Skip Header

Contribute Send feedback
Read comments (?) or add your own

B6EIZ8 (B6EIZ8_ALISL) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 24. Feed History...

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

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP MF_01815
Beta-ketoacyl-ACP synthase III HAMAP MF_01815
Gene names
Name:fabH HAMAP MF_01815 EMBL CAQ79923.1
Ordered Locus Names:VSAL_I2239
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP] EMBL CAQ79923.1
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Aliivibrio

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

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815 SAAS SAAS013747

Subunit structure

Homodimer By similarity. HAMAP MF_01815 SAAS SAAS013747

Subcellular location

Cytoplasm By similarity HAMAP MF_01815 SAAS SAAS013747.

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. HAMAP MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region245 – 2495ACP-binding By similarity HAMAP MF_01815

Sites

Active site1121 By similarity HAMAP MF_01815
Active site2441 By similarity HAMAP MF_01815
Active site2741 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
B6EIZ8 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: C37619BD2AA8360F

FASTA31733,978
        10         20         30         40         50         60 
MYSKILGTGS YLPAQVRTNA DLEKMVDTSD EWILARTGIS ERRIAGEGES VATMGHLASV 

        70         80         90        100        110        120 
KAIEMAGIDK NDIDLIILAT STPTYSFPSS ACEVQGLLEI QGCPAFDLSA ACSGFVYALS 

       130        140        150        160        170        180 
VADQHIKTGM AKNVLVIGSD AVSHTCDPTD RSTVILFGDG AGAVVVGQSE EPGIISTHLH 

       190        200        210        220        230        240 
ADGKFGELLS LPVPSRRNEE ADKWLYMAGN EVFKVAVTQL SNLVKETLHK NQMDKSELDW 

       250        260        270        280        290        300 
LVPHQANLRI IKATAKKLSM SMDQVVVTLD RHGNTSAATV PTALDEAVRD GRIKRGQTLL 

       310 
LEAFGGGFTW GSALVKF

« Hide

References

[1]"The complete genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238."
Hjerde E., Lorentzen M.S., Holden M.T.G., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.-P., Thomson N.R.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM178379 Genomic DNA. Translation: CAQ79923.1.
RefSeqYP_002263604.1. NC_011312.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB6EIZ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6988989.
GenomeReviewsGene locus VSAL_I2239 in contig FM178379_GR.
KEGGvsa:VSAL_I2239.
PATRIC20854873. VBIAliSal95923_2441.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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 nameB6EIZ8_ALISL
AccessionPrimary (citable) accession number: B6EIZ8
Entry history
Integrated into UniProtKB/TrEMBL: November 25, 2008
Last sequence update: November 25, 2008
Last modified: December 14, 2011
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info