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A1VEK1 (FABH_DESVV) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:Dvul_1850
OrganismDesulfovibrio vulgaris subsp. vulgaris (strain DP4) [Complete proteome] [HAMAP]
Taxonomic identifier391774 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length330 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 – 3303303-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056353

Regions

Region258 – 2625ACP-binding By similarity

Sites

Active site1141 By similarity
Active site2571 By similarity
Active site2871 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1VEK1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 9452353FBBEB65EA

FASTA33034,666
        10         20         30         40         50         60 
MTSPSLLRGF GAYAPERILT NADIESMVET TDEWITTRTG IRQRHVVAPG QTTSDLAVEA 

        70         80         90        100        110        120 
ARAALADAAL DTADITHVLV ATCTPDASCP NTACIVARKL GMTGVMALDC NAACSGFLYG 

       130        140        150        160        170        180 
LELAQGIVAA RPASRVLLVA AEALSLRCNW KDRTTCVLFG DGAGATVVTA DVDATQGTAV 

       190        200        210        220        230        240 
LEDSIVTSDG SLGDLLTIGG GTANPYAIGD SVGEEYFVRM QGRDVFKHAV RSMTQVCNDL 

       250        260        270        280        290        300 
LARNGFTTED VDLVIPHQAN LRIIEAVGDR LGFASEKVFV NVHDFGNTSA ASIPLALADA 

       310        320        330 
RAQGRIRPGM RVLLTTFGGG FTWGAALLRF 

« Hide

References

[1]"Contribution of mobile genetic elements to Desulfovibrio vulgaris genome plasticity."
Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S., He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P., Stahl D.A.
Environ. Microbiol. 11:2244-2252(2009) [PubMed: 19737303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000527 Genomic DNA. Translation: ABM28867.1.
RefSeqYP_967294.1. NC_008751.1.

3D structure databases

ProteinModelPortalA1VEK1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1VEK1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4662350.
GenomeReviewsGene locus Dvul_1850 in contig CP000527_GR.
KEGGdvl:Dvul_1850.
PATRIC21767582. VBIDesVul62463_2064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAQANTRIV.
PhylomeDBA1VEK1.
ProtClustDBCLSK705098.

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_DESVV
AccessionPrimary (citable) accession number: A1VEK1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 36 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