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A3CQ60 (FABH_STRSV) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 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:SSA_1940
OrganismStreptococcus sanguinis (strain SK36) [Complete proteome] [HAMAP]
Taxonomic identifier388919 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length324 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 – 3243243-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056427

Regions

Region250 – 2545ACP-binding By similarity

Sites

Active site1121 By similarity
Active site2491 By similarity
Active site2791 By similarity

Sequences

Sequence LengthMass (Da)Tools
A3CQ60 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 801254EC8E12C6DC

FASTA32434,765
        10         20         30         40         50         60 
MNYAKISQVA HYAPRQVVSN DDLAEIMDTS DEWISSRTGI KNRHLSSDET TSDLATKVAE 

        70         80         90        100        110        120 
NLLQKSGISA QDLDFIIVAT ITPDSLMPSA AARVQANIGA KNAFAFDLTA ACSGFIFALS 

       130        140        150        160        170        180 
TGEKFISSGR YQKGLVIGSE TLSKTVDWSD RSTAVLFGDG AGGVLLESAS EQHFLAESQF 

       190        200        210        220        230        240 
TDGSRGDSLT CGKIGLSSPF SEKGENQPYL TMDGRAIFDF AIRDVARSIK ETIESSQLSA 

       250        260        270        280        290        300 
EDLDFLLLHQ ANIRILDKMA KKLGVAREKL PANMMEYGNT SAASIPILLS ECVEQGLIKL 

       310        320 
NGNQTILMSG FGGGLTWGTL IVTI 

« Hide

References

[1]"Genome of the opportunistic pathogen Streptococcus sanguinis."
Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L., Buck G.A.
J. Bacteriol. 189:3166-3175(2007) [PubMed: 17277061] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SK36.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000387 Genomic DNA. Translation: ABN45315.1.
RefSeqYP_001035865.1. NC_009009.1.

3D structure databases

ProteinModelPortalA3CQ60.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3CQ60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000052267; EBSTRP00000048531; EBSTRG00000052257.
GeneID4806841.
GenomeReviewsGene locus SSA_1940 in contig CP000387_GR.
KEGGssa:SSA_1940.
NMPDRfig|388919.8.peg.1723.
PATRIC19770795. VBIStrSan33173_1839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
GeneTreeEBGT00050000027516.
HOGENOMHBG649927.
OMATSHEWIS.
PhylomeDBA3CQ60.
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_STRSV
AccessionPrimary (citable) accession number: A3CQ60
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: December 14, 2011
This is version 39 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