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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 2

Gene

fabF

Organism
Staphylococcus aureus (strain COL)
Status
Reviewed-Annotation score: Annotation score: 2 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.By similarity

Catalytic activityi

(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

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)DescriptionActionsGraphical viewLength
Active sitei165PROSITE-ProRule annotation1

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

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC:2.3.1.179)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
Short name:
KAS II
Gene namesi
Name:fabF
Ordered Locus Names:SACOL0988
OrganismiStaphylococcus aureus (strain COL)
Taxonomic identifieri93062 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000530 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001803201 – 4143-oxoacyl-[acyl-carrier-protein] synthase 2Add BLAST414

Proteomic databases

PRIDEiQ5HHA1.

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL0988.

Structurei

Secondary structure

1414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 1610
Beta strandi19 – 213
Helixi22 – 309
Beta strandi36 – 383
Beta strandi51 – 533
Helixi60 – 623
Turni67 – 715
Helixi74 – 9017
Turni96 – 983
Helixi99 – 1013
Beta strandi102 – 1076
Helixi113 – 12614
Helixi128 – 1303
Helixi135 – 1395
Helixi143 – 15210
Beta strandi156 – 1594
Helixi164 – 1663
Helixi167 – 18014
Beta strandi185 – 1939
Helixi198 – 2069
Turni216 – 2183
Beta strandi235 – 2439
Helixi244 – 2507
Beta strandi256 – 26510
Beta strandi270 – 2723
Helixi275 – 2773
Helixi278 – 29114
Helixi295 – 2973
Beta strandi300 – 3023
Helixi309 – 32315
Helixi324 – 3274
Beta strandi331 – 3333
Helixi336 – 3394
Helixi343 – 3453
Helixi346 – 36015
Beta strandi382 – 3843
Beta strandi391 – 3988
Helixi400 – 4023
Beta strandi403 – 4108

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GQDX-ray2.30A1-414[»]
ProteinModelPortaliQ5HHA1.
SMRiQ5HHA1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5HHA1.

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-ketoacyl-ACP synthases family.Curated

Phylogenomic databases

eggNOGiENOG4105C0Q. Bacteria.
COG0304. LUCA.
HOGENOMiHOG000060166.
KOiK09458.
OMAiQKASRPY.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR017568. 3-oxoacyl-ACP_synth-2.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000447. KAS_II. 1 hit.
SMARTiSM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR03150. fabF. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5HHA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQNKRVVIT GMGALSPIGN DVKTTWENAL KGVNGIDKIT RIDTEPYSVH
60 70 80 90 100
LAGELKNFNI EDHIDKKEAR RMDRFTQYAI VAAREAVKDA QLDINENTAD
110 120 130 140 150
RIGVWIGSGI GGMETFEIAH KQLMDKGPRR VSPFFVPMLI PDMATGQVSI
160 170 180 190 200
DLGAKGPNGA TVTACATGTN SIGEAFKIVQ RGDADAMITG GTEAPITHMA
210 220 230 240 250
IAGFSASRAL STNDDIETAC RPFQEGRDGF VMGEGAGILV IESLESAQAR
260 270 280 290 300
GANIYAEIVG YGTTGDAYHI TAPAPEGEGG SRAMQAAMDD AGIEPKDVQY
310 320 330 340 350
LNAHGTSTPV GDLNEVKAIK NTFGEAAKHL KVSSTKSMTG HLLGATGGIE
360 370 380 390 400
AIFSALSIKD SKVAPTIHAV TPDPECDLDI VPNEAQDLDI TYAMSNSLGF
410
GGHNAVLVFK KFEA
Length:414
Mass (Da):43,739
Last modified:February 15, 2005 - v1
Checksum:i2DB06BB5DD48D175
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW36456.1.
RefSeqiWP_000081240.1. NC_002951.2.

Genome annotation databases

EnsemblBacteriaiAAW36456; AAW36456; SACOL0988.
GeneIDi28381472.
KEGGisac:SACOL0988.
PATRICi19528216. VBIStaAur112458_0963.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW36456.1.
RefSeqiWP_000081240.1. NC_002951.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GQDX-ray2.30A1-414[»]
ProteinModelPortaliQ5HHA1.
SMRiQ5HHA1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL0988.

Proteomic databases

PRIDEiQ5HHA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW36456; AAW36456; SACOL0988.
GeneIDi28381472.
KEGGisac:SACOL0988.
PATRICi19528216. VBIStaAur112458_0963.

Phylogenomic databases

eggNOGiENOG4105C0Q. Bacteria.
COG0304. LUCA.
HOGENOMiHOG000060166.
KOiK09458.
OMAiQKASRPY.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

EvolutionaryTraceiQ5HHA1.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR017568. 3-oxoacyl-ACP_synth-2.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000447. KAS_II. 1 hit.
SMARTiSM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR03150. fabF. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABF_STAAC
AccessioniPrimary (citable) accession number: Q5HHA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 82 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, Complete proteome

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.