Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
     (EC 4.2.1.17)
     (EC 5.3.3.8)
     (EC 5.1.2.3)
3-hydroxyacyl-CoA dehydrogenase
     (EC 1.1.1.35)

Gene name

	Name:	fadB
	OrderedLocusNames:	PSPPH_3210

From

Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)

[TaxID: 264730]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.187.18.6488-6498.2005; PubMed=16159782 [NCBI, ExPASy, EBI, Israel, Japan]
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.;
"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition.";
J. Bacteriol. 187:6488-6498(2005).

Comments

FUNCTION: Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities (By similarity).
CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH.
CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H₂O.
CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
PATHWAY: Lipid metabolism; fatty acid beta-oxidation .
SUBUNIT: Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) (By similarity).
SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000058; AAZ34330.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_275370.1; -.

3D structure databases

SMR

Q48GW3; 1-715.

ModBase

Q48GW3.

Ontologies

GO:0003857;	Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0008692;	Molecular function: 3-hydroxybutyryl-CoA epimerase activity (inferred from electronic annotation from HAMAP).
GO:0004165;	Molecular function: dodecenoyl-CoA delta-isomerase activity (inferred from electronic annotation from HAMAP).
GO:0004300;	Molecular function: enoyl-CoA hydratase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01621; -; 1.
PBIL [Tree]

InterPro

IPR006180; 3-OHacyl-CoA_DHase_CS.
IPR006176; 3-OHacyl-CoA_DHase_NAD-bd.
IPR006108; 3HC_DHase_C.
IPR001753; Crotonase_core.
IPR013328; DHase_multihelical.
IPR012799; FadB.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.

Pfam

PF00725; 3HCDH; 1.
PF02737; 3HCDH_N; 1.
PF00378; ECH; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02437; FadB; 1.

PROSITE

PS00067; 3HCDH; 1.
PS00166; ENOYL_COA_HYDRATASE; FALSE_NEG.

Genome annotation databases

GeneID

3556880; -.

GenomeReviews

CP000058_GR; PSPPH_3210.

KEGG

psp:PSPPH_3210; -.

NMPDR

fig|264730.3.peg.3186; -.

Phylogenomic databases

HOGENOM

Q48GW3; -.

Genome annotation databases

CMR

Q48GW3; PSPPH_3210.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Fatty acid metabolism; Isomerase; Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 721`	`721`	`Fatty acid oxidation complex subunit alpha.`	`PRO_0000109280`
`REGION`	`1 190`	`190`	`Enoyl-CoA hydratase/isomerase (By similarity).`
`REGION`	`312 721`	`410`	`3-hydroxyacyl-CoA dehydrogenase (By similarity).`

Sequence information

Length: 721 AA [This is the length of the unprocessed precursor]

Molecular weight: 77630 Da [This is the MW of the unprocessed precursor]

CRC64: C66C6B34D3EFFC89 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIYEGKAITV KALESGIVEL NFDLKGESVN KFNRLTLNEL RQAVDAIKAD ASVKGVIVSS 

        70         80         90        100        110        120 
GKDVFIVGAD ITEFVDNFKL PEAELVAGNL QANRIFSDFE DLGVPTVVAI NGIALGGGLE 

       130        140        150        160        170        180 
MCLAADYRVI SSSARIGLPE VKLGLYPGFG GTVRLPRIIG ADNAIEWIAS GKESSAEDAL 

       190        200        210        220        230        240 
KVGAVDAVVA PEKLQAAALD LIQRAISGEF DYKAKRQPKL DKLKLNAIEQ MMAFETAKGF 

       250        260        270        280        290        300 
VAGQAGPNYP APVEAIKTIQ KAANFGRDKA LEIEAAGFVK MAKTSAAQSL IGLFLNDQEL 

       310        320        330        340        350        360 
KKKAKGYDAV AKDVKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI QLGLNEASKL 

       370        380        390        400        410        420 
LGGRLEKGRL TAAKMAEALN AIRPTLSYGD FGNVDLVVEA VVENPKVKQA VLAEVEANVG 

       430        440        450        460        470        480 
EHTILASNTS TISISLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SEEAVATTVA 

       490        500        510        520        530        540 
YARKMGKNPI VVNDCPGFLV NRVLFPYFGG FARLVSAGVD FVRIDKVMEK FGWPMGPAYL 

       550        560        570        580        590        600 
MDVVGIDTGH HGRDVMAEGF PDRMKDDRRS VVDALYEAKR LGQKNGKGFY AYETDKKGKP 

       610        620        630        640        650        660 
KKVNDPAVLD VLKPIVYEQR EVSDEDIINW MMIPLCLETV RCLEDGIVET AAEADMGLIY 

       670        680        690        700        710        720 
GIGFPPFRGG ALRYIDSIGV AEFVALADQY AELGALYQPT AKLREMASKG QSFFGQASSE 


E

Q48GW3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools