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:	VC0395_A2534

From

Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395)

[TaxID: 345073]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Heidelberg J.; Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.

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

CP000627; ABQ19542.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001218427.1; -.

3D structure databases

ModBase

A5F465.

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.
IPR012799; FadB.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 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

5136027; -.

GenomeReviews

CP000627_GR; VC0395_A2534.

KEGG

vco:VC0395_A2534; -.

CMR

A5F465; VC0395_A2534.

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`	`1 723`	`723`	`Fatty acid oxidation complex subunit alpha.`	`PRO_1000073635`
`REGION`	`1 189`	`189`	`Enoyl-CoA hydratase/isomerase (By similarity).`
`REGION`	`312 723`	`412`	`3-hydroxyacyl-CoA dehydrogenase (By similarity).`

Sequence information

Length: 723 AA [This is the length of the unprocessed precursor]

Molecular weight: 78076 Da [This is the MW of the unprocessed precursor]

CRC64: 9E512BE6A218C80D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIYQAKTLQV KQLANGIAEL SFCAPASVNK LDLHTLESLD KALDALAADS SVKGLLLSSD 

        70         80         90        100        110        120 
KEAFIVGADI TEFLGLFAKP EAELDEWLQF ANRIFNKLED LPFPTLSALK GHTLGGGCEC 

       130        140        150        160        170        180 
VLATDFRIGD ATTSIGLPET KLGIMPGFGG TVRLPRLIGA DSAMEIITQG KACRAEEALK 

       190        200        210        220        230        240 
VGLLDAIVDS DKLIDSAITT LTQAIEEKLD WQKRRQQKTS ALTLSKLEAM MSFTMAKGMV 

       250        260        270        280        290        300 
AQVAGKHYPA PMTSVVTIEE AARLPRDAAL DIERKHFIKL AKSTEAQALV GIFLNDQYIK 

       310        320        330        340        350        360 
GLAKQSAKAA SQDTQHAAVL GAGIMGGGIA YQSALKGVPV LMKDIAPHSL ELGMTEAAKL 

       370        380        390        400        410        420 
LNKQLERGKI DGFKMAGILA SITPSLHYAG IDQADVIVEA VVENPKVKAA VLSEVEGLVD 

       430        440        450        460        470        480 
AETILTSNTS TIPINLLAKS LKRPQNFCGM HFFNPVHRMP LVEIIRGEHT SEDTINRVVA 

       490        500        510        520        530        540 
YAAKMGKSPI VVNDCPGFFV NRVLFPYFAG FSLLMRDGAN FTEIDKVMER QFGWPMGPAY 

       550        560        570        580        590        600 
LLDVVGIDTA HHAQAVMAEG FPTRMAKSGR EAIDALYEAK KFGQKNGSGF YQYTVDKKGK 

       610        620        630        640        650        660 
PKKAFSDDVL AILAPVCGAP QNFDPQTLIE RTMIPMINEV VLCLEEGIIA SAQEADMALV 

       670        680        690        700        710        720 
YGLGFPPFRG GVFRYLDTIG IANYVAMAEK YADLGALYQV PQLLKNMAQQ GTSFYSAQQA 


SAL

A5F465 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