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P73283 (FABF_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:fabF
Ordered Locus Names:sll1069
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4164163-oxoacyl-[acyl-carrier-protein] synthase 2
PRO_0000180326

Sites

Active site1671

Secondary structure

1 ................................................................... 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P73283 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B0740A438A91A6C1

FASTA41644,004
        10         20         30         40         50         60 
MANLEKKRVV VTGLGAITPI GNTLQDYWQG LMEGRNGIGP ITRFDASDQA CRFGGEVKDF 

        70         80         90        100        110        120 
DATQFLDRKE AKRMDRFCHF AVCASQQAIN DAKLVINELN ADEIGVLIGT GIGGLKVLED 

       130        140        150        160        170        180 
QQTILLDKGP SRCSPFMIPM MIANMASGLT AINLGAKGPN NCTVTACAAG SNAIGDAFRL 

       190        200        210        220        230        240 
VQNGYAKAMI CGGTEAAITP LSYAGFASAR ALSFRNDDPL HASRPFDKDR DGFVMGEGSG 

       250        260        270        280        290        300 
ILILEELESA LARGAKIYGE MVGYAMTCDA YHITAPVPDG RGATRAIAWA LKDSGLKPEM 

       310        320        330        340        350        360 
VSYINAHGTS TPANDVTETR AIKQALGNHA YNIAVSSTKS MTGHLLGGSG GIEAVATVMA 

       370        380        390        400        410 
IAEDKVPPTI NLENPDPECD LDYVPGQSRA LIVDVALSNS FGFGGHNVTL AFKKYQ

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.
[2]"The crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54 A resolution and its relationship to other condensing enzymes."
Moche M., Dehesh K., Edwards P., Lindqvist Y.
J. Mol. Biol. 305:491-503(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000022 Genomic DNA. Translation: BAA17311.1.
PIRS77464.
RefSeqNP_440631.1. NC_000911.1.
YP_005650690.1. NC_017277.1.
YP_007450514.1. NC_020286.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5MX-ray1.54A1-416[»]
ProteinModelPortalP73283.
SMRP73283. Positions 6-416.
ModBaseSearch...

Protein-protein interaction databases

STRING1148.sll1069.

Proteomic databases

PaxDbP73283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA17311; BAA17311; BAA17311.
GeneID12256382.
14616164.
953934.
KEGGsyn:sll1069.
syy:SYNGTS_0737.
PATRIC23838460. VBISynSp132158_0797.

Phylogenomic databases

eggNOGCOG0304.
HOGENOMHOG000060166.
KOK09458.
OMAINMISGF.
ProtClustDBPRK07314.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
InterProIPR017568. 3-oxoacyl-ACP_synth-2.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFPIRSF000447. KAS_II. 1 hit.
SUPFAMSSF53901. Thiolase-like. 2 hits.
TIGRFAMsTIGR03150. fabF. 1 hit.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP73283.

Entry information

Entry nameFABF_SYNY3
AccessionPrimary (citable) accession number: P73283
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: February 1, 1997
Last modified: May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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