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Protein

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

Gene

fabH

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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. Has some substrate preference for butyryl- and isobutyryl-CoA. Its substrate specificity determines the biosynthesis of branched-chain of fatty acids.1 Publication

Catalytic activityi

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

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
Active sitei112 – 1121By similarity
Active sitei238 – 2381By similarity
Active sitei268 – 2681By similarity

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

BioCyciSAUR158878:GJJ5-1001-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC:2.3.1.180)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III
Beta-ketoacyl-ACP synthase III
Short name:
KAS III
SaFabH
Gene namesi
Name:fabH
Ordered Locus Names:SAV0983
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3673.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3133133-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110469Add
BLAST

Proteomic databases

PaxDbiP68795.

2D gel databases

World-2DPAGE0002:P68795.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi158878.SAV0983.

Structurei

3D structure databases

ProteinModelPortaliP68795.
SMRiP68795. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni239 – 2435ACP-bindingBy similarity

Domaini

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

Sequence similaritiesi

Belongs to the FabH family.Curated

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
KOiK00648.
OMAiMNGREVY.
PhylomeDBiP68795.

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.

P68795-1 [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:December 21, 2004 - v1
Checksum:i728D2DCCAB9B95F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57145.1.
RefSeqiWP_001100526.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57145; BAB57145; SAV0983.
KEGGisav:SAV0983.
PATRICi19562657. VBIStaAur52173_1009.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57145.1.
RefSeqiWP_001100526.1. NC_002758.2.

3D structure databases

ProteinModelPortaliP68795.
SMRiP68795. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV0983.

Chemistry

ChEMBLiCHEMBL3673.

2D gel databases

World-2DPAGE0002:P68795.

Proteomic databases

PaxDbiP68795.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB57145; BAB57145; SAV0983.
KEGGisav:SAV0983.
PATRICi19562657. VBIStaAur52173_1009.

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
KOiK00648.
OMAiMNGREVY.
PhylomeDBiP68795.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciSAUR158878:GJJ5-1001-MONOMER.

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_STAAM
AccessioniPrimary (citable) accession number: P68795
Secondary accession number(s): Q99VA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: September 7, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Inhibited by the HR12 (5-chloro-4-phenyl-[1,2]-dithiol-3-one) and HR19 (4-phenyl-5-phenylimino-[1,2,4]dithiazolidin-3-one) antibiotics. Weakly inhibited by thiolactomycin.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.