Skip Header

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

Q0HHJ8 (Q0HHJ8_SHESM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 46. 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 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:Shewmr4_2398
OrganismShewanella sp. (strain MR-4) [Complete proteome] [HAMAP] EMBL ABI39469.1
Taxonomic identifier60480 [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
Q0HHJ8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 0094F6CD4CE6EDB7

FASTA31934,097
        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 SEALGFMTMK GNDVFKVAVT QLSHVVTETL RLNNIDKSEI 

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

       310 
LLLEAFGAGF AWGSALIRF

« Hide

References

[1]"Complete sequence of Shewanella sp. MR-4."
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MR-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000446 Genomic DNA. Translation: ABI39469.1.
RefSeqYP_734526.1. NC_008321.1.

3D structure databases

ProteinModelPortalQ0HHJ8.
SMRQ0HHJ8. Positions 1-319.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0HHJ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4252969.
GenomeReviewsGene locus Shewmr4_2398 in contig CP000446_GR.
KEGGshe:Shewmr4_2398.
PATRIC23581538. VBISheSp133532_2487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAFNAKEEA.
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 nameQ0HHJ8_SHESM
AccessionPrimary (citable) accession number: Q0HHJ8
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: December 14, 2011
This is version 46 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