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Protein

Enoyl-[acyl-carrier-protein] reductase [NADPH] FabI

Gene

fabI

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131NADP; via carbonyl oxygen1 Publication
Sitei40 – 401Critical for cofactor specificityBy similarity
Sitei41 – 411Critical for cofactor specificityBy similarity
Binding sitei94 – 941NADP; via carbonyl oxygen1 Publication
Binding sitei97 – 971Substrate; via amide nitrogen and carbonyl oxygenBy similarity
Active sitei147 – 1471Proton acceptorBy similarity
Active sitei157 – 1571Proton acceptorBy similarity
Binding sitei164 – 1641NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 202NADP1 Publication
Nucleotide bindingi40 – 445NADP1 Publication
Nucleotide bindingi66 – 672NADP1 Publication
Nucleotide bindingi193 – 1975NADP1 Publication

GO - Molecular functioni

GO - Biological processi

  • fatty acid elongation Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-978-MONOMER.
BRENDAi1.3.1.39. 3352.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADPH] FabI (EC:1.3.1.39)
Short name:
ENR
Alternative name(s):
NADPH-dependent enoyl-ACP reductase
Gene namesi
Name:fabI
Ordered Locus Names:SAR0978
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3994.
DrugBankiDB08604. Triclosan.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Enoyl-[acyl-carrier-protein] reductase [NADPH] FabIPRO_0000407979Add
BLAST

Proteomic databases

PRIDEiQ6GI75.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Chemistry

BindingDBiQ6GI75.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Beta strandi16 – 183Combined sources
Helixi20 – 3011Combined sources
Beta strandi34 – 418Combined sources
Helixi42 – 443Combined sources
Helixi45 – 528Combined sources
Helixi53 – 553Combined sources
Beta strandi61 – 644Combined sources
Helixi70 – 8415Combined sources
Beta strandi88 – 925Combined sources
Helixi99 – 1024Combined sources
Helixi106 – 1083Combined sources
Helixi111 – 12111Combined sources
Helixi123 – 13311Combined sources
Beta strandi140 – 1467Combined sources
Helixi148 – 1503Combined sources
Turni155 – 1573Combined sources
Helixi158 – 17821Combined sources
Helixi179 – 1813Combined sources
Beta strandi183 – 1908Combined sources
Helixi196 – 1983Combined sources
Helixi204 – 21411Combined sources
Helixi223 – 23412Combined sources
Helixi236 – 2383Combined sources
Beta strandi245 – 2495Combined sources
Helixi252 – 2543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GNSX-ray2.71A1-256[»]
3GNTX-ray2.75A/B1-256[»]
3GR6X-ray2.28A/D/G/J1-256[»]
4FS3X-ray1.80A1-256[»]
ProteinModelPortaliQ6GI75.
SMRiQ6GI75. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6GI75.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK00208.
OMAiSACKREG.
OrthoDBiEOG6HF644.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PTHR24322:SF317. PTHR24322:SF317. 2 hits.
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6GI75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNLENKTYV IMGIANKRSI AFGVAKVLDQ LGAKLVFTYR KERSRKELEK
60 70 80 90 100
LLEQLNQPEA HLYQIDVQSD EEVINGFEQI GKDVGNIDGV YHSIAFANME
110 120 130 140 150
DLRGRFSETS REGFLLAQDI SSYSLTIVAH EAKKLMPEGG SIVATTYLGG
160 170 180 190 200
EFAVQNYNVM GVAKASLEAN VKYLALDLGP DNIRVNAISA GPIRTLSAKG
210 220 230 240 250
VGGFNTILKE IEERAPLKRN VDQVEVGKTA AYLLSDLSSG VTGENIHVDS

GFHAIK
Length:256
Mass (Da):27,992
Last modified:July 19, 2004 - v1
Checksum:i69487F3F410B9A15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG39983.1.
RefSeqiWP_000933195.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG39983; CAG39983; SAR0978.
KEGGisar:SAR0978.
PATRICi19545491. VBIStaAur71814_0978.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG39983.1.
RefSeqiWP_000933195.1. NC_002952.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GNSX-ray2.71A1-256[»]
3GNTX-ray2.75A/B1-256[»]
3GR6X-ray2.28A/D/G/J1-256[»]
4FS3X-ray1.80A1-256[»]
ProteinModelPortaliQ6GI75.
SMRiQ6GI75. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ6GI75.
ChEMBLiCHEMBL3994.
DrugBankiDB08604. Triclosan.

Proteomic databases

PRIDEiQ6GI75.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG39983; CAG39983; SAR0978.
KEGGisar:SAR0978.
PATRICi19545491. VBIStaAur71814_0978.

Phylogenomic databases

KOiK00208.
OMAiSACKREG.
OrthoDBiEOG6HF644.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciSAUR282458:GJA5-978-MONOMER.
BRENDAi1.3.1.39. 3352.

Miscellaneous databases

EvolutionaryTraceiQ6GI75.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PTHR24322:SF317. PTHR24322:SF317. 2 hits.
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MRSA252.
  2. "Structural insights into Staphylococcus aureus enoyl-ACP reductase (FabI), in complex with NADP and triclosan."
    Priyadarshi A., Kim E.E., Hwang K.Y.
    Proteins 78:480-486(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH NADP AND INHIBITOR, SUBUNIT.

Entry informationi

Entry nameiFABI_STAAR
AccessioniPrimary (citable) accession number: Q6GI75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: July 19, 2004
Last modified: April 13, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.