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Q084G7 (Q084G7_SHEFN) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | 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 1 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III 1 HAMAP MF_01815
Beta-ketoacyl-ACP synthase III 1 HAMAP MF_01815
Gene names
Name:fabH1 HAMAP MF_01815
Ordered Locus Names:Sfri_1497
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP] EMBL ABI71348.1
Taxonomic identifier318167 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length319 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

Region247 – 2515ACP-binding By similarity HAMAP MF_01815

Sites

Active site1121 By similarity HAMAP MF_01815
Active site2461 By similarity HAMAP MF_01815
Active site2761 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q084G7 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 8A818E26123A9A6F

FASTA31933,834
        10         20         30         40         50         60 
MHTKILGTGS YLPVQVRSNQ DLEKMVETSD QWIVDRTGIS ERRIAASDES VSTMGYQAAL 

        70         80         90        100        110        120 
KALEMAGIEA SDLDMIVCGT TSASNAFPAA ACEIQALLGV KNIPAFDIAA ACSGFIYALS 

       130        140        150        160        170        180 
VADQFVKTGS AKKVLVIGSD VLSRMCDPAD RSTVILFGDG AGAAIIGVSD TPGIIATHIY 

       190        200        210        220        230        240 
ADGSQGDLLK CSFPPRANES SEAVGFMTMK GNDVFKVAVT QLSNVVTETL RLNNVDKSEI 

       250        260        270        280        290        300 
DWLVPHQANF RIINATAKKL HMSLDKVVLT LARHGNTSAA SVPIALDEAV RDGRIQRGHL 

       310 
LLLEAFGGGF AWGSALVRF

« Hide

References

[1]"Complete sequence of Shewanella frigidimarina NCIMB 400."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H., Newman D., Tiedje J.M. expand/collapse author list , Zhou J., Romine M.F., Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIMB 400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000447 Genomic DNA. Translation: ABI71348.1.
RefSeqYP_750186.1. NC_008345.1.

3D structure databases

ProteinModelPortalQ084G7.
SMRQ084G7. Positions 1-319.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ084G7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4278063.
GenomeReviewsGene locus Sfri_1497 in contig CP000447_GR.
KEGGsfr:Sfri_1497.
NMPDRfig|318167.10.peg.1449.
PATRIC23496923. VBISheFri14343_1554.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAFNAKEEA.
PhylomeDBQ084G7.
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 nameQ084G7_SHEFN
AccessionPrimary (citable) accession number: Q084G7
Entry history
Integrated into UniProtKB/TrEMBL: October 31, 2006
Last sequence update: October 31, 2006
Last modified: December 14, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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