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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei164 – 1641PROSITE-ProRule 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

BioCyciBSUB:BSU11340-MONOMER.
RETL1328306-WGS:GSTH-2496-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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4134133-oxoacyl-[acyl-carrier-protein] synthase 2PRO_0000360846Add
BLAST

Proteomic databases

PaxDbiO34340.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006266.

Structurei

Secondary structure

1
413
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1510Combined sources
Beta strandi18 – 203Combined sources
Helixi21 – 299Combined sources
Beta strandi35 – 373Combined sources
Helixi43 – 453Combined sources
Beta strandi50 – 523Combined sources
Helixi59 – 613Combined sources
Helixi65 – 684Combined sources
Helixi73 – 8917Combined sources
Turni95 – 973Combined sources
Helixi98 – 1003Combined sources
Beta strandi101 – 1066Combined sources
Helixi112 – 12514Combined sources
Helixi127 – 1293Combined sources
Helixi134 – 1385Combined sources
Helixi142 – 15110Combined sources
Beta strandi155 – 1584Combined sources
Helixi163 – 1653Combined sources
Helixi166 – 17914Combined sources
Beta strandi184 – 1929Combined sources
Helixi197 – 2059Combined sources
Turni215 – 2173Combined sources
Beta strandi234 – 2429Combined sources
Helixi243 – 2486Combined sources
Beta strandi255 – 26410Combined sources
Beta strandi269 – 2713Combined sources
Helixi274 – 2763Combined sources
Helixi277 – 29014Combined sources
Helixi294 – 2963Combined sources
Beta strandi299 – 3013Combined sources
Helixi308 – 32215Combined sources
Helixi323 – 3275Combined sources
Beta strandi329 – 3324Combined sources
Helixi335 – 3384Combined sources
Helixi342 – 3443Combined sources
Helixi345 – 35915Combined sources
Beta strandi370 – 3723Combined sources
Beta strandi381 – 3833Combined sources
Beta strandi390 – 3989Combined sources
Turni399 – 4013Combined sources
Beta strandi402 – 4098Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-412.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091I → F in strain: GS77; resistant to cerulenin. 1 Publication

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
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. Positions 1-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006266.

Proteomic databases

PaxDbiO34340.

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.
RETL1328306-WGS:GSTH-2496-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: September 7, 2016
This is version 103 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.