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G0VSY6 (G0VSY6_PAEPO) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 12. 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 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:fabH3 EMBL CCC84782.1
Synonyms:fabH HAMAP-Rule MF_01815
ORF Names:PPM_1845 EMBL CCC84782.1
OrganismPaenibacillus polymyxa M1 EMBL CCC84782.1
Taxonomic identifier1052684 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus ›

Protein attributes

Sequence length329 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 SAAS004655

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815 SAAS SAAS004655

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01815 SAAS SAAS004655

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01815 SAAS SAAS004655.

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

Region257 – 2615ACP-binding By similarity HAMAP-Rule MF_01815

Sites

Active site1161 By similarity HAMAP-Rule MF_01815
Active site2561 By similarity HAMAP-Rule MF_01815
Active site2861 By similarity HAMAP-Rule MF_01815

Sequences

Sequence LengthMass (Da)Tools
G0VSY6 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: F9668DF2351DF5DC

FASTA32934,985
        10         20         30         40         50         60 
MNKLRPVGVI GTGKYVPEKI LTNKDLEEIV ETSDEWIVSR TGIQERHIAA PEQATSDLAY 

        70         80         90        100        110        120 
EAAVKALESA GMTAQDLDLI IVATVTPDMA FPSTACILQD KLGAKGAAAF DLSAACSGFV 

       130        140        150        160        170        180 
YGLATATSFI KTGIYNNALI IGADCLSRIT DYTDRNTCVL FGDGAGAVVI GEVPEGRGFQ 

       190        200        210        220        230        240 
SFDLGAEGAG GTLLKLEAGG SRLPASADTL ENKQHYIYMN GREVFKFAVR VMGTATVDVL 

       250        260        270        280        290        300 
EKAGMSKDDI DLFVPHQANI RIIQSAMQRL DLPEEKVVIN VNKYANTSAA SIPLALVEAA 

       310        320 
EEGRMKEGDR ILMVGFGGGL TWGASVLIW

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References

[1]"The Genome of the Plant Growth-Promoting Rhizobacterium Paenibacillus polymyxa M-1 Contains Nine Sites Dedicated to Nonribosomal Synthesis of Lipopeptides and Polyketides."
Niu B., Rueckert C., Blom J., Wang Q., Borriss R.
J. Bacteriol. 193:5862-5863(2011)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: M1 EMBL CCC84782.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		HE577054 Genomic DNA. Translation: CCC84782.1.
RefSeqYP_005959489.1. NC_017542.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC84782; CCC84782; PPM_1845.
GeneID12550548.
KEGGppo:PPM_1845.

Phylogenomic databases

KOK00648.

Enzyme and pathway databases

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. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG0VSY6_PAEPO
AccessionPrimary (citable) accession number: G0VSY6
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: April 3, 2013
This is version 12 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