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Q8D8G6 (FABH1_VIBVU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. 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 protein 1

EC=2.3.1.180
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III protein 1
Beta-ketoacyl-ACP synthase III 1
Short name=KAS III 1
Gene names
Name:fabH1
Ordered Locus Names:VV1_3011
OrganismVibrio vulnificus [Complete proteome] [HAMAP]
Taxonomic identifier672 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length316 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

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3163163-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1 HAMAP MF_01815
PRO_0000110506

Regions

Region244 – 2485ACP-binding By similarity

Sites

Active site1121 By similarity
Active site2431 By similarity
Active site2731 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8D8G6 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A416A5830EE4AC7C

FASTA31633,856
        10         20         30         40         50         60 
MYSKILGTGS YLPSQIRTNA DLEKMVETSD EWIVARTGIK ERRIAAENET VADMGFYAAQ 

        70         80         90        100        110        120 
NAIEMAGIDK NDIDLIIVAT TSGSHTFPSS ACQVQAKLGI KGCPAFARAA ACSGFVYALS 

       130        140        150        160        170        180 
IADQHIKTGM CKNVLVIGSD TLSKTCDPTD RSTIILFGDG AGAVVVGASE EPGILSTHIY 

       190        200        210        220        230        240 
ADGEFGDLLS LEVPERGKDA DKWLHMAGNE VFKVAVTQLS KLVKDTLEAN GMHKSELDWL 

       250        260        270        280        290        300 
VPHQANYRII SATAKKLSMS LDQVVITLDR HGNTSAATVP TALDEAVRDG RIQRGQTLLL 

       310 
EAFGGGFTWG SALVRF 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Vibrio vulnificus CMCP6."
Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CMCP6.
[2]"Integrative genome-scale metabolic analysis of Vibrio vulnificus for drug targeting and discovery."
Kim H.U., Kim S.Y., Jeong H., Kim T.Y., Kim J.J., Choy H.E., Yi K.Y., Rhee J.H., Lee S.Y.
Mol. Syst. Biol. 7:460-460(2011) [PubMed: 21245845] [Abstract]
Cited for: SEQUENCE REVISION TO 107-108.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016795 Genomic DNA. Translation: AAO11338.2.
RefSeqNP_761811.2. NC_004459.3.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1179841.
GenomeReviewsGene locus VV1_3011 in contig AE016795_GR.
KEGGvvu:VV1_3011.
PATRIC20162997. VBIVibVul94426_2973.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMARILNFLA.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycVVUL216895:VV1_3011-MONOMER.

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 nameFABH1_VIBVU
AccessionPrimary (citable) accession number: Q8D8G6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 68 of the entry and version 2 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