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A7MFQ4 (FABH_CROS8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3

EC=2.3.1.41
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III
Beta-ketoacyl-ACP synthase III
Short name=KAS III
Gene names
Name:fabH
Ordered Locus Names:ESA_02254
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids By similarity. HAMAP MF_01815

Catalytic activity

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. HAMAP MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815

Subunit structure

Homodimer By similarity. HAMAP MF_01815

Subcellular location

Cytoplasm Probable HAMAP MF_01815.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP MF_01815

Sequence similarities

Belongs to the FabH family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3173173-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056361

Regions

Region245 – 2495ACP-binding By similarity

Sites

Active site1121 By similarity
Active site2441 By similarity
Active site2741 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7MFQ4 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: C005F77BFCA15914

FASTA31733,539
        10         20         30         40         50         60 
MYTKIIGTGS YLPEHVRTNA DLEKMVETSD EWIVTRTGIR ERRIAAPGET VATMGYEAAL 

        70         80         90        100        110        120 
RAIDMAGIDK GQIGLIIVAT TSATHAFPSA ACQVQGMLGI KGCPAFDVAA ACAGFTYALS 

       130        140        150        160        170        180 
IADQYVKSGA VNNALVIGSD VLARTLDPED RGTIILFGDG AGAVVLGASE EPGILSTHLH 

       190        200        210        220        230        240 
ADGSYGELLT LPNQDRVNPD SPTFLTMAGN EVFKVAVTEL AHIVDETLEA NKLDRADLDW 

       250        260        270        280        290        300 
LVPHQANLRI ISATAKKLGM SMDNVVVTLD RHGNTSAASV PCALDEAVRD GRIQRGQLVL 

       310 
LEAFGGGFTW GSALVRF 

« Hide

References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed: 20221447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU77503.1.
RefSeqYP_001438339.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7MFQ4.
SMRA7MFQ4. Positions 1-317.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7MFQ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5551744.
GenomeReviewsGene locus ESA_02254 in contig CP000783_GR.
KEGGesa:ESA_02254.
PATRIC20396453. VBICroSak107175_2014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMARILNFLA.
ProtClustDBPRK09352.

Family and domain databases

HAMAPMF_01815. FabH.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KOK00648.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. FabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH_CROS8
AccessionPrimary (citable) accession number: A7MFQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 2007
Last modified: January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families