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Protein

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

Gene

fabF

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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. Has a preference for short chain acid substrates.

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 sitei1671

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

BRENDAi2.3.1.179. 382.
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:sll1069
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001803261 – 4163-oxoacyl-[acyl-carrier-protein] synthase 2Add BLAST416

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 18Combined sources10
Beta strandi21 – 23Combined sources3
Helixi24 – 32Combined sources9
Beta strandi38 – 40Combined sources3
Beta strandi53 – 55Combined sources3
Helixi62 – 64Combined sources3
Helixi68 – 72Combined sources5
Helixi76 – 92Combined sources17
Turni98 – 100Combined sources3
Helixi101 – 103Combined sources3
Beta strandi104 – 109Combined sources6
Helixi115 – 128Combined sources14
Helixi130 – 132Combined sources3
Helixi137 – 141Combined sources5
Helixi145 – 154Combined sources10
Helixi166 – 168Combined sources3
Helixi169 – 182Combined sources14
Beta strandi187 – 195Combined sources9
Helixi200 – 208Combined sources9
Helixi219 – 221Combined sources3
Beta strandi238 – 246Combined sources9
Helixi247 – 252Combined sources6
Beta strandi259 – 268Combined sources10
Beta strandi273 – 275Combined sources3
Helixi281 – 294Combined sources14
Helixi298 – 300Combined sources3
Beta strandi303 – 305Combined sources3
Helixi312 – 326Combined sources15
Helixi327 – 332Combined sources6
Beta strandi333 – 336Combined sources4
Helixi339 – 342Combined sources4
Helixi346 – 348Combined sources3
Helixi349 – 363Combined sources15
Beta strandi373 – 375Combined sources3
Beta strandi385 – 387Combined sources3
Beta strandi394 – 402Combined sources9
Turni403 – 405Combined sources3
Beta strandi406 – 413Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E5MX-ray1.54A1-416[»]
ProteinModelPortaliP73283.
SMRiP73283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP73283.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000060166.
InParanoidiP73283.
KOiK09458.
OMAiFEVEQYL.
PhylomeDBiP73283.

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.

P73283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANLEKKRVV VTGLGAITPI GNTLQDYWQG LMEGRNGIGP ITRFDASDQA
60 70 80 90 100
CRFGGEVKDF DATQFLDRKE AKRMDRFCHF AVCASQQAIN DAKLVINELN
110 120 130 140 150
ADEIGVLIGT GIGGLKVLED QQTILLDKGP SRCSPFMIPM MIANMASGLT
160 170 180 190 200
AINLGAKGPN NCTVTACAAG SNAIGDAFRL VQNGYAKAMI CGGTEAAITP
210 220 230 240 250
LSYAGFASAR ALSFRNDDPL HASRPFDKDR DGFVMGEGSG ILILEELESA
260 270 280 290 300
LARGAKIYGE MVGYAMTCDA YHITAPVPDG RGATRAIAWA LKDSGLKPEM
310 320 330 340 350
VSYINAHGTS TPANDVTETR AIKQALGNHA YNIAVSSTKS MTGHLLGGSG
360 370 380 390 400
GIEAVATVMA IAEDKVPPTI NLENPDPECD LDYVPGQSRA LIVDVALSNS
410
FGFGGHNVTL AFKKYQ
Length:416
Mass (Da):44,004
Last modified:February 1, 1997 - v1
Checksum:iB0740A438A91A6C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17311.1.
PIRiS77464.

Genome annotation databases

EnsemblBacteriaiBAA17311; BAA17311; BAA17311.
KEGGisyn:sll1069.
PATRICi23838460. VBISynSp132158_0797.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA17311.1.
PIRiS77464.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E5MX-ray1.54A1-416[»]
ProteinModelPortaliP73283.
SMRiP73283.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17311; BAA17311; BAA17311.
KEGGisyn:sll1069.
PATRICi23838460. VBISynSp132158_0797.

Phylogenomic databases

HOGENOMiHOG000060166.
InParanoidiP73283.
KOiK09458.
OMAiFEVEQYL.
PhylomeDBiP73283.

Enzyme and pathway databases

UniPathwayiUPA00094.
BRENDAi2.3.1.179. 382.

Miscellaneous databases

EvolutionaryTraceiP73283.

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_SYNY3
AccessioniPrimary (citable) accession number: P73283
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 118 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. 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
  4. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.