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:	YPO3766, y0464, YP_3282

From

Yersinia pestis

[TaxID: 632]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Yersinia.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CO-92 / Biovar Orientalis; DOI=10.1038/35097083; PubMed=11586360 [NCBI, ExPASy, EBI, Israel, Japan] Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.; "Genome sequence of Yersinia pestis, the causative agent of plague."; Nature 413:523-527(2001).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=KIM5 / Biovar Mediaevalis; DOI=10.1128/JB.184.16.4601-4611.2002; PubMed=12142430 [NCBI, ExPASy, EBI, Israel, Japan] Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.; "Genome sequence of Yersinia pestis KIM."; J. Bacteriol. 184:4601-4611(2002).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=91001 / Biovar Mediaevalis; DOI=10.1093/dnares/11.3.179; PubMed=15368893 [NCBI, ExPASy, EBI, Israel, Japan] Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.; "Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."; DNA Res. 11:179-197(2004).

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

AL590842; CAL22353.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE009952; AAM84053.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017042; AAS63449.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AF0458; AF0458.

RefSeq

NP_667802.1; -.
NP_994572.1; -.

3D structure databases

HSSP

P00348; 3HDH. [HSSP ENTRY / PDB]

ModBase

Q8ZAN0.

Enzyme and pathway databases

BioCyc

YPES187410:Y0464-MON; -.
YPES214092:YPO3766-MON; -.
YPES229193:YP3282-MON; -.

Ontologies

GO:0016507;	Cellular component: fatty acid beta-oxidation multienzyme complex (inferred from electronic annotation from InterPro).
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:0050662;	Molecular function: coenzyme binding (inferred from electronic annotation from InterPro).
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:0009062;	Biological process: fatty acid catabolic process (inferred from electronic annotation from InterPro).
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; 1.

ProtoNet

Q8ZAN0.

Genome annotation databases

GeneID

1145411; -.
2764613; -.

GenomeReviews

AE009952_GR; y0464.
AE017042_GR; YP_3282.
AL590842_GR; YPO3766.

KEGG

ype:YPO3766; -.
ypk:y0464; -.
ypm:YP_3282; -.

Phylogenomic databases

HOGENOM

Q8ZAN0; -.

Genome annotation databases

CMR

Q8ZAN0; YPO3766.

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_0000109295`
`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: 78826 Da [This is the MW of the unprocessed precursor]

CRC64: 2C534B2963B09491 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLYQSETLQL HWLENGIAEL VFDAPGSVNK LDTKTVANLG EALNVLEKQS ELKGLLLRSA 

        70         80         90        100        110        120 
KTALIVGADI TEFLSLFNAP PEKLHQWLVF ANTIFNRLED LPVPTISAIN GYALGGGCEC 

       130        140        150        160        170        180 
ILATDFRIAS PEARIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIATG KDVTANDALK 

       190        200        210        220        230        240 
IGLVDAVVDP EKLVGSALTM LKQAIDGKLD WQAARRPKLE PLKLNPTEAA MCFTIAKGRV 

       250        260        270        280        290        300 
MQVAGKHYPA PLTAVKTIEA AAKFGRTEAL NLETNSFVPL AGSNEARALV GIFLNDQYVK 

       310        320        330        340        350        360 
AQAKKLSKGV AAPKLAAVLG AGIMGGGIAY QSALKSVPVI MKDINENSLD LGMNEAAKLL 

       370        380        390        400        410        420 
NKQLERGKVD GLKMASILAT IRPTLDYAGI ERAQVIVEAV VENPKVKAAV LAEVEALIGE 

       430        440        450        460        470        480 
DTVLASNTST IPIDQLAKSL KRPENFCGMH FFNPVHRMPL VEIIRGAKTS DKTLAAVVAY 

       490        500        510        520        530        540 
ATQMGKTPIV VNDCPGFFVN RVLFPYLAGF GMLVRDGGDF HQIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PERMNKDYRD AVDVMFDNQR FGQKNGQGFY RYTQDAKGKP 

       610        620        630        640        650        660 
RKENDEQVDK LLAEISQPLQ EFSDEDIIAR TMIPMINEVV RCLEEGIIAS AAEGDMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG VFRYLDTLGS ANYVEMAQRY AHLGALYHVP AGLRAKAEHN ESYYPVAAAL 


LDVSTNQPA

Q8ZAN0 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