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Q6A930 (Q6A930_PROAC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 58. 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 MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP MF_01815
Beta-ketoacyl-ACP synthase III HAMAP MF_01815
Gene names
Name:fabH HAMAP MF_01815
Ordered Locus Names:PPA0983
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP] EMBL AAT82736.1
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium

Protein attributes

Sequence length332 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

Region258 – 2625ACP-binding By similarity HAMAP MF_01815

Sites

Active site1221 By similarity HAMAP MF_01815
Active site2571 By similarity HAMAP MF_01815
Active site2881 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q6A930 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 32E6E657C2334A74

FASTA33235,276
        10         20         30         40         50         60 
MTAIKTRPVH GYSKFLSTGS ARGSRVVTNK EMCTLIDSTP EWIEQRTGIT ERRWATNSET 

        70         80         90        100        110        120 
VASMGTTAAR TALERSGLEA SQIDAIIVAT VSHHRPSPSL AAYIARELGL GDAAAFDLNG 

       130        140        150        160        170        180 
ACAGFCYSTA LADSMIRTGS ANYVLVIGVE KLSEMTNLDD RSTAFLFSDG AGAAIIGASD 

       190        200        210        220        230        240 
EPGIGPVVWG SRSDQLKTIE LEDWPTASAD PNKIHPLIRM EGRAVFKWAM TDVAKRAAEA 

       250        260        270        280        290        300 
IAEAGITPAD LDVFIPHQAN DRITDVVSRH LKLPESVTVC HDIADMGNTS AASVPIAIDR 

       310        320        330 
MLQRGQAHSG DLALIIGFGA GLVYAGQVIR LP

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References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed: 15286373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017283 Genomic DNA. Translation: AAT82736.1.
RefSeqYP_055694.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A930.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2932329.
GenomeReviewsGene locus PPA0983 in contig AE017283_GR.
KEGGpac:PPA0983.
NMPDRfig|267747.1.peg.971.
PATRIC23036691. VBIProAcn64440_1018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMASNCFIFA.
ProtClustDBCLSK2763650.

Enzyme and pathway databases

BioCycPACN267747:PPA0983-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 nameQ6A930_PROAC
AccessionPrimary (citable) accession number: Q6A930
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2004
Last sequence update: September 13, 2004
Last modified: December 14, 2011
This is version 58 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