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A8FWL0 (A8FWL0_SHESH) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 32. 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 2 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III 2 HAMAP MF_01815
Beta-ketoacyl-ACP synthase III 2 HAMAP MF_01815
Gene names
Name:fabH2 HAMAP MF_01815
Ordered Locus Names:Ssed_2626
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP] EMBL ABV37233.1
Taxonomic identifier425104 [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
A8FWL0 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: E9323CAE5299B30A

FASTA31933,939
        10         20         30         40         50         60 
MHTKILGTGS YLPAQVRSNQ DLEQMVETTD QWIVERTGIS ERRIAAADES VSTMGYEAAV 

        70         80         90        100        110        120 
KALEMAGIDA NELDMIVCGT TSASNAFPAA ACEIQAKLGV HTIPAFDIAA ACSGFVYALS 

       130        140        150        160        170        180 
VADQFVKSGA AKKVLVIGAD VLSRLCEPED RSTIILFGDG AGAAVVGASS EPGILSTHIY 

       190        200        210        220        230        240 
ADGRQADLLK CSFPPRMGEA TEAVGYMTMK GNDVFKVAVT QLSQVVTDTL RINQIDKSEI 

       250        260        270        280        290        300 
DWLVPHQANF RIIKATAKKL NMSLDKVVLT LAKHGNTSAA SVPIALDEAV RDGRIQRGQL 

       310 
IMLEAFGAGF AWGSALIRF

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000821 Genomic DNA. Translation: ABV37233.1.
RefSeqYP_001474361.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FWL0.
SMRA8FWL0. Positions 1-319.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FWL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5613232.
GenomeReviewsGene locus Ssed_2626 in contig CP000821_GR.
KEGGsse:Ssed_2626.
NMPDRfig|425104.3.peg.2325.
PATRIC23562921. VBISheSed62411_2799.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAFNAKEEA.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycSSED425104:SSED_2626-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 nameA8FWL0_SHESH
AccessionPrimary (citable) accession number: A8FWL0
Entry history
Integrated into UniProtKB/TrEMBL: November 13, 2007
Last sequence update: November 13, 2007
Last modified: December 14, 2011
This is version 32 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