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C6XDK8 (C6XDK8_METSD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 34. 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

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP-Rule MF_01815

EC=2.3.1.180 HAMAP-Rule MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP-Rule MF_01815
Beta-ketoacyl-ACP synthase III HAMAP-Rule MF_01815
Gene names
Name:fabH HAMAP-Rule MF_01815
Ordered Locus Names:Msip34_1388 EMBL ACT50633.1
OrganismMethylovorus sp. (strain SIP3-4) (Methylotenera sp. (strain SIP3-4)) [Complete proteome] [HAMAP] EMBL ACT50633.1
Taxonomic identifier582744 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylovorus

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-Rule MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP-Rule MF_01815 SAAS SAAS013751

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815 SAAS SAAS013751

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01815 SAAS SAAS013751

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01815 SAAS SAAS013751.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP-Rule MF_01815

Sequence similarities

Belongs to the FabH family. HAMAP-Rule MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region245 – 2495ACP-binding By similarity HAMAP-Rule MF_01815

Sites

Active site1131 By similarity HAMAP-Rule MF_01815
Active site2441 By similarity HAMAP-Rule MF_01815
Active site2741 By similarity HAMAP-Rule MF_01815

Sequences

Sequence LengthMass (Da)Tools
C6XDK8 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: B9E8C6A81C90D768

FASTA31734,033
        10         20         30         40         50         60 
MTYSRIAGTG SYLPERILTN AELERMVDTS DEWIVTRTGI RERHIAAEGQ FTSDLAYEAA 

        70         80         90        100        110        120 
LRAIEAAGIT HEEIDLVIVA TTTPDRVFPS TACLVQARLG LGPCPAFDIQ AVCSGFVYAL 

       130        140        150        160        170        180 
ATADNFIKSG AAKTALVIGA ETMSRITDWT DRSNCILWGD GAGAVILRAS DEMGILSTHL 

       190        200        210        220        230        240 
HADGQYARLL NVPTGVSQKE GSKTIHMEGN AVFKVAVNTL DAIVDETLEA NGLQKSDVDW 

       250        260        270        280        290        300 
LVPHQANIRI LQSTAKKLGM GMEKVVVTVD RHGNTSAASI PLALDVAVRD GRIKRGETLL 

       310 
MEAFGGGFTW GSVLVKF 

« Hide

References

[1]"Complete sequence of chromosome of Methylovorus sp. SIP3-4."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SIP3-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001674 Genomic DNA. Translation: ACT50633.1.
RefSeqYP_003051160.1. NC_012969.1.

3D structure databases

ProteinModelPortalC6XDK8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING582744.Msip34_1388.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT50633; ACT50633; Msip34_1388.
GeneID8173870.
KEGGmei:Msip34_1388.
PATRIC22617816. VBIMetSp110381_1397.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
KOK00648.
OMAIRIMQGT.
OrthoDBEOG6J74XN.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycMGLU582744:GHXQ-1424-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
HAMAPMF_01815. FabH.
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 1 hit.
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC6XDK8_METSD
AccessionPrimary (citable) accession number: C6XDK8
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: February 19, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)