyVLC- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 926 QEEIADHTLTMLRGAMGECrMGNPGRLTTDIGPVIDaeakeniERHIQSLRA--KGRTVfqaVRENSEDAREwqsgTFIP 1003
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIIN-------DRHFQRLKKllSGGKV---AIGGQTDEKE----RYIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1004 PT-LIELESFDEL-KKEVFGPVLHVVryNRNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGA 1081
Cdd:cd07132 314 PTvLTDVKPSDPVmQEEIFGPILPIV--TVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHY 391
|
410
....*....|....*.
gi 1588278917 1082 VVGVQPFGGEGLSGTG 1097
Cdd:cd07132 392 TLDSLPFGGVGNSGMG 407
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
704-1102 |
7.71e-21 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 98.11 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 704 QERAAILER-AAVLMEDQMQtLIGILVReAGKTFSNAIAEVREAVDFLHYYAGQVRDDFDNETHRPLGPV---------- 772
Cdd:cd07128 59 HERAAMLKAlAKYLMERKED-LYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVeplskdgtfv 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 773 ------------VCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGV-PPGVIQLLPGrgeTVG 839
Cdd:cd07128 137 gqhiltprrgvaVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICG---SVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 840 AALttdERVRG---VMFTGSTEVATLLQR--NIASRldaqgrPTPLIAETGGMNAMIV--DSSALTEQ---VVIDVLASA 909
Cdd:cd07128 214 DLL---DHLGEqdvVAFTGSAATAAKLRAhpNIVAR------SIRFNAEADSLNAAILgpDATPGTPEfdlFVKEVAREM 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 910 FDSAGQRCSALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAVREN 989
Cdd:cd07128 285 TVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 990 SEDAREWQSGTFIPPTLIELESFDELKK----EVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQ-VT 1064
Cdd:cd07128 365 EVVGADAEKGAFFPPTLLLCDDPDAATAvhdvEAFGPVATLMPY--DSLAEAIELAARGRGSLVASVVTNDPAFARElVL 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1588278917 1065 GSAK-VGNLYV-NRNMVGAVVG---VQP---FGGEGLSGTGPKAGG 1102
Cdd:cd07128 443 GAAPyHGRLLVlNRDSAKESTGhgsPLPqlvHGGPGRAGGGEELGG 488
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
768-1097 |
1.65e-20 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 95.94 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgVAILLEAGVPPGVIQLLPGrGETVGAALtTDER 847
Cdd:cd07137 101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSAL-LAKLIPEYLDTKAIKVIEG-GVPETTAL-LEQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 848 VRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDS-AGQRCSALRILCLQ 926
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHL------TPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVLVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 927 EEIADHTLTMLRGAMGECRMGNPgRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAVREnsedarewQSGTFIPPTL 1006
Cdd:cd07137 252 ESFAPTLIDALKNTLEKFFGENP-KESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERD--------EKNLYIEPTI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1007 IELESFDEL--KKEVFGPVLHVVRYNRneLDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAVVG 1084
Cdd:cd07137 323 LLDPPLDSSimTEEIFGPLLPIITVKK--IEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
330
....*....|...
gi 1588278917 1085 VQPFGGEGLSGTG 1097
Cdd:cd07137 401 TLPFGGVGESGFG 413
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
709-1073 |
3.93e-20 |
|
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: 95.64 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 709 ILERAAVLM-----EDQMQTLIGilvREAGKTFSNAIAEVREAVDFLHYYAG-QVR----------DDFDNETHR---PL 769
Cdd:cd07126 67 VSHRVAHELrkpevEDFFARLIQ---RVAPKSDAQALGEVVVTRKFLENFAGdQVRflarsfnvpgDHQGQQSSGyrwPY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 770 GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGAALtTDERVR 849
Cdd:cd07126 144 GPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL-LEANPR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 850 GVMFTGSTEVATLLQRniasrlDAQGRptpLIAETGGMNAMIVDSSALTEQVVIDVL-ASAFDSAGQRCSALRILCLQEE 928
Cdd:cd07126 223 MTLFTGSSKVAERLAL------ELHGK---VKLEDAGFDWKILGPDVSDVDYVAWQCdQDAYACSGQKCSAQSILFAHEN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 929 IADHTLTMLRGAMGECRmgNPGRLTtdIGPVIDAEaKENIERHIQSLRA-KGRTVFQAVRENSEDAREWQSGT------F 1001
Cdd:cd07126 294 WVQAGILDKLKALAEQR--KLEDLT--IGPVLTWT-TERILDHVDKLLAiPGAKVLFGGKPLTNHSIPSIYGAyeptavF 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588278917 1002 IP-PTLIELESFDELKKEVFGPVLHVVRYNRNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLY 1073
Cdd:cd07126 369 VPlEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
768-1097 |
4.61e-20 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 95.18 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAqgvaiLLEAGVP----PGVIQLLPGrGETVGAALt 843
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPkyldSKAVKVIEG-GPAVGEQL- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 844 TDERVRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVD---SSALTEQVVIDVLASAFDS-AGQRCSA 919
Cdd:PLN02203 181 LQHKWDKIFFTGSPRVGRIIMTAAAKHL------TPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 920 LRILCLQEEIADHTLTMLRgAMGECRMGNPGRLTTDIGPVIDaeakeniERHIQSLR---AKGRTVFQAVRENSEDAREw 996
Cdd:PLN02203 255 IDYVLVEERFAPILIELLK-STIKKFFGENPRESKSMARILN-------KKHFQRLSnllKDPRVAASIVHGGSIDEKK- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 997 qsgTFIPPTLIELESFDE--LKKEVFGPVLHVVRYNRNEldQLVEQINASGYGLTLGVHTRiDETIAQ-VTGSAKVGNLY 1073
Cdd:PLN02203 326 ---LFIEPTILLNPPLDSdiMTEEIFGPLLPIITVKKIE--DSIAFINSKPKPLAIYAFTN-NEKLKRrILSETSSGSVT 399
|
330 340
....*....|....*....|....
gi 1588278917 1074 VNRNMVGAVVGVQPFGGEGLSGTG 1097
Cdd:PLN02203 400 FNDAIIQYACDSLPFGGVGESGFG 423
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
768-1097 |
1.28e-19 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 93.34 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgVAILLEAGVPPGVIQLLPGRGETVGAALttDER 847
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKV-IAKIIEETFDEEYVAVVEGGVEENQELL--DQK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 848 VRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFDSAGQRCSALRILCLQE 927
Cdd:cd07136 177 FDYIFFTGSVRVGKIVMEAAAKHL------TPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 928 EIADHTLTMLRGAMGEcRMGNPGRLTTDIGPVIDaeakeniERHIQSLRA---KGRTVFQAvrENSEDARewqsgtFIPP 1004
Cdd:cd07136 251 SVKEKFIKELKEEIKK-FYGEDPLESPDYGRIIN-------EKHFDRLAGlldNGKIVFGG--NTDRETL------YIEP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1005 TLIELESFDE--LKKEVFGPVLHVVRYnrNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAV 1082
Cdd:cd07136 315 TILDNVTWDDpvMQEEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLA 392
|
330
....*....|....*
gi 1588278917 1083 VGVQPFGGEGLSGTG 1097
Cdd:cd07136 393 NPYLPFGGVGNSGMG 407
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
768-1101 |
6.69e-17 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 85.48 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 768 PLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQgVAILLEAGVPPGVIQLLPGRGETVGAALttDER 847
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAL-LAKLLEQYLDSSAVRVVEGAVTETTALL--EQK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 848 VRGVMFTGSTEVATLLQRNIASRLdaqgrpTPLIAETGGMNAMIVDSSALTEQVVIDVLASAFD-SAGQRCSALRILCLQ 926
Cdd:PLN02174 189 WDKIFYTGSSKIGRVIMAAAAKHL------TPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 927 EEIADHTLTMLRGAMGECRMGNPGRlTTDIGPVIDAEAKENIERHIQSLRAKGRTVF--QAVRENSEdarewqsgtfIPP 1004
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYggEKDRENLK----------IAP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 1005 TLIELESFDEL--KKEVFGPVLHVVryNRNELDQLVEQINASGYGLTLGVHTRIDETIAQVTGSAKVGNLYVNRNMVGAV 1082
Cdd:PLN02174 332 TILLDVPLDSLimSEEIFGPLLPIL--TLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLA 409
|
330
....*....|....*....
gi 1588278917 1083 VGVQPFGGEGLSGTGPKAG 1101
Cdd:PLN02174 410 LHTLPFGGVGESGMGAYHG 428
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
89-136 |
2.52e-16 |
|
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: 74.04 E-value: 2.52e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1588278917 89 SVTRASITAAYRRAETDAVPMLLEQARLPQPLAEQAHKLAYQLAEKLR 136
Cdd:pfam18327 1 SPLRQAITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
705-1029 |
4.87e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 82.83 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 705 ERAAILERAAVLMEDQMQTLIGILVREAGKTFSNAIAEVREAVDFLHYYA------GQVRDDFDNETHR----------- 767
Cdd:PRK11903 64 QRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAklgaalGDARLLRDGEAVQlgkdpafqgqh 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 768 ---PL-GPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGVAILLEAGV-PPGVIQLLPGRGETVGAAL 842
Cdd:PRK11903 144 vlvPTrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 843 TTDERVRgvmFTGSTEVATLLqRNIASRLDAQGRptpLIAETGGMNAMI-----VDSSALTEQVVIDVLASAFDSAGQRC 917
Cdd:PRK11903 224 QPFDVVS---FTGSAETAAVL-RSHPAVVQRSVR---VNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQKC 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 918 SALRILCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLRAKGRTVFQAVRENSEDArEWQ 997
Cdd:PRK11903 297 TAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGGFALVDA-DPA 375
|
330 340 350
....*....|....*....|....*....|....*.
gi 1588278917 998 SGTFIPPTLIELESFDELKK----EVFGPVLHVVRY 1029
Cdd:PRK11903 376 VAACVGPTLLGASDPDAATAvhdvEVFGPVATLLPY 411
|
|
| PutA1 |
COG3905 |
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
2-67 |
1.46e-14 |
|
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];
Pssm-ID: 443111 Cd Length: 69 Bit Score: 69.47 E-value: 1.46e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1588278917 2 GTTTMGVKLDDATRERIKFAASRIDRTPHWLIKQAIFNYLEKLENDETLPE--LPALLAGAANESDDV 67
Cdd:COG3905 1 STTTTTVRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQegLAAADAGEFVSHEEV 68
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
767-1082 |
1.06e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 65.96 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 767 RPLGPVVCISP---WNFPLAIFtgqiaAALAAGNSVLAKPAEQTPLIAAQGV----AILLEAGVPPGVIQLLP-GRGETV 838
Cdd:cd07127 194 RGVALVIGCSTfptWNGYPGLF-----ASLATGNPVIVKPHPAAILPLAITVqvarEVLAEAGFDPNLVTLAAdTPEEPI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 839 GAALTTDERVRGVMFTGSTEVATLLQRNIasrldaqgRPTPLIAETGGMNAMIVDSsalTEQVVIDVLASAFDSA---GQ 915
Cdd:cd07127 269 AQTLATRPEVRIIDFTGSNAFGDWLEANA--------RQAQVYTEKAGVNTVVVDS---TDDLKAMLRNLAFSLSlysGQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 916 RCSALRILCLQ-------------EEIADHTLTMLRGAmgecrMGNPGRLTTDIGPVIDaeakENIERHIQSLRAKGRTV 982
Cdd:cd07127 338 MCTTPQNIYVPrdgiqtddgrksfDEVAADLAAAIDGL-----LADPARAAALLGAIQS----PDTLARIAEARQLGEVL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 983 FQA-VRENSE--DARewqsgtFIPPTLIELESFDE--LKKEVFGPVLHVVRYNRNE--LDQLVEQINASGyGLTLGVHTR 1055
Cdd:cd07127 409 LASeAVAHPEfpDAR------VRTPLLLKLDASDEaaYAEERFGPIAFVVATDSTDhsIELARESVREHG-AMTVGVYST 481
|
330 340
....*....|....*....|....*..
gi 1588278917 1056 IDETIAQVTGSAKVGNLYVNRNMVGAV 1082
Cdd:cd07127 482 DPEVVERVQEAALDAGVALSINLTGGV 508
|
|
| RHH_CopAso-like |
cd22233 |
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
4-46 |
9.80e-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: 49.29 E-value: 9.80e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1588278917 4 TTMGVKLDDATRERIKFAASRIDRTPHWLIKQAIFNYLEKLEN 46
Cdd:cd22233 1 TTLSVRLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLEREEW 43
|
|
| RHH_CopG_NikR-like |
cd21631 |
ribbon-helix-helix domains of transcription repressor CopG, nickel responsive transcription ... |
4-45 |
1.34e-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: 45.96 E-value: 1.34e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1588278917 4 TTMGVKLDDATRERIKFAASRIDRTPHWLIKQAIFNYLEKLE 45
Cdd:cd21631 1 KRVTIKLDDELLERLDELARKRGVSRSELIREALREYLERLE 42
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| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
768-996 |
1.75e-03 |
|
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: 42.21 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 768 PLGPVVCISPWNFPLAIFTgQIAAALAAGNSVLAKPAEQTPlIAAQGVAILLEAGVPPG----VIQLLPGRGETVGAALT 843
Cdd:cd07077 100 PIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAAHgpkiLVLYVPHPSDELAEELL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588278917 844 TDERVRGVMFTGSTEVATLLQRNiasrldaqGRPTPLIAETGGMNAMIVDSSALTEQVVIDVLASA-FDSAGqrCSALRI 922
Cdd:cd07077 178 SHPKIDLIVATGGRDAVDAAVKH--------SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKfFDQNA--CASEQN 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1588278917 923 LCLQEEIADHTLTMLRGAMGECRMGNPGRLTTDIGPVIDAEAKENIERHIQSLrakgrTVFQAVRENSEDAREW 996
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLKLVVEGLKVPQETKPLSKETTPSFDDEALESMTPLE-----CQFRVLDVISAVENAW 316
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|
| COG4710 |
COG4710 |
Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
1-45 |
5.66e-03 |
|
Predicted DNA-binding protein with an HTH domain [General function prediction only];
Pssm-ID: 443745 Cd Length: 76 Bit Score: 36.80 E-value: 5.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1588278917 1 MGTTTmgVKLDDATRERIKFAASRIDRTPHWLIKQAIFNYLEKLE 45
Cdd:COG4710 1 MKMLS--IRLPEELEARLDALAKRTGRSKSFYVREAIEEYLDDLE 43
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