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Q820V5 (FABI_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismEnterococcus faecalis (strain ATCC 700802 / V583) [Reference proteome] [HAMAP]
Taxonomic identifier226185 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceInferred 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

An acyl-[acyl-carrier protein] + NAD+ = a 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000407977

Regions

Nucleotide binding18 – 192NAD By similarity
Nucleotide binding61 – 622NAD By similarity
Nucleotide binding188 – 1925NAD By similarity

Sites

Active site1421Proton acceptor By similarity
Active site1521Proton acceptor By similarity
Binding site121NAD; via carbonyl oxygen By similarity
Binding site391NAD By similarity
Binding site891NAD; via carbonyl oxygen By similarity
Binding site921Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1591NAD By similarity
Site1971Involved in acyl-ACP binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q820V5 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A0A4DA491D22F78E

FASTA25026,767
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016830 Genomic DNA. Translation: AAO80145.1.
RefSeqNP_814074.1. NC_004668.1.

3D structure databases

ProteinModelPortalQ820V5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226185.EF0282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO80145; AAO80145; EF_0282.
GeneID1199200.
KEGGefa:EF0282.
PATRIC21851013. VBIEntFae7065_0260.

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMACFATIKE.
OrthoDBEOG6HF644.

Enzyme and pathway databases

BioCycEFAE226185:GHI1-289-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Entry information

Entry nameFABI_ENTFA
AccessionPrimary (citable) accession number: Q820V5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways