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A0KYB8 (A0KYB8_SHESA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 41. 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:Shewana3_2560
OrganismShewanella sp. (strain ANA-3) [Complete proteome] [HAMAP] EMBL ABK48787.1
Taxonomic identifier94122 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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
A0KYB8 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 508EE4568BEB5B6C

FASTA31934,069
        10         20         30         40         50         60 
MHTKILGTGS YLPVQVRSNQ DLEKMVETSD QWIVERTGIS ERRIAAQDET VSTMGYQAAL 

        70         80         90        100        110        120 
KALEMAGIEA SELDMIICGT TSAANAFPAA ACEIQAMLGV HTIPAFDIAA ACSGFVYALS 

       130        140        150        160        170        180 
VADQFVKNGT AKKVLVIGAD VLSRLCEPED RTTIILFGDG AGAAVIGASD EPGIISTHIY 

       190        200        210        220        230        240 
ADGRQGDLLK CAFPPRQGET SEAVGFMTMK GNDVFKVAVT QLSHVVTETL RLNNIDKSEI 

       250        260        270        280        290        300 
DWLVPHQANF RIINATAKKL DMSLDKVVLT LAKHGNTSAA SVPIALDEAV RDGRIQRGQL 

       310 
LLLEAFGAGF AWGSALVRF

« Hide

References

[1]"Complete sequence of chromosome 1 of Shewanella sp. ANA-3."
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., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000469 Genomic DNA. Translation: ABK48787.1.
RefSeqYP_870193.1. NC_008577.1.

3D structure databases

ProteinModelPortalA0KYB8.
SMRA0KYB8. Positions 1-319.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0KYB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4479222.
GenomeReviewsGene locus Shewana3_2560 in contig CP000469_GR.
KEGGshn:Shewana3_2560.
PATRIC23573020. VBISheSp134792_2886.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAFNAKEEA.
PhylomeDBA0KYB8.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycSSP94122:SHEWANA3_2560-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 nameA0KYB8_SHESA
AccessionPrimary (citable) accession number: A0KYB8
Entry history
Integrated into UniProtKB/TrEMBL: December 12, 2006
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 41 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