Q820V5 (FABI_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
Short name=ENR
EC=1.3.1.9

Alternative name(s):
NADH-dependent enoyl-ACP reductase

Gene names

Name:	fabI
Ordered Locus Names:	EF_0282

Organism

Enterococcus faecalis (strain ATCC 700802 / V583) [Reference proteome] [HAMAP]

Taxonomic identifier

226185 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Enterococcaceae › Enterococcus › Enterococcus faecalis

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism By similarity.
Catalytic activity	Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Enzyme regulation	Inhibited by triclosan and its diphenyl ether analgues. Ref.2
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid elongation Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 250	250	Enoyl-[acyl-carrier-protein] reductase [NADH] FabI		PRO_0000407977
Regions
	Nucleotide binding	18 – 19	2	NAD By similarity
	Nucleotide binding	61 – 62	2	NAD By similarity
	Nucleotide binding	188 – 192	5	NAD By similarity
Sites
	Active site	142	1	Proton acceptor By similarity
	Active site	152	1	Proton acceptor By similarity
	Binding site	12	1	NAD; via carbonyl oxygen By similarity
	Binding site	39	1	NAD By similarity
	Binding site	89	1	NAD; via carbonyl oxygen By similarity
	Binding site	92	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	159	1	NAD By similarity
	Site	197	1	Involved in acyl-ACP binding By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q820V5 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A0A4DA491D22F78E	FASTA	250	26,767
	10 20 30 40 50 60 MFLQNKNVVV MGVANKKSIA WGCAKALKDQ GANVIYTYQN ERMKKQVVKL ADENDLLVEC 70 80 90 100 110 120 DVASDASIQA AFETIKNEVG TIDGLVHAIA FAKKEELSGN VSDITRDGFL LAQDISSYSL 130 140 150 160 170 180 LAVTHYAKPL LNPGSGIVTL TYLGSERAIP NYNMMGIAKA SLETAVKYLA FELAADKIRV 190 200 210 220 230 240 NGISAGAIKT LAVTGVKDYD QLISISNERT PDKTGVTIEE VGNTCAFLVS DLASGVVGDI 250 IYVDKGVHLT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis." Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M. Science 299:2071-2074(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700802 / V583.
[2]	"Mechanism and inhibition of saFabI, the enoyl reductase from Staphylococcus aureus." Xu H., Sullivan T.J., Sekiguchi J., Kirikae T., Ojima I., Stratton C.F., Mao W., Rock F.L., Alley M.R., Johnson F., Walker S.G., Tonge P.J. Biochemistry 47:4228-4236(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016830 Genomic DNA. Translation: AAO80145.1.
RefSeq	NP_814074.1. NC_004668.1.
3D structure databases
HSSP	HSSP built from PDB template 1DFI based on UniProtKB P29132.
ProteinModelPortal	Q820V5.
ModBase	Search...
Protein-protein interaction databases
STRING	226185.EF0282.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO80145; AAO80145; EF_0282.
GeneID	1199200.
KEGG	efa:EF0282.
PATRIC	21851013. VBIEntFae7065_0260.
Phylogenomic databases
eggNOG	COG0623.
KO	K00208.
OMA	DCDVGSD.
ProtClustDB	PRK06079.
Enzyme and pathway databases
BioCyc	EFAE226185:GHI1-416-MONOMER.
UniPathway	UPA00094.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR014358. Enoyl-ACP_Rdtase_NADH. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
PIRSF	PIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTS	PR00081. GDHRDH.
ProtoNet	Search...

Entry information

Entry name

FABI_ENTFA

Accession

Primary (citable) accession number: Q820V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 3, 2011
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program