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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 3

Gene

fabH

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.UniRule annotation

Catalytic activityi

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2.UniRule annotation

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
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
Active sitei112 – 1121UniRule annotation
Active sitei238 – 2381UniRule annotation
Active sitei268 – 2681UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-947-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3UniRule annotation (EC:2.3.1.180UniRule annotation)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase IIIUniRule annotation
Beta-ketoacyl-ACP synthase IIIUniRule annotation
Short name:
KAS IIIUniRule annotation
Gene namesi
Name:fabHUniRule annotation
Ordered Locus Names:SAR0946
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3133133-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110471Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Beta strandi14 – 185Combined sources
Helixi19 – 246Combined sources
Helixi30 – 378Combined sources
Beta strandi40 – 445Combined sources
Helixi51 – 6515Combined sources
Helixi70 – 723Combined sources
Beta strandi75 – 795Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 989Combined sources
Beta strandi104 – 1096Combined sources
Helixi111 – 1133Combined sources
Helixi114 – 12714Combined sources
Beta strandi134 – 1418Combined sources
Helixi142 – 1454Combined sources
Helixi151 – 1544Combined sources
Beta strandi159 – 16810Combined sources
Beta strandi174 – 1829Combined sources
Helixi184 – 1896Combined sources
Beta strandi190 – 1923Combined sources
Turni194 – 1963Combined sources
Beta strandi199 – 2013Combined sources
Helixi203 – 22422Combined sources
Turni229 – 2313Combined sources
Beta strandi233 – 2375Combined sources
Helixi242 – 25211Combined sources
Helixi256 – 2583Combined sources
Helixi263 – 2664Combined sources
Helixi270 – 2723Combined sources
Helixi273 – 28311Combined sources
Beta strandi292 – 2998Combined sources
Turni300 – 3023Combined sources
Beta strandi303 – 3108Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IL7X-ray2.60A/B1-313[»]
ProteinModelPortaliQ6GIA4.
SMRiQ6GIA4. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6GIA4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni239 – 2435ACP-bindingUniRule annotation

Domaini

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.UniRule annotation

Sequence similaritiesi

Belongs to the FabH family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000246674.
KOiK00648.
OMAiMNGREVY.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH. 1 hit.
InterProiIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
TIGRFAMsiTIGR00747. fabH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6GIA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVGIKGFGA YAPEKIIDNA YFEQFLDTSD EWISKMTGIK ERHWADDDQD
60 70 80 90 100
TSDLAYEASV KAIADAGIQP EDIDMIIVAT ATGDMPFPTV ANMLQERLGT
110 120 130 140 150
GKVASMDQLA ACSGFMYSMI TAKQYVQSGD YHNILVVGAD KLSKITDLTD
160 170 180 190 200
RSTAVLFGDG AGAVIIGEVS EGRGIISYEM GSDGTGGKHL YLDKDTGKLK
210 220 230 240 250
MNGREVFKFA VRIMGDASTR VVEKANLTSD DIDLFIPHQA NIRIMESARE
260 270 280 290 300
RLGISKDKMS VSVNKYGNTS AASIPLSIDQ ELKNGKLKDD DTIVLVGFGG
310
GLTWGAMTIK WGK
Length:313
Mass (Da):33,879
Last modified:July 19, 2004 - v1
Checksum:i728D2DCCAB9B95F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG39952.1.
RefSeqiWP_001100526.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG39952; CAG39952; SAR0946.
KEGGisar:SAR0946.
PATRICi19545425. VBIStaAur71814_0945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG39952.1.
RefSeqiWP_001100526.1. NC_002952.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IL7X-ray2.60A/B1-313[»]
ProteinModelPortaliQ6GIA4.
SMRiQ6GIA4. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG39952; CAG39952; SAR0946.
KEGGisar:SAR0946.
PATRICi19545425. VBIStaAur71814_0945.

Phylogenomic databases

HOGENOMiHOG000246674.
KOiK00648.
OMAiMNGREVY.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciSAUR282458:GJA5-947-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ6GIA4.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH. 1 hit.
InterProiIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
TIGRFAMsiTIGR00747. fabH. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFABH_STAAR
AccessioniPrimary (citable) accession number: Q6GIA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 19, 2004
Last modified: September 7, 2016
This is version 84 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, Multifunctional enzyme

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.