|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
1-862 |
0e+00 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 1703.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 1 MSINSIEELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAY 80
Cdd:PRK13805 6 MAVTNVAELDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEDKVIKNHFASEYIYNSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 81 KDEKTCGVLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAVEA 160
Cdd:PRK13805 86 KDEKTVGVIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAAVAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 161 GAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTF 240
Cdd:PRK13805 166 GAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSSGKPALGVGAGNVPAYIDKTADIKRAVNDILLSKTF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 241 DNGVICASEQSVVVVDTVYNAVRERFASHGGYLLQGKELKAVQGILLK--NGALNAAIVGQSAVKIAEMAGISVPADTKI 318
Cdd:PRK13805 246 DNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFGkeNGALNADIVGQSAYKIAEMAGFKVPEDTKI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 319 LIGEVKAIDDSEPFAHEKLSPTLAMYRAKDFADAVEKAVKLVDMGGIGHTSCLYTdqdNQAARVMTFGEKMKTARILINT 398
Cdd:PRK13805 326 LIAEVKGVGESEPLSHEKLSPVLAMYKAKDFEDAVEKAEKLVEFGGLGHTAVIYT---NDDELIKEFGLRMKACRILVNT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 399 PTSHGGIGDLYNfSLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVitDG 478
Cdd:PRK13805 403 PSSQGGIGDLYN-KLAPSLTLGCGSWGGNSVSENVGAKHLLNIKTVAKRRENMQWFKVPKKIYFERGSLPYLLDEL--DG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 479 HKRALIVTDRFLFNNGYADQITSVLKA--AGVETEVFFEVEADPTLTIVRKGAELANAFKPDVIIALGGGSPMDAAKIMW 556
Cdd:PRK13805 480 KKRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMW 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 557 VIYEHPETHFEELALRFMDIRKRIYTFPKMGVKARMVAITTTSGTGSEVTPFAVVTDDTTGQKYPLADYALTPDMAIVDA 636
Cdd:PRK13805 560 LFYEHPETDFEDLAQKFMDIRKRIYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 637 NLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGSKNPVARERVHNAATIAGIAFAN 716
Cdd:PRK13805 640 NLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGAKDPEAREKMHNASTIAGMAFAN 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 717 AFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPtKQTAFSQYDRPQARRRYAEIADHLGLsaPGDRTAAKIE 796
Cdd:PRK13805 720 AFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPP-KQAAFPQYEYPRADERYAEIARHLGL--PGSTTEEKVE 796
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883866115 797 KLLAWLESIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLVAELRQILLASY 862
Cdd:PRK13805 797 SLIKAIEELKAELGIPMSIKEAGVDEADFLAKLDELAELAFDDQCTGANPRYPLISELKEILLDAY 862
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
9-447 |
0e+00 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, 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: 143440 [Multi-domain] Cd Length: 436 Bit Score: 730.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 9 LNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGV 88
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYVYNDIKDMKTVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 89 LGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAVEAGAPPDIIG 168
Cdd:cd07122 81 IEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 169 WIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICAS 248
Cdd:cd07122 161 WIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 249 EQSVVVVDTVYNAVRERFASHGGYLLQGKELKAVQGILLK-NGALNAAIVGQSAVKIAEMAGISVPADTKILIGEVKAID 327
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDdGGTLNPDIVGKSAQKIAELAGIEVPEDTKVLVAEETGVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 328 DSEPFAHEKLSPTLAMYRAKDFADAVEKAVKLVDMGGIGHTSCLYTDQDnqaARVMTFGEKMKTARILINTPTSHGGIGD 407
Cdd:cd07122 321 PEEPLSREKLSPVLAFYRAEDFEEALEKARELLEYGGAGHTAVIHSNDE---EVIEEFALRMPVSRILVNTPSSLGGIGD 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1883866115 408 LYNFsLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKR 447
Cdd:cd07122 398 TYNG-LAPSLTLGCGSWGGNSTSDNVGPKHLLNIKRVAYR 436
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
455-859 |
0e+00 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 726.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 455 KLPKSIYFRRGSLPIALDEviTDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANA 534
Cdd:cd08178 1 KVPPKIYFEPGCLPYLLLE--LPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 535 FKPDVIIALGGGSPMDAAKIMWVIYEHPETHFEELALRFMDIRKRIYTFPKMGVKARMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08178 79 FKPDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 615 TTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGs 694
Cdd:cd08178 159 KTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNG- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 695 KNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPTKQTAFSQYDRPQARRR 774
Cdd:cd08178 238 NDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKQAAFPQYKYYVAKER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 775 YAEIADHLGLsaPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:cd08178 318 YAEIADLLGL--GGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISEL 395
|
....*
gi 1883866115 855 RQILL 859
Cdd:cd08178 396 KEILL 400
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
9-447 |
0e+00 |
|
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: 704.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 9 LNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGV 88
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 89 LGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAVEAGAPPDIIG 168
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 169 WIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICAS 248
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 249 EQSVVVVDTVYNAVRERFASHGGYLLQGKELKAVQGILLKNGALNAAIVGQSAVKIAEMAGISVPADTKILIGEVKAIDD 328
Cdd:cd07081 241 EQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQETRILIGEVTSLAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 329 SEPFAHEKLSPTLAMYRAKDFADAVEKAVKLVDMGGIGHTSCLYTDQDNQAARVMTFGEKMKTARILINTPTSHGGIGDL 408
Cdd:cd07081 321 HEPFAHEKLSPVLAMYRAANFADADAKALALKLEGGCGHTSAMYSDNIKAIENMNQFANAMKTSRFVKNGPCSQGGLGDL 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 1883866115 409 YNFSLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKR 447
Cdd:cd07081 401 YNFRGWPSMTLGCGTWGGNSVSENVGPKHLVNLKTVALR 439
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
5-445 |
3.22e-168 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 497.46 E-value: 3.22e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 5 SIEELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEK 84
Cdd:TIGR02518 6 SIQQVRNLIRSAKVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIVYDSIKDMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 85 TCGVLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAVEAGAPP 164
Cdd:TIGR02518 86 TIGILSEDKEKKVIEIAVPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 165 DIIGWIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGV 244
Cdd:TIGR02518 166 GAIGCITVPTIEGTNELMKNKDTSLILATGGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 245 ICASEQSVVVVDTVYNAVRERFASHGGYLLQGKELKAVQGILLK-NGALNAAIVGQSAVKIAEMAGISVPADTKILIGEV 323
Cdd:TIGR02518 246 ICASEQSIIVEECNKDAVVEELKKQGGYFLTAEEAEKLGKFILRpNGTMNPQIVGKSPQVIANLAGLTVPEDAKVLIGEQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 324 KAIDDSEPFAHEKLSPTLAMYRAKDFADAVEKAVKLVDMGGIGHTSCLYTDQDNQaarVMTFGEKMKTARILINTPTSHG 403
Cdd:TIGR02518 326 NGVGNKNPYSREKLTTILAFYTEENWHEACELSIELLQNEGAGHTLIIHSENKDI---VREFALKKPVSRMLVNTGGSLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1883866115 404 GIGDLYNfsLAPSLTLGCGSWGGNSISENVGPKHLINKKTVA 445
Cdd:TIGR02518 403 GIGATTN--LVPAFTLGCGAVGGSSTSDNITPENLINIRRVA 442
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
450-862 |
3.15e-163 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 480.39 E-value: 3.15e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 450 NMLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGA 529
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 530 ELANAFKPDVIIALGGGSPMDAAKIMWVIYEHPEThfeelalrFMDIrkrIYTFPKMGVKARMVAITTTSGTGSEVTPFA 609
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALLATNPGD--------LEDY---LGIKKVPGPPLPLIAIPTTAGTGSEVTPFA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 610 VVTDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPAS 689
Cdd:COG1454 150 VITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 690 YHEGSkNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrP 769
Cdd:COG1454 230 VADGD-DLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNA---------------P 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 770 QARRRYAEIADHLGLsAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYP 849
Cdd:COG1454 294 AAPERYAEIARALGL-DVGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDL----PELAELALADRCLANNPRPL 368
|
410
....*....|...
gi 1883866115 850 LVAELRQILLASY 862
Cdd:COG1454 369 TEEDIEAILRAAY 381
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
456-863 |
7.10e-161 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 473.99 E-value: 7.10e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 456 LPKSIYFRRGSLpialdEVITD-GHKRALIVTD-RFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELAN 533
Cdd:cd08179 4 VPRDIYFGEGAL-----EYLKTlKGKRAFIVTGgGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 534 AFKPDVIIALGGGSPMDAAKIMWVIYEHPETHFEELALRFmdirkriyTFPKMGVKARMVAITTTSGTGSEVTPFAVVTD 613
Cdd:cd08179 79 EFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALVPF--------PLPELRKKARFIAIPSTSGTGSEVTRASVITD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 614 DTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEG 693
Cdd:cd08179 151 TEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 694 sKNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDnptkqtafsqydrPQARR 773
Cdd:cd08179 231 -KDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKD-------------PEARA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 774 RYaeIADHLGLSApgdrtAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLVAE 853
Cdd:cd08179 297 RY--AALLIGLTD-----EELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAENAMNDACTGTNPRKPTVEE 369
|
410
....*....|
gi 1883866115 854 LRQILLASYY 863
Cdd:cd08179 370 MKELLKAAYY 379
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
14-446 |
2.17e-137 |
|
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: 414.31 E-value: 2.17e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 14 ARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESG-------------MGIVEDKVIKNHFASEYIYNAy 80
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiamMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 81 kDEKTCGVLGEDEaFGTMTIAEPIGLICGIVPTTNPTStAIFKSLISLKTRNGIVFSPHPRAKnATNRAAEIVLRAAVEA 160
Cdd:cd07077 80 -VGHIQDVLLPDN-GETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 161 GAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSS--GKPAIGVGAGNTPVVIDETADVKRAVASILMSK 238
Cdd:cd07077 156 HGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 239 TFDNgVICASEQSVVVVDTVYNAVRERFASHGGYllqgkelkavqgillkngalnaaivgqsavkiaemAGISVPADTKI 318
Cdd:cd07077 236 FFDQ-NACASEQNLYVVDDVLDPLYEEFKLKLVV-----------------------------------EGLKVPQETKP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 319 LIGEVkaIDDSEPFAHEKLSPTLAMYRAKDFADAVEKAVKLVDMGGIGHTSCLYTDQDNqaaRVMTFGEKMKTARILINT 398
Cdd:cd07077 280 LSKET--TPSFDDEALESMTPLECQFRVLDVISAVENAWMIIESGGGPHTRCVYTHKIN---KVDDFVQYIDTASFYPNE 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1883866115 399 PTSHGGiGDLYNFSLAPSLTLGCGSWGGnsisENVGPKHLINKKTVAK 446
Cdd:cd07077 355 SSKKGR-GAFAGKGVERIVTSGMNNIFG----AGVGHDALRPLKRLVR 397
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
457-854 |
1.12e-122 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 375.02 E-value: 1.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPiALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:pfam00465 1 PTRIVFGAGALA-ELGEELKRLGARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIYEHPETHFEELALRfmdirkriytfPKMGVKARMVAITTTSGTGSEVTPFAVVTDDTT 616
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGK-----------PLTKPALPLIAIPTTAGTGSEVTPLAVITDTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 617 GQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGSkN 696
Cdd:pfam00465 149 GEKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGE-D 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 697 PVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrPQARRRYA 776
Cdd:pfam00465 228 LEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNA---------------PAAPEKLA 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1883866115 777 EIADHLGlsapGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:pfam00465 293 QLARALG----EDSDEEAAEEAIEALRELLRELGLPTTLSELGVTEEDL----DALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
457-858 |
3.26e-122 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 374.09 E-value: 3.26e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIYEHPEThfeelALRFMDIRKriytFPKMGVKarMVAITTTSGTGSEVTPFAVVTDDTT 616
Cdd:cd08551 81 ADLVIAVGGGSVLDTAKAIAVLATNGGS-----IRDYEGIGK----VPKPGLP--LIAIPTTAGTGSEVTPNAVITDPET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 617 GQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGSkN 696
Cdd:cd08551 150 GRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGS-D 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 697 PVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPtkqtafsqydrpqarRRYA 776
Cdd:cd08551 229 LEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACP---------------EKYA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 777 EIADHLGLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGAN-PRYPLVAELR 855
Cdd:cd08551 294 EIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDI----PELAEDAMKSGRLLSNnPRPLTEEDIR 369
|
...
gi 1883866115 856 QIL 858
Cdd:cd08551 370 EIY 372
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
453-858 |
8.16e-121 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 370.40 E-value: 8.16e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 453 WHKLPKSIYFRRGSLPiALDEVITdghKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELA 532
Cdd:cd14862 2 WYFSSPKIVFGEDALS-HLEQLSG---KRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 533 NAFKPDVIIALGGGSPMDAAKIMWVIYEHPETHFEEL-ALRFMDIRKriytfpkmgvKARMVAITTTSGTGSEVTPFAVV 611
Cdd:cd14862 78 REFEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDIsPLDLLGLRK----------KAKLIAIPTTSGTGSEATWAIVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 612 TDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYh 691
Cdd:cd14862 148 TDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAY- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 692 EGSKNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDnptkqtafsqydrpqA 771
Cdd:cd14862 227 KDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKV---------------T 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 772 RRRYAEIAdHLGLSAPGDRTAAKieKLLAWLESIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLV 851
Cdd:cd14862 292 DERYDLLK-LLGIEARDEEEALK--KLVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSE 368
|
....*..
gi 1883866115 852 AELRQIL 858
Cdd:cd14862 369 EDLKKLF 375
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
455-859 |
1.42e-114 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 352.57 E-value: 1.42e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 455 KLPKSIYFRRGSLPiALDEVitdGHKRALIVTDRFLFNNGYADQITSVLKAAgVETEVFFEVEADPTLTIVRKGAELANA 534
Cdd:cd08180 2 SLKTKIYSGEDSLE-RLKEL---KGKRVFIVTDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 535 FKPDVIIALGGGSPMDAAKimwviyehpethfeelALRFMdirkrIYTFPKMGVKARMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAK----------------AIIYF-----ALKQKGNIKKPLFIAIPTTSGTGSEVTSFAVITDP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 615 TTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGS 694
Cdd:cd08180 136 EKGIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 695 kNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYnandnptkqtafsqydrpqarrr 774
Cdd:cd08180 216 -DLEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF----------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 775 yaeiadhlglsapgdrtaakiekLLAWLESIKAELGIPKSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:cd08180 272 -----------------------LIAAIRRLNKKLGIPSTLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDL 328
|
....*
gi 1883866115 855 RQILL 859
Cdd:cd08180 329 IELLR 333
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
457-862 |
5.99e-112 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 347.60 E-value: 5.99e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIYEHPEthfeelalrfmDIRKriYTFPKMGVKAR--MVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGG-----------PIRD--YMGPRKVDKPGlpLIAIPTTAGTGSEVTRFTVITDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 615 TTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGs 694
Cdd:cd08194 148 ETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADG- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 695 KNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPTkqtafsqydrpqarrR 774
Cdd:cd08194 227 DDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPE---------------R 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 775 YAEIADHLGLSAPGDRTAAKIEKLLAWLESIKAELGIPkSIREAGVQEADFLAHVDKLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:cd08194 292 YAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEEI 370
|
....*...
gi 1883866115 855 RQILLASY 862
Cdd:cd08194 371 IELYREAW 378
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
456-858 |
2.74e-110 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 343.37 E-value: 2.74e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 456 LPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAF 535
Cdd:cd08176 5 LNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 536 KPDVIIALGGGSPMDAAKIMWVIYEHPethfeelalrFMDIRKRIYTFPKMGVKARMVAITTTSGTGSEVTPFAVVTDDT 615
Cdd:cd08176 85 GADGIIAVGGGSSIDTAKAIGIIVANP----------GADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 616 TGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGsK 695
Cdd:cd08176 155 KKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANP-N 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 696 NPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPTKqtafsqydrpqarrrY 775
Cdd:cd08176 234 NVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEK---------------Y 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 776 AEIADHLGLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLVAELR 855
Cdd:cd08176 299 RDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEED----IEALAEDALNDVCTPGNPREATKEDII 374
|
...
gi 1883866115 856 QIL 858
Cdd:cd08176 375 ALY 377
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
456-857 |
9.99e-104 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 326.01 E-value: 9.99e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 456 LPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAF 535
Cdd:cd08188 5 IPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 536 KPDVIIALGGGSPMDAAKIMWViyehpethfeeLALRFMDIRKR--IYTFPKMGVKarMVAITTTSGTGSEVTPFAVVTD 613
Cdd:cd08188 85 GCDFIISVGGGSAHDCAKAIGI-----------LATNGGEIEDYegVDKSKKPGLP--LIAINTTAGTASEVTRFAVITD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 614 DTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEG 693
Cdd:cd08188 152 EERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 694 sKNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNandnptkqtafsqydRPQARR 773
Cdd:cd08188 232 -KDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFN---------------LPACPE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 774 RYAEIADHLGLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLVAE 853
Cdd:cd08188 296 RFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDF----PLLAENALKDACGPTNPRQATKED 371
|
....
gi 1883866115 854 LRQI 857
Cdd:cd08188 372 VIAI 375
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
465-858 |
4.95e-96 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 305.93 E-value: 4.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 465 GSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFKPDVIIALG 544
Cdd:cd08189 13 GSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIAIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 545 GGSPMDAAKIMWVIYEHPETHFEELAlRFMDIRKRIYTFpkmgvkarmVAITTTSGTGSEVTPFAVVTDDTTGQKYPLAD 624
Cdd:cd08189 93 GGSVIDCAKVIAARAANPKKSVRKLK-GLLKVRKKLPPL---------IAVPTTAGTGSEATIAAVITDPETHEKYAIND 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 625 YALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGSkNPVARERVH 704
Cdd:cd08189 163 PKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGS-DLEARENML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 705 NAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNandnptkqtafsqydRPQARRRYAEIADHLGL 784
Cdd:cd08189 242 LASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFY---------------GPAAEKRLAELADAAGL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1883866115 785 SAPGDRTAAKIEKLLAWLESIKAELGIPKSIreAGVQEADFlahvDKLSEDAFDDqctgANPRYPL-----VAELRQIL 858
Cdd:cd08189 307 GDSGESDSEKAEAFIAAIRELNRRMGIPTTL--EELKEEDI----PEIAKRALKE----ANPLYPVprimdRKDCEELL 375
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
478-862 |
5.93e-94 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 300.22 E-value: 5.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 478 GHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFKPDVIIALGGGSPMDAAKIMWV 557
Cdd:cd14863 26 GCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 558 IYEHPEThfeelALRFMDIRKRIytfPKMGVKarMVAITTTSGTGSEVTPFAVVTDDTTGQKYPLADYALTPDMAIVDAN 637
Cdd:cd14863 106 LLTNPGP-----IIDYALAGPPV---PKPGIP--LIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLAILDPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 638 LVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGsKNPVARERVHNAATIAGIAFANA 717
Cdd:cd14863 176 LTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDG-DNLEARENMLLASNLAGIAFNNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 718 FLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPTKqtafsqydrpqarrrYAEIADHLGLSAPGDRTAAKIEK 797
Cdd:cd14863 255 GTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEK---------------VKKIAKALGVSFPGESDEELGEA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1883866115 798 LLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLVAELRQILLASY 862
Cdd:cd14863 320 VADAIREFMKELGIPSLFEDYGIDKEDL----DKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
7-383 |
1.03e-93 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 301.46 E-value: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 7 EELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEyiynaykdeKTC 86
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAE---------KTP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 87 GVlgED---EAF---GTMTIAE--PIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAV 158
Cdd:cd07121 75 GT--EDlttTAWsgdNGLTLVEyaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 159 EAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSK 238
Cdd:cd07121 153 EAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 239 TFDNGVICASEQSVVVVDTVYNAVRERFASHGGYLLQGKELKAVQGILLKNG---ALNAAIVGQSAVKIAEMAGISVPAD 315
Cdd:cd07121 233 SFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLLTNkgaTPNKKWVGKDASKILKAAGIEVPAD 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1883866115 316 TKILIGEVkaiDDSEPFA-HEKLSPTLAMYRAKDFADAVEKAVKLvdMGGIGHTSCLYT---DQDNQAARVM 383
Cdd:cd07121 313 IRLIIVET---DKDHPFVvEEQMMPILPVVRVKNFDEAIELAVEL--EHGNRHTAIIHSknvENLTKMARAM 379
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
7-383 |
1.95e-93 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 301.82 E-value: 1.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 7 EELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEyiynaykdeKTC 86
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKNVAAAE---------KTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 87 GVlgED---EAF---GTMTIAE--PIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAV 158
Cdd:PRK15398 107 GV--EDlttEALtgdNGLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 159 EAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSK 238
Cdd:PRK15398 185 AAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 239 TFDNGVICASEQSVVVVDTVYNAVRERFASHGGYLLQGKELKAVQGILLKNG-ALNAAIVGQSAVKIAEMAGISVPADTK 317
Cdd:PRK15398 265 SFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKNGgTVNKKWVGKDAAKILEAAGINVPKDTR 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 318 ILIGEVkaiDDSEPFA-HEKLSPTLAMYRAKDFADAVEKAVKLvdMGGIGHTSCLYT---DQDNQAARVM 383
Cdd:PRK15398 345 LLIVET---DANHPFVvTELMMPVLPVVRVKDVDEAIALAVKL--EHGNRHTAIMHSrnvDNLNKMARAI 409
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
457-862 |
6.52e-93 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 297.92 E-value: 6.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:cd14865 6 PTKIVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIYEHPETHFEELALRFMDIRKRIytfPkmgvkarMVAITTTSGTGSEVTPFAVVTDDTT 616
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANRLTRPLK---P-------LIAIPTTAGTGSEVTLVAVIKDEEK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 617 GQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGsKN 696
Cdd:cd14865 156 KVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNG-KD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 697 PVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrPQARRRYA 776
Cdd:cd14865 235 LEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNL---------------DAAAERYA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 777 EIADHLGLSA--PGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFLAhvdkLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:cd14865 300 ELALALAYGVtpAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEA----IAELALNDGAILFNPREVDPEDI 375
|
....*...
gi 1883866115 855 RQILLASY 862
Cdd:cd14865 376 LAILEAAY 383
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
456-857 |
3.35e-89 |
|
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase. [Energy metabolism, Sugars]
Pssm-ID: 131686 [Multi-domain] Cd Length: 379 Bit Score: 287.80 E-value: 3.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 456 LPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAF 535
Cdd:TIGR02638 6 LNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAFKAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 536 KPDVIIALGGGSPMDAAKIMWVIYEHPEthfeelalrFMDIRKRIYTFPKMGVKARMVAITTTSGTGSEVTPFAVVTDDT 615
Cdd:TIGR02638 86 GADYLIAIGGGSPIDTAKAIGIISNNPE---------FADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 616 TGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYhEGSK 695
Cdd:TIGR02638 157 NKRKFVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAV-EGGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 696 NPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrPQARRRY 775
Cdd:TIGR02638 236 DLEAREQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNA---------------EFTGEKY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 776 AEIADHLGLSAPG--DRTAAKiekllAWLESIKA---ELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPL 850
Cdd:TIGR02638 301 REIAKAMGVKTEGmsDEEARD-----AAVEAVKTlskRVGIPEGLSELGVKEED----IPALAEAALADVCTGGNPRETT 371
|
....*..
gi 1883866115 851 VAELRQI 857
Cdd:TIGR02638 372 VEEIEEL 378
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
460-861 |
1.61e-86 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 280.55 E-value: 1.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 460 IYFRRGS---LPIALDEvitDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:cd14861 6 IRFGAGAiaeLPEELKA---LGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIYEHPE--THFEELALRFMDIRKRIytfpkmgvkARMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd14861 83 CDGIIALGGGSAIDAAKAIALMATHPGplWDYEDGEGGPAAITPAV---------PPLIAIPTTAGTGSEVGRAAVITDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 615 TTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGS 694
Cdd:cd14861 154 DTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 695 kNPVARERVHNAATIAGIAFANAfLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNandnptkqtafsqydRPQARRR 774
Cdd:cd14861 234 -DLEARGEMMMAALMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFN---------------RPAVEDK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 775 YAEIADHLGLSAPGDrtaakiEKLLAWLESIKAELGIPKSIREAGVQEadflAHVDKLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:cd14861 297 LARLARALGLGLGGF------DDFIAWVEDLNERLGLPATLSELGVTE----DDLDELAELALADPCHATNPRPVTAEDY 366
|
....*..
gi 1883866115 855 RQILLAS 861
Cdd:cd14861 367 RALLREA 373
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
456-858 |
2.22e-85 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 277.46 E-value: 2.22e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 456 LPKSIYFRRGSLPiALDEVITDGHKRALIVTDR-FLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANA 534
Cdd:cd08185 3 QPTRILFGAGKLN-ELGEEALRPGKKALIVTGKgSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 535 FKPDVIIALGGGSPMDAAKIMWVIYEHPETHFEelalrfmdirkriYTFPKMGVKAR------MVAITTTSGTGSEVTPF 608
Cdd:cd08185 82 EGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWD-------------YIFGGTGKGPPpekalpIIAIPTTAGTGSEVDPW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 609 AVVTDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPA 688
Cdd:cd08185 149 AVITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 689 SYHEGSkNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQF-HIPHGLANALMICNVIRYNANDNPTKqtafsqyd 767
Cdd:cd08185 229 AVKDGS-DLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEK-------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 768 rpqarrrYAEIADhlgLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAFD--DQCTGAN 845
Cdd:cd08185 300 -------FAFVAR---AEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDI----PWLAENAMEtmGGLFANN 365
|
410
....*....|...
gi 1883866115 846 PRYPLVAELRQIL 858
Cdd:cd08185 366 PVELTEEDIVEIY 378
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
457-836 |
1.32e-84 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 275.55 E-value: 1.32e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIYEHPEThfeeLAlrfmdirkRIYtfpkmGV-KAR-----MVAITTTSGTGSEVTPFAV 610
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQP----LD--------DIY-----GVgKATgprlpLILVPTTAGTGSEVTPISI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 611 VTDDTTgQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVS-VLASEFSDGQALQALKLLKAYLPAS 689
Cdd:cd08193 147 VTTGET-EKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 690 YHEGSkNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrP 769
Cdd:cd08193 226 VEDGS-DLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNL---------------P 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1883866115 770 QARRRYAEIADHLGLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADflahVDKLSEDA 836
Cdd:cd08193 290 AAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEED----LPMLAEDA 352
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
460-857 |
3.05e-83 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 271.72 E-value: 3.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 460 IYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFKPDV 539
Cdd:cd17814 7 FIFGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 540 IIALGGGSPMDAAKIMWVIYEHPethfeelalrfMDIRKRIytfpkmGV-KAR-----MVAITTTSGTGSEVTPFAVVTD 613
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIVVSNG-----------GHILDYE------GVdKVRrplppLICIPTTAGSSADVSQFAIITD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 614 DTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEg 693
Cdd:cd17814 150 TERRVKMAIISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVAD- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 694 SKNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrPQARR 773
Cdd:cd17814 229 PDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNF---------------PAAPE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 774 RYAEIADHLGLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLVAE 853
Cdd:cd17814 294 RYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEED----IPELAKRAMKDPCLVTNPRRPTRED 369
|
....
gi 1883866115 854 LRQI 857
Cdd:cd17814 370 IEEI 373
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
455-858 |
3.97e-82 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 268.68 E-value: 3.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 455 KLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKaaGVETEVFFEVEADPTLTIVRKGAELANA 534
Cdd:cd08196 4 YQPVKIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLK--GRIVAVFSDVEPNPTVENVDKCARLARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 535 FKPDVIIALGGGSPMDAAKIMWVIYEHPEThfeelalrFMDIRKRIYTFPKMGVKarMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08196 82 NGADFVIAIGGGSVLDTAKAAACLAKTDGS--------IEDYLEGKKKIPKKGLP--LIAIPTTAGTGSEVTPVAVLTDK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 615 TTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGS 694
Cdd:cd08196 152 EKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 695 kNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPTKQTAFSQYdrpqarrr 774
Cdd:cd08196 232 -DKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQ-------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 775 yaeiadhLGLSAPGDrTAAKIEKLlawlesiKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:cd08196 303 -------LGFKDAEE-LADKIEEL-------KKRIGLRTRLSELGITEED----LEEIVEESFHPNRANNNPVEVTKEDL 363
|
....
gi 1883866115 855 RQIL 858
Cdd:cd08196 364 EKLL 367
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
461-857 |
8.98e-80 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 262.62 E-value: 8.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 461 YFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFKPDVI 540
Cdd:PRK10624 12 YFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 541 IALGGGSPMDAAKIMWVIYEHPEthfeelalrFMDIRKRIYTFPKMGVKARMVAITTTSGTGSEVTPFAVVTDDTTGQKY 620
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGIISNNPE---------FADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 621 PLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEgskNPVAR 700
Cdd:PRK10624 163 VCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAG---DKEAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 701 ERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrPQARRRYAEIAD 780
Cdd:PRK10624 240 EGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA---------------DFTGEKYRDIAR 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1883866115 781 HLGLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLVAELRQI 857
Cdd:PRK10624 305 AMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEED----IPALAQAAFDDVCTGGNPREATLEDIVEL 377
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
457-858 |
1.03e-78 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 259.74 E-value: 1.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPIALDEVITDGhKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFfEVEADPTLTIVRKGAELANAFK 536
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALF-SVSGEPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIYEHPEThfeelALRFMDI--RKRIYTFPKmgvkARMVAITTTSGTGSEVTPFAVVTDD 614
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGS-----VLDYLEVvgKGRPLTEPP----LPFIAIPTTAGTGSEVTKNAVLSSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 615 TTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGS 694
Cdd:cd08183 150 EHGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 695 kNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkQTAFSQYDRPQARRR 774
Cdd:cd08183 230 -DLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANL------RALREREPDSPALAR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 775 YAEIADHLGLSApgdrtAAKIEKLLAWLESIKAELGIPkSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:cd08183 303 YRELAGILTGDP-----DAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDF----PEIVEKARGSSSMKGNPIELSDEEL 372
|
....
gi 1883866115 855 RQIL 858
Cdd:cd08183 373 LEIL 376
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
456-862 |
2.35e-76 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 254.08 E-value: 2.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 456 LPKSIYFRRGSLPiALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAF 535
Cdd:cd08191 3 SPSRLLFGPGARR-ALGRVAARLGSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 536 KPDVIIALGGGSPMDAAKIMWVIYEH---PETHFEELALrfmdirkriytfPKMGVKarMVAITTTSGTGSEVTPFAVVT 612
Cdd:cd08191 82 DPDVVIGLGGGSNMDLAKVVALLLAHggdPRDYYGEDRV------------PGPVLP--LIAVPTTAGTGSEVTPVAVLT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 613 DDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEF---------------SDGQALQ 677
Cdd:cd08191 148 DPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPPFprldpdpvyvgknplTDLLALE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 678 ALKLLKAYLPASYHEGSKNPvARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNandnp 757
Cdd:cd08191 228 AIRLIGRHLPRAVRDGDDLE-ARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFN----- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 758 tkqtafsqydRPQARRRYAEIADHLGLsAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAF 837
Cdd:cd08191 302 ----------RPARAAELAEIARALGV-TTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADL----PGLAEKAL 366
|
410 420
....*....|....*....|....*.
gi 1883866115 838 DDQ-CTGANPRYPLVAELRQILLASY 862
Cdd:cd08191 367 SVTrLIANNPRPPTEEDLLRILRAAF 392
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
460-858 |
6.62e-71 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 238.28 E-value: 6.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 460 IYFRRGSLPiALDEVITD-GHKRALIVTDRFLFNNGYADQITSVLkAAGVETEVFFEVEADPTLTIVRKGAELANAFKPD 538
Cdd:cd08182 4 IIFGPGALA-ELKDLLGGlGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 539 VIIALGGGSPMDAAKIMWVIYEHPETHFEELAlrfmdIRKRIYTFPKMgvkaRMVAITTTSGTGSEVTPFAVVTDDTTGQ 618
Cdd:cd08182 82 VIIAVGGGSVIDTAKAIAALLGSPGENLLLLR-----TGEKAPEENAL----PLIAIPTTAGTGSEVTPFATIWDEAEGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 619 KYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPAsYHEGSKNPV 698
Cdd:cd08182 153 KYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPL-LLENLPNLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 699 ARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafSQYDRPQARRRYAEI 778
Cdd:cd08182 232 AREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNA----------GADDECDDDPRGREI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 779 ADHLGlsapgdrtAAKIEKLLAWLESIKAELGIPKSIREAGVQEADflahVDKLSEDAFDDQCTGANPRYPLVAELRQIL 858
Cdd:cd08182 302 LLALG--------ASDPAEAAERLRALLESLGLPTRLSEYGVTAED----LEALAASVNTPERLKNNPVRLSEEDLLRLL 369
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
459-862 |
1.48e-66 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 227.81 E-value: 1.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 459 SIYFRRGslpiALDEVITD----GHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANA 534
Cdd:cd08190 3 NIRFGPG----ATRELGMDlkrlGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 535 FKPDVIIALGGGSPMDAAKIMWVIYEHPEthfeelalRFMDirkriYTFPKMGVKAR-------MVAITTTSGTGSEVTP 607
Cdd:cd08190 79 GDFDAFVAVGGGSVIDTAKAANLYATHPG--------DFLD-----YVNAPIGKGKPvpgplkpLIAIPTTAGTGSETTG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 608 FAVVTDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVL------------------ASE 669
Cdd:cd08190 146 VAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 670 FSDGQALQALKLLKAYLPASYHEGSkNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQ-------------FHIP 736
Cdd:cd08190 226 ISDVWAEKAIELIGKYLRRAVNDGD-DLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 737 HGLANALMICNVIRYNANDNPtkqtafsqydrpqarRRYAEIADHLGLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIR 816
Cdd:cd08190 305 HGLSVALTAPAVFRFTAPACP---------------ERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLS 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1883866115 817 EAGVQEADflahVDKLSEDAFDDQ-CTGANPRYPLVAELRQILLASY 862
Cdd:cd08190 370 ALGYSEDD----IPALVEGTLPQQrLLKLNPRPVTEEDLEEIFEDAL 412
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
455-759 |
5.52e-62 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 213.60 E-value: 5.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 455 KLPKSIYFRRGSLPIALDEVITDGhKRALIVTDRF-LFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELAN 533
Cdd:cd08181 2 YMPTKVYFGKNCVEKHADELAALG-KKALIVTGKHsAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 534 AFKPDVIIALGGGSPMDAAKIMWVIYEHPEtHFEELalrfmdirkriYTFPKMGVKARMVAITTTSGTGSEVTPFAVVTD 613
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKD-GDEDL-----------FQNGKYNPPLPIVAIPTTAGTGSEVTPYSILTD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 614 DTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPAsYHEG 693
Cdd:cd08181 149 HEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPN-LLGD 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883866115 694 SKNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPTK 759
Cdd:cd08181 228 ELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEK 293
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
465-861 |
1.02e-59 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 208.27 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 465 GSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFKPDVIIALG 544
Cdd:PRK09860 17 DSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 545 GGSPMDAAKIMWVIyehpethfeelALRFMDIRKriYTFPKMGVKAR--MVAITTTSGTGSEVTPFAVVTDDTTGQKYPL 622
Cdd:PRK09860 97 GGSPHDCAKGIALV-----------AANGGDIRD--YEGVDRSAKPQlpMIAINTTAGTASEMTRFCIITDEARHIKMAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 623 ADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGSkNPVARER 702
Cdd:PRK09860 164 VDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGS-NAKAREA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 703 VHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANdnptkqtafsqydrpQARRRYAEIADHL 782
Cdd:PRK09860 243 MAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK---------------VAAARLRDCAAAM 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1883866115 783 GLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLVAELRQILLAS 861
Cdd:PRK09860 308 GVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDF----AVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
465-858 |
3.92e-55 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 196.02 E-value: 3.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 465 GSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFKPDVIIALG 544
Cdd:PRK15454 35 GAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 545 GGSPMDAAKIMWVIYEHPETHFEELALRfMDIRKRIytfpkmgvkaRMVAITTTSGTGSEVTPFAVVTDDTTGQKYPLAD 624
Cdd:PRK15454 115 GGSVLDAAKAVALLVTNPDSTLAEMSET-SVLQPRL----------PLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 625 YALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGsKNPVARERVH 704
Cdd:PRK15454 184 ASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYG-HDLAARESML 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 705 NAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNandnptkqtafsqydRPQARRRYAEIADHLGL 784
Cdd:PRK15454 263 LASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFN---------------RMVCRERFSQIGRALRT 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883866115 785 SAPGDRTAakieklLAWLESIKAELGIPKSIREAGVQEadflAHVDKLSEDAFDDQCTGANPRyplVAELRQIL 858
Cdd:PRK15454 328 KKSDDRDA------INAVSELIAEVGIGKRLGDVGATS----AHYGAWAQAALEDICLRSNPR---TASLEQIV 388
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
14-446 |
7.16e-55 |
|
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: 194.37 E-value: 7.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 14 ARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESG--MGIVEDKVIKNHFASEYIYNAYKDEKTCGVLGE 91
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 92 DEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVlraaVEAGAPPDIIGWID 171
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELL----QEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 172 EPTVDLSNRLMHHPDINLILATGGPGMVKAAY----SSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICA 247
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMkaaaENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 248 SEQSVVVVDTVYNAVRERFashggyllqgkelkavqgillkngalnaaivgqsavkiaemAGISVPADTKIligevkaid 327
Cdd:cd06534 237 AASRLLVHESIYDEFVEKL-----------------------------------------VTVLVDVDPDM--------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 328 dsePFAHEKLSPTLAMYRAkdfADAVEKAVKLVDMGGIGHTSCLYTDQDNqaaRVMTFGEKMKTARILINTPTSHGGigd 407
Cdd:cd06534 267 ---PIAQEEIFGPVLPVIR---FKDEEEAIALANDTEYGLTAGVFTRDLN---RALRVAERLRAGTVYINDSSIGVG--- 334
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1883866115 408 lynfslaPSLTLG--CGSWGGNSiSENVGPKHLINKKTVAK 446
Cdd:cd06534 335 -------PEAPFGgvKNSGIGRE-GGPYGLEEYTRTKTVVI 367
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
457-858 |
5.39e-48 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 175.13 E-value: 5.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFL-FNNGYADQITSVLKAAGVETevFFEVEADPTLTIVRKGAELANAF 535
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLGASRVFIVTSKSLaTKTDVIKRLEEALGDRHVGV--FSGVRQHTPREDVLEAARAVREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 536 KPDVIIALGGGSPMDAAKIMWVIYEHPETHFEELALRFMDIRKRIYtfpKMGVKARMVAITTT-SgtGSEVTPFAVVTDD 614
Cdd:cd08192 79 GADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEDGKRIDPN---VTGPTLPHIAIPTTlS--GAEFTAGAGATDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 615 TTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPAsYHEGS 694
Cdd:cd08192 154 DTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPR-SKADP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 695 KNPVARERVHNAATIAGIAFANAF-LGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPTKqtafsqydrpQARR 773
Cdd:cd08192 233 EDLEARLKCQLAAWLSLFGLGSGVpMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAER----------QRLI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 774 RYAEIADHLGLSAPGDRTAAKIEKLLawlesikAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPRYPLV-A 852
Cdd:cd08192 303 ARALGLVTGGLGREAADAADAIDALI-------RELGLPRTLRDVGVGRDQL----EKIAENALTDVWCRTNPRPITDkD 371
|
....*.
gi 1883866115 853 ELRQIL 858
Cdd:cd08192 372 DVLEIL 377
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
457-860 |
2.53e-45 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 167.79 E-value: 2.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGS---LPIALDEVitdGHKRALIVTDRFLfnNGYADQITSVLKAAGVE-TEVFFEVEADPTLTIVRKGAELA 532
Cdd:cd14866 5 PLRLFSGRGAlarLGRELDRL---GARRALVVCGSSV--GANPDLMDPVRAALGDRlAGVFDGVRPHSPLETVEAAAEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 533 NAFKPDVIIALGGGSPMDAAKIMWVIYEHPEThFEELALRFMDirKRIYTFPK-MGVKARMVAITTTSGTGSEVTPFAVv 611
Cdd:cd14866 80 READADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAE--DGLMVSPRlDAPKLPIFVVPTTPTTADVKAGSAV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 612 TDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASyh 691
Cdd:cd14866 156 TDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRL-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 692 EGSKNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrPQA 771
Cdd:cd14866 234 ADDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNA---------------PAT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 772 RRRYAEIADHLGLSAPGDRTAAkiEKLLAWLESIKAELGIPKSIREAGVQEADFlahvDKLSEDAFDDQCTGANPR-YPL 850
Cdd:cd14866 299 DGRLDRLAEALGVADAGDEASA--AAVVDAVEALLDALGVPTRLRDLGVSREDL----PAIAEAAMDDWFMDNNPRpVPT 372
|
410
....*....|
gi 1883866115 851 VAELRQILLA 860
Cdd:cd14866 373 AEELEALLEA 382
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
455-862 |
7.07e-43 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 160.54 E-value: 7.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 455 KLPKSIYFRRGSLPIALDEVITDGhKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANA 534
Cdd:cd14864 2 KIPPNIVFGADSLERIGEEVKEYG-SRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 535 FKPDVIIALGGGSPMDAAKIMWVIYEhpETHFeelALRFMDIRKriytfpkmgVKAR---MVAITTTSGTGSEVTPFAVV 611
Cdd:cd14864 81 AGADGIIAVGGGKVLDTAKAVAILAN--NDGG---AYDFLEGAK---------PKKKplpLIAVPTTPRSGFEFSDRFPV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 612 TDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPaSYH 691
Cdd:cd14864 147 VDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLD-GAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 692 EGSKNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrPQA 771
Cdd:cd14864 226 ADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAA---------------TSA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 772 RRRYAEIADHLGLSAPGDRTAAKIEKLLAWLESIKAELGIPKSIREAGVQeadflAHVDKLSEDAFDDQCTGANPRYPLV 851
Cdd:cd14864 291 PDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDLA-----SSLEQLAAIAEDAPKLNGLPRSMSS 365
|
410
....*....|.
gi 1883866115 852 AELRQILLASY 862
Cdd:cd14864 366 DDIFDILKAAF 376
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
459-870 |
1.06e-42 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 160.12 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 459 SIYFRRGSLPiALDEVITD-GHKRALIVTDRFLFN-NGYADQITSVLKAAGVETEVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:cd08186 3 TLYFGVGAIA-KIKDILKDlGIDKVIIVTGRSSYKkSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIYEHPETHFEELalrfmdirkriYTFPKMGVKAR-MVAITTTSGTGSEVTPFAVVTDDT 615
Cdd:cd08186 82 ADAVIAIGGGSPIDTAKSVAVLLAYGGKTARDL-----------YGFRFAPERALpLVAINLTHGTGSEVDRFAVATIPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 616 TGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEgSK 695
Cdd:cd08186 151 KGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALAN-PK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 696 NPVARERVHNAATIAGIAFANAFLGVCHSMAHKL-GSQFHIPHGLANALMICNVIRYNANDNPtkqtafsqydrpqarrr 774
Cdd:cd08186 230 DLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLsGLKPELPHGLGLALLGPAVVKYIYKAVP----------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 775 yAEIADHLGLSAPGDRT----AAKIEKLL-AWLESIkaelGIPKSIREAGVQEADflahVDKLSEDAFddqctgANPRYP 849
Cdd:cd08186 293 -ETLADILRPIVPGLKGtpdeAEKAARGVeEFLFSV----GFTEKLSDYGFTEDD----VDRLVELAF------TTPSLD 357
|
410 420
....*....|....*....|....*..
gi 1883866115 850 LVAEL------RQILLasyygDIYREA 870
Cdd:cd08186 358 LLLSLapvevtEEVVR-----EIYEES 379
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
480-824 |
1.60e-36 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 141.97 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 480 KRALIVTDRFLFNNGYADQitsVLKAAGVETEVFFEVEadPTLTIVRKGAELANAFKPDVIIALGGGSPMDAAKIMWVIY 559
Cdd:cd14860 27 KDDLVLTNEYIYEPYFEPL---NLDCAVIFQEKYGTGE--PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 560 EHPethFEELALRFMDIRKriytfpkmgvKARMVAITTTSGTGSEVTPFAVVTDDTTGQKYPLADYALTPDMAIVDANLV 639
Cdd:cd14860 102 ISP---VLDLFDGKIPLIK----------EKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 640 MDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKL-LKAYLP-ASYHEGSKNPVARERVhNAATIAGIAFANA 717
Cdd:cd14860 169 KGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMiLEGYQEiAEKGEEARFPLLGDFL-IASNYAGIAFGNA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 718 FLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPT----KQTAFsqydrpqarrryaeIADHLGLSApgDRTAA 793
Cdd:cd14860 248 GCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPDgeikKLNEF--------------LAKILGCDE--EDVYD 311
|
330 340 350
....*....|....*....|....*....|..
gi 1883866115 794 KIEKLLAWLesikaelgIP-KSIREAGVQEAD 824
Cdd:cd14860 312 ELEELLNKI--------LPkKPLHEYGMKEEE 335
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
457-862 |
6.00e-31 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 124.54 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPIALDEVITDGHKRALIVTDRFlfNNGYADQITSVLKAAGVEteVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGARRALVLSTPR--QRALAERVAALLGDRVAG--VFDGAVMHVPVEVAERALAAAREAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKImwviyehpethfeeLALRfmdirkriytfpkmgVKARMVAITTTSgTGSEVTPFAVVTDDtt 616
Cdd:cd08177 77 ADGLVAIGGGSAIGLAKA--------------IALR---------------TGLPIVAVPTTY-AGSEMTPIWGETED-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 617 GQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKLLKAYLPASYHEGSkN 696
Cdd:cd08177 125 GVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPS-D 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 697 PVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNAndnptkqtafsqydrPQARRRYA 776
Cdd:cd08177 204 LEARSDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNA---------------PAAPDAMA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 777 EIADHLGlsapGDRTAAKIEKLLawlesikAELGIPKSIREAGVQEADflahVDKLSEDAFDDQctGANPRyPLVAE-LR 855
Cdd:cd08177 269 RLARALG----GGDAAGGLYDLA-------RRLGAPTSLRDLGMPEDD----IDRAADLALANP--YPNPR-PVERDaLR 330
|
....*..
gi 1883866115 856 QILLASY 862
Cdd:cd08177 331 ALLERAW 337
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
457-766 |
7.64e-26 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 107.83 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 457 PKSIYFRRGSLPiALDEVITDGHKRALIVTDRFLfNNGYADQITSVLKAaGVETEVFFEVEADPTLTIVRKGAELANAFK 536
Cdd:cd07766 1 PTRIVFGEGAIA-KLGEIKRRGFDRALVVSDEGV-VKGVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 PDVIIALGGGSPMDAAKIMWVIyehpethfeelalrfmdirkriytfpkMGVKARMVAITTTSGTGSEVTPFAVVTDDTT 616
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAAL---------------------------LNRGIPFIIVPTTASTDSEVSPKSVITDKGG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 617 GQKYplADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEayvsvlasefsdgqalqalkllkaylpasyhegskn 696
Cdd:cd07766 131 KNKQ--VGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------ 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1883866115 697 pvaRERVHNAATIAGIAFANA-FLGVCHSMAHKLGSQFHIPHGLANALMICNVIRYNANDNPTKQTAFSQY 766
Cdd:cd07766 173 ---LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAV 240
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
462-741 |
1.43e-23 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 103.12 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 462 FRRGS---LPIALDEVITDGHKRALIVTDRFLFNNGYADQitsvLKAAGVETEVFFEVEADPTLTIVRkgaELANAFK-- 536
Cdd:cd08184 6 FGRGSfdqLGELLAERRKSNNDYVVFFIDDVFKGKPLLDR----LPLQNGDLLIFVDTTDEPKTDQID---ALRAQIRae 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 537 ----PDVIIALGGGSPMDAAKIMWVIYEHPE--THFEELALrfmdIRKR-IYTfpkmgvkarmVAITTTSGTGSEVTPFA 609
Cdd:cd08184 79 ndklPAAVVGIGGGSTMDIAKAVSNMLTNPGsaADYQGWDL----VKNPgIYK----------IGVPTLSGTGAEASRTA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 610 VVTDdtTGQKYPL-ADYALtPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDGQALQALKL-LKAYLp 687
Cdd:cd08184 145 VLTG--PEKKLGInSDYTV-FDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELcRDVFL- 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1883866115 688 asyHEGSKNPVARERVHNAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLAN 741
Cdd:cd08184 221 ---SDDMMSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVAN 271
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
49-404 |
2.54e-20 |
|
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: 94.58 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 49 LAKMAVAESGMGIVE-----DKVIKN-HFASEYIYNAYKDEKTCGVLGEDeafgTMTIAEPIGLICGIVPTTNPTSTAIF 122
Cdd:cd07078 40 LAALETLETGKPIEEalgevARAADTfRYYAGLARRLHGEVIPSPDPGEL----AIVRREPLGVVGAITPWNFPLLLAAW 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 123 KSLISLKTRNGIVFSPHPRAKNATNRAAEIvlraAVEAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPG----M 198
Cdd:cd07078 116 KLAPALAAGNTVVLKPSELTPLTALLLAEL----LAEAGLPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAvgkaI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 199 VKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFAshggyllqgke 278
Cdd:cd07078 192 MRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLV----------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 279 lKAVQGILLKNGALNAAIVG-----------QSAVKIAEMAGISVPADTKILIGEVKA---------IDDSEPFAHEKL- 337
Cdd:cd07078 261 -ERVKALKVGNPLDPDTDMGplisaaqldrvLAYIEDAKAEGAKLLCGGKRLEGGKGYfvpptvltdVDPDMPIAQEEIf 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1883866115 338 SPTLAMYRAKDFADAVEKAVKLVDmggiGHTSCLYTdqdNQAARVMTFGEKMKTARILINTPTSHGG 404
Cdd:cd07078 340 GPVLPVIPFKDEEEAIELANDTEY----GLAAGVFT---RDLERALRVAERLEAGTVWINDYSVGAE 399
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
7-407 |
4.44e-20 |
|
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: 94.14 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 7 EELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVE-----DKVIknHFASEYIYNAYK 81
Cdd:pfam00171 29 EDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEargevDRAI--DVLRYYAGLARR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 82 DEKTcgVLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRaknaTNRAAEIVLRAAVEAG 161
Cdd:pfam00171 107 LDGE--TLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSEL----TPLTALLLAELFEEAG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 162 APPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPG----MVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMS 237
Cdd:pfam00171 181 LPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvgrhIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 238 KTFDNGVICASEQSVVVVDTVYNAVRERFAshggyllqgkelKAVQGILLKNGALNAAIVG-----------QSAVKIAE 306
Cdd:pfam00171 261 AFGNAGQVCTATSRLLVHESIYDEFVEKLV------------EAAKKLKVGDPLDPDTDMGpliskaqlervLKYVEDAK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 307 MAGISVPADTK------------ILIGeVK---AIDDSEPFAheklsPTLAMYRAKDFADAVEKA--VKLvdmggiGHTS 369
Cdd:pfam00171 329 EEGAKLLTGGEagldngyfveptVLAN-VTpdmRIAQEEIFG-----PVLSVIRFKDEEEAIEIAndTEY------GLAA 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1883866115 370 CLYTDQDNqaaRVMTFGEKMKTARILINTPT-------SHGGIGD 407
Cdd:pfam00171 397 GVFTSDLE---RALRVARRLEAGMVWINDYTtgdadglPFGGFKQ 438
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
97-407 |
9.23e-19 |
|
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: 90.19 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 97 TMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRaknaTNRAAEIVLRAAVEAGAPPDIIGWIDEPTVD 176
Cdd:COG1012 135 AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQ----TPLSALLLAELLEEAGLPAGVLNVVTGDGSE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 177 LSNRLMHHPDINLILATGGPG----MVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSV 252
Cdd:COG1012 211 VGAALVAHPDVDKISFTGSTAvgrrIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 253 VVVDTVYNAVRERFAshggyllqgkelKAVQGILLKNGALNAAIVG-----------QSAVKIAEMAGISVPADTKILIG 321
Cdd:COG1012 291 LVHESIYDEFVERLV------------AAAKALKVGDPLDPGTDMGpliseaqlervLAYIEDAVAEGAELLTGGRRPDG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 322 E---------VKAIDDSEPFAHEKL-SPTLAMYRAKDFADAVEkavkLVDMGGIGHTSCLYTdQDnqAARVMTFGEKMKT 391
Cdd:COG1012 359 EggyfveptvLADVTPDMRIAREEIfGPVLSVIPFDDEEEAIA----LANDTEYGLAASVFT-RD--LARARRVARRLEA 431
|
330 340
....*....|....*....|...
gi 1883866115 392 ARILINTPTS-------HGGIGD 407
Cdd:COG1012 432 GMVWINDGTTgavpqapFGGVKQ 454
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
5-387 |
2.01e-16 |
|
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: 83.08 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 5 SIEELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMgIVEDKVIKNHFASEYI-Y---NAY 80
Cdd:cd07088 33 TAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGK-TLSLARVEVEFTADYIdYmaeWAR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 81 KDEKTcgVLGEDEAFGTMTIA-EPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHprakNATNRAAEIVLRAAVE 159
Cdd:cd07088 112 RIEGE--IIPSDRPNENIFIFkVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPS----EETPLNALEFAELVDE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 160 AGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNTPVVIDETADVKRAVASI 234
Cdd:cd07088 186 AGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEagqkiMEAAAENITKVSLELG-GKAPAIVMKDADLDLAVKAI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 235 LMSKTFDNGVICASEQSVVVVDTVYNAVRERFASHggyllqgkeLKAVQ-GILLKNGALNAAIVGQSAV-KIAEMAGISV 312
Cdd:cd07088 265 VDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEK---------MKAVKvGDPFDAATDMGPLVNEAALdKVEEMVERAV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 313 PADTKILIG------------EVKAID----DSEPFAHEKLSPTLAMYRAKDFADAVEKAvklvDMGGIGHTSCLYTDQD 376
Cdd:cd07088 336 EAGATLLTGgkrpegekgyfyEPTVLTnvrqDMEIVQEEIFGPVLPVVKFSSLDEAIELA----NDSEYGLTSYIYTENL 411
|
410
....*....|....
gi 1883866115 377 NQAARVMT---FGE 387
Cdd:cd07088 412 NTAMRATNeleFGE 425
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
7-356 |
1.39e-14 |
|
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: 77.09 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 7 EELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKV--------IKNhfASEYIYN 78
Cdd:cd07094 21 ADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVevdraidtLRL--AAEEAER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 79 AYKDEKTCGVLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVlraaV 158
Cdd:cd07094 99 IRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKIL----V 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 159 EAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPGM---VKAAYSSGKPAIGVGaGNTPVVIDETADVKRAVASIL 235
Cdd:cd07094 175 EAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVgeaLRANAGGKRIALELG-GNAPVIVDRDADLDAAIEALA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 236 MSKTFDNGVICASEQSVVVVDTVYNAVRERFASHGGYLLQGKELKAVQGIllknGALnaaIVGQSAVKIAEMAGISVPAD 315
Cdd:cd07094 254 KGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDV----GPL---ISEEAAERVERWVEEAVEAG 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1883866115 316 TKILIG----------EVKAID--DSEPFAHEKLSPTLAMYRAKDFADAVEKA 356
Cdd:cd07094 327 ARLLCGgerdgalfkpTVLEDVprDTKLSTEETFGPVVPIIRYDDFEEAIRIA 379
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
99-354 |
1.40e-14 |
|
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: 77.01 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 99 TIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRaknaTNRAAEIVLRAAVEAGAPPDIIGW-IDEPTvDL 177
Cdd:cd07146 116 TLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK----TPLSAIYLADLLYEAGLPPDMLSVvTGEPG-EI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 178 SNRLMHHPDINLILATGGPGMVK--AAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVV 255
Cdd:cd07146 191 GDELITHPDVDLVTFTGGVAVGKaiAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 256 DTVYNAVRERFASHGGYLLQGKELK--AVQGILLKNGalnAAIVGQSAVKIAEMAGisvpadTKILIGEVK--------A 325
Cdd:cd07146 271 ESVADEFVDLLVEKSAALVVGDPMDpaTDMGTVIDEE---AAIQIENRVEEAIAQG------ARVLLGNQRqgalyaptV 341
|
250 260 270
....*....|....*....|....*....|...
gi 1883866115 326 ID----DSEPFAHEKLSPTLAMYRAKDFADAVE 354
Cdd:cd07146 342 LDhvppDAELVTEETFGPVAPVIRVKDLDEAIA 374
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
5-407 |
1.22e-13 |
|
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: 74.29 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 5 SIEELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGmGIVEDKVIKNHFASEYIYNA----- 79
Cdd:cd07150 19 SRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGG-STYGKAWFETTFTPELLRAAagecr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 80 -YKDEktcgVLGEDEAfGT--MTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVlra 156
Cdd:cd07150 98 rVRGE----TLPSDSP-GTvsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIM--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 157 aVEAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATG----GPGM-VKAAYSSGKPAIGVGaGNTPVVIDETADVKRAV 231
Cdd:cd07150 170 -EEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGstavGREIaEKAGRHLKKITLELG-GKNPLIVLADADLDYAV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 232 ASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFASHGGYLLQGKELKA--VQGILLKNGALnAAIVGQSAVKIAEMAg 309
Cdd:cd07150 248 RAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPdtVIGPLISPRQV-ERIKRQVEDAVAKGA- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 310 isvpadtKILIGE------------VKAIDDSEPFAHEKLSPTLAMYRAKDFADAVEKAvklvDMGGIGHTSCLYTDQDN 377
Cdd:cd07150 326 -------KLLTGGkydgnfyqptvlTDVTPDMRIFREETFGPVTSVIPAKDAEEALELA----NDTEYGLSAAILTNDLQ 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 1883866115 378 QAarvMTFGEKMKTARILINTPTSH-------GGIGD 407
Cdd:cd07150 395 RA---FKLAERLESGMVHINDPTILdeahvpfGGVKA 428
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
49-400 |
2.45e-13 |
|
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: 73.15 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 49 LAKMAVAESGMGIVEDKVIKN-------HFASE-------------YIYNaykdektcgvlgedEAFGTMTIAEPIGLIC 108
Cdd:cd07145 63 LAKLLTIEVGKPIKQSRVEVErtirlfkLAAEEakvlrgetipvdaYEYN--------------ERRIAFTVREPIGVVG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 109 GIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAVEAGA------PPDIIGwiDEptvdlsnrLM 182
Cdd:cd07145 129 AITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPGVinvvtgYGSEVG--DE--------IV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 183 HHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVaSILMSKTFDN-GVICASEQSVVVVDT 257
Cdd:cd07145 199 TNPKVNMISFTGstavGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAV-SIAVRGRFENaGQVCNAVKRILVEEE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 258 VYnavrERFASHggYLLQGKELKaVQGILLKNGALNAAIVGQSAVKIAEMAGISVPADTKILIG-----------EVKAI 326
Cdd:cd07145 278 VY----DKFLKL--LVEKVKKLK-VGDPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGgkrdegsffppTVLEN 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883866115 327 D--DSEPFAHEKLSPTLAMYRAKDfadaVEKAVKLVDMGGIGHTSCLYTDQDNQAARvmtFGEKMKTARILINTPT 400
Cdd:cd07145 351 DtpDMIVMKEEVFGPVLPIAKVKD----DEEAVEIANSTEYGLQASVFTNDINRALK---VARELEAGGVVINDST 419
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
493-834 |
4.80e-13 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 71.75 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 493 NGYADQITSVLKaaGVETEVFFEVEADPTLTIVRKGAELANAFKPDVIIALGGGSPMDAAKIMWVIYEHPETH--FEELA 570
Cdd:PRK15138 44 TGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 571 LRFMDIRKRIytfpKMGvkarmvAITTTSGTGSEVTPFAVVTDDTTGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFG 650
Cdd:PRK15138 122 TGGKEIKSAI----PMG------SVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 651 GLDAVTHAIEAYVSV-----LASEFSDGQALQAL----KLLKAylPASYHegsknpvARERVHNAATIAGIAFANAflGV 721
Cdd:PRK15138 192 VVDAFVHTVEQYVTYpvdakIQDRFAEGILLTLIeegpKALKE--PENYD-------VRANVMWAATQALNGLIGA--GV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 722 CHSMA-HKLGSQFHIPHGLANALMICNVIrynandnptkqTAFSQYDRPQARRR---YAEIADHLGLSAPGDRTAAKIEK 797
Cdd:PRK15138 261 PQDWAtHMLGHELTAMHGLDHAQTLAIVL-----------PALWNEKRDTKRAKllqYAERVWNITEGSDDERIDAAIAA 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 1883866115 798 LLAWLESikaeLGIPKSIREAGVQEADFLAHVDKLSE 834
Cdd:PRK15138 330 TRNFFEQ----MGVPTRLSDYGLDGSSIPALLKKLEE 362
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
88-268 |
1.47e-11 |
|
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: 67.46 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 88 VLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLraavEAGAPPDII 167
Cdd:cd07115 102 VIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMA----EAGFPAGVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 168 GWIDEPTVDLSNRLMHHPDINLILATGGP----GMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNG 243
Cdd:cd07115 178 NVVTGFGEVAGAALVEHPDVDKITFTGSTavgrKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQG 257
|
170 180
....*....|....*....|....*
gi 1883866115 244 VICASEQSVVVVDTVYNAVRERFAS 268
Cdd:cd07115 258 QMCTAGSRLLVHESIYDEFLERFTS 282
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
98-267 |
1.59e-11 |
|
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: 67.62 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 98 MTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLraavEAGAPPDIIGWIDEPTVDL 177
Cdd:cd07149 118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLL----EAGLPKGALNVVTGSGETV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 178 SNRLMHHPDINLILATGGPGMVKA-AYSSG--KPAIGVGaGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVV 254
Cdd:cd07149 194 GDALVTDPRVRMISFTGSPAVGEAiARKAGlkKVTLELG-SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFV 272
|
170
....*....|...
gi 1883866115 255 VDTVYNAVRERFA 267
Cdd:cd07149 273 HEDIYDEFLERFV 285
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
453-738 |
5.82e-11 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 65.19 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 453 WHKLPKSIYFRRGSLPiALDEVITDGHKRALIVTDRFLFNNgYADQITSVLKAAGVETEvFFEVEADPTLTIVRKGAELA 532
Cdd:COG0371 2 VIILPRRYVQGEGALD-ELGEYLADLGKRALIITGPTALKA-AGDRLEESLEDAGIEVE-VEVFGGECSEEEIERLAEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 533 NAFKPDVIIALGGGSPMDAAKimwviyehpethfeelALRFMdirkriytfpkmgVKARMVAITTTSGTGSEVTPFAVVT 612
Cdd:COG0371 79 KEQGADVIIGVGGGKALDTAK----------------AVAYR-------------LGLPVVSVPTIASTDAPASPLSVIY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 613 DDTTGQKYPLAdYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAIEAYVSVLASEFSDG---------QALQALKLLK 683
Cdd:COG0371 130 TEDGAFDGYSF-LAKNPDLVLVDTDIIAKAPVRLLAAGIGDALAKWYEARDWSLAHRDLAGeyyteaavaLARLCAETLL 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1883866115 684 AYLPASYHEGSKNPV--ARERVHNAATI-AGIAFANAF----LGVCHSMAH---KLGSQFHIPHG 738
Cdd:COG0371 209 EYGEAAIKAVEAGVVtpALERVVEANLLlSGLAMGIGSsrpgSGAAHAIHNgltALPETHHALHG 273
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
98-401 |
7.08e-11 |
|
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: 65.45 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 98 MTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVlraaVEAGAPPDIIGWIDEPTVDL 177
Cdd:cd07131 130 MTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELF----AEAGLPPGVVNVVHGRGEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 178 SNRLMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVV 253
Cdd:cd07131 206 GEALVEHPDVDVVSFTGstevGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 254 VVDTVYNAVRERFashggyllqgkeLKAVQGILLKNGALNAAIVG----QSAV-KIAEMAGISVPADTKILIGEVKAIDD 328
Cdd:cd07131 286 VHESVYDEFLKRF------------VERAKRLRVGDGLDEETDMGplinEAQLeKVLNYNEIGKEEGATLLLGGERLTGG 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 329 S-------EPFAHEKLSPTLAMYRAKDFA--------DAVEKAVKLVDMGGIGHTSCLYTDQDNQAARVMtfgEKMKTAR 393
Cdd:cd07131 354 GyekgyfvEPTVFTDVTPDMRIAQEEIFGpvvalievSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRAR---RDLEAGI 430
|
....*...
gi 1883866115 394 ILINTPTS 401
Cdd:cd07131 431 TYVNAPTI 438
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
98-406 |
3.26e-10 |
|
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: 63.35 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 98 MTIAEPIGlICGIVPTTN-PTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAVEAGAPPDIIGWIDEPTvD 176
Cdd:cd07086 128 MEQWNPLG-VVGVITAFNfPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGG-D 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 177 LSNRLMHHPDINLILATGGPGM-----VKAAYSSGKPAIGVGaGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQS 251
Cdd:cd07086 206 GGELLVHDPRVPLVSFTGSTEVgrrvgETVARRFGRVLLELG-GNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 252 VVVVDTVYNAVRERFashggyllqgkeLKAVQGILLKNGALNAAIVG-----------QSAVKIAEMAGISVPADTKILI 320
Cdd:cd07086 285 LIVHESVYDEFLERL------------VKAYKQVRIGDPLDEGTLVGplinqaavekyLNAIEIAKSQGGTVLTGGKRID 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 321 GEVK------AI-----DDSEPFAHEKLSPTLAMYRAKDFadavEKAVKLVDMGGIGHTSCLYTDQDNQAARVMtfGEKM 389
Cdd:cd07086 353 GGEPgnyvepTIvtgvtDDARIVQEETFAPILYVIKFDSL----EEAIAINNDVPQGLSSSIFTEDLREAFRWL--GPKG 426
|
330
....*....|....*...
gi 1883866115 390 KTARIL-INTPTSHGGIG 406
Cdd:cd07086 427 SDCGIVnVNIPTSGAEIG 444
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
7-280 |
5.30e-10 |
|
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: 62.71 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 7 EELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTC 86
Cdd:cd07090 19 EDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDIDSSADCLEYYAGLAPTLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 87 GV---LGEDeAFGtMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVlraaVEAGAP 163
Cdd:cd07090 99 GEhvpLPGG-SFA-YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEIL----TEAGLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 164 PDIIGWIdEPTVDLSNRLMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKT 239
Cdd:cd07090 173 DGVFNVV-QGGGETGQLLCEHPDVAKVSFTGsvptGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANF 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1883866115 240 FDNGVICASEQSVVVVDTVYNAVRERFASHGGYLLQGKELK 280
Cdd:cd07090 252 LSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLD 292
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
150-356 |
1.29e-09 |
|
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: 61.47 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 150 AEIVLRAAVEAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATG---------------GPGMVKAayssgKPAIGVGA 214
Cdd:cd07124 209 AAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGsrevglriyeraakvQPGQKWL-----KRVIAEMG 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 215 GNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFashggyllqgkeLKAVQGILLKNGALNA 294
Cdd:cd07124 284 GKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERL------------VERTKALKVGDPEDPE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 295 AIVG----QSAV-KIAEMAGISVPADTKILIGEVKA---------------IDDSEPFAHEKL-SPTLAMYRAKDFADAV 353
Cdd:cd07124 352 VYMGpvidKGARdRIRRYIEIGKSEGRLLLGGEVLElaaegyfvqptifadVPPDHRLAQEEIfGPVLAVIKAKDFDEAL 431
|
...
gi 1883866115 354 EKA 356
Cdd:cd07124 432 EIA 434
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
93-268 |
1.32e-09 |
|
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: 61.30 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 93 EAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIvlraAVEAGAPPDIIGWIDE 172
Cdd:cd07113 132 ERYTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAEL----AKEAGIPDGVLNVVNG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 173 pTVDLSNRLMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICAS 248
Cdd:cd07113 208 -KGAVGAQLISHPDVAKVSFTGsvatGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAA 286
|
170 180
....*....|....*....|....
gi 1883866115 249 EQSVVV----VDTVYNAVRERFAS 268
Cdd:cd07113 287 PERFYVhrskFDELVTKLKQALSS 310
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
91-269 |
3.76e-09 |
|
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: 60.06 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 91 EDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIvlraAVEAGAPPDIIGWI 170
Cdd:cd07110 108 PSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEI----AAEAGLPPGVLNVV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 171 DEPTVDLSNRLMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVIC 246
Cdd:cd07110 184 TGTGDEAGAPLAAHPGIDKISFTGstatGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQIC 263
|
170 180
....*....|....*....|...
gi 1883866115 247 ASEQSVVVVDTVYNAVRERFASH 269
Cdd:cd07110 264 SATSRLLVHESIADAFLERLATA 286
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
71-265 |
1.34e-08 |
|
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: 58.27 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 71 FASEYIYNAYKDEKTCG-VLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPhpraKNATNRA 149
Cdd:cd07142 108 AARLFRYYAGWADKIHGmTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKP----AEQTPLS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 150 AEIVLRAAVEAGAPPDIIGWID--EPTVDLSnrLMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTPVVID 222
Cdd:cd07142 184 ALLAAKLAAEAGLPDGVLNIVTgfGPTAGAA--IASHMDVDKVAFTGSTEvgkiiMQLAAKSNLKPVTLELGGKSPFIVC 261
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1883866115 223 ETADVKRAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRER 265
Cdd:cd07142 262 EDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEK 304
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
80-386 |
3.55e-08 |
|
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: 56.82 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 80 YKDEKTCGVLGEDEAfgtmTIAEPIGLICGIVPTTNPTstAIFKSLIS--LKTRNGIVFSPHPRAKNATNRAAEIvlraA 157
Cdd:cd07083 135 YPAVEVVPYPGEDNE----SFYVGLGAGVVISPWNFPV--AIFTGMIVapVAVGNTVIAKPAEDAVVVGYKVFEI----F 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 158 VEAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSSG----------KPAIGVGAGNTPVVIDETADV 227
Cdd:cd07083 205 HEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAarlapgqtwfKRLYVETGGKNAIIVDETADF 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 228 KRAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRERfashggylLQGKELKAVQGILLKNGA-LNAAIVGQSAVKIAE 306
Cdd:cd07083 285 ELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLER--------LLKRAERLSVGPPEENGTdLGPVIDAEQEAKVLS 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 307 -----------MAGISVPADTKILIGE--VKAIDDSEPFAHEKL-SPTLAMYRAKDfaDAVEKAVKLVDMGGIGHTSCLY 372
Cdd:cd07083 357 yiehgknegqlVLGGKRLEGEGYFVAPtvVEEVPPKARIAQEEIfGPVLSVIRYKD--DDFAEALEVANSTPYGLTGGVY 434
|
330
....*....|....*..
gi 1883866115 373 TDQDN---QAARVMTFG 386
Cdd:cd07083 435 SRKREhleEARREFHVG 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
99-269 |
4.96e-08 |
|
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: 56.26 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 99 TIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPhprAKNaTNRAAEIVLRAAVEAGAPPDIIGWIDEPTVDLS 178
Cdd:cd07144 140 TLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKP---AEN-TPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 179 NRLMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVV 254
Cdd:cd07144 216 SALAEHPDVDKIAFTGstatGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYV 295
|
170
....*....|....*
gi 1883866115 255 VDTVYNAVRERFASH 269
Cdd:cd07144 296 QESIYDKFVEKFVEH 310
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
97-266 |
5.85e-08 |
|
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: 56.06 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 97 TMTIAEPIGlICG-IVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLraavEAGAPPDIIGWIDEPTV 175
Cdd:cd07091 135 AYTRREPIG-VCGqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIK----EAGFPPGVVNIVPGFGP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 176 DLSNRLMHHPDINLI-----LATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQ 250
Cdd:cd07091 210 TAGAAISSHMDVDKIaftgsTAVGRTIMEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGS 289
|
170
....*....|....*.
gi 1883866115 251 SVVVVDTVYNAVRERF 266
Cdd:cd07091 290 RIFVQESIYDEFVEKF 305
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
480-854 |
1.28e-07 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 54.46 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 480 KRALIVTDrflfNNGYA---DQITSVLKAAGVETEVFFeVEADPTLTIVRKGAELANAFKPDVIIALGGGSPMDAAKImw 556
Cdd:cd08550 23 KKALIIGG----KTALEavgEKLEKSLEEAGIDYEVEV-FGGECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAKA-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 557 viyehpethfeeLALRfmdirkriytfpkMGVKarMVAITTTSGTGSEVTPFAVVTDDtTGQKYPLADYALTPDMAIVDA 636
Cdd:cd08550 96 ------------VADR-------------LGLP--VVTVPTIAATCAAWSALSVLYDE-EGEFLGYSLLKRSPDLVLVDT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 637 NLVMDMPKSLCAFGGLDAVTHAIEAYVSvLASEFSDG-------QALQALKLLKAYLPASYHEgsknpVARERVHNAatI 709
Cdd:cd08550 148 DIIAAAPVRYLAAGIGDTLAKWYEARPS-SRGGPDDLalqaavqLAKLAYDLLLEYGVQAVED-----VRQGKVTPA--L 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 710 AGIAFANAFL-GVCHSMAHKlGSQFHIPHGLANALmicnvirynandnptkqTAFsqydrPQARRRYaeiadH------- 781
Cdd:cd08550 220 EDVVDAIILLaGLVGSLGGG-GCRTAAAHAIHNGL-----------------TKL-----PETHGTL-----Hgekvafg 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883866115 782 -LGLSAPGDRTAAKIEKLLAWLEsikaELGIPKSIREAGVQEADflAHVDKLSEDAFDDQCTGANPRYPLVAEL 854
Cdd:cd08550 272 lLVQLALEGRSEEEIEELIEFLR----RLGLPVTLEDLGLELTE--EELRKIAEYACDPPDMAHMLPFPVTPEM 339
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
104-254 |
1.50e-07 |
|
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: 55.18 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 104 IGLI--CGIVPTTNpTSTAIFKSLIslkTRNGIVFSPHPRAKNATNRAAEIVLRAAVEAGAPPDIIGWI-DEPTVDLSNR 180
Cdd:cd07127 196 VALVigCSTFPTWN-GYPGLFASLA---TGNPVIVKPHPAAILPLAITVQVAREVLAEAGFDPNLVTLAaDTPEEPIAQT 271
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883866115 181 LMHHPDINLILATGGP--GMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVV 254
Cdd:cd07127 272 LATRPEVRIIDFTGSNafGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYV 347
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
98-407 |
4.46e-07 |
|
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: 53.35 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 98 MTIAEPIGLICGIVPTTNPT--------------STAIFKslislktrnGIVFSPhpraknatnRAAEIVLRAAVEAGAP 163
Cdd:cd07105 93 MVVKEPVGVVLGIAPWNAPVilgtraiayplaagNTVVLK---------ASELSP---------RTHWLIGRVFHEAGLP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 164 PDIIGWI-----DEPTVdlSNRLMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASI 234
Cdd:cd07105 155 KGVLNVVthspeDAPEV--VEALIAHPAVRKVNFTGstrvGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 235 LMSKTFDNGVICASEQSVVVVDTVYNAVRERFAshggyllqgkelKAVQGILLKNGALNAAIVGQSAVKIAEM------- 307
Cdd:cd07105 233 LFGAFLNSGQICMSTERIIVHESIADEFVEKLK------------AAAEKLFAGPVVLGSLVSAAAADRVKELvddalsk 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 308 --------------AGISVPAdtkILIGEVKA---IDDSEPFAheklsPTLAMYRAKDfadaVEKAVKLVDMGGIGHTSC 370
Cdd:cd07105 301 gaklvvggladespSGTSMPP---TILDNVTPdmdIYSEESFG-----PVVSIIRVKD----EEEAVRIANDSEYGLSAA 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1883866115 371 LYTDQDNQAARVmtfGEKMKTARILINTPT-------SHGGIGD 407
Cdd:cd07105 369 VFTRDLARALAV---AKRIESGAVHINGMTvhdeptlPHGGVKS 409
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
102-268 |
1.00e-06 |
|
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: 52.33 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 102 EPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRaaveaGAPPDIIGWIDEPTVDLSNRL 181
Cdd:cd07092 117 EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE-----VLPPGVVNVVCGGGASAGDAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 182 MHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVDT 257
Cdd:cd07092 192 VAHPRVRMVSLTGsvrtGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHES 271
|
170
....*....|.
gi 1883866115 258 VYNAVRERFAS 268
Cdd:cd07092 272 VYDEFVAALVE 282
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
157-398 |
1.05e-06 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 52.39 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 157 AVEAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNTPVVIDETADVKRAV 231
Cdd:PLN02278 210 ALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAvgkklMAGAAATVKRVSLELG-GNAPFIVFDDADLDVAV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 232 ASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFAshggyllqgkelKAVQGILLKNGALNAAIVG----QSAV-KIAE 306
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFS------------KAVQKLVVGDGFEEGVTQGplinEAAVqKVES 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 307 MAGISVPADTKILIGE---------------VKAIDDSEPFAHEKLSPTLAMYRAKDfadaVEKAVKLVDMGGIGHTSCL 371
Cdd:PLN02278 357 HVQDAVSKGAKVLLGGkrhslggtfyeptvlGDVTEDMLIFREEVFGPVAPLTRFKT----EEEAIAIANDTEAGLAAYI 432
|
250 260
....*....|....*....|....*..
gi 1883866115 372 YTdQDNQaaRVMTFGEKMKTARILINT 398
Cdd:PLN02278 433 FT-RDLQ--RAWRVSEALEYGIVGVNE 456
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
77-280 |
1.10e-06 |
|
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: 52.15 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 77 YNAYKDEKTCGVLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVlra 156
Cdd:cd07143 118 YGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLI--- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 157 aVEAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAV 231
Cdd:cd07143 195 -PEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLvgrkvMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAV 273
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1883866115 232 ASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFAShggyllQGKELK 280
Cdd:cd07143 274 VWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKE------KAKKLK 316
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
480-553 |
1.97e-06 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 50.87 E-value: 1.97e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1883866115 480 KRALIVTDRFLFNNgYADQITSVLKAAGVE-TEVFFEVEADPTlTIVRKgAELANAFKPDVIIALGGGSPMDAAK 553
Cdd:cd08170 23 KKALVIADPFVLDL-VGERLEESLEKAGLEvVFEVFGGECSRE-EIERL-AAIARANGADVVIGIGGGKTIDTAK 94
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
102-269 |
2.13e-06 |
|
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: 51.15 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 102 EPIGLICGIVPTTNPTSTAIfKSLI-SLKTRNGIVFSPhprAKNATNRAAEIVLRAAVEAGAPPDIIGWIDEPTVDLSNR 180
Cdd:cd07151 129 EPLGVVGVISPWNFPLHLSM-RSVApALALGNAVVLKP---ASDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 181 LMHHPDINLILATGGP--GMVKAAYSSG---KPAIGVGaGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVV 255
Cdd:cd07151 205 FVEHPVPRLISFTGSTpvGRHIGELAGRhlkKVALELG-GNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVH 283
|
170
....*....|....
gi 1883866115 256 DTVYNAVRERFASH 269
Cdd:cd07151 284 EDVYDEFVEKFVER 297
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
102-397 |
2.19e-06 |
|
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: 51.15 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 102 EPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLRAAVEAGAPPD----IIGWideptVDL 177
Cdd:cd07098 119 EPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDlvqlVTCL-----PET 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 178 SNRLMHHPDINLILATGGPG---MV-KAAYSSGKPAIGVGAGNTPVVIDETADVKrAVASILMSKTFDN-GVICASEQSV 252
Cdd:cd07098 194 AEALTSHPVIDHITFIGSPPvgkKVmAAAAESLTPVVLELGGKDPAIVLDDADLD-QIASIIMRGTFQSsGQNCIGIERV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 253 VVVDTVYNAVRERFASHGGYLLQGKelkavqgILLKNGALNAAIVGQSAVKIAEMAGISVPADTKILIGEVKAIDDSEPF 332
Cdd:cd07098 273 IVHEKIYDKLLEILTDRVQALRQGP-------PLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQ 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 333 AH-------------------EKLSPTLAMYRAKDFADAVEKAvklvDMGGIGHTSCLYTDQDNQAARVmtfGEKMKTAR 393
Cdd:cd07098 346 GHyfpptllvdvtpdmkiaqeEVFGPVMVVMKASDDEEAVEIA----NSTEYGLGASVFGKDIKRARRI---ASQLETGM 418
|
....
gi 1883866115 394 ILIN 397
Cdd:cd07098 419 VAIN 422
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
456-555 |
2.71e-06 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 50.24 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 456 LPKSIYFRRGSLPIaLDEVITDGH--KRALIVTDRFLFNNgYADQITSVLKAAGVETEV--FFEVEADPTLTIVRKgaeL 531
Cdd:cd08173 1 LPRNVVVGHGAINK-IGEVLKKLLlgKRALIITGPNTYKI-AGKRVEDLLESSGVEVVIvdIATIEEAAEVEKVKK---L 75
|
90 100
....*....|....*....|....
gi 1883866115 532 ANAFKPDVIIALGGGSPMDAAKIM 555
Cdd:cd08173 76 IKESKADFIIGVGGGKVIDVAKYA 99
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
97-268 |
3.45e-06 |
|
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: 50.44 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 97 TMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEI---VLRAAV---------EAGAPp 164
Cdd:cd07108 111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEIlaqVLPAGVlnvitgygeECGAA- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 165 diigwideptvdlsnrLMHHPDINLILATGGPGMVKAAY-SSGKPAIGVG---AGNTPVVIDETADVKRAVASILMSKTF 240
Cdd:cd07108 190 ----------------LVDHPDVDKVTFTGSTEVGKIIYrAAADRLIPVSlelGGKSPMIVFPDADLDDAVDGAIAGMRF 253
|
170 180
....*....|....*....|....*....
gi 1883866115 241 D-NGVICASEQSVVVVDTVYNAVRERFAS 268
Cdd:cd07108 254 TrQGQSCTAGSRLFVHEDIYDAFLEKLVA 282
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
3-269 |
4.26e-06 |
|
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: 50.22 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 3 INSIEELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESG------MGIVEDKV-IKNHFASey 75
Cdd:cd07106 15 VASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGkplaeaQFEVGGAVaWLRYTAS-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 76 iyNAYKDEktcgVLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIvLR 155
Cdd:cd07106 93 --LDLPDE----VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGEL-AQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 156 AAVeagaPPDIIGWIDEPTvDLSNRLMHHPDINLILATG----GPGMVKAAYSSGKPA---IGvgaGNTPVVIDETADVK 228
Cdd:cd07106 166 EVL----PPGVLNVVSGGD-ELGPALTSHPDIRKISFTGstatGKKVMASAAKTLKRVtleLG---GNDAAIVLPDVDID 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1883866115 229 RAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFASH 269
Cdd:cd07106 238 AVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVAL 278
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
103-429 |
5.28e-06 |
|
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: 49.93 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 103 PIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHprakNATNRAAEIVLRAAVEAGA-PPDIIGWIdEPTVDLSNRL 181
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPH----TAVSIVMQIMVRLLHYAGLlPPEDVTLI-NGDGKTMQAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 182 MHHPDINLILATGGPGMVKAAYSSGKPA--IGVGAGNTPVVIDETADVKRAVA-SILMSKTFDNGVICASEQSVVVVDT- 257
Cdd:cd07084 175 LLHPNPKMVLFTGSSRVAEKLALDAKQAriYLELAGFNWKVLGPDAQAVDYVAwQCVQDMTACSGQKCTAQSMLFVPENw 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 258 ----VYNAVRERFA--SHGGYLLQGKELKAVQGILLKNGALNAAIV--GQSAVKIAEMAGISVPADTKILIGEVKAIDDS 329
Cdd:cd07084 255 sktpLVEKLKALLArrKLEDLLLGPVQTFTTLAMIAHMENLLGSVLlfSGKELKNHSIPSIYGACVASALFVPIDEILKT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 330 EPfAHEK--LSP--TLAMYRAKDFADAVEKAVKLVdmggiGH-TSCLYTDQDNQAARVMtfGEKMKTARILINTPTSHGG 404
Cdd:cd07084 335 YE-LVTEeiFGPfaIVVEYKKDQLALVLELLERMH-----GSlTAAIYSNDPIFLQELI--GNLWVAGRTYAILRGRTGV 406
|
330 340
....*....|....*....|....*.
gi 1883866115 405 -IGDLYNFSLAPSlTLGCGSWGGNSI 429
Cdd:cd07084 407 aPNQNHGGGPAAD-PRGAGIGGPEAI 431
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
98-290 |
5.90e-06 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 49.89 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 98 MTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIvlraAVEAGAPPDIIGWIDEPTVDL 177
Cdd:PRK09847 152 MIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGL----AKEAGLPDGVLNVVTGFGHEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 178 SNRLMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAG--NTPVVIDETADVKRAVASILMSKTFDNGVICASEQS 251
Cdd:PRK09847 228 GQALSRHNDIDAIAFTGstrtGKQLLKDAGDSNMKRVWLEAGgkSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTR 307
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1883866115 252 VVVVDTVYNAVRERFASHGGYLLQGKEL--KAVQGILLKNG 290
Cdd:PRK09847 308 LLLEESIADEFLALLKQQAQNWQPGHPLdpATTMGTLIDCA 348
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
77-267 |
7.44e-06 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 49.43 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 77 YNAYKDEKTCG-VLGEDEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRaknaTNRAAEIVLR 155
Cdd:PLN02766 131 YYAGAADKIHGeTLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQ----TPLSALFYAH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 156 AAVEAGAPPDIIGWID--EPTVDLSnrLMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTPVVIDETADVK 228
Cdd:PLN02766 207 LAKLAGVPDGVINVVTgfGPTAGAA--IASHMDVDKVSFTGSTEvgrkiMQAAATSNLKQVSLELGGKSPLLIFDDADVD 284
|
170 180 190
....*....|....*....|....*....|....*....
gi 1883866115 229 RAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFA 267
Cdd:PLN02766 285 MAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLV 323
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
8-267 |
8.49e-06 |
|
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: 49.07 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 8 ELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGmGIVEDKVIKNHFASEYIYNA------YK 81
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESG-STRPKAAFEVGAAIAILREAaglprrPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 82 DEktcgVLGEDEAfGTMTIA--EPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRA-AEIVLRAAV 158
Cdd:cd07104 80 GE----ILPSDVP-GKESMVrrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEAGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 159 EAG------APPDIIGwideptvdlsNRLMHHPDINLILATGGPGM-----VKAAYSSGKPAIGVGaGNTPVVIDETADV 227
Cdd:cd07104 155 PKGvlnvvpGGGSEIG----------DALVEHPRVRMISFTGSTAVgrhigELAGRHLKKVALELG-GNNPLIVLDDADL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1883866115 228 KRAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFA 267
Cdd:cd07104 224 DLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLV 263
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
146-239 |
9.13e-06 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 48.91 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 146 TNRA-AEIVLRAAVEAGAPPDIIGWIDEPTVDLSNRLMHHPD-INLILATGGPGMVKAAYSSGK-PAIGVGAGNTPVVID 222
Cdd:PRK00197 155 SNRAlVAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGyVDVIIPRGGAGLIRRVVENATvPVIEHGDGICHIYVD 234
|
90
....*....|....*..
gi 1883866115 223 ETADVKRAVASILMSKT 239
Cdd:PRK00197 235 ESADLDKALKIVLNAKT 251
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
102-267 |
1.47e-05 |
|
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: 48.39 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 102 EPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIvlraAVEAGAPPDIIGWIDEPTVDLSNRL 181
Cdd:cd07089 122 EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEI----IAETDLPAGVVNVVTGSDNAVGEAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 182 MHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVD 256
Cdd:cd07089 198 TTDPRVDMVSFTGSTAvgrriMAQAAATLKRVLLELG-GKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPR 276
|
170
....*....|.
gi 1883866115 257 TVYNAVRERFA 267
Cdd:cd07089 277 SRYDEVVEALA 287
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
97-267 |
1.93e-05 |
|
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: 48.08 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 97 TMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLraavEAGAPPDIIGWIDEPTVD 176
Cdd:cd07119 128 SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIE----EAGLPAGVVNLVTGSGAT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 177 LSNRLMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGAGNTPVVIDEtADVKRAVASILMSKTFDNGVICASEQS 251
Cdd:cd07119 204 VGAELAESPDVDLVSFTGGTAtgrsiMRAAAGNVKKVALELGGKNPNIVFAD-ADFETAVDQALNGVFFNAGQVCSAGSR 282
|
170
....*....|....*.
gi 1883866115 252 VVVVDTVYNAVRERFA 267
Cdd:cd07119 283 LLVEESIHDKFVAALA 298
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
132-407 |
2.55e-05 |
|
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: 47.65 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 132 NGIVFSPHPRaknaTNRAAEIVLRAAVEAGAPPDIIGWIdEPTVDLSNRLMHHPDINLILATGGP--GMVKAAYSSGKP- 208
Cdd:cd07095 126 NTVVFKPSEL----TPAVAELMVELWEEAGLPPGVLNLV-QGGRETGEALAAHEGIDGLLFTGSAatGLLLHRQFAGRPg 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 209 ---AIGVGaGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVDT-VYNAVRERFASHGGYLLQGKELKAVQ- 283
Cdd:cd07095 201 kilALEMG-GNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPf 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 284 --GILLKNGALNAAIVGQSAVKI---AEMAGISVPADTKIL---IGEVKAID---DSEPFAheklsPTLAMYRAKDFada 352
Cdd:cd07095 280 mgPLIIAAAAARYLLAQQDLLALggePLLAMERLVAGTAFLspgIIDVTDAAdvpDEEIFG-----PLLQVYRYDDF--- 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1883866115 353 vEKAVKLVDMGGIGHTSCLYTDQDNQAARvmtFGEKMKTARILINTPTS-------HGGIGD 407
Cdd:cd07095 352 -DEAIALANATRFGLSAGLLSDDEALFER---FLARIRAGIVNWNRPTTgasstapFGGVGL 409
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
48-267 |
5.17e-05 |
|
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: 46.57 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 48 PLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGVLGEDE--AFGTMtIAEPIGLICGIVPTTNPTSTAIfKSL 125
Cdd:cd07120 61 RLARLLALENGKILGEARFEISGAISELRYYAGLARTEAGRMIEPEpgSFSLV-LREPMGVAGIIVPWNSPVVLLV-RSL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 126 I-SLKTRNGIVFSPHPRAKNATNRAAEIVlrAAVEaGAPPDIIGWIDEPTVDLSNRLMHHPDINLI-----LATGGPGMV 199
Cdd:cd07120 139 ApALAAGCTVVVKPAGQTAQINAAIIRIL--AEIP-SLPAGVVNLFTESGSEGAAHLVASPDVDVIsftgsTATGRAIMA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1883866115 200 KAAYSSGKPAIGVGaGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFA 267
Cdd:cd07120 216 AAAPTLKRLGLELG-GKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLA 282
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
102-403 |
5.42e-05 |
|
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: 46.80 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 102 EPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPhpraknATNRA--AEIVLRAAVEAGAPPDIIGWIDEPTVDLSN 179
Cdd:cd07082 140 EPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP------ATQGVllGIPLAEAFHDAGFPKGVVNVVTGRGREIGD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 180 RLMHHPDINLILATGGPG----MVKAAysSGKPAI-GVGAGNtPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVV 254
Cdd:cd07082 214 PLVTHGRIDVISFTGSTEvgnrLKKQH--PMKRLVlELGGKD-PAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 255 VDTVYNAVRERFAshggyllqgKEL-KAVQGILLKNGALNAAIVGQSAVKiaEMAGISVPADTK---ILIGEVKAIDDS- 329
Cdd:cd07082 291 HESVADELVELLK---------EEVaKLKVGMPWDNGVDITPLIDPKSAD--FVEGLIDDAVAKgatVLNGGGREGGNLi 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 330 EPFAHEKLSPTLAMYRAKDFA--------DAVEKAVKLVDMGGIGHTSCLYTDQDNQAARVmtfGEKMKTARILINTPTS 401
Cdd:cd07082 360 YPTLLDPVTPDMRLAWEEPFGpvlpiirvNDIEEAIELANKSNYGLQASIFTKDINKARKL---ADALEVGTVNINSKCQ 436
|
..
gi 1883866115 402 HG 403
Cdd:cd07082 437 RG 438
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
52-267 |
7.43e-05 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 46.18 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 52 MAVAESGMGIVEDKVIKNHFASeyiYNAYKDEKTCGVLGEDEAFgtmTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTR 131
Cdd:PTZ00381 64 TKMTEVLLTVAEIEHLLKHLDE---YLKPEKVDTVGVFGPGKSY---IIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 132 NGIVFSPHPRAKNATNRAAEIVLRAAveagaPPDIIGWIdEPTVDLSNRLMHHPdINLILATGGP--GMV--KAAYSSGK 207
Cdd:PTZ00381 138 NTVVLKPSELSPHTSKLMAKLLTKYL-----DPSYVRVI-EGGVEVTTELLKEP-FDHIFFTGSPrvGKLvmQAAAENLT 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883866115 208 PAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVV----VDTVYNAVRERFA 267
Cdd:PTZ00381 211 PCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVhrsiKDKFIEALKEAIK 274
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
97-267 |
8.21e-05 |
|
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: 46.00 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 97 TMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLraavEAGAPPDIIGWI--DEPT 174
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAE----EAGFPPGVVNVVtgFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 175 VdlSNRLMHHPDINLILATGGP----GMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMsktfdnGVICASEQ 250
Cdd:cd07114 189 T--GEALVEHPLVAKIAFTGGTetgrHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVA------GIFAAAGQ 260
|
170 180
....*....|....*....|...
gi 1883866115 251 SVV------VVDTVYNAVRERFA 267
Cdd:cd07114 261 TCVagsrllVQRSIYDEFVERLV 283
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
99-267 |
1.57e-04 |
|
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: 45.30 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 99 TIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIvlraAVEAGAPPDIIGWIDEPTVDLS 178
Cdd:cd07109 113 TVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAEL----AEEAGLPAGALNVVTGLGAEAG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 179 NRLMHHPDINLILATGGPGMVKA-AYSSGKPAIGVG---AGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVV 254
Cdd:cd07109 189 AALVAHPGVDHISFTGSVETGIAvMRAAAENVVPVTlelGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLV 268
|
170
....*....|...
gi 1883866115 255 VDTVYNAVRERFA 267
Cdd:cd07109 269 HRSIYDEVLERLV 281
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
49-398 |
3.03e-04 |
|
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: 44.37 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 49 LAKMAVAESGMGIVEDKVIKNHFASEYI-YNA---YKDEKTCGVLGEDeafgTMTIA--EPIGLICGIVPTTNPTSTAIF 122
Cdd:cd07117 80 LAMVETLDNGKPIRETRAVDIPLAADHFrYFAgviRAEEGSANMIDED----TLSIVlrEPIGVVGQIIPWNFPFLMAAW 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 123 KSLISLKTRNGIVFSPhprakNATNRAAEIVLRAAVEAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATG----GPGM 198
Cdd:cd07117 156 KLAPALAAGNTVVIKP-----SSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGstevGRDV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 199 VKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVDTVYNAVRERFAshggyllqgKE 278
Cdd:cd07117 231 AIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLK---------EK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 279 LKAVQ--GILLKNGALNAAIVGQSAVKIAEMAGISVPADTKILIGEVKAIDDS-------EP-----------FAHEKL- 337
Cdd:cd07117 302 FENVKvgNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldkgffiEPtlivnvtndmrVAQEEIf 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1883866115 338 SPTLAMYRAKDfadaVEKAVKLVDMGGIGHTSCLYTDQDNQAARVmtfGEKMKTARILINT 398
Cdd:cd07117 382 GPVATVIKFKT----EDEVIDMANDSEYGLGGGVFTKDINRALRV---ARAVETGRVWVNT 435
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
102-266 |
4.22e-04 |
|
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: 43.77 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 102 EPIGLICGIVPTTNPTSTAIfKSLI-SLKTRNGIVFSPHPRaknaTNRAAEIVLRAAVEAGAPPDIIGWIdEPTVDLSNR 180
Cdd:cd07102 115 EPLGVVLIIAPWNYPYLTAV-NAVIpALLAGNAVILKHSPQ----TPLCGERFAAAFAEAGLPEGVFQVL-HLSHETSAA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 181 LMHHPDINLILATGG-PGMVKAAYSSGKPAIGVG---AGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVD 256
Cdd:cd07102 189 LIADPRIDHVSFTGSvAGGRAIQRAAAGRFIKVGlelGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHE 268
|
170
....*....|
gi 1883866115 257 TVYNAVRERF 266
Cdd:cd07102 269 SIYDAFVEAF 278
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
92-265 |
4.94e-04 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 43.57 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 92 DEAFGTMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIvlraAVEAGAPPDIIGWID 171
Cdd:PLN02467 140 METFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADI----CREVGLPPGVLNVVT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 172 EPTVDLSNRLMHHPDINLILATG----GPGMVKAAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICA 247
Cdd:PLN02467 216 GLGTEAGAPLASHPGVDKIAFTGstatGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICS 295
|
170
....*....|....*...
gi 1883866115 248 SEQSVVVVDTVYNAVRER 265
Cdd:PLN02467 296 ATSRLLVHERIASEFLEK 313
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
478-553 |
5.49e-04 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 42.89 E-value: 5.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883866115 478 GHKRALIVTDRFLfNNGYADQITSVLKAAGVETEVffEVEADPTLTIVRKgaELANAFKPDVIIALGGGSPMDAAK 553
Cdd:cd08174 24 GFGKVAIVTGEGI-DELLGEDILESLEEAGEIVTV--EENTDNSAEELAE--KAFSLPKVDAIVGIGGGKVLDVAK 94
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
480-555 |
6.94e-04 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 42.88 E-value: 6.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1883866115 480 KRALIVTDRFLFNNgYADQITSVLKAAGVE-TEVFFEVEAdpTLTIVRKGAELANAFKPDVIIALGGGSPMDAAKIM 555
Cdd:PRK09423 30 KRALVIADEFVLGI-VGDRVEASLKEAGLTvVFEVFNGEC--SDNEIDRLVAIAEENGCDVVIGIGGGKTLDTAKAV 103
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
103-276 |
8.42e-04 |
|
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: 42.62 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 103 PIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRaknaTNRAAEIVLRAAVEAGAPPDIIGWIDEPTvDLSNRLM 182
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR----TPLSALILGEVLAETGLPKGAFSVLPCSR-DDADLLV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 183 HHPDINLILATGGPG---MVKAAYSSGKPAIGVGaGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVVVDTVY 259
Cdd:cd07147 198 TDERIKLLSFTGSPAvgwDLKARAGKKKVVLELG-GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVY 276
|
170
....*....|....*..
gi 1883866115 260 NAVRERFASHGGYLLQG 276
Cdd:cd07147 277 DEFKSRLVARVKALKTG 293
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
7-403 |
1.27e-03 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 42.44 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 7 EELNALVARVKKAQRQYAGFTQQQVDKIFRAAALAAADARIPLAKMAVAESGMGiVEDKVIKNHFASEYIynAYKDEKTC 86
Cdd:PLN00412 53 EEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKP-AKDAVTEVVRSGDLI--SYTAEEGV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 87 GVLGE------DEAFGT------MTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPhpRAKNATnrAAEIVL 154
Cdd:PLN00412 130 RILGEgkflvsDSFPGNernkycLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP--PTQGAV--AALHMV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 155 RAAVEAGAPPDIIGWIDEPTVDLSNRLMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPV-VIDETADVKRAVAS 233
Cdd:PLN00412 206 HCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGDTGIAISKKAGMVPLQMELGGKDAcIVLEDADLDLAAAN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 234 ILMSKTFDNGVICASEQSVVVVDTVYNAVRERFAShggyllqgKELKAVQGILLKNGALNAAIVGQSA------VKIAEM 307
Cdd:PLN00412 286 IIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA--------KVAKLTVGPPEDDCDITPVVSESSAnfieglVMDAKE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 308 AGISVPADTK--------ILIGEVKA---IDDSEPFAheklsPTLAMYRAKDfadaVEKAVKLVDMGGIGHTSCLYTDQD 376
Cdd:PLN00412 358 KGATFCQEWKregnliwpLLLDNVRPdmrIAWEEPFG-----PVLPVIRINS----VEEGIHHCNASNFGLQGCVFTRDI 428
|
410 420
....*....|....*....|....*..
gi 1883866115 377 NQAARVmtfGEKMKTARILINTPTSHG 403
Cdd:PLN00412 429 NKAILI---SDAMETGTVQINSAPARG 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
99-265 |
1.48e-03 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 42.18 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 99 TIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVlraaVEAGAPP----------DIIG 168
Cdd:PRK13252 138 TRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIY----TEAGLPDgvfnvvqgdgRVGA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 169 WideptvdlsnrLMHHPDINLILATGGPGMVK----AAYSSGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGV 244
Cdd:PRK13252 214 W-----------LTEHPDIAKVSFTGGVPTGKkvmaAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQ 282
|
170 180
....*....|....*....|.
gi 1883866115 245 ICASEQSVVVVDTVYNAVRER 265
Cdd:PRK13252 283 VCTNGTRVFVQKSIKAAFEAR 303
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
97-399 |
1.51e-03 |
|
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: 42.12 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 97 TMTIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIvlraAVEAGAPPDIIGWI--DEPT 174
Cdd:cd07085 130 TYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAEL----LQEAGLPDGVLNVVhgGKEA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 175 VdlsNRLMHHPDINLILATGGPGMVKAAYS----SGKPAIGVGAGNTPVVIDETADVKRAVASILMSKTFDNGVICASEQ 250
Cdd:cd07085 206 V---NALLDHPDIKAVSFVGSTPVGEYIYEraaaNGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 251 SVVVVDTVYNAVRERFASH------GGYLLQGKELKAVqgIllkNGALNAAIVG--QSAVKI-AEMA----GISVPADTK 317
Cdd:cd07085 283 VAVAVGDEADEWIPKLVERakklkvGAGDDPGADMGPV--I---SPAAKERIEGliESGVEEgAKLVldgrGVKVPGYEN 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 318 ------ILIGEVKAidDSEPFAHEKLSPTLAMYRAKDFADAVEkavkLVDMGGIGHTSCLYTdQDNQAARvmTFGEKMKT 391
Cdd:cd07085 358 gnfvgpTILDNVTP--DMKIYKEEIFGPVLSIVRVDTLDEAIA----IINANPYGNGAAIFT-RSGAAAR--KFQREVDA 428
|
....*...
gi 1883866115 392 ARILINTP 399
Cdd:cd07085 429 GMVGINVP 436
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
215-269 |
2.41e-03 |
|
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: 41.44 E-value: 2.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1883866115 215 GNTPVVIDETADVKRAVASILMSKTFDNGVICaseqsvVVVDTVY--NAVRERFASH 269
Cdd:cd07134 209 GKSPTIVDETADLKKAAKKIAWGKFLNAGQTC------IAPDYVFvhESVKDAFVEH 259
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
215-269 |
2.63e-03 |
|
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: 41.32 E-value: 2.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1883866115 215 GNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSVVV----VDTVYNAVRERFASH 269
Cdd:cd07133 210 GKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVpedkLEEFVAAAKAAVAKM 268
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
103-397 |
2.78e-03 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 41.00 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 103 PIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPrakNATNrAAEIVLRAAVEAGAPPDIIGWIDePTVDLSNRLM 182
Cdd:PRK13968 126 PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAP---NVMG-CAQLIAQVFKDAGIPQGVYGWLN-ADNDGVSQMI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 183 HHPDINLILATGGpgmVKAAYSSGKPAigvGA----------GNTPVVIDETADVKRAVASILMSKTFDNGVICASEQSV 252
Cdd:PRK13968 201 NDSRIAAVTVTGS---VRAGAAIGAQA---GAalkkcvlelgGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRF 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 253 VVVDTVYNAVRERFASHGGYLLQG------------------KELKAVQGILLKNGAlnAAIVGqsAVKIAEMAGISVPA 314
Cdd:PRK13968 275 IIEEGIASAFTERFVAAAAALKMGdprdeenalgpmarfdlrDELHHQVEATLAEGA--RLLLG--GEKIAGAGNYYAPT 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 315 dtkiLIGEVKAidDSEPFAHEKLSPTLAMYRAKDfadaVEKAVKLVDMGGIGHTSCLYTDQDNQAARvmtFGEKMKTARI 394
Cdd:PRK13968 351 ----VLANVTP--EMTAFREELFGPVAAITVAKD----AEHALELANDSEFGLSATIFTTDETQARQ---MAARLECGGV 417
|
...
gi 1883866115 395 LIN 397
Cdd:PRK13968 418 FIN 420
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
459-546 |
2.93e-03 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 40.89 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 459 SIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNgYADQITSVLKAAGVETEVFfEVEAD------PTLT-IVRKGAEl 531
Cdd:cd08195 3 PILIGSGLLDKLGELLELKKGSKVVIVTDENVAKL-YGELLLKSLEAAGFKVEVI-VIPAGekskslETVErIYDFLLE- 79
|
90
....*....|....*
gi 1883866115 532 ANAFKPDVIIALGGG 546
Cdd:cd08195 80 AGLDRDSLLIALGGG 94
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
453-554 |
3.35e-03 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 40.65 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 453 WHKLPKSIYFRRGSLPiALDEVITDGH--KRALIVTDRfLFNNGYADQITSVLKAAGvETEVFFEVEAdpTLTIVRKGAE 530
Cdd:PRK00843 7 WIQLPRDVVVGHGVLD-DIGDVCSDLKltGRALIVTGP-TTKKIAGDRVEENLEDAG-DVEVVIVDEA--TMEEVEKVEE 81
|
90 100
....*....|....*....|....
gi 1883866115 531 LANAFKPDVIIALGGGSPMDAAKI 554
Cdd:PRK00843 82 KAKDVNAGFLIGVGGGKVIDVAKL 105
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
470-552 |
6.03e-03 |
|
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.
Pssm-ID: 341478 Cd Length: 349 Bit Score: 39.82 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 470 ALDEVITDGHKRALIVTDRFLFNNgYADQITSVLKAAGVETEVF-FEV-EADPTLTIVRKGAELANAFKPD---VIIALG 544
Cdd:cd08199 17 TLADAYGRPGRRRLVVVDENVDRL-YGARIRAYFAAHGIEATILvLPGgEANKTMETVLRIVDALDDFGLDrrePVIAIG 95
|
....*...
gi 1883866115 545 GGSPMDAA 552
Cdd:cd08199 96 GGVLLDVV 103
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
91-267 |
9.45e-03 |
|
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: 39.47 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 91 EDEAFGTM------TIAEPIGLICGIVPTTNPTSTAIFKSLISLKTRNGIVFSPHPRAKNATNRAAEIVLraavEAGAPP 164
Cdd:cd07093 99 DGESYPQDggalnyVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELAN----EAGLPP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883866115 165 DIIGWIDEPTVDLSNRLMHHPDINLILATGGPG-----MVKAAYSSGKPAIGVGaGNTPVVIDETADVKRAVASILMSKT 239
Cdd:cd07093 175 GVVNVVHGFGPEAGAALVAHPDVDLISFTGETAtgrtiMRAAAPNLKPVSLELG-GKNPNIVFADADLDRAVDAAVRSSF 253
|
170 180
....*....|....*....|....*...
gi 1883866115 240 FDNGVICASEQSVVVVDTVYNAVRERFA 267
Cdd:cd07093 254 SNNGEVCLAGSRILVQRSIYDEFLERFV 281
|
|
| |
