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
	Synonyms:	oldB
	OrderedLocusNames:	Z5367, ECs4774

From

Escherichia coli O157:H7

[TaxID: 83334]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).

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. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (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

AE005174; AAG59040.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB38197.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D86072; D86072.
F91225; F91225.

RefSeq

NP_290476.1; -.
NP_312801.1; -.

3D structure databases

HSSP

P00348; 3HDH. [HSSP ENTRY / PDB]

ModBase

Q8X8I2.

Enzyme and pathway databases

BioCyc

ECOL83334:ECS4774-MON; -.

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; 2.
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; 1.

Genome annotation databases

GeneID

915128; -.
960314; -.

GenomeReviews

BA000007_GR; ECs4774.
AE005174_GR; Z5367.

KEGG

ece:Z5367; -.
ecs:ECs4774; -.

Phylogenomic databases

HOGENOM

Q8X8I2; -.

Genome annotation databases

CMR

Q8X8I2; Z5367.

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`	`1 729`	`729`	`Fatty acid oxidation complex subunit alpha.`	`PRO_0000109269`
`REGION`	`1 189`	`189`	`Enoyl-CoA hydratase/isomerase (By similarity).`
`REGION`	`311 729`	`419`	`3-hydroxyacyl-CoA dehydrogenase (By similarity).`

Sequence information

Length: 729 AA [This is the length of the unprocessed precursor]

Molecular weight: 79559 Da [This is the MW of the unprocessed precursor]

CRC64: C13EBBFFFA749183 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN 

        70         80         90        100        110        120 
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC 

       130        140        150        160        170        180 
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK 

       190        200        210        220        230        240 
IGLVDGVVKA EKLIEGAMAI LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV 

       250        260        270        280        290        300 
AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK 

       310        320        330        340        350        360 
GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLA LGMTEAAKLL 

       370        380        390        400        410        420 
NKQLERGKID GLKLAGVIST IHPTLDYAGF ERVDVVVEAI VENPKVKKAV LAETEQKVRP 

       430        440        450        460        470        480 
DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW HYKEDSKGKP 

       610        620        630        640        650        660 
KKEEDAAVDD LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA 


RPVGDLKTA

Q8X8I2 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