|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
7-1030 |
0e+00 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 1431.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 7 DLPSSLASFAGIRDNLFRDEAEAIGSLLPLARLDEQAEKAVHVRTLSLAQGVRQAASKNH-FEAFLQSYGLGSEEGVALM 85
Cdd:PRK11904 6 ILQSLDELRAAISALYRVDEAAYLRELLELAPLSPEEKARVTARATQLVEAVRAKKKKLGgIDAFLQEYSLSTEEGIALM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 86 ALAEALLRIPDTNTQDQLIRDLLESRDWRR--SQTATWLVSAASRALLFTDSWIDASEGRHW-----FDRLLRKMGEPVL 158
Cdd:PRK11904 86 CLAEALLRIPDAATADALIRDKLSGADWKKhlGRSDSLFVNASTWGLMLTGKVVKLDKKADGtpsgvLKRLVNRLGEPVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 159 RSAMKAGMKVMANNFVVGETIEEALNNA----DKRWRYSYDMLGEAALTNADAEAYFRAYHEAIAALGRREDKQQGFARQ 234
Cdd:PRK11904 166 RKAMRQAMKIMGKQFVLGRTIEEALKRArsarNKGYRYSFDMLGEAALTAADAERYFKAYARAIEAIGRAAGGADLPARP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 235 SISVKLSAIHPRYEFAQLERVQTELYGRLLDLAQAAAKADLVFSIDAEESERLEISLWLYERLLREPSLKNWRGLGLVVQ 314
Cdd:PRK11904 246 GISIKLSALHPRYEAAQRERVLAELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGFGLAVQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 315 AYQKRAPFVIDWLAELAADTGRVLPIRLVKGAYWDSEIKRAQQNGLAGYPVYTRKHHTDVAYLACARKLLDHgPERFYPQ 394
Cdd:PRK11904 326 AYQKRALPVLDWLADLARRQGRRIPVRLVKGAYWDSEIKRAQELGLPGYPVFTRKAATDVSYLACARKLLSA-RGAIYPQ 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 395 FASHNAQTLSWIVEATRNRGnsFEIQRLHGMGEALHSQIHEREGVASRVYAPVGRFHALLPYLVRRLLENGANSSFVHQL 474
Cdd:PRK11904 405 FATHNAHTVAAILEMAGHRG--FEFQRLHGMGEALYDALLDAPGIPCRIYAPVGSHKDLLPYLVRRLLENGANSSFVHRL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 475 ADTRVPLESIADNPAQTVAR--QAVTPGVKAPCDVFAP-RRNSQGFAMTDIVTLEPLRQRLAALESGTFHATPIVGGqrp 551
Cdd:PRK11904 483 VDPDVPIEELVADPVEKLRSfeTLPNPKIPLPRDIFGPeRKNSKGLNLNDRSELEPLAAAIAAFLEKQWQAGPIING--- 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 552 AGTGQPRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTL 631
Cdd:PRK11904 560 EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 632 PDALGELREAVDYCRFYAHEARRLMGAAIALPGVTGESNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKP 711
Cdd:PRK11904 640 QDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKP 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 712 SRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLIAETGG 791
Cdd:PRK11904 720 AEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIVPLIAETGG 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 792 LNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQR 871
Cdd:PRK11904 800 QNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKA 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 872 DLQAYCDKLAGTARLVGRTPQPAELSGGCFFAPHAFEVA-LDQLpTFETFGPVLHIARFKGDQLADAVHRVNKLGFGLTM 950
Cdd:PRK11904 880 NLDAHIERMKREARLLAQLPLPAGTENGHFVAPTAFEIDsISQL-EREVFGPILHVIRYKASDLDKVIDAINATGYGLTL 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 951 GVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTGFKAGGPHYLLRFACERTVTINTAAVGGNVKLMA 1030
Cdd:PRK11904 959 GIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTVTVNTTAAGGNASLLS 1038
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
4-1009 |
0e+00 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 1257.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 4 LYPDLPSSLASFAGIRDNLFRDEAEAIGSLLPLARLDEQAEKAVHVRTLSLAQGVRQAASKNHFEAFLQSYGLGSEEGVA 83
Cdd:PRK11905 5 FAPPFRPQSALRQAITAAYRRDEAEAVQALLEAATLSDEARAAIRERARKLVEALRAKRKGTGVEALLQEYSLSSQEGVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 84 LMALAEALLRIPDTNTQDQLIRDLLESRDWRR--SQTATWLVSAASRALLFTDSWIDASEGR---HWFDRLLRKMGEPVL 158
Cdd:PRK11905 85 LMCLAEALLRIPDTATRDALIRDKIAPGDWKShlGGSKSLFVNAATWGLMLTGKLLSTVNDRglsAALTRLIARLGEPVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 159 RSAMKAGMKVMANNFVVGETIEEALNNADKRW----RYSYDMLGEAALTNADAEAYFRAYHEAIAALGRREDKQQGFARQ 234
Cdd:PRK11905 165 RKAVDMAMRMMGEQFVTGETIEEALKRARELEargyRYSYDMLGEAARTAADAERYYRDYERAIHAIGKAATGRGVYDGP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 235 SISVKLSAIHPRYEFAQLERVQTELYGRLLDLAQAAAKADLVFSIDAEESERLEISLWLYERLLREPSLKNWRGLGLVVQ 314
Cdd:PRK11905 245 GISVKLSALHPRYERAQRERVMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGIGFVVQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 315 AYQKRAPFVIDWLAELAADTGRVLPIRLVKGAYWDSEIKRAQQNGLAGYPVYTRKHHTDVAYLACARKLLDHgPERFYPQ 394
Cdd:PRK11905 325 AYQKRCPFVIDYLIDLARRSGRRLMVRLVKGAYWDAEIKRAQVDGLEGFPVFTRKVHTDVSYIACARKLLAA-RDVIYPQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 395 FASHNAQTLSWIVEATRNRgNSFEIQRLHGMGEALHSQI--HEREGVASRVYAPVGRFHALLPYLVRRLLENGANSSFVH 472
Cdd:PRK11905 404 FATHNAQTLAAIYELAGGK-GDFEFQCLHGMGEPLYDQVvgKEKLGRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVN 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 473 QLADTRVPLESIADNPAQTVARQAVT--PGVKAPCDVFAP-RRNSQGFAMTDIVTLEPLRQRLAALESGTFHATPIVGGQ 549
Cdd:PRK11905 483 RIVDENVPVEELIADPVEKVAAMGVAphPQIPLPRDLYGPeRRNSKGLDLSDEATLAALDEALNAFAAKTWHAAPLLAGG 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 550 RPAGTGQPRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGK 629
Cdd:PRK11905 563 DVDGGTRPVLNPADHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGK 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 630 TLPDALGELREAVDYCRFYAHEARRLMGAAIALPgvtgesnelrlsgRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIA 709
Cdd:PRK11905 643 TLANAIAEVREAVDFLRYYAAQARRLLNGPGHKP-------------LGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 710 KPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLIAET 789
Cdd:PRK11905 710 KPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLIAET 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 790 GGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLS 869
Cdd:PRK11905 790 GGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEA 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 870 QRDLQAYCDKLAGTARLVGRTPQPAELSGGCFFAPHAFEVA-LDQLpTFETFGPVLHIARFKGDQLADAVHRVNKLGFGL 948
Cdd:PRK11905 870 QANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAPTLIEIDsISDL-EREVFGPVLHVVRFKADELDRVIDDINATGYGL 948
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708270319 949 TMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTGFKAGGPHYLLRF 1009
Cdd:PRK11905 949 TFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRL 1009
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
1-1037 |
0e+00 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 1063.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 1 MTPLYPDLPSSLASFAGIRDNLFRDEAEAIGSLLPLARLDEQAEKAVHVRTLSLAQGVRQAASKNHFEAFLQSYGLGSEE 80
Cdd:COG4230 3 FALFAPLLRPALPLRAAIAAAERAEELLAAAALLAAAALAAAAAAAAAAAALAARERVRARRGGGGGLLLLLELSSLSSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 81 GVALMALAEALLRIPDTNTQDQLIRDLL-ESRDWRRSQTATWLVSAASRALLFTDSWIDASEGRHW----FDRLLRKMGE 155
Cdd:COG4230 83 ALALLLLALLLLALAATRDAAARDDDDKgDGASHLGSSSSSSSSAAAATLLLLGLLLLTALESSLSlasgLLRLLGRLGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 156 PVLRSAMKAGMKVMANNFVVGETIEEALNNADKRWR----YSYDMLGEAALTNADAEAYFRAYHEAIAALGRREDKQQGF 231
Cdd:COG4230 163 PGIRRAMRAAMMMMMGLFGVGFVTEEAAEAARKAARkreyYYYDMLGEAAAAAADAAAYAYAYAAAAAAAIAAAGGGSGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 232 ARQSI----SVKLSAIHPRYEFAQLERVQTELYGRLLDLAQAAAKADLVFSIDAEESERLEISLWLYERLLREPSLKNWR 307
Cdd:COG4230 243 PGPSIssslSVLLSARHPRYRRRREERLLLLLLPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 308 GLGLVVQAYQKRAPFVIDWLAELAADTGRVLPIRLVKGAYWDSEIKRAQQNGLAGYPVYTRKHHTDVAYLACARKLLDHG 387
Cdd:COG4230 323 GVGQAVQAYAKALLLVLDLLARRRRRRRRRLVVRLVKGAEWDREIQRAQVLGYVVYPVTTRKVLYDAAALALALLLLAAQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 388 PeRFYPQFASHNAQTLswIVEATRNRGNSFEIQRLHGMGEALHSQI-HEREGVASRVYAPVGRFHALLPYLVRRLLENGA 466
Cdd:COG4230 403 P-AFAPQFATHAAATA--AAAAAAGGGGEFEFQCLHGMGEYLYDQVgRGKLGRPCRIYAPVGSHEDLLAYLVRRLLENGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 467 NSSFVHQLADTRVPLESIADNPAQTVARQAVT--PGVKAPCDVFAP-RRNSQGFAMTDIVTLEPLRQRLAALESGTFHAT 543
Cdd:COG4230 480 NSSFVNRIADEDVPVEELIADPVEKARALGGAphPRIPLPRDLYGPeRRNSAGLDLSDEAVLAALSAALAAAAEKQWQAA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 544 PIVGGQRPAGTGQPRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWLL 623
Cdd:COG4230 560 PLIAGEAASGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 624 SREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIalpgvtgesnelRLSGRGPFIAIAPWNFPLAIFLGQITAALAA 703
Cdd:COG4230 640 VREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPT------------VLRGRGVFVCISPWNFPLAIFTGQVAAALAA 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 704 GNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIA 783
Cdd:COG4230 708 GNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 784 SLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGP 863
Cdd:COG4230 788 PLIAETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGP 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 864 TIDTLSQRDLQAYCDKLAGTARLVGRTPQPAELSGGCFFAPHAFEVA-LDQLPTfETFGPVLHIARFKGDQLADAVHRVN 942
Cdd:COG4230 868 VIDAEARANLEAHIERMRAEGRLVHQLPLPEECANGTFVAPTLIEIDsISDLER-EVFGPVLHVVRYKADELDKVIDAIN 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 943 KLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTGFKAGGPHYLLRFACERTVTINTAAV 1022
Cdd:COG4230 947 ATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTVTVNTTAA 1026
|
1050
....*....|....*
gi 1708270319 1023 GGNVKLMAGGEGEHA 1037
Cdd:COG4230 1027 GGNASLLALGDWLAS 1041
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
24-1013 |
0e+00 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 988.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 24 RDEAEAIGSLLPLARLDEQAEKAVHVRTLSLAQGVRQAASKN----HFEAFLQSYGLGSEEGVALMALAEALLRIPDTNT 99
Cdd:PRK11809 101 RPETEAVPMLLEQARLPAPLAEAAHKLAYQLAEKLRNQKSAGgragMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKAT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 100 QDQLIRDLLESRDWR----RSQTAtwLVSAASRALLFTDSWI----DASEGRHwFDRLLRKMGEPVLRSAMKAGMKVMAN 171
Cdd:PRK11809 181 RDALIRDKISNGNWQshlgRSPSL--FVNAATWGLLFTGKLVsthnEASLSSS-LNRIIGKSGEPLIRKGVDMAMRLMGE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 172 NFVVGETIEEALNNA----DKRWRYSYDMLGEAALTNADAEAYFRAYHEAIAALGRREDKQQGFARQSISVKLSAIHPRY 247
Cdd:PRK11809 258 QFVTGETIAEALANArkleEKGFRYSYDMLGEAALTEADAQAYLASYEQAIHAIGKASNGRGIYEGPGISIKLSALHPRY 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 248 EFAQLERVQTELYGRLLDLAQAAAKADLVFSIDAEESERLEISLWLYERLLREPSLKNWRGLGLVVQAYQKRAPFVIDWL 327
Cdd:PRK11809 338 SRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 328 AELAADTGRVLPIRLVKGAYWDSEIKRAQQNGLAGYPVYTRKHHTDVAYLACARKLLDhGPERFYPQFASHNAQTLSWIV 407
Cdd:PRK11809 418 IDLARRSRRRLMIRLVKGAYWDSEIKRAQVDGLEGYPVYTRKVYTDVSYLACARKLLA-VPNLIYPQFATHNAHTLAAIY 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 408 EATrnrGNS-----FEIQRLHGMGEALHSQIHERegVAS-------RVYAPVGRFHALLPYLVRRLLENGANSSFVHQLA 475
Cdd:PRK11809 497 HLA---GQNyypgqYEFQCLHGMGEPLYEQVVGK--VADgklnrpcRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIA 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 476 DTRVPLESIADNPAQTVARQAVT--------PGVKAPCDVFAP-RRNSQGFAMTDivtleplRQRLAALESG-------T 539
Cdd:PRK11809 572 DTSLPLDELVADPVEAVEKLAQQegqlglphPKIPLPRDLYGKgRANSAGLDLAN-------EHRLASLSSAllasahqK 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 540 FHATPIVGGQRPAGTGQPRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEF 619
Cdd:PRK11809 645 WQAAPMLEDPVAAGEMSPVINPADPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTL 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 620 LWLLSREAGKTLPDALGELREAVDYCRFYAHEARRlmgaaialpgvtGESNElrlSGR--GPFIAIAPWNFPLAIFLGQI 697
Cdd:PRK11809 725 MGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRD------------DFDND---THRplGPVVCISPWNFPLAIFTGQV 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 698 TAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAA 777
Cdd:PRK11809 790 AAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAG 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 778 R---DSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDP 854
Cdd:PRK11809 870 RldpQGRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNP 949
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 855 LQLATDVGPTIDTLSQRDLQAYCDKLAGTARLVGRTPQP--AELSGGCFFAPHAFEV-ALDQLpTFETFGPVLHIARFKG 931
Cdd:PRK11809 950 DRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAAREnsEDWQSGTFVPPTLIELdSFDEL-KREVFGPVLHVVRYNR 1028
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 932 DQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTGFKAGGPHYLLRFAC 1011
Cdd:PRK11809 1029 NQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLA 1108
|
..
gi 1708270319 1012 ER 1013
Cdd:PRK11809 1109 TR 1110
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
466-1029 |
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: 667.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 466 ANSSFVHQLADTRVPLEsiadnpaqtvarqavtpgvkapcdvfaprrnsqgfamtdivtlePLRQRLAALESGTFHATPI 545
Cdd:cd07125 1 ANSSFVNRIFDLEVPLE--------------------------------------------ALADALKAFDEKEWEAIPI 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 546 VGGQR-PAGTGQPRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWLLS 624
Cdd:cd07125 37 INGEEtETGEGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 625 REAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIaLPGVTGESNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAG 704
Cdd:cd07125 117 AEAGKTLADADAEVREAIDFCRYYAAQARELFSDPE-LPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 705 NTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIAS 784
Cdd:cd07125 196 NTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 785 LIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPT 864
Cdd:cd07125 276 LIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 865 IDTLSQRDLQAYCDKLAGTARLVGRTPQPAElsGGCFFAPHAFE-VALDQLPTfETFGPVLHIARFKGDQLADAVHRVNK 943
Cdd:cd07125 356 IDKPAGKLLRAHTELMRGEAWLIAPAPLDDG--NGYFVAPGIIEiVGIFDLTT-EVFGPILHVIRFKAEDLDEAIEDINA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 944 LGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTGFKAGGPHYLLRFACERTVTINTAAVG 1023
Cdd:cd07125 433 TGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGPNYLLRFGNEKTVSLNTTAAG 512
|
....*.
gi 1708270319 1024 GNVKLM 1029
Cdd:cd07125 513 GNPSLL 518
|
|
| PutA |
COG0506 |
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ... |
37-1025 |
4.99e-173 |
|
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: 531.93 E-value: 4.99e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 37 ARLDEQAEKAVHVRTLSLAQGVRqAASKNHFEAFLQSYGLGSEEGVALMALAEALLRIPDTNTQDQLIRDLLesrdwrrS 116
Cdd:COG0506 3 AALDEALRARAVALARRLVEAIR-AAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKL-------A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 117 QTATWLVSAASRALLFTdswidasegrhwfdrLLRKMGEPVLRSAMKAGMKVMANNFVVGETIEEALNNADKRW----RY 192
Cdd:COG0506 75 KSPSFLVNASTWGLMLT---------------LVGRLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRakgyRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 193 SYDMLGEAALTNADAEAYFRAYHEAIAALGRRedkqqGFARQSISVKLSAIHPRYEFAQLERVQTELYGRLLDLAQAAAK 272
Cdd:COG0506 140 SLDLLGEAVLTEAEAERYLDAYLEALEAIGAA-----GVDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAARE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 273 ADLVFSIDAEESERLEISLWLYERLLREPSLKNWRGLGLVVQAYQKRAPFVIDWLAELAADTGRVLPIRLVKGAYWDSEI 352
Cdd:COG0506 215 AGIFVTIDMEEYDRLDLTLDVFERLLADPELAGWPGVGIVLQAYLKRAEADLDRLAALARRGGRRIRVRLVKGAYWDPEI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 353 KRAQQNGLaGYPVYTRKHHTDVAYLACARKLLDHGpERFYPQFASHNAQTLSWIVEATRNRG---NSFEIQRLHGMGEAL 429
Cdd:COG0506 295 VRAQVHGW-PYPVFTRKADTDANYLRCARKLLEAG-DAIYPQFATHNARTIAAALALAGERGrppDRFEFQMLYGMGEDL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 430 HSQIHEREGVASRVYAPVG---RFHALLPYLVRRLLENGANSSFVHQLADTRVPLESIADNPAQTVARQAVTPGVKAPcD 506
Cdd:COG0506 373 QRALAAVDGGRLLLYCPVVapvGGDAALAYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPP-P 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 507 VFAPRRNSQGFAMTDIVTLEPLRQRLAALESGTF----HATPIVGGQRPAGTGQPRVSPIDLERKIGTLVATDAAAVAKA 582
Cdd:COG0506 452 LRRQRRRRRRARGGALAAALAAAAAAAALAAAAAaaaaLAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 583 LDLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAL 662
Cdd:COG0506 532 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAAAAAARAAAPPPP 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 663 PGVTGESNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGE 742
Cdd:COG0506 612 PPGGLVALLPLGPLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGG 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 743 SGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFnSAGQRC 822
Cdd:COG0506 692 GAGGAAALTLAAAAAAATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASA-SASASL 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 823 SALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLAGTARLVGRTPQPAELSGGCFF 902
Cdd:COG0506 771 LSLLALLLLDADLVILLLALAAAAAALLVGGPGAAALALGIVEDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAP 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 903 APHAFEVALDQLPTFETFGPVLHIARFKGDQLADAVHRVNKLGFGLTM-GVHTRLDSTVETVRKLAKVGNLYINRNQIGA 981
Cdd:COG0506 851 LLVALILGLIVLVLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGgIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGG 930
|
970 980 990 1000
....*....|....*....|....*....|....*....|....
gi 1708270319 982 VVGSQPFGGEGLSGTGFKAGGPHYLLRFACERTVTINTAAVGGN 1025
Cdd:COG0506 931 GGGGGGGGGGGGGGGGGGGGGAGTLALAAAAAAATALAAAAAAA 974
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
506-1009 |
8.34e-166 |
|
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: 496.74 E-value: 8.34e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 506 DVFA-PRRNSQGFAMTDIVTLEPLRQRLAALESGTFHATPIVGGQ-RPAGTGQPRVSPIDLERKIGTLVATDAAAVAKAL 583
Cdd:TIGR01238 1 DLYGeGRKNSLGIDLDNESELKPLEAQIHAWADKTWQAAPIIGHSyKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 584 DLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALP 663
Cdd:TIGR01238 81 DSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 664 gvtgesnelrlsgRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGES 743
Cdd:TIGR01238 161 -------------RGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 744 GGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCS 823
Cdd:TIGR01238 228 ADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 824 ALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLAGTARLVGR--TPQPAELSGGCF 901
Cdd:TIGR01238 308 ALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQltLDDSRACQHGTF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 902 FAPHAFEV-ALDQLPTfETFGPVLHIARFKGDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIG 980
Cdd:TIGR01238 388 VAPTLFELdDIAELSE-EVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVG 466
|
490 500
....*....|....*....|....*....
gi 1708270319 981 AVVGSQPFGGEGLSGTGFKAGGPHYLLRF 1009
Cdd:TIGR01238 467 AVVGVQPFGGQGLSGTGPKAGGPHYLYRL 495
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
526-1018 |
3.59e-145 |
|
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: 443.17 E-value: 3.59e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 526 EPLRQRLAALESGTFHATPIVGGQRPAGTG--QPRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAA 603
Cdd:cd07083 2 RAMREALRRVKEEFGRAYPLVIGGEWVDTKerMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 604 LLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGVTGESNELRLSGRGPFIAI 683
Cdd:cd07083 82 LLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 684 APWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTG 763
Cdd:cd07083 162 SPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 764 STGAAWKINRTLA---ARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIE 840
Cdd:cd07083 242 SLETGKKIYEAAArlaPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 841 RLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLAGTARLVGRTPQPAelSGGCFFAPHAFEVALDQLPTF--E 918
Cdd:cd07083 322 RLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRLE--GEGYFVAPTVVEEVPPKARIAqeE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 919 TFGPVLHIARFKGDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTGF 998
Cdd:cd07083 400 IFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNA 479
|
490 500
....*....|....*....|
gi 1708270319 999 KAGGPHYLLRFACERTVTIN 1018
Cdd:cd07083 480 KTGGPHYLRRFLEMKAVAER 499
|
|
| Pro_dh |
pfam01619 |
Proline dehydrogenase; |
182-473 |
4.72e-129 |
|
Proline dehydrogenase;
Pssm-ID: 426348 [Multi-domain] Cd Length: 296 Bit Score: 393.01 E-value: 4.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 182 ALNNADKRW----RYSYDMLGEAALTNADAEAYFRAYHEAIAALGRREDKQQGFARQSISVKLSAIHPRYEFAQLERVQT 257
Cdd:pfam01619 1 ALKTIEKLRkqgyRFSLDMLGEAALTEADADRYLDAYLRAIDALGKAAGPWPLGPRPGISVKLSALHPRYEPLERERVMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 258 ELYGRLLDLAQAAAKADLVFSIDAEESERLEISLWLYERLLREPSLKNWRGLGLVVQAYQKRAPFVIDWLAELAADTGRV 337
Cdd:pfam01619 81 ELLERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNGVGITLQAYLKDALAVLDWLLELARRRGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 338 LPIRLVKGAYWDSEIKRAQQnGLAGYPVYTRKHHTDVAYLACARKLLDHgPERFYPQFASHNAQTLSWIVEATRNRG--- 414
Cdd:pfam01619 161 LGVRLVKGAYWDSEIKRAQQ-GGWPYPVFTRKEATDANYEACARFLLEN-HDRIYPQFATHNARSVAAALALAEELGipp 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1708270319 415 NSFEIQRLHGMGEALHSQIHErEGVASRVYAPVGRFHALLPYLVRRLLENGANSSFVHQ 473
Cdd:pfam01619 239 RRFEFQQLYGMGDNLSFALVA-AGYRVRKYAPVGPHEELLAYLVRRLLENTANSSFVRR 296
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
544-1019 |
1.48e-119 |
|
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: 376.56 E-value: 1.48e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 544 PIVGGQRPAGTGQ-PRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWL 622
Cdd:cd07124 35 LVIGGKEVRTEEKiESRNPADPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 623 LSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAiaLPGVTGESNELRLSGRGPFIAIAPWNFPLAIFLGQITAALA 702
Cdd:cd07124 115 MVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFP--VEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 703 AGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRtLAARDSS- 781
Cdd:cd07124 193 TGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE-RAAKVQPg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 782 ---IASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLA 858
Cdd:cd07124 272 qkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 859 TDVGPTIDTLSQRDLQAYCDKLAGTARLVGRTPQPAELSGGCFFAPHAFE-VALD-QLPTFETFGPVLHIARFkgDQLAD 936
Cdd:cd07124 352 VYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEGYFVQPTIFAdVPPDhRLAQEEIFGPVLAVIKA--KDFDE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 937 AVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTGFKAGGPHYLLRFACERTVT 1016
Cdd:cd07124 430 ALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVT 509
|
...
gi 1708270319 1017 INT 1019
Cdd:cd07124 510 ENF 512
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
590-1019 |
1.50e-113 |
|
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: 359.44 E-value: 1.50e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGvTGES 669
Cdd:COG1012 56 FPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDA-PGTR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDK 749
Cdd:COG1012 135 AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILL 829
Cdd:COG1012 215 LVAHPDVDKISFTGSTAVGRRIAAAAAEN---LKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV--GRTPQPAelsGGCFFAPHA 906
Cdd:COG1012 292 VHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDaVAEGAELLtgGRRPDGE---GGYFVEPTV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 907 FEVALDQLPTF--ETFGPVLHIARFKGdqLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVG 984
Cdd:COG1012 369 LADVTPDMRIAreEIFGPVLSVIPFDD--EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ 446
|
410 420 430
....*....|....*....|....*....|....*
gi 1708270319 985 sQPFGGEGLSGTGfKAGGPHYLLRFACERTVTINT 1019
Cdd:COG1012 447 -APFGGVKQSGIG-REGGREGLEEYTETKTVTIRL 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
590-1017 |
5.71e-107 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 340.34 E-value: 5.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAaIALPGVTGES 669
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGE-VIPSPDPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDK 749
Cdd:cd07078 90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAArdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILL 829
Cdd:cd07078 170 LASHPRVDKISFTGSTAVGKAIMRAAAE---NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLVGRTPQpaELSGGCFFAPHAF 907
Cdd:cd07078 247 VHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEdaKAEGAKLLCGGKRL--EGGKGYFVPPTVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 EVALDQLP--TFETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAvVGS 985
Cdd:cd07078 325 TDVDPDMPiaQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA-EPS 401
|
410 420 430
....*....|....*....|....*....|..
gi 1708270319 986 QPFGGEGLSGTGfKAGGPHYLLRFACERTVTI 1017
Cdd:cd07078 402 APFGGVKQSGIG-REGGPYGLEEYTEPKTVTI 432
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
590-1015 |
3.10e-106 |
|
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: 339.51 E-value: 3.10e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIalPGVTGES 669
Cdd:pfam00171 42 FPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETL--PSDPGRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDK 749
Cdd:pfam00171 120 AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILL 829
Cdd:pfam00171 200 LVEHPDVRKVSFTGSTAVGRHIAEAAAQN---LKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDtLSQRD-LQAYCDK-LAGTARLVgrTPQPAELSGGCFFAPHAF 907
Cdd:pfam00171 277 VHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLIS-KAQLErVLKYVEDaKEEGAKLL--TGGEAGLDNGYFVEPTVL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 EVALDQLPTF--ETFGPVLHIARFKGdqLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGS 985
Cdd:pfam00171 354 ANVTPDMRIAqeEIFGPVLSVIRFKD--EEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDADGL 431
|
410 420 430
....*....|....*....|....*....|
gi 1708270319 986 qPFGGEGLSGTGfKAGGPHYLLRFACERTV 1015
Cdd:pfam00171 432 -PFGGFKQSGFG-REGGPYGLEEYTEVKTV 459
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
541-1016 |
4.55e-93 |
|
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: 306.02 E-value: 4.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 541 HATPIVGGQRPAGTGQ-PRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEF 619
Cdd:TIGR01237 32 TYPLVINGERVETENKiVSINPCDKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 620 LWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALpGVTGESNELRLSGRGPFIAIAPWNFPLAIFLGQITA 699
Cdd:TIGR01237 112 SALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVN-SREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 700 ALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLA--- 776
Cdd:TIGR01237 191 PIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvq 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 777 ARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQ 856
Cdd:TIGR01237 271 PGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 857 LATDVGPTIDTLSQRDLQAYCDKLAGTARLV-GRTPQPAElsgGCFFAPHAFEvALDQLPTF---ETFGPVLHIARFKGD 932
Cdd:TIGR01237 351 ADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVsGGCGDDSK---GYFIGPTIFA-DVDRKARLaqeEIFGPVVAFIRASDF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 933 QlaDAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTGFKAGGPHYLLRFACE 1012
Cdd:TIGR01237 427 D--EALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDSKAGGPDYLALFMQA 504
|
....
gi 1708270319 1013 RTVT 1016
Cdd:TIGR01237 505 KTVT 508
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
593-1016 |
5.82e-90 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 297.62 E-value: 5.82e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPgVTGESNEL 672
Cdd:PRK03137 89 WKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQMLKLADGKPVES-RPGEHNRY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLG 752
Cdd:PRK03137 168 FYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 753 DPRVAGVAFTGSTGAAWKINrTLAARDSS----IASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:PRK03137 248 HPKTRFITFTGSREVGLRIY-ERAAKVQPgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQlATDVGPTIDTLSQRDLQAYCDKLAGTARLVgrTPQPAELSGGCFFAPHAF- 907
Cdd:PRK03137 327 IVHEDVYDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEGRLV--LGGEGDDSKGYFIQPTIFa 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 EVA-LDQLPTFETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQ 986
Cdd:PRK03137 404 DVDpKARIMQEEIFGPVVAFIKAK--DFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYH 481
|
410 420 430
....*....|....*....|....*....|
gi 1708270319 987 PFGGEGLSGTGFKAGGPHYLLRFACERTVT 1016
Cdd:PRK03137 482 PFGGFNMSGTDSKAGGPDYLLLFLQAKTVS 511
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
590-1017 |
1.43e-86 |
|
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: 283.35 E-value: 1.43e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPgVTGES 669
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP-DPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDK 749
Cdd:cd06534 86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAardSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILL 829
Cdd:cd06534 166 LLSHPRVDKISFTGSTAVGKAIMKAAA---ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQVIERLglamqelrmgdpLQLATDVgptidtlsqrdlqaycdklagtarlvgrtpqpaelsggcffaPHAFEV 909
Cdd:cd06534 243 VHESIYDEFVEKL------------VTVLVDV------------------------------------------DPDMPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 910 AldqlpTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGaVVGSQPFG 989
Cdd:cd06534 269 A-----QEEIFGPVLPVIRF--KDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG-VGPEAPFG 340
|
410 420
....*....|....*....|....*...
gi 1708270319 990 GEGLSGTGfKAGGPHYLLRFACERTVTI 1017
Cdd:cd06534 341 GVKNSGIG-REGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
546-1018 |
3.02e-75 |
|
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: 256.12 E-value: 3.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 546 VGGQ-RPAGTGQ--PRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWL 622
Cdd:cd07131 3 IGGEwVDSASGEtfDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 623 LSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIA--LPGvtgESNELRLSGRGPFIAIAPWNFPLAIFLGQITAA 700
Cdd:cd07131 83 VTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPseLPN---KDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 701 LAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDS 780
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 781 SIAsliAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATD 860
Cdd:cd07131 240 RVA---LEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 861 VGPTIDTLSQRDLQAYCDklagTARLVGRT-------PQPAELSGGCFFAPHAFEVALDQL--PTFETFGPVLHIARFKG 931
Cdd:cd07131 317 MGPLINEAQLEKVLNYNE----IGKEEGATlllggerLTGGGYEKGYFVEPTVFTDVTPDMriAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 932 DQLADAVHrvNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVgSQPFGGEGLSGTGFKAGGPHYLLRFAC 1011
Cdd:cd07131 393 LEEAIEIA--NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFTE 469
|
....*..
gi 1708270319 1012 ERTVTIN 1018
Cdd:cd07131 470 WKAVYVD 476
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
546-1015 |
4.77e-74 |
|
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: 252.56 E-value: 4.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 546 VGGQR-PAGTGQPRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLEKAADLLEARQDEFLWLLS 624
Cdd:cd07097 5 IDGEWvAGGDGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 625 REAGKTLPDALGELREAVDYCRFYAHEARRLMG--AAIALPGVTGESNELRLsgrGPFIAIAPWNFPLAIFLGQITAALA 702
Cdd:cd07097 85 REEGKTLPEARGEVTRAGQIFRYYAGEALRLSGetLPSTRPGVEVETTREPL---GVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 703 AGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARdssI 782
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAAR---G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 783 ASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVG 862
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 863 PTIDtlsQRDLQ---AYCDK--------LAGTARLVGRTPqpaelsgGCFFAPHAFEVALDQLPTF--ETFGPVLHIARF 929
Cdd:cd07097 319 PVVS---ERQLEkdlRYIEIarsegaklVYGGERLKRPDE-------GYYLAPALFAGVTNDMRIAreEIFGPVAAVIRV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 930 KGdqLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGaVVGSQPFGGEGLSGTGFKAGGPHYLLRF 1009
Cdd:cd07097 389 RD--YDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG-VDYHVPFGGRKGSSYGPREQGEAALEFY 465
|
....*.
gi 1708270319 1010 ACERTV 1015
Cdd:cd07097 466 TTIKTV 471
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
546-1018 |
1.24e-72 |
|
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: 249.02 E-value: 1.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 546 VGGQRPAGTGQPRV---SPIDLErKIGTLVATDAAAVAKALDLADAAQDGWADQ-APtARAALLEKAADLLEARQDEFLW 621
Cdd:cd07086 2 VIGGEWVGSGGETFtsrNPANGE-PIARVFPASPEDVEAAVAAAREAFKEWRKVpAP-RRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 622 LLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIA--LPGvtgESNELRLSGRGPFIAIAPWNFPLAIFLGQITA 699
Cdd:cd07086 80 LVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPseRPG---HRLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 700 ALAAGNTVIAKPSRRTPLIGMRA----IEALLDAGIPADVLHYLPGEsGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTL 775
Cdd:cd07086 157 ALVCGNTVVWKPSETTPLTAIAVtkilAEVLEKNGLPPGVVNLVTGG-GDGGELLVHDPRVPLVSFTGSTEVGRRVGETV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 776 AARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPL 855
Cdd:cd07086 236 ARR---FGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 856 QLATDVGPTIDTLSQRDLQAYCDK--------LAGTARLVGRTPqpaelsgGCFFAPHAFEVALDQLPTF--ETFGPVLH 925
Cdd:cd07086 313 DEGTLVGPLINQAAVEKYLNAIEIaksqggtvLTGGKRIDGGEP-------GNYVEPTIVTGVTDDARIVqeETFAPILY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 926 IARFKGdqLADAVHRVNKLGFGLTMGVHTRLDSTVETVR--KLAKVGNLYINRNQIGAVVGSqPFGGEGLSGTGFKAGGP 1003
Cdd:cd07086 386 VIKFDS--LEEAIAINNDVPQGLSSSIFTEDLREAFRWLgpKGSDCGIVNVNIPTSGAEIGG-AFGGEKETGGGRESGSD 462
|
490
....*....|....*.
gi 1708270319 1004 hyLLRFACER-TVTIN 1018
Cdd:cd07086 463 --AWKQYMRRsTCTIN 476
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
590-1004 |
1.45e-71 |
|
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: 245.03 E-value: 1.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIalpgvtges 669
Cdd:cd07103 32 FKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEARRIYGRTI--------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 nELRLSGR---------GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLP 740
Cdd:cd07103 103 -PSPAPGKrilvikqpvGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAGLPAGVLNVVT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 741 GESGGLSDKLLGDPRVAGVAFTGSTGaawkINRTLAARDSS-IASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAG 819
Cdd:cd07103 182 GSPAEIGEALCASPRVRKISFTGSTA----VGKLLMAQAADtVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 820 QRC-SALRIlLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdtlSQRDLQAYC----DKLAGTARLV--GRTPQ 892
Cdd:cd07103 258 QTCvCANRI-YVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLI---NERAVEKVEalveDAVAKGAKVLtgGKRLG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 893 PaelsGGCFFAPHAFEVALDQLPTF--ETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRldsTVETVRKLAK-- 968
Cdd:cd07103 334 L----GGYFYEPTVLTDVTDDMLIMneETFGPVAPIIPF--DTEDEVIARANDTPYGLAAYVFTR---DLARAWRVAEal 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 1708270319 969 -VGNLYINRNQIGAVVgsQPFGGEGLSGTGfKAGGPH 1004
Cdd:cd07103 405 eAGMVGINTGLISDAE--APFGGVKESGLG-REGGKE 438
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
601-997 |
2.58e-70 |
|
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: 241.73 E-value: 2.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 601 RAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGVTGESNELRLSGRGPF 680
Cdd:cd07149 45 RAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGRIGFTIREPI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 681 ---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVA 757
Cdd:cd07149 125 gvvAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 758 GVAFTGSTGAAWKInrtlaARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQ 837
Cdd:cd07149 205 MISFTGSPAVGEAI-----ARKAGLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 838 VIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV------GRTPQPAELSGgcffAPHAFEVA 910
Cdd:cd07149 280 FLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEWVEEaVEGGARLLtggkrdGAILEPTVLTD----VPPDMKVV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 911 LDqlptfETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLAkVGNLYIN-----RnqigavVG 984
Cdd:cd07149 356 CE-----EVFAPVVSLNPF--DTLDEAIAMANDSPYGLQAGVFTNdLQKALKAARELE-VGGVMINdsstfR------VD 421
|
410
....*....|...
gi 1708270319 985 SQPFGGEGLSGTG 997
Cdd:cd07149 422 HMPYGGVKESGTG 434
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
557-1017 |
1.27e-68 |
|
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: 236.95 E-value: 1.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 557 PRVSPIDLERKIGTLVATdaaavakaldladaaQDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG 636
Cdd:cd07094 16 PADDRADAEEALATARAG---------------AENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 637 ELREAVDYCRFYAHEARRLMGAAIALPGVTGESNELRLSGR---GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSR 713
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLAWTIRepvGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 714 RTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKInrtlaARDSSIASLIAETGGLN 793
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL-----RANAGGKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 794 AMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDL 873
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 874 QAYCDKL--AGTARLVGRTPQpaelsgGCFFAPHAFE-VALD-QLPTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLT 949
Cdd:cd07094 316 ERWVEEAveAGARLLCGGERD------GALFKPTVLEdVPRDtKLSTEETFGPVVPIIRY--DDFEEAIRIANSTDYGLQ 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708270319 950 MGVHTR-LDSTVETVRKLaKVGNLYINRNQIgAVVGSQPFGGEGLSGTGfKAGGPHYLLRFACERTVTI 1017
Cdd:cd07094 388 AGIFTRdLNVAFKAAEKL-EVGGVMVNDSSA-FRTDWMPFGGVKESGVG-REGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
591-997 |
2.11e-67 |
|
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: 233.78 E-value: 2.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGVTGESN 670
Cdd:cd07145 35 DVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNER 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 671 ELRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLS 747
Cdd:cd07145 115 RIAFTVREPIgvvGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 748 DKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIaslIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRI 827
Cdd:cd07145 195 DEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKV---ALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 828 LLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLAGTArlvGRTPQPAELSGGCFFAPHAF 907
Cdd:cd07145 272 ILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVNDAVEKG---GKILYGGKRDEGSFFPPTVL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 EVALDQLPTF--ETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYINrNQIGAVVG 984
Cdd:cd07145 349 ENDTPDMIVMkeEVFGPVLPIAKVKDDE--EAVEIANSTEYGLQASVFTNdINRALKVAREL-EAGGVVIN-DSTRFRWD 424
|
410
....*....|...
gi 1708270319 985 SQPFGGEGLSGTG 997
Cdd:cd07145 425 NLPFGGFKKSGIG 437
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
590-1017 |
3.12e-67 |
|
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: 232.42 E-value: 3.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAlPGVTGES 669
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILP-SDVPGKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAI-EALLDAGIPADVLHYLPGESGGLSD 748
Cdd:cd07104 92 SMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLNVVPGGGSEIGD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKINRtLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:cd07104 172 ALVEHPRVRMISFTGSTAVGRHIGE-LAGRHLKKVAL--ELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTlSQRD--LQAYCDKLAGTARLV-GRTPQpaelsgGCFFAPH 905
Cdd:cd07104 249 LVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINE-RQVDrvHAIVEDAVAAGARLLtGGTYE------GLFYQPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 906 AFEVALDQLPTF--ETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTRldsTVETVRKLAK---VGNLYINRNQI- 979
Cdd:cd07104 322 VLSDVTPDMPIFreEIFGPVAPVIPFDDDE--EAVELANDTEYGLSAAVFTR---DLERAMAFAErleTGMVHINDQTVn 396
|
410 420 430
....*....|....*....|....*....|....*....
gi 1708270319 980 -GAVVgsqPFGGEGLSGtGFKAGGPHYLLRFACERTVTI 1017
Cdd:cd07104 397 dEPHV---PFGGVKASG-GGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
593-1001 |
8.29e-63 |
|
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: 220.89 E-value: 8.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALpgvtGESNEL 672
Cdd:cd07114 37 WRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAGLADKIEGAVIPV----DKGDYL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDK 749
Cdd:cd07114 113 NFTRREPLgvvAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILL 829
Cdd:cd07114 193 LVEHPLVAKIAFTGGTETGRHIARAAAEN---LAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdTLSQRD-LQAYCDK-LAGTARLV--GRTPQPAELSGGCFFAPH 905
Cdd:cd07114 270 VQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLA-TERQLEkVERYVARaREEGARVLtgGERPSGADLGAGYFFEPT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 906 AFEVALDQLPTF--ETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYINRNQigAV 982
Cdd:cd07114 349 ILADVTNDMRIAqeEVFGPVLSVIPFDDE--EEAIALANDSEYGLAAGIWTRdLARAHRVARAI-EAGTVWVNTYR--AL 423
|
410
....*....|....*....
gi 1708270319 983 VGSQPFGGEGLSGTGFKAG 1001
Cdd:cd07114 424 SPSSPFGGFKDSGIGRENG 442
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
590-1017 |
5.78e-62 |
|
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: 218.67 E-value: 5.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAlPGVTGES 669
Cdd:cd07088 48 QKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIP-SDRPNEN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDK 749
Cdd:cd07088 127 IFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAArdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILL 829
Cdd:cd07088 207 LVAHPKVGMISLTGSTEAGQKIMEAAAE---NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVY 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdtlSQRDLQAYCDKL-----AGTARLVGRTpqPAELSGGCFFAP 904
Cdd:cd07088 284 VHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV---NEAALDKVEEMVeraveAGATLLTGGK--RPEGEKGYFYEP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 905 HAFEVALDQLPTF--ETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRnqigav 982
Cdd:cd07088 359 TVLTNVRQDMEIVqeEIFGPVLPVVKF--SSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINR------ 430
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1708270319 983 vgsqpFGGEGLSG--TGFK------AGGPHYLLRFACERTVTI 1017
Cdd:cd07088 431 -----ENFEAMQGfhAGWKksglggADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
560-1017 |
7.75e-62 |
|
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: 218.59 E-value: 7.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 560 SPIDLERkIGTLVATDAAAVAKALDLADAAQDGWADQAPTA-RAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGEL 638
Cdd:cd07082 22 SPIDGEV-IGSVPALSALEILEAAETAYDAGRGWWPTMPLEeRIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 639 REAVDYCRFYAHEARRLMGAAIALPGVTGESNELRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRT 715
Cdd:cd07082 101 DRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQVRREPLgvvLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 716 PLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKInrtlaARDSSIASLIAETGGLNAM 795
Cdd:cd07082 181 VLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRL-----KKQHPMKRLVLELGGKDPA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 796 IADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQ- 874
Cdd:cd07082 256 IVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEg 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 875 AYCDKLAGTARLVgrtpQPAELSGGCFFAPHAFEVALDQLPTF--ETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGV 952
Cdd:cd07082 336 LIDDAVAKGATVL----NGGGREGGNLIYPTLLDPVTPDMRLAweEPFGPVLPIIRVN--DIEEAIELANKSNYGLQASI 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708270319 953 HTRldsTVETVRKLAK---VGNLYINRN-QIGavVGSQPFGGEGLSGTGFKagGPHYLLRFACERTVTI 1017
Cdd:cd07082 410 FTK---DINKARKLADaleVGTVNINSKcQRG--PDHFPFLGRKDSGIGTQ--GIGDALRSMTRRKGIV 471
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
601-1001 |
1.27e-60 |
|
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: 214.53 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 601 RAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGVTGESNELRLSGRGPF 680
Cdd:cd07146 42 RSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAADVLRFAAAEALRDDGESFSCDLTANGKARKIFTLREPL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 681 ---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVA 757
Cdd:cd07146 122 gvvLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 758 GVAFTGSTGAAWKINRTLAARdssiaSLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQ 837
Cdd:cd07146 202 LVTFTGGVAVGKAIAATAGYK-----RQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 838 VIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKL--AGTARLVGRTPQpaelsgGCFFAPhafeVALDQLP 915
Cdd:cd07146 277 FVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAiaQGARVLLGNQRQ------GALYAP----TVLDHVP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 916 ------TFETFGPVLHIARFKGdqLADAVHRVNKLGFGLTMGVHT-RLDSTVETVRKLaKVGNLYINrNQIGAVVGSQPF 988
Cdd:cd07146 347 pdaelvTEETFGPVAPVIRVKD--LDEAIAISNSTAYGLSSGVCTnDLDTIKRLVERL-DVGTVNVN-EVPGFRSELSPF 422
|
410
....*....|...
gi 1708270319 989 GGEGLSGTGFKAG 1001
Cdd:cd07146 423 GGVKDSGLGGKEG 435
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
591-1017 |
1.36e-59 |
|
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: 211.65 E-value: 1.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDA-LGELREAVDYCRFYAHEARRLMGAAIALPGvtGES 669
Cdd:cd07093 33 PGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTRDIPRAAANFRFFADYILQLDGESYPQDG--GAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDK 749
Cdd:cd07093 111 NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILL 829
Cdd:cd07093 191 LVAHPDVDLISFTGETATGRTIMRAAAPN---LKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRIL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV--GRTPQPAELSGGCFFAPHA 906
Cdd:cd07093 268 VQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELaRAEGATILtgGGRPELPDLEGGYFVEPTV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 907 FEVALDQLPTF--ETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYIN----RNQi 979
Cdd:cd07093 348 ITGLDNDSRVAqeEIFGPVVTVIPFDDE--EEAIELANDTPYGLAAYVWTRdLGRAHRVARRL-EAGTVWVNcwlvRDL- 423
|
410 420 430
....*....|....*....|....*....|....*....
gi 1708270319 980 gavvgSQPFGGEGLSGTGFKagGPHYLLRFACE-RTVTI 1017
Cdd:cd07093 424 -----RTPFGGVKASGIGRE--GGDYSLEFYTElKNVCI 455
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
528-1015 |
1.56e-59 |
|
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: 213.22 E-value: 1.56e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 528 LRQRLAALESGTFHATPIVGGQRPA-GTGQPRVSPIDLERKIGTLVATDAAAVAKALDLADAAQDGWADQAPTARAALLE 606
Cdd:cd07123 19 LQEALAELKSLTVEIPLVIGGKEVRtGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 607 KAADLLEARQDEflWLLSREA---GKTL----PDALGELreaVDYCRFYAHEARRLMgAAIALPGVTGESNELRLSGRGP 679
Cdd:cd07123 99 KAADLLSGKYRY--ELNAATMlgqGKNVwqaeIDAACEL---IDFLRFNVKYAEELY-AQQPLSSPAGVWNRLEYRPLEG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 680 FI-AIAPWNFPlAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAG 758
Cdd:cd07123 173 FVyAVSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 759 VAFTGSTGAAWKINRTLAARDS---SIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIA 835
Cdd:cd07123 252 LHFTGSTPTFKSLWKQIGENLDryrTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLW 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 836 DQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLV-GRTPQPAElsgGCFFAPHAFEVALD 912
Cdd:cd07123 332 PEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDhaKSDPEAEIIaGGKCDDSV---GYFVEPTVIETTDP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 913 QLPTF--ETFGPVLHIARFKGDQLADAVHRVNKLG-FGLTMGVHTRLDSTVETVRKLAK--VGNLYINRNQIGAVVGSQP 987
Cdd:cd07123 409 KHKLMteEIFGPVLTVYVYPDSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDALRnaAGNFYINDKPTGAVVGQQP 488
|
490 500
....*....|....*....|....*...
gi 1708270319 988 FGGEGLSGTGFKAGGPHYLLRFACERTV 1015
Cdd:cd07123 489 FGGARASGTNDKAGSPLNLLRWVSPRTI 516
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
592-1017 |
2.19e-59 |
|
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: 211.03 E-value: 2.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 592 GWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAlPGVTGESNE 671
Cdd:cd07150 36 AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRGETLP-SDSPGTVSM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLL 751
Cdd:cd07150 115 SVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 752 GDPRVAGVAFTGSTGAAWKINrTLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQ 831
Cdd:cd07150 195 DDPRVRMVTFTGSTAVGREIA-EKAGRHLKKITL--ELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 832 DDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTlSQRDL--QAYCDKLAGTARLVGrtpqpAELSGGCFFAPHAFEV 909
Cdd:cd07150 272 EPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISP-RQVERikRQVEDAVAKGAKLLT-----GGKYDGNFYQPTVLTD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 910 ALDQLPTF--ETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYINRNQI--GAVVg 984
Cdd:cd07150 346 VTPDMRIFreETFGPVTSVIPAKDAE--EALELANDTEYGLSAAILTNdLQRAFKLAERL-ESGMVHINDPTIldEAHV- 421
|
410 420 430
....*....|....*....|....*....|...
gi 1708270319 985 sqPFGGEGLSGTGfKAGGPHYLLRFACERTVTI 1017
Cdd:cd07150 422 --PFGGVKASGFG-REGGEWSMEEFTELKWITV 451
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
590-995 |
6.35e-59 |
|
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: 209.05 E-value: 6.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELRE-------AVDYCRFYAHEARRLMGAAIAL 662
Cdd:cd07095 13 FPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAmagkidiSIKAYHERTGERATPMAQGRAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 663 pgvtgesneLRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPG- 741
Cdd:cd07095 93 ---------LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGg 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 742 -ESGGLsdkLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQ 820
Cdd:cd07095 164 rETGEA---LAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILAL--EMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 821 RCS-ALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLAGtarLVGRTPQPAEL--S 897
Cdd:cd07095 239 RCTcARRLIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLA---LGGEPLLAMERlvA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 898 GGCFFAPHAFEV-ALDQLPTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINR 976
Cdd:cd07095 316 GTAFLSPGIIDVtDAADVPDEEIFGPLLQVYRY--DDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNR 393
|
410
....*....|....*....
gi 1708270319 977 NQIGAvVGSQPFGGEGLSG 995
Cdd:cd07095 394 PTTGA-SSTAPFGGVGLSG 411
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
592-1001 |
1.29e-58 |
|
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: 208.83 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 592 GWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGAAIALPGvtGESN 670
Cdd:cd07115 34 AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVPRAADTFRYYAGWADKIEGEVIPVRG--PFLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 671 ELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKL 750
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 751 LGDPRVAGVAFTGSTGAAWKINRTlAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLV 830
Cdd:cd07115 192 VEHPDVDKITFTGSTAVGRKIMQG-AAGNLKRVSL--ELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 831 QDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLVGRTPQPAElsgGCFFAPHAFE 908
Cdd:cd07115 269 HESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDvgREEGARLLTGGKRPGAR---GFFVEPTIFA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 909 VA--LDQLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYInrNQIGAVVGSQ 986
Cdd:cd07115 346 AVppEMRIAQEEIFGPVVSVMRFRDE--EEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWI--NTYNRFDPGS 421
|
410
....*....|....*
gi 1708270319 987 PFGGEGLSGTGFKAG 1001
Cdd:cd07115 422 PFGGYKQSGFGREMG 436
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
601-997 |
6.83e-58 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 206.71 E-value: 6.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 601 RAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAL---PGVTGESNELRLSGR 677
Cdd:cd07147 45 RAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATRIYGEVLPLdisARGEGRQGLVRRFPI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 678 GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGlSDKLLGDPRVA 757
Cdd:cd07147 125 GPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 758 GVAFTGSTGAAWKInRTLAARDssiaSLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQ 837
Cdd:cd07147 204 LLSFTGSPAVGWDL-KARAGKK----KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 838 VIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKL--AGTARLVGrtpqpAELSGGCFFAPHAFEVALDQ-L 914
Cdd:cd07147 279 FKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAvdAGAKLLTG-----GKRDGALLEPTILEDVPPDMeV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 915 PTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYInrNQIGAV-VGSQPFGGEGL 993
Cdd:cd07147 354 NCEEVFGPVVTVEPY--DDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVI--NDVPTFrVDHMPYGGVKD 429
|
....
gi 1708270319 994 SGTG 997
Cdd:cd07147 430 SGIG 433
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
590-1003 |
2.04e-57 |
|
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: 204.83 E-value: 2.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGaaIALPGVTGES 669
Cdd:cd07152 26 QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQG--EILPSAPGRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALL-DAGIPADVLHYLPGEsGGLSD 748
Cdd:cd07152 104 SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLFeEAGLPAGVLHVLPGG-ADAGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKINRtLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:cd07152 183 ALVEDPNVAMISFTGSTAVGRKVGE-AAGRHLKKVSL--ELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTlSQRD--LQAYCDKLAGTARLV-GRTPQpaelsgGCFFAPH 905
Cdd:cd07152 260 LVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINA-RQLDrvHAIVDDSVAAGARLEaGGTYD------GLFYRPT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 906 AFEVALDQLPTF--ETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINrNQIGAVV 983
Cdd:cd07152 333 VLSGVKPGMPAFdeEIFGPVAPVTVFDSD--EEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIN-DQTVNDE 409
|
410 420
....*....|....*....|
gi 1708270319 984 GSQPFGGEGLSGTGFKAGGP 1003
Cdd:cd07152 410 PHNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
590-997 |
9.12e-56 |
|
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: 200.54 E-value: 9.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAL------- 662
Cdd:cd07109 33 ESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADVEAAARYFEYYGGAADKLHGETIPLgpgyfvy 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 663 ----P-GVTGEsnelrlsgrgpfiaIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLH 737
Cdd:cd07109 113 tvrePhGVTGH--------------IIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAGLPAGALN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 738 YLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTlAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNS 817
Cdd:cd07109 179 VVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRA-AAENVVPVTL--ELGGKSPQIVFADADLEAALPVVVNAIIQN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 818 AGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLAtDVGPTIDTLSQRDLQAYCD--KLAGTARLVGRTPQPAE 895
Cdd:cd07109 256 AGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDP-DLGPLISAKQLDRVEGFVAraRARGARIVAGGRIAEGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 896 LSGGCFFAPHAFEV--ALDQLPTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNL 972
Cdd:cd07109 335 PAGGYFVAPTLLDDvpPDSRLAQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGVWTRdGDRALRVARRL-RAGQV 411
|
410 420
....*....|....*....|....*.
gi 1708270319 973 YInrNQIGAVVGSQ-PFGGEGLSGTG 997
Cdd:cd07109 412 FV--NNYGAGGGIElPFGGVKKSGHG 435
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
592-1018 |
1.40e-55 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 199.91 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 592 GWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGvtgesNE 671
Cdd:cd07107 34 EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTELKGETIPVGG-----RN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRLSGRGPF--IA-IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEaLLDAGIPADVLHYLPGESGGLSD 748
Cdd:cd07107 109 LHYTLREPYgvVArIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAE-LAREVLPPGVFNILPGDGATAGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKINRTLAardSSIASLIAETGGLNAMIADSSAHVEQLI--IDVLMSaFNSAGQRCSALR 826
Cdd:cd07107 188 ALVRHPDVKRIALIGSVPTGRAIMRAAA---EGIKHVTLELGGKNALIVFPDADPEAAAdaAVAGMN-FTWCGQSCGSTS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 827 ILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV--GRTPQPAELSGGCFFA 903
Cdd:cd07107 264 RLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSaKREGARLVtgGGRPEGPALEGGFYVE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 904 PHAF-EVALD-QLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYIN---RN 977
Cdd:cd07107 344 PTVFaDVTPGmRIAREEIFGPVLSVLRWRDE--AEMVAQANGVEYGLTAAIWTNdISQAHRTARRV-EAGYVWINgssRH 420
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1708270319 978 QIGAvvgsqPFGGEGLSGTGfKAGGPHYLLRFACERTVTIN 1018
Cdd:cd07107 421 FLGA-----PFGGVKNSGIG-REECLEELLSYTQEKNVNVR 455
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
590-997 |
2.00e-55 |
|
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: 199.75 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDG-WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDAL-GELREAVDYCRFYAhEARRLMGAAIAlpgvTG 667
Cdd:cd07112 38 ESGvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALaVDVPSAANTFRWYA-EAIDKVYGEVA----PT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 668 ESNELRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGeSG 744
Cdd:cd07112 113 GPDALALITREPLgvvGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPG-FG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 745 GLSDKLLG-DPRVAGVAFTGSTgaawKINRTL--AARDSSIASLIAETGGLNAMI-ADSSAHVEQLIIDVLMSAFNSAGQ 820
Cdd:cd07112 192 HTAGEALGlHMDVDALAFTGST----EVGRRFleYSGQSNLKRVWLECGGKSPNIvFADAPDLDAAAEAAAAGIFWNQGE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 821 RCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV-GRTPQPAElSG 898
Cdd:cd07112 268 VCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIESgKAEGARLVaGGKRVLTE-TG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 899 GCFFAPHAFEVALDQLPTF--ETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYInr 976
Cdd:cd07112 347 GFFVEPTVFDGVTPDMRIAreEIFGPVLSVITFDSE--EEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV-- 422
|
410 420
....*....|....*....|.
gi 1708270319 977 NQIGAVVGSQPFGGEGLSGTG 997
Cdd:cd07112 423 NCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
590-997 |
1.17e-54 |
|
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: 198.12 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAiaLPGVTGES 669
Cdd:cd07085 51 FPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEY--LENVARGI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELrlSGRGP---FIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGeSGGL 746
Cdd:cd07085 129 DTY--SYRQPlgvVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 SDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLiaeTGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALR 826
Cdd:cd07085 206 VNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKRVQAL---GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 827 ILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV--GRTPQPAELSGGCFFA 903
Cdd:cd07085 283 VAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIESgVEEGAKLVldGRGVKVPGYENGNFVG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 904 PHAFE-VALD-QLPTFETFGPVLHIARfkGDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINrnqIG- 980
Cdd:cd07085 363 PTILDnVTPDmKIYKEEIFGPVLSIVR--VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPi 437
|
410
....*....|....*...
gi 1708270319 981 AV-VGSQPFGGEGLSGTG 997
Cdd:cd07085 438 PVpLAFFSFGGWKGSFFG 455
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
592-997 |
2.19e-54 |
|
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: 196.21 E-value: 2.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 592 GWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAhearrlmgaAIALPGVTGESN- 670
Cdd:cd07106 34 GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAWLRYTA---------SLDLPDEVIEDDd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 671 ----ELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAgIPADVLHYLPGeSGGL 746
Cdd:cd07106 105 trrvELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GDEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 SDKLLGDPRVAGVAFTGSTGAAWKINRTlAARDssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALR 826
Cdd:cd07106 183 GPALTSHPDIRKISFTGSTATGKKVMAS-AAKT--LKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 827 ILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPtIDTLSQRD-LQAYCD--KLAGTARLVGRTPQPaelSGGCFFA 903
Cdd:cd07106 260 RLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGP-VQNKMQYDkVKELVEdaKAKGAKVLAGGEPLD---GPGYFIP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 904 PHAFEVALDQLPTF--ETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTrldSTVETVRKLAK---VGNLYInrNQ 978
Cdd:cd07106 336 PTIVDDPPEGSRIVdeEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVWS---SDLERAEAVARrleAGTVWI--NT 408
|
410
....*....|....*....
gi 1708270319 979 IGAVVGSQPFGGEGLSGTG 997
Cdd:cd07106 409 HGALDPDAPFGGHKQSGIG 427
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
593-997 |
1.09e-53 |
|
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: 195.12 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDAL-GELREAVDYCRFYAHEARRLMGAAIALPGvtgesNE 671
Cdd:cd07091 59 WRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIPIDG-----NF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSD 748
Cdd:cd07091 134 LAYTRREPIgvcGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKINRtlAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:cd07091 214 AISSHMDVDKIAFTGSTAVGRTIME--AAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGtARLV-GRTPQPaelSGGCFFAPH 905
Cdd:cd07091 292 FVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIEsgKKEG-ATLLtGGERHG---SKGYFIQPT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 906 AF-EVALD-QLPTFETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINR-NQIGAV 982
Cdd:cd07091 368 VFtDVKDDmKIAKEEIFGPVVTILKFK--TEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAA 445
|
410
....*....|....*
gi 1708270319 983 VgsqPFGGEGLSGTG 997
Cdd:cd07091 446 V---PFGGFKQSGFG 457
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
593-1009 |
2.57e-53 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 194.91 E-value: 2.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALP--------- 663
Cdd:PLN02278 78 WSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPfpdrrllvl 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 664 ----GVTGesnelrlsgrgpfiAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYL 739
Cdd:PLN02278 158 kqpvGVVG--------------AITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 740 PGESGGLSDKLLGDPRVAGVAFTGSTGAAWKInrtLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAG 819
Cdd:PLN02278 224 MGDAPEIGDALLASPKVRKITFTGSTAVGKKL---MAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 820 QRC-SALRIlLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYC-DKLAGTAR-LVGRTPQPAel 896
Cdd:PLN02278 301 QTCvCANRI-LVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVqDAVSKGAKvLLGGKRHSL-- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 897 sGGCFFAPHAFEVALDQLPTF--ETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYI 974
Cdd:PLN02278 378 -GGTFYEPTVLGDVTEDMLIFreEVFGPVAPLTRFKTE--EEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGV 454
|
410 420 430
....*....|....*....|....*....|....*
gi 1708270319 975 NRNQIGAVVGsqPFGGEGLSGTGfKAGGPHYLLRF 1009
Cdd:PLN02278 455 NEGLISTEVA--PFGGVKQSGLG-REGSKYGIDEY 486
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
593-997 |
1.29e-52 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 190.75 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMgAAIALPGVTGESnEL 672
Cdd:cd07100 15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFL-ADEPIETDAGKA-YV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLSGRGPFIAIAPWNFPL---AIFLGqitAALAAGNTVIAKPSRRTPLIGmRAIEALL-DAGIPADVLHYLPGESGGLSD 748
Cdd:cd07100 93 RYEPLGVVLGIMPWNFPFwqvFRFAA---PNLMAGNTVLLKHASNVPGCA-LAIEELFrEAGFPEGVFQNLLIDSDQVEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 kLLGDPRVAGVAFTGSTGAAwkinrtlaardSSIASLIA--------ETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQ 820
Cdd:cd07100 169 -IIADPRVRGVTLTGSERAG-----------RAVAAEAGknlkksvlELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 821 RCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPtidtLSQRDLQaycDKL---------AG-TARLVGRT 890
Cdd:cd07100 237 SCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGP----LARKDLR---DELheqveeavaAGaTLLLGGKR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 891 PQPAelsgGCFFAPHAFE-VALDQlPTF--ETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRldsTVETVRKLA 967
Cdd:cd07100 310 PDGP----GAFYPPTVLTdVTPGM-PAYdeELFGPVAAVIKVKDE--EEAIALANDSPFGLGGSVFTT---DLERAERVA 379
|
410 420 430
....*....|....*....|....*....|....*.
gi 1708270319 968 K---VGNLYINrnqigAVVGSQ---PFGGEGLSGTG 997
Cdd:cd07100 380 RrleAGMVFIN-----GMVKSDprlPFGGVKRSGYG 410
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
592-1017 |
2.75e-52 |
|
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: 190.65 E-value: 2.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 592 GWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTL-PDALGELREAVDYCRFYAHEARRLMGAAIAL-PGVtges 669
Cdd:cd07108 34 EWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPEAAVLADLFRYFGGLAGELKGETLPFgPDV---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 neLRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEaLLDAGIPADVLHYLPGESGGL 746
Cdd:cd07108 110 --LTYTVREPLgvvGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAE-ILAQVLPAGVLNVITGYGEEC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 SDKLLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSA-FNSAGQRCSAL 825
Cdd:cd07108 187 GAALVDHPDVDKVTFTGSTEVGKIIYRAAADR---LIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 826 RILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdtlSQRDLQAYCDKLA-------GTARLVGRTPQPAELSG 898
Cdd:cd07108 264 SRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAII---SEKQFAKVCGYIDlglstsgATVLRGGPLPGEGPLAD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 899 GCFFAPHAFEVALDQLPTF--ETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGnlYIN 975
Cdd:cd07108 341 GFFVQPTIFSGVDNEWRLAreEIFGPVLCAIPWKDE--DEVIAMANDSHYGLAAYVWTRdLGRALRAAHAL-EAG--WVQ 415
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1708270319 976 RNQIGAVVGSQPFGGEGLSGTGFKAGGPHYLLRFACERTVTI 1017
Cdd:cd07108 416 VNQGGGQQPGQSYGGFKQSGLGREASLEGMLEHFTQKKTVNI 457
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
593-997 |
2.99e-52 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 190.63 E-value: 2.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WAdQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAL-PGVtgesne 671
Cdd:cd07120 37 WA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRMIEPePGS------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRLSGRGPF-IA--IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDA-GIPADVLHYLPGESGGLS 747
Cdd:cd07120 110 FSLVLREPMgVAgiIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 748 DKLLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRI 827
Cdd:cd07120 190 AHLVASPDVDVISFTGSTATGRAIMAAAAPT---LKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 828 LLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLVGR-TPQPAELSGGCFFAPH 905
Cdd:cd07120 267 VLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERaIAAGAEVVLRgGPVTEGLAKGAFLRPT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 906 AFEVALDQLPTF--ETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYINR-NQIGA 981
Cdd:cd07120 347 LLEVDDPDADIVqeEIFGPVLTLETF--DDEAEAVALANDTDYGLAASVWTRdLARAMRVARAI-RAGTVWINDwNKLFA 423
|
410
....*....|....*.
gi 1708270319 982 vvgSQPFGGEGLSGTG 997
Cdd:cd07120 424 ---EAEEGGYRQSGLG 436
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
590-1016 |
7.94e-52 |
|
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: 189.06 E-value: 7.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMG---AAIALPGVT 666
Cdd:cd07101 31 QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERLLKprrRRGAIPVLT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 667 gESNELRlSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGgl 746
Cdd:cd07101 111 -RTTVNR-RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGS-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 sdkLLGDPRVAG---VAFTGSTGAAWKINRTLAARdssiasLI---AETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQ 820
Cdd:cd07101 187 ---EVGGAIVDNadyVMFTGSTATGRVVAERAGRR------LIgcsLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 821 RCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdtlSQRDL---QAYCD--KLAGTARLVGRTPQPaE 895
Cdd:cd07101 258 LCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLI---SQAQLdrvTAHVDdaVAKGATVLAGGRARP-D 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 896 LsGGCFFAPHAFE-VALD-QLPTFETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTRldsTVETVRKLA---KVG 970
Cdd:cd07101 334 L-GPYFYEPTVLTgVTEDmELFAEETFGPVVSIYRVADDD--EAIELANDTDYGLNASVWTR---DGARGRRIAarlRAG 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1708270319 971 NLYINrNQIGAVVGS--QPFGGEGLSGTGFKAgGPHYLLRFACERTVT 1016
Cdd:cd07101 408 TVNVN-EGYAAAWASidAPMGGMKDSGLGRRH-GAEGLLKYTETQTVA 453
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
592-997 |
8.51e-52 |
|
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: 189.07 E-value: 8.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 592 GWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDAL-GELREAVDYCRFYAHEARRLMGAAIA--LPGVTge 668
Cdd:cd07092 34 SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDELPGAVDNFRFFAGAARTLEGPAAGeyLPGHT-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 669 sNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRaIEALLDAGIPADVLHYLPGESGGLSD 748
Cdd:cd07092 112 -SMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLL-LAELAAEVLPPGVVNVVCGGGASAGD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKINRTLAArdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:cd07092 190 ALVAHPRVRMVSLTGSVRTGKKVARAAAD---TLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdTLSQRD-LQAYCDKLAGTARLV---GRTPQPaelsgGCFFAP 904
Cdd:cd07092 267 YVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLN-SAAQRErVAGFVERAPAHARVLtggRRAEGP-----GYFYEP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 905 HAFEVAL--DQLPTFETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIgaV 982
Cdd:cd07092 341 TVVAGVAqdDEIVQEEIFGPVVTVQPFDDED--EAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIP--L 416
|
410
....*....|....*
gi 1708270319 983 VGSQPFGGEGLSGTG 997
Cdd:cd07092 417 AAEMPHGGFKQSGYG 431
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
591-997 |
4.76e-51 |
|
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: 187.17 E-value: 4.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRL---MGAAIALPgVTG 667
Cdd:cd07110 33 PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDVDDVAGCFEYYADLAEQLdakAERAVPLP-SED 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 668 ESNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLS 747
Cdd:cd07110 112 FKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 748 DKLLGDPRVAGVAFTGSTGAAWKINRTlAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRI 827
Cdd:cd07110 192 APLAAHPGIDKISFTGSTATGSQVMQA-AAQDIKPVSL--ELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 828 LLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLVGRTPQPAELSGGCFFAPHA 906
Cdd:cd07110 269 LLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARgKEEGARLLCGGRRPAHLEKGYFIAPTV 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 907 F-EVALD-QLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIgaVVG 984
Cdd:cd07110 349 FaDVPTDsRIWREEIFGPVLCVRSFATE--DEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSQP--CFP 424
|
410
....*....|...
gi 1708270319 985 SQPFGGEGLSGTG 997
Cdd:cd07110 425 QAPWGGYKRSGIG 437
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
590-1017 |
5.21e-51 |
|
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: 186.66 E-value: 5.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGA-AIALPGVT-G 667
Cdd:cd07099 31 QRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVLAPrKVPTGLLMpN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 668 ESNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGeSGGLS 747
Cdd:cd07099 111 KKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTG-DGATG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 748 DKLLgDPRVAGVAFTGSTGAAWKINRTLAARdssiasLI---AETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSA 824
Cdd:cd07099 190 AALI-DAGVDKVAFTGSVATGRKVMAAAAER------LIpvvLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCIS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 825 LRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDT----LSQRDLQaycDKLAGTARLVgrTPQPAELSGGC 900
Cdd:cd07099 263 VERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTArqldIVRRHVD---DAVAKGAKAL--TGGARSNGGGP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 901 FFAP-------HAFEVAldqlpTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRldsTVETVRKLA---KVG 970
Cdd:cd07099 338 FYEPtvltdvpHDMDVM-----REETFGPVLPVMPV--ADEDEAIALANDSRYGLSASVFSR---DLARAEAIArrlEAG 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1708270319 971 NLYINRNQIGAVVGSQPFGGEGLSGTGfKAGGPHYLLRFACERTVTI 1017
Cdd:cd07099 408 AVSINDVLLTAGIPALPFGGVKDSGGG-RRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
591-1001 |
7.84e-51 |
|
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: 186.39 E-value: 7.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTA-RAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGvtgeS 669
Cdd:cd07118 34 KGPWPRMSGAeRAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDSYNNLG----D 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIA---IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGL 746
Cdd:cd07118 110 DMLGLVLREPIGVvgiITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 SDKLLGDPRVAGVAFTGSTGAAWKINRTlAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALR 826
Cdd:cd07118 190 GQAMTEHPDVDMVSFTGSTRVGKAIAAA-AARNLKKVSL--ELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 827 ILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLVG--RTPQPAelsgGCFF 902
Cdd:cd07118 267 RLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDagRAEGATLLLGgeRLASAA----GLFY 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 903 APHAFEVALDQLPTF--ETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYINRNQI 979
Cdd:cd07118 343 QPTIFTDVTPDMAIAreEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKdIDTALTVARRI-RAGTVWVNTFLD 419
|
410 420
....*....|....*....|..
gi 1708270319 980 GAVvgSQPFGGEGLSGTGFKAG 1001
Cdd:cd07118 420 GSP--ELPFGGFKQSGIGRELG 439
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
593-1003 |
8.83e-51 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 186.63 E-value: 8.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTL--------PDALGELREAVDYCRFYAHEARRlmgaaialPG 664
Cdd:cd07139 54 WPRLSPAERAAVLRRLADALEARADELARLWTAENGMPIswsrraqgPGPAALLRYYAALARDFPFEERR--------PG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 665 VTGESNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESg 744
Cdd:cd07139 126 SGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADR- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 745 GLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMI----ADSSAHVEQLIIDVLMsafNSaGQ 820
Cdd:cd07139 205 EVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER---LARVTLELGGKSAAIvlddADLDAAVPGLVPASLM---NN-GQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 821 RCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdTLSQRD-LQAYCDK-LAGTARLVGRTPQPAELSG 898
Cdd:cd07139 278 VCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLA-SARQRErVEGYIAKgRAEGARLVTGGGRPAGLDR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 899 GCFFAPHAF-------EVALDqlptfETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVG 970
Cdd:cd07139 357 GWFVEPTLFadvdndmRIAQE-----EIFGPVLSVIPY--DDEDDAVRIANDSDYGLSGSVWTAdVERGLAVARRI-RTG 428
|
410 420 430
....*....|....*....|....*....|....*
gi 1708270319 971 NLYIN--RNQIGAvvgsqPFGGEGLSGTGfKAGGP 1003
Cdd:cd07139 429 TVGVNgfRLDFGA-----PFGGFKQSGIG-REGGP 457
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
591-997 |
1.52e-50 |
|
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: 185.52 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTA-RAALLEKAADLLEARQDEFLWLLSREAGKT--------LPDALGELREAVDYCRFYAHEARRLMGAAIA 661
Cdd:cd07089 33 DTGDWSTDAEeRARCLRQLHEALEARKEELRALLVAEVGAPvmtaramqVDGPIGHLRYFADLADSFPWEFDLPVPALRG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 662 LPGvtgesneLRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHY 738
Cdd:cd07089 113 GPG-------RRVVRREPVgvvAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETDLPAGVVNV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 739 LPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAArdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSA 818
Cdd:cd07089 186 VTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA---TLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 819 GQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdTLSQRD-LQAYCDK-LAGTARLVGRTPQPAEL 896
Cdd:cd07089 263 GQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLI-SAAQRDrVEGYIARgRDEGARLVTGGGRPAGL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 897 SGGCFFAPHAF-------EVALDqlptfETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaK 968
Cdd:cd07089 342 DKGFYVEPTLFadvdndmRIAQE-----EIFGPVLVVIPYDDDD--EAVRIANDSDYGLSGGVWSAdVDRAYRVARRI-R 413
|
410 420 430
....*....|....*....|....*....|.
gi 1708270319 969 VGNLYINrnqiGAVVGS--QPFGGEGLSGTG 997
Cdd:cd07089 414 TGSVGIN----GGGGYGpdAPFGGYKQSGLG 440
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
592-1021 |
1.68e-50 |
|
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: 185.98 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 592 GWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGVTgESNE 671
Cdd:cd07119 52 EWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPHV-ISRT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRlSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLL 751
Cdd:cd07119 131 VR-EPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 752 GDPRVAGVAFTGSTGAAWKINRTLAARDSSIAsliAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQ 831
Cdd:cd07119 210 ESPDVDLVSFTGGTATGRSIMRAAAGNVKKVA---LELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 832 DDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV--GRTPQPAELSGGCFFAPHAF- 907
Cdd:cd07119 287 ESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLgKEEGARLVcgGKRPTGDELAKGYFVEPTIFd 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 EVALD-QLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYInrNQIGAVVGSQ 986
Cdd:cd07119 367 DVDRTmRIVQEEIFGPVLTVERFDTE--EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWI--NDYHPYFAEA 442
|
410 420 430
....*....|....*....|....*....|....*
gi 1708270319 987 PFGGEGLSGTGfKAGGPHYLLRFACERTVTINTAA 1021
Cdd:cd07119 443 PWGGYKQSGIG-RELGPTGLEEYQETKHININLSP 476
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
590-997 |
2.47e-50 |
|
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: 184.81 E-value: 2.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGvtGES 669
Cdd:cd07090 32 QKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTLSGEHVPLPG--GSF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGEsGGLSDK 749
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVFNVVQGG-GETGQL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKInrtLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCS-ALRIl 828
Cdd:cd07090 189 LCEHPDVAKVSFTGSVPTGKKV---MSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSnGTRV- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLVG--RTPQPAELSGGCFFAP 904
Cdd:cd07090 265 FVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIEsaKQEGAKVLCGgeRVVPEDGLENGFYVSP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 905 HAFEVALDQLPTF--ETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYINRNQIGA 981
Cdd:cd07090 345 CVLTDCTDDMTIVreEIFGPVMSILPFDTEE--EVIRRANDTTYGLAAGVFTRdLQRAHRVIAQL-QAGTCWINTYNISP 421
|
410
....*....|....*.
gi 1708270319 982 VvgSQPFGGEGLSGTG 997
Cdd:cd07090 422 V--EVPFGGYKQSGFG 435
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
590-1017 |
4.46e-50 |
|
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: 184.43 E-value: 4.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRlMGAAIALPGVTGES 669
Cdd:cd07151 45 QKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAATFPLR-MEGRILPSDVPGKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALL-DAGIPADVLHYLPGESGGLSD 748
Cdd:cd07151 124 NRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLAKIFeEAGLPKGVLNVVVGAGSEIGD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKINRtLAARdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:cd07151 204 AFVEHPVPRLISFTGSTPVGRHIGE-LAGR--HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTlSQRD-LQAYCDKL--AGTARLVGRTPQpaelsgGCFFAPH 905
Cdd:cd07151 281 IVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINE-SQVDgLLDKIEQAveEGATLLVGGEAE------GNVLEPT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 906 AFEVALDQLPTF--ETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTrldSTVETVRKLAK---VGNLYINR---N 977
Cdd:cd07151 354 VLSDVTNDMEIAreEIFGPVAPIIKADDEE--EALELANDTEYGLSGAVFT---SDLERGVQFARridAGMTHINDqpvN 428
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1708270319 978 QIGAVvgsqPFGGEGLSGTGfKAGGPHYLLRFACERTVTI 1017
Cdd:cd07151 429 DEPHV----PFGGEKNSGLG-RFNGEWALEEFTTDKWISV 463
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
590-1008 |
3.13e-49 |
|
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: 181.85 E-value: 3.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWAdqAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGVTGES 669
Cdd:cd07148 37 RNNWL--PAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPMGLTPASA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGR---GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGl 746
Cdd:cd07148 115 GRIAFTTRepiGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAV- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 SDKLLGDPRVAGVAFTGSTGAAWKINRTLAArdssiASLIA-ETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSAL 825
Cdd:cd07148 194 AEKLVTDPRVAFFSFIGSARVGWMLRSKLAP-----GTRCAlEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 826 RILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLVGrtpqPAELSGGCFFAP 904
Cdd:cd07148 269 QRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEaVAAGARLLC----GGKRLSDTTYAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 905 hafEVALD-----QLPTFETFGPVlhIARFKGDQLADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLAKVGnLYINrNQ 978
Cdd:cd07148 345 ---TVLLDpprdaKVSTQEIFGPV--VCVYSYDDLDEAIAQANSLPVAFQAAVFTKdLDVALKAVRRLDATA-VMVN-DH 417
|
410 420 430
....*....|....*....|....*....|
gi 1708270319 979 IGAVVGSQPFGGEGLSGTGfkAGGPHYLLR 1008
Cdd:cd07148 418 TAFRVDWMPFAGRRQSGYG--TGGIPYTMH 445
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
590-976 |
7.49e-49 |
|
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: 180.52 E-value: 7.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMgAAIALPGVTGES 669
Cdd:cd07102 31 QKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEAL-ADIRVPEKDGFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGeSGGLSDK 749
Cdd:cd07102 110 RYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHL-SHETSAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMI----ADSSAHVEQlIIDVLMsaFNSaGQRCSAL 825
Cdd:cd07102 189 LIADPRIDHVSFTGSVAGGRAIQRAAAGR---FIKVGLELGGKDPAYvrpdADLDAAAES-LVDGAF--FNS-GQSCCSI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 826 RILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQ-RDLQAYCDKLAGTARLV---GRTPQPAElsGGCF 901
Cdd:cd07102 262 ERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAAdFVRAQIADAIAKGARALidgALFPEDKA--GGAY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 902 FAP-------HAFEVALDqlptfETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLAkVGNLY 973
Cdd:cd07102 340 LAPtvltnvdHSMRVMRE-----ETFGPVVGIMKVKSD--AEAIALMNDSEYGLTASVWTKdIARAEALGEQLE-TGTVF 411
|
...
gi 1708270319 974 INR 976
Cdd:cd07102 412 MNR 414
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
591-997 |
1.19e-48 |
|
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: 180.39 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTL--------PDALGELREAVDYCRFYAHEARRlmGAAIAL 662
Cdd:cd07138 50 PAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPItlaraaqvGLGIGHLRAAADALKDFEFEERR--GNSLVV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 663 --P-GVTGesnelrlsgrgpfiAIAPWNFPLaiflGQIT----AALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADV 735
Cdd:cd07138 128 rePiGVCG--------------LITPWNWPL----NQIVlkvaPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 736 LHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTlAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAF 815
Cdd:cd07138 190 FNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA-AADTVKRVAL--ELGGKSANIILDDADLEKAVPRGVAACF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 816 NSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdTLSQRD-LQAYCDK-LAGTARLV-GRTPQ 892
Cdd:cd07138 267 ANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLA-SAAQFDrVQGYIQKgIEEGARLVaGGPGR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 893 PAELSGGCFFAPHAF-EVALD-QLPTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVG 970
Cdd:cd07138 346 PEGLERGYFVKPTVFaDVTPDmTIAREEIFGPVLSIIPY--DDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAG 423
|
410 420
....*....|....*....|....*...
gi 1708270319 971 NLYINrnqiGAVVGSQ-PFGGEGLSGTG 997
Cdd:cd07138 424 QVHIN----GAAFNPGaPFGGYKQSGNG 447
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
591-955 |
2.64e-47 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 176.64 E-value: 2.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGAAIA--LPGVTg 667
Cdd:PRK13473 53 PEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGeyLEGHT- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 668 esNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAgIPADVLHYLPGESGGLS 747
Cdd:PRK13473 132 --SMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 748 DKLLGDPRVAGVAFTGSTGAAWKInrtLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRI 827
Cdd:PRK13473 209 DALVGHPKVRMVSLTGSIATGKHV---LSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 828 LLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdTLSQRD-LQAYCD--KLAGTARLV--GRTPQPAelsgGCFF 902
Cdd:PRK13473 286 IYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI-SAAHRDrVAGFVEraKALGHIRVVtgGEAPDGK----GYYY 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1708270319 903 APHAFEVAL--DQLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTR 955
Cdd:PRK13473 361 EPTLLAGARqdDEIVQREVFGPVVSVTPFDDE--DQAVRWANDSDYGLASSVWTR 413
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
590-1018 |
3.99e-47 |
|
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: 176.18 E-value: 3.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTA-RAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGAAIalpgvtg 667
Cdd:cd07143 58 ETDWGLKVSGSkRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVI------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 668 ESNELRLSGR-----GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGE 742
Cdd:cd07143 131 ETDIKKLTYTrhepiGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 743 SGGLSDKLLGDPRVAGVAFTGSTGAAWKINRtlAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRC 822
Cdd:cd07143 211 GRTCGNAISSHMDIDKVAFTGSTLVGRKVME--AAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVC 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 823 SALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLVGRTPQPAElsgGC 900
Cdd:cd07143 289 CAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIEsgKAEGATVETGGKRHGNE---GY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 901 FFAPHAF-EVALD-QLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYIN-RN 977
Cdd:cd07143 366 FIEPTIFtDVTEDmKIVKEEIFGPVVAVIKFKTE--EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNcYN 443
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1708270319 978 QIGAVVgsqPFGGEGLSGTGfKAGGPHYLLRFACERTVTIN 1018
Cdd:cd07143 444 LLHHQV---PFGGYKQSGIG-RELGEYALENYTQIKAVHIN 480
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
593-1017 |
4.46e-47 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 176.15 E-value: 4.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGAAI----ALPgvtg 667
Cdd:cd07140 61 WGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGKTIpinqARP---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 668 eSNELRLSGRGPFIA---IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESG 744
Cdd:cd07140 137 -NRNLTLTKREPIGVcgiVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 745 GLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAarDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSA 824
Cdd:cd07140 216 LVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA--VSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 825 LRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV---GRTPQPaelsgGC 900
Cdd:cd07140 294 AGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERgVKEGATLVyggKQVDRP-----GF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 901 FFAPHAFEVALDQL--PTFETFGPVLHIARFKGDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQ 978
Cdd:cd07140 369 FFEPTVFTDVEDHMfiAKEESFGPIMIISKFDDGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYN 448
|
410 420 430
....*....|....*....|....*....|....*....
gi 1708270319 979 IGAVvgSQPFGGEGLSGTGfKAGGPHYLLRFACERTVTI 1017
Cdd:cd07140 449 KTDV--AAPFGGFKQSGFG-KDLGEEALNEYLKTKTVTI 484
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
593-1011 |
7.71e-47 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 175.48 E-value: 7.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIalPGVTGESNEL 672
Cdd:PRK11241 64 WRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTI--PGHQADKRLI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLSGR-GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLL 751
Cdd:PRK11241 142 VIKQPiGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 752 GDPRVAGVAFTGSTgaawKINRTL---AARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:PRK11241 222 SNPLVRKLSFTGST----EIGRQLmeqCAKDIKKVSL--ELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAY-CDKLAGTARLVgrTPQPAELSGGCFFAPHAF 907
Cdd:PRK11241 296 YVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHiADALEKGARVV--CGGKAHELGGNFFQPTIL 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 -EVALD-QLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGs 985
Cdd:PRK11241 374 vDVPANaKVAKEETFGPLAPLFRFKDE--ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA- 450
|
410 420 430
....*....|....*....|....*....|
gi 1708270319 986 qPFGG---EGLSGTGFKAGGPHYL-LRFAC 1011
Cdd:PRK11241 451 -PFGGikaSGLGREGSKYGIEDYLeIKYMC 479
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
546-997 |
1.19e-46 |
|
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: 174.55 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 546 VGGQRPAGTGQPRVSPID--LERKIGTLVATDAAAVAKALDLADAAQDG-WADQAPTARAALLEKAADLLEARQDEFLWL 622
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNpaTEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 623 LSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGAAIA--LPGVTGE--SNELRLSGRGPFIAIAPWNFPLAIFLGQI 697
Cdd:cd07113 84 ETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLApsIPSMQGEryTAFTRREPVGVVAGIVPWNFSVMIAVWKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 698 TAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGeSGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTlAA 777
Cdd:cd07113 164 GAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-KGAVGAQLISHPDVAKVSFTGSVATGKKIGRQ-AA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 778 RDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQL 857
Cdd:cd07113 242 SDLTRVTL--ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 858 ATDVGPTIDtlsqrdlQAYCDKL--------AGTARLV--GRTPqPAElsgGCFFAPHAFEVALDQLPTF--ETFGPVLH 925
Cdd:cd07113 320 SVMFGPLAN-------QPHFDKVcsylddarAEGDEIVrgGEAL-AGE---GYFVQPTLVLARSADSRLMreETFGPVVS 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708270319 926 IARFKGDQlaDAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYINRNQIgaVVGSQPFGGEGLSGTG 997
Cdd:cd07113 389 FVPYEDEE--ELIQLINDTPFGLTASVWTNnLSKALRYIPRI-EAGTVWVNMHTF--LDPAVPFGGMKQSGIG 456
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
590-1016 |
9.47e-46 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 173.14 E-value: 9.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMG---AAIALPGVT 666
Cdd:PRK09407 67 QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAprrRAGALPVLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 667 gESNELRLSgRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGgl 746
Cdd:PRK09407 147 -KTTELRQP-KGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGP-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 sdkLLGDPRVAG---VAFTGSTGAAWKINRTLAARdssiasLI---AETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQ 820
Cdd:PRK09407 223 ---VVGTALVDNadyLMFTGSTATGRVLAEQAGRR------LIgfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 821 RC-SALRIlLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIdtlSQRDL---QAYCD--KLAGTARLVGRTPQPa 894
Cdd:PRK09407 294 LCiSIERI-YVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLI---SEAQLetvSAHVDdaVAKGATVLAGGKARP- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 895 ELsGGCFFAPHAFE-VALD-QLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRldsTVETVRKLA---KV 969
Cdd:PRK09407 369 DL-GPLFYEPTVLTgVTPDmELAREETFGPVVSVYPVADV--DEAVERANDTPYGLNASVWTG---DTARGRAIAariRA 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1708270319 970 GNLYINrNQIGAVVGS--QPFGGEGLSGTGfKAGGPHYLLRFACERTVT 1016
Cdd:PRK09407 443 GTVNVN-EGYAAAWGSvdAPMGGMKDSGLG-RRHGAEGLLKYTESQTIA 489
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
590-997 |
1.52e-44 |
|
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: 168.74 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTL-PDALGELREAVDYCRFYAHEARRLMGAAIALpgvtgE 668
Cdd:cd07144 59 ESWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPT-----S 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 669 SNELRLSGRGPFIA---IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGG 745
Cdd:cd07144 134 PNKLAYTLHEPYGVcgqIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 746 LSDKLLGDPRVAGVAFTGSTGAAWKInrtLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSAL 825
Cdd:cd07144 214 AGSALAEHPDVDKIAFTGSTATGRLV---MKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 826 RILLVQDDIADQVIERL-GLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLVGRTPQPAELSGGCFF 902
Cdd:cd07144 291 SRIYVQESIYDKFVEKFvEHVKQNYKVGSPFDDDTVVGPQVSKTQYDRVLSYIEkgKKEGAKLVYGGEKAPEGLGKGYFI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 903 APHAFevaLDQLPTF-----ETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRN 977
Cdd:cd07144 371 PPTIF---TDVPQDMrivkeEIFGPVVVISKFKTYE--EAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS 445
|
410 420
....*....|....*....|
gi 1708270319 978 QIGAVvgSQPFGGEGLSGTG 997
Cdd:cd07144 446 NDSDV--GVPFGGFKMSGIG 463
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
593-1018 |
2.26e-44 |
|
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: 167.77 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAlpgvtgesnel 672
Cdd:cd07130 50 WRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIP----------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 rlSGR------------GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPL--IGMRAI--EALLDAGIPADVL 736
Cdd:cd07130 119 --SERpghrmmeqwnplGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLtaIAVTKIvaRVLEKNGLPGAIA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 737 HYLPGEsGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFN 816
Cdd:cd07130 197 SLVCGG-ADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAAR---FGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 817 SAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK--------LAGTARLVG 888
Cdd:cd07130 273 TAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEaksqggtvLFGGKVIDG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 889 rtpqpaelsGGCFFAPHAFEvALDQLPTF--ETFGPVLHIARFKGdqLADAVHRVNKLGFGLTMGVHTRLDSTVEtvRKL 966
Cdd:cd07130 353 ---------PGNYVEPTIVE-GLSDAPIVkeETFAPILYVLKFDT--LEEAIAWNNEVPQGLSSSIFTTDLRNAF--RWL 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708270319 967 AKVG------NLYINRNqiGAVVGSQpFGGEGLSGTGFKAGG---PHYLLRfaceRTVTIN 1018
Cdd:cd07130 419 GPKGsdcgivNVNIGTS--GAEIGGA-FGGEKETGGGRESGSdawKQYMRR----STCTIN 472
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
592-995 |
3.75e-44 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 167.44 E-value: 3.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 592 GWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVD----YCRFYAH---EARRLMGAAIALpg 664
Cdd:PRK09457 52 AWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAMINkiaiSIQAYHErtgEKRSEMADGAAV-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 665 vtgesneLRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPG--E 742
Cdd:PRK09457 130 -------LRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGgrE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 743 SGglsDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRC 822
Cdd:PRK09457 203 TG---KALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKILAL--EMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRC 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 823 SALRILLVQDDI-ADQVIERLGLAMQELRMGDPL-QLATDVGPTID-------TLSQRDLQAycdkLAGTARLVGRTPQP 893
Cdd:PRK09457 278 TCARRLLVPQGAqGDAFLARLVAVAKRLTVGRWDaEPQPFMGAVISeqaaqglVAAQAQLLA----LGGKSLLEMTQLQA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 894 aelsGGCFFAPHAFEV-ALDQLPTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGnl 972
Cdd:PRK09457 354 ----GTGLLTPGIIDVtGVAELPDEEYFGPLLQVVRY--DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAG-- 425
|
410 420
....*....|....*....|....
gi 1708270319 973 YINRN-QIGAVVGSQPFGGEGLSG 995
Cdd:PRK09457 426 IVNWNkPLTGASSAAPFGGVGASG 449
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
593-1001 |
4.00e-43 |
|
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: 164.20 E-value: 4.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDA-LGELREAVDYCRFYAhearrlmGAAIALPGVTGESNe 671
Cdd:cd07142 59 WPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQArYAEVPLAARLFRYYA-------GWADKIHGMTLPAD- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 lrlsgrGPFIA------------IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYL 739
Cdd:cd07142 131 ------GPHHVytlhepigvvgqIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 740 PGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRtlAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAG 819
Cdd:cd07142 205 TGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ--LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 820 QRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLVgrTPQPAELSG 898
Cdd:cd07142 283 QCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHgKEEGATLI--TGGDRIGSK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 899 GCFFAPHAFEVALDQLPTF--ETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYInr 976
Cdd:cd07142 361 GYYIQPTIFSDVKDDMKIArdEIFGPVQSILKFK--TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWV-- 436
|
410 420
....*....|....*....|....*
gi 1708270319 977 NQIGAVVGSQPFGGEGLSGTGFKAG 1001
Cdd:cd07142 437 NCYDVFDASIPFGGYKMSGIGREKG 461
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
590-997 |
1.80e-41 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 159.66 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALgelreAVDYC------RFYAhearrlmGAAialP 663
Cdd:PRK13252 57 QKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETS-----VVDIVtgadvlEYYA-------GLA---P 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 664 GVTGESNELRLSG-----RGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADV 735
Cdd:PRK13252 122 ALEGEQIPLRGGSfvytrREPLgvcAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 736 LHYLPGeSGGLSDKLLGDPRVAGVAFTGSTGAAWKInrtLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAF 815
Cdd:PRK13252 202 FNVVQG-DGRVGAWLTEHPDIAKVSFTGGVPTGKKV---MAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 816 NSAGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLV--GRTPQ 892
Cdd:PRK13252 278 YSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKgKAEGARLLcgGERLT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 893 PAELSGGCFFAPHAFEVALDQLPTF--ETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVG 970
Cdd:PRK13252 358 EGGFANGAFVAPTVFTDCTDDMTIVreEIFGPVMSVLTF--DDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAG 435
|
410 420
....*....|....*....|....*..
gi 1708270319 971 NLYInrNQIGAVVGSQPFGGEGLSGTG 997
Cdd:PRK13252 436 ICWI--NTWGESPAEMPVGGYKQSGIG 460
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
591-997 |
4.12e-41 |
|
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: 158.28 E-value: 4.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGAAIALpgvtgES 669
Cdd:cd07559 52 KTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEI-----DE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTP---LIGMRAIEALLdagiPADVLHYLPGES 743
Cdd:cd07559 127 DTLSYHFHEPLgvvGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPlsiLVLMELIGDLL----PKGVVNVVTGFG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 744 GGLSDKLLGDPRVAGVAFTGSTGAAWKInrTLAARDSSI-ASLiaETGGLNAMIADSSAHVEQLIID------VLMSAFN 816
Cdd:cd07559 203 SEAGKPLASHPRIAKLAFTGSTTVGRLI--MQYAAENLIpVTL--ELGGKSPNIFFDDAMDADDDFDdkaeegQLGFAFN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 817 SaGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAY--------CDKLAGTARLVG 888
Cdd:cd07559 279 Q-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYvdigkeegAEVLTGGERLTL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 889 rtpqpAELSGGCFFAPHAFEVALDQLPTF--ETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTRLDSTVETVRKL 966
Cdd:cd07559 358 -----GGLDKGYFYEPTLIKGGNNDMRIFqeEIFGPVLAVITFKDEE--EAIAIANDTEYGLGGGVWTRDINRALRVARG 430
|
410 420 430
....*....|....*....|....*....|..
gi 1708270319 967 AKVGNLYIN-RNQIGAvvgSQPFGGEGLSGTG 997
Cdd:cd07559 431 IQTGRVWVNcYHQYPA---HAPFGGYKKSGIG 459
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
593-1017 |
1.79e-40 |
|
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: 155.43 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAlpgvTGESNEL 672
Cdd:cd07105 16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIP----SDKPGTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLSGR---GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYL---PGESGGL 746
Cdd:cd07105 92 AMVVKepvGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 SDKLLGDPRVAGVAFTGSTGAAWKINRTlAARdsSIASLIAETGGLNAMI----ADSSAHVEQliidVLMSAFNSAGQRC 822
Cdd:cd07105 172 VEALIAHPAVRKVNFTGSTRVGRIIAET-AAK--HLKPVLLELGGKAPAIvledADLDAAANA----ALFGAFLNSGQIC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 823 -SALRIlLVQDDIADQVIERLGLAMQELRMGDplqlaTDVGPTIDTLSQRDLQA-YCDKLAGTARLVGRTPQPAELSgGC 900
Cdd:cd07105 245 mSTERI-IVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKElVDDALSKGAKLVVGGLADESPS-GT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 901 FFAPHAFE-VALD-QLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLAkVGNLYINrn 977
Cdd:cd07105 318 SMPPTILDnVTPDmDIYSEESFGPVVSIIRVKDE--EEAVRIANDSEYGLSAAVFTRdLARALAVAKRIE-SGAVHIN-- 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1708270319 978 qiGAVVGSQ---PFGGEGLSGTG-FkaGGPHYLLRFACERTVTI 1017
Cdd:cd07105 393 --GMTVHDEptlPHGGVKSSGYGrF--NGKWGIDEFTETKWITI 432
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
593-1017 |
4.12e-40 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 155.82 E-value: 4.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDAL-GELREAVDYCRFYAHEARRLMGAaIALPGvtgeSNE 671
Cdd:PRK09847 75 WSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLrDDIPGAARAIRWYAEAIDKVYGE-VATTS----SHE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSD 748
Cdd:PRK09847 150 LAMIVREPVgviAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKINRTlaARDSSIASLIAETGGLNAMI--ADsSAHVEQLIIDVLMSAFNSAGQRCSALR 826
Cdd:PRK09847 230 ALSRHNDIDAIAFTGSTRTGKQLLKD--AGDSNMKRVWLEAGGKSANIvfAD-CPDLQQAASATAAGIFYNQGQVCIAGT 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 827 ILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDtlsqrdlQAYCDKLA---------GTARLVGR-TPQPAEL 896
Cdd:PRK09847 307 RLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLID-------CAHADSVHsfiregeskGQLLLDGRnAGLAAAI 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 897 SGGCFfaphafeVALD---QLPTFETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLY 973
Cdd:PRK09847 380 GPTIF-------VDVDpnaSLSREEIFGPVLVVTRFTSEE--QALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVF 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1708270319 974 INRNQIGAVvgSQPFGGEGLSGTGfKAGGPHYLLRFACERTVTI 1017
Cdd:PRK09847 451 VNNYNDGDM--TVPFGGYKQSGNG-RDKSLHALEKFTELKTIWI 491
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
593-1017 |
7.42e-39 |
|
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: 151.73 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDA-LGELREAVDYCRFYAHEARRLMGAAIALPGvtgesNE 671
Cdd:cd07141 63 WRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDG-----DF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 L---RLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSD 748
Cdd:cd07141 138 FtytRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKINRtlAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:cd07141 218 AISSHPDIDKVAFTGSTEVGKLIQQ--AAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGtARLV---GRTPQPaelsgGCFFA 903
Cdd:cd07141 296 FVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIEsgKKEG-AKLEcggKRHGDK-----GYFIQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 904 PHAFEVALD--QLPTFETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINrnqIGA 981
Cdd:cd07141 370 PTVFSDVTDdmRIAKEEIFGPVQQIFKFK--TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CYN 444
|
410 420 430
....*....|....*....|....*....|....*...
gi 1708270319 982 VVGSQ-PFGGEGLSGTGFKAGgpHYLLRFACE-RTVTI 1017
Cdd:cd07141 445 VVSPQaPFGGYKMSGNGRELG--EYGLQEYTEvKTVTI 480
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
591-1011 |
1.07e-38 |
|
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: 151.39 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLpdalgelREAVD-----YCRFYAHEArrlmGAAIALpgv 665
Cdd:cd07111 73 ESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPI-------RESRDcdiplVARHFYHHA----GWAQLL--- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 666 tgesnELRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGe 742
Cdd:cd07111 139 -----DTELAGWKPVgvvGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 743 SGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAArdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRC 822
Cdd:cd07111 213 NGSFGSALANHPGVDKVAFTGSTEVGRALRRATAG---TGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 823 SALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDtLSQRDLQAYCDKlAGTARLVGRTPQPAELSG-GCF 901
Cdd:cd07111 290 CAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVD-PAQLKRIRELVE-EGRAEGADVFQPGADLPSkGPF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 902 FAPHAFE--VALDQLPTFETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHT-RLDSTVETVRKLaKVGNLYIN-RN 977
Cdd:cd07111 368 YPPTLFTnvPPASRIAQEEIFGPVLVVLTFR--TAKEAVALANNTPYGLAASVWSeNLSLALEVALSL-KAGVVWINgHN 444
|
410 420 430
....*....|....*....|....*....|....
gi 1708270319 978 QIGAVVgsqPFGGEGLSGTGfKAGGPHYLLRFAC 1011
Cdd:cd07111 445 LFDAAA---GFGGYRESGFG-REGGKEGLYEYLR 474
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
605-1006 |
1.82e-38 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 148.73 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 605 LEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAlpgvTGESNELRLSGRGPF---I 681
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQ----SDRPGENILLFKRALgvtT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 682 AIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLLGDPRVAGVAF 761
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 762 TGSTGAAWKInrtLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIER 841
Cdd:PRK10090 157 TGSVSAGEKI---MAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 842 LGLAMQELRMGDPLQ-LATDVGPTIdtlSQRDLQAYCDKLA-----GTARLVGrtPQPAELSGgcFFAPHAFEVALDQLP 915
Cdd:PRK10090 234 LGEAMQAVQFGNPAErNDIAMGPLI---NAAALERVEQKVAraveeGARVALG--GKAVEGKG--YYYPPTLLLDVRQEM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 916 TF---ETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTR-LDSTVETVRKLaKVGNLYINRNQIGAVVGSQpfGGE 991
Cdd:PRK10090 307 SImheETFGPVLPVVAF--DTLEEAIAMANDSDYGLTSSIYTQnLNVAMKAIKGL-KFGETYINRENFEAMQGFH--AGW 381
|
410
....*....|....*
gi 1708270319 992 GLSGTGfKAGGPHYL 1006
Cdd:PRK10090 382 RKSGIG-GADGKHGL 395
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
601-997 |
5.55e-38 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 148.73 E-value: 5.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 601 RAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPGVTGESNEL-RLSGRGP 679
Cdd:PRK09406 47 RARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALLADEPADAAAVGASRAYvRYQPLGV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 680 FIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLsDKLLGDPRVAGV 759
Cdd:PRK09406 127 VLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLLVGSGAV-EAILRDPRVAAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 760 AFTGSTGAAwkinRTLAA-RDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQV 838
Cdd:PRK09406 206 TLTGSEPAG----RAVAAiAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAF 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 839 IERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLAG---TARLVGRTPQpaelSGGCFFAPhafEVALDQLP 915
Cdd:PRK09406 282 AEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAagaTILCGGKRPD----GPGWFYPP---TVITDITP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 916 -----TFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINrnqiGAVVG--SQPF 988
Cdd:PRK09406 355 dmrlyTEEVFGPVASLYRV--ADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN----GMTVSypELPF 428
|
....*....
gi 1708270319 989 GGEGLSGTG 997
Cdd:PRK09406 429 GGVKRSGYG 437
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
593-997 |
2.49e-37 |
|
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: 147.22 E-value: 2.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGAAIALpgvtgESNE 671
Cdd:cd07117 54 WRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMI-----DEDT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRLSGRGPFI---AIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLiGMRAIEALLDAGIPADVLHYLPGESGGLSD 748
Cdd:cd07117 129 LSIVLREPIGvvgQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSL-SLLELAKIIQDVLPKGVVNIVTGKGSKSGE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAWKInrTLAARDSSIASLIaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:cd07117 208 YLLNHPGLDKLAFTGSTEVGRDV--AIAAAKKLIPATL-ELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK--------LAGTARLVGrtpqpAELSGGC 900
Cdd:cd07117 285 FVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIakeegakiLTGGHRLTE-----NGLDKGF 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 901 FFAPHAFEVALD--QLPTFETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINR-N 977
Cdd:cd07117 360 FIEPTLIVNVTNdmRVAQEEIFGPVATVIKFKTED--EVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTyN 437
|
410 420
....*....|....*....|
gi 1708270319 978 QIGAvvgSQPFGGEGLSGTG 997
Cdd:cd07117 438 QIPA---GAPFGGYKKSGIG 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
593-1001 |
1.36e-35 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 143.02 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGAAIALPG---VTGE 668
Cdd:PLN02466 113 WPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGphhVQTL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 669 SNELRLSGRgpfiaIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSD 748
Cdd:PLN02466 193 HEPIGVAGQ-----IIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 749 KLLGDPRVAGVAFTGSTGAAwKINRTLAARdSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRIL 828
Cdd:PLN02466 268 ALASHMDVDKLAFTGSTDTG-KIVLELAAK-SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 829 LVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDK-LAGTARLVGRTPQPAelSGGCFFAPHAF 907
Cdd:PLN02466 346 FVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSgVESGATLECGGDRFG--SKGYYIQPTVF 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 EVALDQLPTF--ETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYIN-RNQIGAVVg 984
Cdd:PLN02466 424 SNVQDDMLIAqdEIFGPVQSILKFK--DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcFDVFDAAI- 500
|
410
....*....|....*..
gi 1708270319 985 sqPFGGEGLSGTGFKAG 1001
Cdd:PLN02466 501 --PFGGYKMSGIGREKG 515
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
593-1001 |
2.50e-35 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 141.50 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLpdALGELRE---AVDYCRFYAhearrlmGAAIALPGVTges 669
Cdd:PLN02766 76 WPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLF--ALGKAVDipaAAGLLRYYA-------GAADKIHGET--- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 neLRLSGR----------GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYL 739
Cdd:PLN02766 144 --LKMSRQlqgytlkepiGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 740 PGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAG 819
Cdd:PLN02766 222 TGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSNLKQVSL--ELGGKSPLLIFDDADVDMAVDLALLGIFYNKG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 820 QRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLVGRTPQPAEls 897
Cdd:PLN02766 300 EICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEhgKREGATLLTGGKPCGDK-- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 898 gGCFFAPHAF-EVALD-QLPTFETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYIn 975
Cdd:PLN02766 378 -GYYIEPTIFtDVTEDmKIAQDEIFGPVMSLMKFK--TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWV- 453
|
410 420
....*....|....*....|....*.
gi 1708270319 976 rNQIGAVVGSQPFGGEGLSGTGFKAG 1001
Cdd:PLN02766 454 -NCYFAFDPDCPFGGYKMSGFGRDQG 478
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
590-1016 |
6.21e-34 |
|
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: 136.66 E-value: 6.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDA-LGELREAVDYCRFYAHEARRlmgaAIALPGVTGE 668
Cdd:cd07098 31 QREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEILVTCEKIRWTLKHGEK----ALRPESRPGG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 669 SNELRLSGR------GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGM---RAIEALLDA-GIPADVLHY 738
Cdd:cd07098 107 LLMFYKRARveyeplGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGfflSIIRECLAAcGHDPDLVQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 739 LPGeSGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAardSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSA 818
Cdd:cd07098 187 VTC-LPETAEALTSHPVIDHITFIGSPPVGKKVMAAAA---ESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 819 GQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYC-DKLAGTARLVG---RTPQPa 894
Cdd:cd07098 263 GQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVaDAVEKGARLLAggkRYPHP- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 895 ELSGGCFFAPhafEVALDQLPTF-----ETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKV 969
Cdd:cd07098 342 EYPQGHYFPP---TLLVDVTPDMkiaqeEVFGPVMVVMKASDD--EEAVEIANSTEYGLGASVFGKDIKRARRIASQLET 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1708270319 970 GNLYINRNQIGAVVGSQPFGGEGLSGTGfKAGGPHYLLRFACERTVT 1016
Cdd:cd07098 417 GMVAINDFGVNYYVQQLPFGGVKGSGFG-RFAGEEGLRGLCNPKSVT 462
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
593-997 |
4.88e-33 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 134.86 E-value: 4.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMG---AAIALPGVTGES 669
Cdd:PLN02467 66 WARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkqkAPVSLPMETFKG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRlSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPG---ESGGl 746
Cdd:PLN02467 146 YVLK-EPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGlgtEAGA- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 sdKLLGDPRVAGVAFTGSTGAAWKINRTlAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALR 826
Cdd:PLN02467 224 --PLASHPGVDKIAFTGSTATGRKIMTA-AAQMVKPVSL--ELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 827 ILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARLVGRTpQPAELSGGCFFAP 904
Cdd:PLN02467 299 RLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFIStaKSEGATILCGGK-RPEHLKKGFFIEP 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 905 HAF-EVALD-QLPTFETFGPVLHIARFKGDqlADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQigAV 982
Cdd:PLN02467 378 TIItDVTTSmQIWREEVFGPVLCVKTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQ--PC 453
|
410
....*....|....*
gi 1708270319 983 VGSQPFGGEGLSGTG 997
Cdd:PLN02467 454 FCQAPWGGIKRSGFG 468
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
593-1018 |
9.53e-32 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 131.11 E-value: 9.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAlpgvTGESNEL 672
Cdd:PLN02315 72 WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIP----SERPNHM 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLSGRGPFI---AIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEalldagIPADVL--HYLPGE----- 742
Cdd:PLN02315 148 MMEVWNPLGivgVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTK------LVAEVLekNNLPGAiftsf 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 743 SGG--LSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARdssIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQ 820
Cdd:PLN02315 222 CGGaeIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR---FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 821 RCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLA--GTARLVGRTpqpAELSG 898
Cdd:PLN02315 299 RCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKsqGGKILTGGS---AIESE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 899 GCFFAPHAFEVALD-QLPTFETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRldsTVETVRKL-----AKVGNL 972
Cdd:PLN02315 376 GNFVQPTIVEISPDaDVVKEELFGPVLYVMKFK--TLEEAIEINNSVPQGLSSSIFTR---NPETIFKWigplgSDCGIV 450
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1708270319 973 YINRNQIGAVVGSQpFGGEGLSGTGFKAGG---PHYLLRFACertvTIN 1018
Cdd:PLN02315 451 NVNIPTNGAEIGGA-FGGEKATGGGREAGSdswKQYMRRSTC----TIN 494
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
591-997 |
9.95e-32 |
|
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: 130.26 E-value: 9.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALG-ELREAVDYCRFYAHEARRLMGA---------AI 660
Cdd:cd07116 52 EAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSiseidentvAY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 661 ALP---GVTGEsnelrlsgrgpfiaIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTP---LIGMRAIEALLdagiPAD 734
Cdd:cd07116 132 HFHeplGVVGQ--------------IIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPasiLVLMELIGDLL----PPG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 735 VLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAardSSIASLIAETGGL--NAMIADSSAH----VEQLII 808
Cdd:cd07116 194 VVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS---ENIIPVTLELGGKspNIFFADVMDAddafFDKALE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 809 DVLMSAFNSaGQRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCD--KLAGTARL 886
Cdd:cd07116 271 GFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDigKEEGAEVL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 887 VG--RTPQPAELSGGCFFAPHAFevALDQLPTF--ETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTRLDSTVET 962
Cdd:cd07116 350 TGgeRNELGGLLGGGYYVPTTFK--GGNKMRIFqeEIFGPVLAVTTFKDEE--EALEIANDTLYGLGAGVWTRDGNTAYR 425
|
410 420 430
....*....|....*....|....*....|....*
gi 1708270319 963 VRKLAKVGNLYInrNQIGAVVGSQPFGGEGLSGTG 997
Cdd:cd07116 426 MGRGIQAGRVWT--NCYHLYPAHAAFGGYKQSGIG 458
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
593-997 |
8.27e-31 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 127.28 E-value: 8.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPgvtgESNEL 672
Cdd:PRK13968 45 WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEHGPAMLKAEPTLV----ENQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLSGR--GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLSdKL 750
Cdd:PRK13968 121 VIEYRplGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVS-QM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 751 LGDPRVAGVAFTGSTGAAWKINRTLAArdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLV 830
Cdd:PRK13968 200 INDSRIAAVTVTGSVRAGAAIGAQAGA---ALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFII 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 831 QDDIADQVIERLGLAMQELRMGDPLQLATDVGPTI-----DTLSQRdLQAycdKLAGTARLV--GRtpqpaELSG-GCFF 902
Cdd:PRK13968 277 EEGIASAFTERFVAAAAALKMGDPRDEENALGPMArfdlrDELHHQ-VEA---TLAEGARLLlgGE-----KIAGaGNYY 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 903 APHAFEVALDQLPTF--ETFGPVLHIARFKgdqlaDAVHRV---NKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYInrN 977
Cdd:PRK13968 348 APTVLANVTPEMTAFreELFGPVAAITVAK-----DAEHALelaNDSEFGLSATIFTTDETQARQMAARLECGGVFI--N 420
|
410 420
....*....|....*....|
gi 1708270319 978 QIGAVVGSQPFGGEGLSGTG 997
Cdd:PRK13968 421 GYCASDARVAFGGVKKSGFG 440
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
590-955 |
7.94e-29 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 121.79 E-value: 7.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIAL-----PG 664
Cdd:PLN00412 66 QKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEGKFLvsdsfPG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 665 vtGESNELRLSGRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPG 741
Cdd:PLN00412 146 --NERNKYCLTSKIPLgvvLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 742 ESGGLSDKLLGDPRVAGVAFT-GSTGAAwkinrtlAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQ 820
Cdd:PLN00412 224 KGSEIGDFLTMHPGVNCISFTgGDTGIA-------ISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 821 RCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLAtDVGPTIDTLSQRDLQAYC-DKLAGTARLVgrtpQPAELSGG 899
Cdd:PLN00412 297 RCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDC-DITPVVSESSANFIEGLVmDAKEKGATFC----QEWKREGN 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708270319 900 CFFAPHAFEVALD-QLPTFETFGPVLHIARFKGDQlaDAVHRVNKLGFGLTMGVHTR 955
Cdd:PLN00412 372 LIWPLLLDNVRPDmRIAWEEPFGPVLPVIRINSVE--EGIHHCNASNFGLQGCVFTR 426
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
601-1009 |
1.10e-28 |
|
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: 120.42 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 601 RAALLEKAADLLEARQDEFLwllsreAGKTLPDALGElREAVDYCRFYAH-EARRLMGAAIALPGVTGES--------NE 671
Cdd:cd07084 23 RADFLARIIQRLAAKSYDIA------AGAVLVTGKGW-MFAENICGDQVQlRARAFVIYSYRIPHEPGNHlgqglkqqSH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGI-PADVLHYLPGeSGGLSDKL 750
Cdd:cd07084 96 GYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLING-DGKTMQAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 751 LGDPRVAGVAFTGSTGAAwkinRTLAArDSSIASLIAETGGLNAMIADSSAHVEQLIID-VLMSAFNSAGQRCSALRILL 829
Cdd:cd07084 175 LLHPNPKMVLFTGSSRVA----EKLAL-DAKQARIYLELAGFNWKVLGPDAQAVDYVAWqCVQDMTACSGQKCTAQSMLF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQ-VIERLGLAMQELRMGDPLqlatdVGPTI--DTLSQ---RDLQAYCDKLAGTARLvgRTPQPAELSGGCfFA 903
Cdd:cd07084 250 VPENWSKTpLVEKLKALLARRKLEDLL-----LGPVQtfTTLAMiahMENLLGSVLLFSGKEL--KNHSIPSIYGAC-VA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 904 PHAFEV-----ALDQLPTFETFGPVLHIARFKGDQLADAVHRVNKLGFGLTMGVHTRLDSTV-ETVRKLAKVGNLY-INR 976
Cdd:cd07084 322 SALFVPideilKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLqELIGNLWVAGRTYaILR 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 1708270319 977 NQIGAVVGSQPFGGEGLSGTGFKAGGP---HYLLRF 1009
Cdd:cd07084 402 GRTGVAPNQNHGGGPAADPRGAGIGGPeaiKLVWRC 437
|
|
| Pro_dh-DNA_bdg |
pfam14850 |
DNA-binding domain of Proline dehydrogenase; This domain lies at the N-terminus of ... |
67-173 |
3.42e-25 |
|
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: 101.04 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 67 FEAFLQSYGLGSEEGVALMALAEALLRIPDTNTQDQLIRDLLESRDWRR--SQTATWLVSAASRALLFTDSWIDASEGRH 144
Cdd:pfam14850 1 VEALLQEYSLSSEEGVALMCLAEALLRVPDAATADALIRDKLGRGDWKShlGHSDSLLVNASTWGLMLTGRLLDDEPEGT 80
|
90 100 110
....*....|....*....|....*....|..
gi 1708270319 145 W---FDRLLRKMGEPVLRSAMKAGMKVMANNF 173
Cdd:pfam14850 81 LagaLKRLVGRLGEPVIRKAVRQAMRLMGRQF 112
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
663-1015 |
4.12e-25 |
|
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: 109.62 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 663 PGVTGESNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGmRAIEALLDAGIPADVLHYLPGE 742
Cdd:cd07134 87 LLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTS-AVIAKIIREAFDEDEVAVFEGD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 743 SgGLSDKLLGDPrVAGVAFTGSTGAAwKINRTLAARdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRC 822
Cdd:cd07134 166 A-EVAQALLELP-FDHIFFTGSPAVG-KIVMAAAAK--HLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 823 SALRILLVQDDIADQVIERLGLAMQELRMGDPLQLAT-DVGPTIDTLSQRDLQAYCDK-LAGTARLV-GRTPQPAElsgg 899
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASpDLARIVNDRHFDRLKGLLDDaVAKGAKVEfGGQFDAAQ---- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 900 CFFAPHAFE-VALD-QLPTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRN 977
Cdd:cd07134 317 RYIAPTVLTnVTPDmKIMQEEIFGPVLPIITY--EDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDV 394
|
330 340 350
....*....|....*....|....*....|....*...
gi 1708270319 978 QIGAVVGSQPFGGEGLSGTGfKAGGPHYLLRFACERTV 1015
Cdd:cd07134 395 VLHFLNPNLPFGGVNNSGIG-SYHGVYGFKAFSHERAV 431
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
601-938 |
4.09e-24 |
|
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: 107.74 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 601 RAALLEKAADLLEARQDEFlWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPgvtgESNELRLSGRGPF 680
Cdd:cd07128 61 RAAMLKALAKYLMERKEDL-YALSAATGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLV----EGDVEPLSKDGTF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 681 IA-------------IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGI-PADVLHYLPGESGGL 746
Cdd:cd07128 136 VGqhiltprrgvavhINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 747 SDKLlgDPRVAgVAFTGS--TGAAWKINRTLAARDssiASLIAETGGLNAMI-----ADSSAHVEQLIIDVLMSAFNSAG 819
Cdd:cd07128 216 LDHL--GEQDV-VAFTGSaaTAAKLRAHPNIVARS---IRFNAEADSLNAAIlgpdaTPGTPEFDLFVKEVAREMTVKAG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 820 QRCSALRILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLAGTARLVGRTPQPAELSG- 898
Cdd:cd07128 290 QKCTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGa 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1708270319 899 ----GCFFAPHAFEV----ALDQLPTFETFGPVLHIARFkgDQLADAV 938
Cdd:cd07128 370 daekGAFFPPTLLLCddpdAATAVHDVEAFGPVATLMPY--DSLAEAI 415
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
683-1015 |
5.62e-24 |
|
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: 106.15 E-value: 5.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 683 IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTP---LIGMRAIEALLDAGIPADVlhylpgeSGGLSD--KLLgDPRVA 757
Cdd:cd07135 115 IGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPhtaALLAELVPKYLDPDAFQVV-------QGGVPEttALL-EQKFD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 758 GVAFTGSTGAAwKINRTLAARdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQ 837
Cdd:cd07135 187 KIFYTGSGRVG-RIIAEAAAK--HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 838 VIERLGLAMQELRMGDPLQlATDVGPTIDTLSQRDLQAYCDKLAGTARLVGRTPQPAelsggCFFAPHA-FEVAL-DQLP 915
Cdd:cd07135 264 FVEELKKVLDEFYPGGANA-SPDYTRIVNPRHFNRLKSLLDTTKGKVVIGGEMDEAT-----RFIPPTIvSDVSWdDSLM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 916 TFETFGPVLHIarFKGDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSG 995
Cdd:cd07135 338 SEELFGPVLPI--IKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDSG 415
|
330 340
....*....|....*....|
gi 1708270319 996 TGfKAGGPHYLLRFACERTV 1015
Cdd:cd07135 416 YG-AYHGKYGFDTFTHERTV 434
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
591-975 |
2.60e-22 |
|
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: 101.46 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 591 DGWADQAPTARAALLEKAADLLEARQDEFLWLLSREAGktLPDAL--GELREAVDYCRFYAHEARR--LMGAAI--ALP- 663
Cdd:cd07129 13 ESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARlqGELGRTTGQLRLFADLVREgsWLDARIdpADPd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 664 GVTGESNELRLS--GRGPFIAIAPWNFPLAI-FLGQITA-ALAAGNTVIAK--PS--RRTPLIGMRAIEALLDAGIPADV 735
Cdd:cd07129 91 RQPLPRPDLRRMlvPLGPVAVFGASNFPLAFsVAGGDTAsALAAGCPVVVKahPAhpGTSELVARAIRAALRATGLPAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 736 LHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIAsLIAETGGLN-------AMIADSSAHVEQLII 808
Cdd:cd07129 171 FSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEPIP-FYAELGSVNpvfilpgALAERGEAIAQGFVG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 809 DVLMsafnSAGQRCSALRILLVQDDIA-DQVIERLGLAMQE---LRMgdplqlatdvgptidtLSQRDLQAYCDKLAGTA 884
Cdd:cd07129 250 SLTL----GAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAapaQTM----------------LTPGIAEAYRQGVEALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 885 RLVGRTP--QPAELSGGCFFAPHAFEVALDQL---PTF--ETFGPVLHIARFKG-DQLADAvhrVNKLGFGLTMGVHTrL 956
Cdd:cd07129 310 AAPGVRVlaGGAAAEGGNQAAPTLFKVDAAAFladPALqeEVFGPASLVVRYDDaAELLAV---AEALEGQLTATIHG-E 385
|
410 420
....*....|....*....|....
gi 1708270319 957 DSTVETVRKLA-----KVGNLYIN 975
Cdd:cd07129 386 EDDLALARELLpvlerKAGRLLFN 409
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
593-975 |
3.17e-22 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 102.52 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAiaLPGVTGESNEL 672
Cdd:PLN02419 167 WRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEY--LPNVSNGVDTY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLsgRGPF---IAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGESGGLsDK 749
Cdd:PLN02419 245 SI--REPLgvcAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASliaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILL 829
Cdd:PLN02419 322 ICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS---NMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVV 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIA---DQVIERlglaMQELRMGDPLQLATDVGPTIDTLSQ----RDLQAYCDKLAGTArLVGRTPQPAELSGGCFF 902
Cdd:PLN02419 399 FVGDAKsweDKLVER----AKALKVTCGSEPDADLGPVISKQAKericRLIQSGVDDGAKLL-LDGRDIVVPGYEKGNFI 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708270319 903 APHAFEVALDQLPTF--ETFGPVLhiARFKGDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYIN 975
Cdd:PLN02419 474 GPTILSGVTPDMECYkeEIFGPVL--VCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
683-997 |
1.93e-21 |
|
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: 98.37 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 683 IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPligmrAIEALLDAGIPadvlHYLPGESGGLsdkLLGDPRVAG---- 758
Cdd:cd07087 107 IGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAP-----ATSALLAKLIP----KYFDPEAVAV---VEGGVEVATalla 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 759 -----VAFTGSTGAAWKINRtLAARdsSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDD 833
Cdd:cd07087 175 epfdhIFFTGSPAVGKIVME-AAAK--HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 834 IADQVIERLGLAMQELrMGDPLQLATDVGPTIdtlSQRDLQaycdklagtaRLVGRTPQPAELSGG------CFFAPHAF 907
Cdd:cd07087 252 IKDELIEELKKAIKEF-YGEDPKESPDYGRII---NERHFD----------RLASLLDDGKVVIGGqvdkeeRYIAPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 EVALDQLP--TFETFGPVLHIARFkgDQLADAVHRVNKLG-------FGLTMGVHTRLDSTVETvrklakvGNLYINRNQ 978
Cdd:cd07087 318 DDVSPDSPlmQEEIFGPILPILTY--DDLDEAIEFINSRPkplalylFSEDKAVQERVLAETSS-------GGVCVNDVL 388
|
330
....*....|....*....
gi 1708270319 979 IGAVVGSQPFGGEGLSGTG 997
Cdd:cd07087 389 LHAAIPNLPFGGVGNSGMG 407
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
601-940 |
5.58e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 97.85 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 601 RAALLEKAADLLEARQDEFLWLLSREAGKTLPDALGELREAVDYCRFYAH-----EARRLM--GAAIALpGVTG--ESNE 671
Cdd:PRK11903 65 RAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKlgaalGDARLLrdGEAVQL-GKDPafQGQH 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 672 LRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGI-PADVLHYLPGESGGLSDKL 750
Cdd:PRK11903 144 VLVPTRGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSAGLLDHL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 751 LGDPRVAgvaFTGSTGAAWKInRTLAARDSSIASLIAETGGLNAMI-----ADSSAHVEQLIIDVLMSAFNSAGQRCSAL 825
Cdd:PRK11903 224 QPFDVVS---FTGSAETAAVL-RSHPAVVQRSVRVNVEADSLNSALlgpdaAPGSEAFDLFVKEVVREMTVKSGQKCTAI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 826 RILLVQDDIADQVIERLGLAMQELRMGDPLQLATDVGPTIDTLSQRDLQAYCDKLAGTARLV----GRTPQPAELSGGCF 901
Cdd:PRK11903 300 RRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLfdggGFALVDADPAVAAC 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1708270319 902 FAPHAFEV----ALDQLPTFETFGPVLHIARFKGDQLADA-VHR 940
Cdd:PRK11903 380 VGPTLLGAsdpdAATAVHDVEVFGPVATLLPYRDAAHALAlARR 423
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
683-997 |
9.15e-19 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 90.86 E-value: 9.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 683 IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGmRAIEALLDAGIPADVLHYLPGESgGLSDKLLGDPrVAGVAFT 762
Cdd:PTZ00381 116 IGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTS-KLMAKLLTKYLDPSYVRVIEGGV-EVTTELLKEP-FDHIFFT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 763 GSTGAAwKINRTLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERL 842
Cdd:PTZ00381 193 GSPRVG-KLVMQAAAENLTPCTL--ELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEAL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 843 GLAMQELrMGDPLQLATDVGPTIDTLSQRDLQAYCDK------LAGTARLVGRTPQPAELSggcffaphafEVALD-QLP 915
Cdd:PTZ00381 270 KEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKDhggkvvYGGEVDIENKYVAPTIIV----------NPDLDsPLM 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 916 TFETFGPVLHIARFKgdQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSG 995
Cdd:PTZ00381 339 QEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSG 416
|
..
gi 1708270319 996 TG 997
Cdd:PTZ00381 417 MG 418
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
594-1015 |
7.95e-18 |
|
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: 87.54 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 594 ADQAPTA--RAALLEKAADLLEARQDEFLWLLS-----REAGKTLpdaLGEL---REAVDYCRfyAH-----EARRLMGA 658
Cdd:cd07133 13 ANPPPSLeeRRDRLDRLKALLLDNQDALAEAISadfghRSRHETL---LAEIlpsIAGIKHAR--KHlkkwmKPSRRHVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 659 AIALPGvtgeSNELRLSGRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGmRAIEALLDAGIPADVLHY 738
Cdd:cd07133 88 LLFLPA----KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTS-ALLAELLAEYFDEDEVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 739 LPGESG------GLS-DKLLgdprvagvaFTGSTGAAWKINRTlAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVL 811
Cdd:cd07133 163 VTGGADvaaafsSLPfDHLL---------FTGSTAVGRHVMRA-AAENLTPVTL--ELGGKSPAIIAPDADLAKAAERIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 812 MSAFNSAGQRCSALRILLVQDDIADQVIERLGLAMQelRMGDPLQLATDVGPTIDTLS-QRdLQAYC-DKLAGTARLVGR 889
Cdd:cd07133 231 FGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVA--KMYPTLADNPDYTSIINERHyAR-LQGLLeDARAKGARVIEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 890 TPQPAELSGGCFFAPHA-FEVALD-QLPTFETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLA 967
Cdd:cd07133 308 NPAGEDFAATRKLPPTLvLNVTDDmRVMQEEIFGPILPILTY--DSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1708270319 968 KVGNLYINRNQIGAVVGSQPFGGEGLSGTGfkaggpHY-----LLRFACERTV 1015
Cdd:cd07133 386 HSGGVTINDTLLHVAQDDLPFGGVGASGMG------AYhgkegFLTFSHAKPV 432
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
593-797 |
2.77e-15 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 81.06 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 593 WADQAPTARAALLEKAADLLEARQDEFLwllsreagktlPDALGELReavdycrfyaheARRLMGAAIALPGVTGESNEL 672
Cdd:PRK11905 1018 PPAHESVDTDAAARDFLAWLDKEGKAAL-----------AAAARDAR------------ARSALGLEQELPGPTGESNLL 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 673 RLSGRGPFIAIAPwnfPLAIFLGQITAALAAGNTVIakpsrrtpligmraieaLLDAGIPADVLHYLPG---ESGGLSDK 749
Cdd:PRK11905 1075 SLHPRGRVLCVAD---TEEALLRQLAAALATGNVAV-----------------VAADSGLAAALADLPGlvaARIDWTQD 1134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASLIAETGGLNAMIA 797
Cdd:PRK11905 1135 WEADDPFAGALLEGDAERARAVRQALAARPGAIVPLIAAEPTDAYDLA 1182
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
683-997 |
2.98e-15 |
|
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: 79.57 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 683 IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPligmrAIEALLDAGIPAdvlhYLPGE-----SGGLSD-KLLGDPRV 756
Cdd:cd07132 107 IGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP-----ATAKLLAELIPK----YLDKEcypvvLGGVEEtTELLKQRF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 757 AGVAFTGSTGAAwKINRTLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIAD 836
Cdd:cd07132 178 DYIFYTGSTSVG-KIVMQAAAKHLTPVTL--ELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 837 QVIERLGLAMQELRMGDPlQLATDVGPTIdtlSQRDLQAYCDKLAGTARLVGRTPQPAElsggCFFAPhafEVALDQLPT 916
Cdd:cd07132 255 KFVEALKKTLKEFYGEDP-KESPDYGRII---NDRHFQRLKKLLSGGKVAIGGQTDEKE----RYIAP---TVLTDVKPS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 917 F-----ETFGPVLHIARFKGdqLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGE 991
Cdd:cd07132 324 DpvmqeEIFGPILPIVTVNN--LDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGV 401
|
....*.
gi 1708270319 992 GLSGTG 997
Cdd:cd07132 402 GNSGMG 407
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
607-952 |
3.10e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 79.85 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 607 KAADLLEARQDE--FLWLLSREAGKTLPDALGELREAVDYCRFYAHEARRLMGAAIALPG-VTGE-SNELRLSgRGPFIA 682
Cdd:cd07126 70 RVAHELRKPEVEdfFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPGdHQGQqSSGYRWP-YGPVAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 683 IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDAGIPADVLHYLPGEsGGLSDKLLGDPRVAGVAFT 762
Cdd:cd07126 149 ITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSD-GPTMNKILLEANPRMTLFT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 763 GSTGAAWKINRTLAARdssiasLIAETGGLNAMI-------ADSSAHV-EQliidvlmSAFNSAGQRCSALRILLVQDDI 834
Cdd:cd07126 228 GSSKVAERLALELHGK------VKLEDAGFDWKIlgpdvsdVDYVAWQcDQ-------DAYACSGQKCSAQSILFAHENW 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 835 ADQ-VIERLGLAMQELRMGDplqlaTDVGPTIdTLSQRDLQAYCDKLA---GTARLVGRTPQPAELSGGCFFA--PHAFE 908
Cdd:cd07126 295 VQAgILDKLKALAEQRKLED-----LTIGPVL-TWTTERILDHVDKLLaipGAKVLFGGKPLTNHSIPSIYGAyePTAVF 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1708270319 909 VALDQ--------LPTFETFGPVLHIARFKGDQLADAVHRVNKLGFGLTMGV 952
Cdd:cd07126 369 VPLEEiaieenfeLVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAV 420
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
678-997 |
6.59e-12 |
|
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: 68.98 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 678 GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPligmrAIEALLDAGIPAdvlhYLPGES-----GGLSD-KLL 751
Cdd:cd07137 103 GVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAP-----ATSALLAKLIPE----YLDTKAikvieGGVPEtTAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 752 GDPRVAGVAFTGSTgaawKINR-TLAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNS-AGQRCSALRILL 829
Cdd:cd07137 174 LEQKWDKIFFTGSP----RVGRiIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 830 VQDDIADQVIERLGLAMQELRMGDPLQlATDVGPTIDTLSQRDLQAYCDKLAGTARLV-GRTPQPAELsggcFFAPHAF- 907
Cdd:cd07137 250 VEESFAPTLIDALKNTLEKFFGENPKE-SKDLSRIVNSHHFQRLSRLLDDPSVADKIVhGGERDEKNL----YIEPTILl 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 908 EVALDQ-LPTFETFGPVLHIARFKGdqLADAVHRVNKLGFGLTMGVHTRlDSTVETvRKLAKV--GNLYINRNQIGAVVG 984
Cdd:cd07137 325 DPPLDSsIMTEEIFGPLLPIITVKK--IEESIEIINSRPKPLAAYVFTK-NKELKR-RIVAETssGGVTFNDTVVQYAID 400
|
330
....*....|...
gi 1708270319 985 SQPFGGEGLSGTG 997
Cdd:cd07137 401 TLPFGGVGESGFG 413
|
|
| PLN02681 |
PLN02681 |
proline dehydrogenase |
250-464 |
1.18e-11 |
|
proline dehydrogenase
Pssm-ID: 215366 [Multi-domain] Cd Length: 455 Bit Score: 68.19 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 250 AQLERVQTELYGRLLDLAQAAAKADLVFSIDAEESeRLEISlwlYERLLREPSLKNWRGLGLVV-----QAYQKRAPFVI 324
Cdd:PLN02681 209 AEEERLLELAHERLQKLCERAAQLGVPLLIDAEYT-SLQPA---IDYITYDLAREFNKGKDRPIvygtyQAYLKDARERL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 325 DWLAELAADTGRVLPIRLVKGAYWDSEIKRAQQNGLAGyPVYTRKHHTDVAYLACARKLLDHGPE-RFYPQFASHNAQTL 403
Cdd:PLN02681 285 RLDLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPS-PVHDTIQDTHACYNRCAEFLLEKASNgDGEVMLATHNVESG 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708270319 404 SWIVEATRNRGNSFEIQRLH-----GMGEALHSQIHEREGVASRvYAPVGRFHALLPYLVRRLLEN 464
Cdd:PLN02681 364 ELAAAKMNELGLHKGDPRVQfaqllGMSDNLSFGLGNAGFRVSK-YLPYGPVEEVIPYLLRRAEEN 428
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
678-1008 |
6.45e-11 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 65.75 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 678 GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGMRAIEALLDA----GIPADVLHYLPGESGGLSDKLLGD 753
Cdd:cd07081 97 GVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIELAQRLMKF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 754 PRVAGVAFTGSTGAawkinrTLAARdSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDD 833
Cdd:cd07081 177 PGIGLLLATGGPAV------VKAAY-SSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 834 IADQVIERLGLAMQELRMGDPLQLATDVgptidTLSQRDLQA-YCDKLAGT-ARLVG-RTPQPAELSGGcffaphafEV- 909
Cdd:cd07081 250 VYDEVMRLFEGQGAYKLTAEELQQVQPV-----ILKNGDVNRdIVGQDAYKiAAAAGlKVPQETRILIG--------EVt 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 910 ALDQLPTF--ETFGPVLHIARFKG--DQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAK----------------- 968
Cdd:cd07081 317 SLAEHEPFahEKLSPVLAMYRAANfaDADAKALALKLEGGCGHTSAMYSDNIKAIENMNQFANamktsrfvkngpcsqgg 396
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1708270319 969 VGNLYINRNQIGAVVGSQPFGGEGLSgtgfKAGGPHYLLR 1008
Cdd:cd07081 397 LGDLYNFRGWPSMTLGCGTWGGNSVS----ENVGPKHLVN 432
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
683-997 |
3.64e-10 |
|
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: 63.29 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 683 IAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPLIGmRAIEALLDAGIPADVLHYLPGEsGGLSDKLLgDPRVAGVAFT 762
Cdd:cd07136 107 IAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTS-KVIAKIIEETFDEEYVAVVEGG-VEENQELL-DQKFDYIFFT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 763 GSTgAAWKINRTLAARDSSIASLiaETGGLNAMIADSSAHVEQLIIDVLMSAFNSAGQRCSALRILLVQDDIADQVIERL 842
Cdd:cd07136 184 GSV-RVGKIVMEAAAKHLTPVTL--ELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKEL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 843 GLAMQELRMGDPLQlATDVGPTIdtlSQRDLQAYCDKLAGTARLVGRTPQPAELsggcFFAPhafeVALDQlPTF----- 917
Cdd:cd07136 261 KEEIKKFYGEDPLE-SPDYGRII---NEKHFDRLAGLLDNGKIVFGGNTDRETL----YIEP----TILDN-VTWddpvm 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 918 --ETFGPVLHIARFkgDQLADAVHRVNKLGFGLTMGVHTRLDSTVETVRKLAKVGNLYINrNQIGAVVGSQ-PFGGEGLS 994
Cdd:cd07136 328 qeEIFGPILPVLTY--DTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN-DTIMHLANPYlPFGGVGNS 404
|
...
gi 1708270319 995 GTG 997
Cdd:cd07136 405 GMG 407
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
658-794 |
1.02e-09 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 63.03 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 658 AAIALPGVTGESNELRLSGRGPFIAIAPwnfPLAIFLGQITAALAAGNTVIakpsrrtpligmrAIEALLDAGIPADVLh 737
Cdd:COG4230 1044 GALTLPGPTGERNTLTLRPRGRVLCLAD---SLEALLAQLAAALATGNRAV-------------VAADLALAGLPAVLL- 1106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708270319 738 ylpgesgglsdkllgdPRVAGVAFTGSTGAawkINRTLAARDSSIASLIA----------ETGGlNA 794
Cdd:COG4230 1107 ----------------PPFDAVLFEGRLRA---LRQALAARDGAIVPVIDagydlerlleEAGG-NA 1153
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
678-842 |
1.41e-08 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 58.58 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 678 GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPligmrAIEALLDAGIPAdvlhYLPGES-----GG--LSDKL 750
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAP-----ATSAFLAANIPK----YLDSKAvkvieGGpaVGEQL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 751 LgDPRVAGVAFTGSTGAAwKINRTLAARDSSIASLiaETGGLNAMIAD---SSAHVEQLIIDVLMSAFNS-AGQRCSALR 826
Cdd:PLN02203 181 L-QHKWDKIFFTGSPRVG-RIIMTAAAKHLTPVAL--ELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGScAGQACIAID 256
|
170
....*....|....*.
gi 1708270319 827 ILLVQDDIADQVIERL 842
Cdd:PLN02203 257 YVLVEERFAPILIELL 272
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
678-997 |
6.08e-08 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 56.59 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 678 GPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRTPlIGMRAIEALLDAGIPADVLHYLPGESGGLSDKLlgDPRVA 757
Cdd:PLN02174 114 GVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAP-ASSALLAKLLEQYLDSSAVRVVEGAVTETTALL--EQKWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 758 GVAFTGSTgaawKINRT-LAARDSSIASLIAETGGLNAMIADSSAHVEQLIIDVLMSAFN-SAGQRCSALRILLVQDDIA 835
Cdd:PLN02174 191 KIFYTGSS----KIGRViMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 836 DQVIERLGLAMQELRMGDPLQlATDVGPTIDTLSQRDLQAYCDKLAGTARLVGRTPQPAElsgGCFFAPHA-FEVALDQL 914
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPME-SKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDRE---NLKIAPTIlLDVPLDSL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 915 -PTFETFGPVLHIARFKGDQLADAVHRVNKLGFGLTMGVHTRldSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGL 993
Cdd:PLN02174 343 iMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNK--KLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGE 420
|
....
gi 1708270319 994 SGTG 997
Cdd:PLN02174 421 SGMG 424
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
590-997 |
2.45e-06 |
|
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: 51.33 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEARQDEFL----------WLLSREAGKtlPDALGELREAVDYCrfyAHEARRLMGAA 659
Cdd:cd07127 97 MPGWRDAGARARAGVCLEILQRLNARSFEMAhavmhttgqaFMMAFQAGG--PHAQDRGLEAVAYA---WREMSRIPPTA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 660 IAL-PGvtGESNELRLS------GRGPFIAIAPWNFPLAIFLGQITAALAAGNTVIAKPSRRT----PLIGMRAIEALLD 728
Cdd:cd07127 172 EWEkPQ--GKHDPLAMEktftvvPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLAE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 729 AGI-PADVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTG-AAWKINRtlaARDssiASLIAETGGLNAMIADSSAHVEQL 806
Cdd:cd07127 250 AGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAfGDWLEAN---ARQ---AQVYTEKAGVNTVVVDSTDDLKAM 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 807 IIDVLMSAFNSAGQRCSALRILLV-QDDIA--------DQVIERLGLAMQELrMGDPLQLATDVGPTIDTLSQRDLqAYC 877
Cdd:cd07127 324 LRNLAFSLSLYSGQMCTTPQNIYVpRDGIQtddgrksfDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI-AEA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 878 DKLAGTARlVGRTPQPAELSGGCFFAPhaFEVALDQLP----TFETFGPVLH-IARFKGDQLADAVHRVNKLGFGLTMGV 952
Cdd:cd07127 402 RQLGEVLL-ASEAVAHPEFPDARVRTP--LLLKLDASDeaayAEERFGPIAFvVATDSTDHSIELARESVREHGAMTVGV 478
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1708270319 953 HTRLDSTVETVRKLAKVGNLYINRNQIGAVVGSQPFGGEGLSGTG 997
Cdd:cd07127 479 YSTDPEVVERVQEAALDAGVALSINLTGGVFVNQSAAFSDFHGTG 523
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
652-842 |
1.28e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 48.76 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 652 ARRLMGAAIALPGVTGESN---ELRLSGRGPFIAIAPWNFPLAIfLGQITAALAAGNTVIAKPSRRTPlIGMRAIEALLD 728
Cdd:cd07077 73 ERGITASVGHIQDVLLPDNgetYVRAFPIGVTMHILPSTNPLSG-ITSALRGIATRNQCIFRPHPSAP-FTNRALALLFQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 729 AGIPA----DVLHYLPGESGGLSDKLLGDPRVAGVAFTGSTGAAwkinrTLAARDSSIASLIAETGGLNAMIADSSAHVE 804
Cdd:cd07077 151 AADAAhgpkILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAV-----DAAVKHSPHIPVIGFGAGNSPVVVDETADEE 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 1708270319 805 QLIIDVLMSAFNSaGQRCSALRILLVQDDIADQVIERL 842
Cdd:cd07077 226 RASGSVHDSKFFD-QNACASEQNLYVVDDVLDPLYEEF 262
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
590-785 |
5.65e-05 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 47.28 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 590 QDGWADQAPTARAALLEKAADLLEarqdeflWLLSREAgktlpdalgelrEAVDYCRFYAHEARrlMGAAIALPGVTGES 669
Cdd:PRK11809 1122 QDAEYPVDAQLRAALLAPLTALRE-------WAAEREP------------ELAALCDQYAELAQ--AGTTRLLPGPTGER 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708270319 670 NELRLSGRGPFIAIAPWNFPLAIflgQITAALAAGNTVIAKPSrrtpligmrAIEALLDAGIPADVLHYLpgesGGLSDK 749
Cdd:PRK11809 1181 NTYTLLPRERVLCLADTEQDALT---QLAAVLAVGSQALWPDD---------ALHRALVAALPAAVQARI----QLAKDW 1244
|
170 180 190
....*....|....*....|....*....|....*.
gi 1708270319 750 LLGDPRVAGVAFTGSTGAAWKINRTLAARDSSIASL 785
Cdd:PRK11809 1245 QLADQPFDAVLFHGDSDQLRALCEQVAQRDGPIVSV 1280
|
|
| PRODH |
pfam18327 |
Proline utilization A proline dehydrogenase N-terminal domain; This is the N-terminal domain ... |
18-59 |
1.54e-03 |
|
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: 37.44 E-value: 1.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1708270319 18 IRDNLFRDEAEAIGSLLPLARLDEQAEKAVHVRTLSLAQGVR 59
Cdd:pfam18327 7 ITAAYRRPEAECVAPLLEAARLPPAERAAIRALARKLVEALR 48
|
|
| |
