Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

fabF

Organism
Bacillus subtilis (strain 168)
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.1 Publication

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].

Enzyme regulationi

Inhibited by cerulenin.1 Publication

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 sitei164PROSITE-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

BioCyciBSUB:BSU11340-MONOMER.
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
Synonyms:yjaY
Ordered Locus Names:BSU11340
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003608461 – 4133-oxoacyl-[acyl-carrier-protein] synthase 2Add BLAST413

Proteomic databases

PaxDbiO34340.
PRIDEiO34340.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006266.

Structurei

Secondary structure

1413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 15Combined sources10
Beta strandi18 – 20Combined sources3
Helixi21 – 29Combined sources9
Beta strandi35 – 37Combined sources3
Helixi43 – 45Combined sources3
Beta strandi50 – 52Combined sources3
Helixi59 – 61Combined sources3
Helixi65 – 68Combined sources4
Helixi73 – 89Combined sources17
Turni95 – 97Combined sources3
Helixi98 – 100Combined sources3
Beta strandi101 – 106Combined sources6
Helixi112 – 125Combined sources14
Helixi127 – 129Combined sources3
Helixi134 – 138Combined sources5
Helixi142 – 151Combined sources10
Beta strandi155 – 158Combined sources4
Helixi163 – 165Combined sources3
Helixi166 – 179Combined sources14
Beta strandi184 – 192Combined sources9
Helixi197 – 205Combined sources9
Turni215 – 217Combined sources3
Beta strandi234 – 242Combined sources9
Helixi243 – 248Combined sources6
Beta strandi255 – 264Combined sources10
Beta strandi269 – 271Combined sources3
Helixi274 – 276Combined sources3
Helixi277 – 290Combined sources14
Helixi294 – 296Combined sources3
Beta strandi299 – 301Combined sources3
Helixi308 – 322Combined sources15
Helixi323 – 327Combined sources5
Beta strandi329 – 332Combined sources4
Helixi335 – 338Combined sources4
Helixi342 – 344Combined sources3
Helixi345 – 359Combined sources15
Beta strandi370 – 372Combined sources3
Beta strandi381 – 383Combined sources3
Beta strandi390 – 398Combined sources9
Turni399 – 401Combined sources3
Beta strandi402 – 409Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LS5X-ray1.80A/B1-413[»]
4LS6X-ray1.56A/B1-413[»]
4LS7X-ray1.67A/B1-413[»]
4LS8X-ray2.10A/B1-413[»]
ProteinModelPortaliO34340.
SMRiO34340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0Q. Bacteria.
COG0304. LUCA.
HOGENOMiHOG000060166.
InParanoidiO34340.
KOiK09458.
OMAiQKASRPY.
PhylomeDBiO34340.

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.

O34340-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKRVVVTG LGALSPLGND VDTSWNNAIN GVSGIGPITR VDAEEYPAKV
60 70 80 90 100
AAELKDFNVE DYMDKKEARK MDRFTQYAVV AAKMAVEDAD LNITDEIAPR
110 120 130 140 150
VGVWVGSGIG GLETLESQFE IFLTKGPRRV SPFFVPMMIP DMATGQISIA
160 170 180 190 200
LGAKGVNSCT VTACATGTNS IGDAFKVIQR GDADVMVTGG TEAPLTRMSF
210 220 230 240 250
AGFSANKALS TNPDPKTASR PFDKNRDGFV MGEGAGIIVL EELEHALARG
260 270 280 290 300
AKIYGEIVGY GSTGDAYHIT APAQDGEGGA RAMQEAIKDA GIAPEEIDYI
310 320 330 340 350
NAHGTSTYYN DKYETMAIKT VFGEHAHKLA VSSTKSMTGH LLGAAGGIEA
360 370 380 390 400
IFSILAIKEG VIPPTINIQT PDEECDLDYV PDEARRQELN YVLSNSLGFG
410
GHNATLIFKK YQS
Length:413
Mass (Da):44,005
Last modified:January 1, 1998 - v1
Checksum:i4667233C9E855740
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti109I → F in strain: GS77; resistant to cerulenin. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12975.1.
PIRiG69842.
RefSeqiNP_389016.1. NC_000964.3.
WP_003244890.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB12975; CAB12975; BSU11340.
GeneIDi939803.
KEGGibsu:BSU11340.
PATRICi18973980. VBIBacSub10457_1184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12975.1.
PIRiG69842.
RefSeqiNP_389016.1. NC_000964.3.
WP_003244890.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LS5X-ray1.80A/B1-413[»]
4LS6X-ray1.56A/B1-413[»]
4LS7X-ray1.67A/B1-413[»]
4LS8X-ray2.10A/B1-413[»]
ProteinModelPortaliO34340.
SMRiO34340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006266.

Proteomic databases

PaxDbiO34340.
PRIDEiO34340.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12975; CAB12975; BSU11340.
GeneIDi939803.
KEGGibsu:BSU11340.
PATRICi18973980. VBIBacSub10457_1184.

Phylogenomic databases

eggNOGiENOG4105C0Q. Bacteria.
COG0304. LUCA.
HOGENOMiHOG000060166.
InParanoidiO34340.
KOiK09458.
OMAiQKASRPY.
PhylomeDBiO34340.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciBSUB:BSU11340-MONOMER.

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_BACSU
AccessioniPrimary (citable) accession number: O34340
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 105 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, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.