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Q5FUN7 (Q5FUN7_GLUOX) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 55. 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:GOX0115
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP] EMBL AAW59909.1
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter

Protein attributes

Sequence length324 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

Region252 – 2565ACP-binding By similarity HAMAP MF_01815

Sites

Active site1181 By similarity HAMAP MF_01815
Active site2511 By similarity HAMAP MF_01815
Active site2811 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q5FUN7 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: D6E227A255437D11

FASTA32434,060
        10         20         30         40         50         60 
MSDPIRVRLT GVGGYLPRDV VTNDDLARKF GIETSDEWIR TRTGIGQRHI ASGDETTASM 

        70         80         90        100        110        120 
AAEAARQALD YAGVDASQVD AVLVATATPD QVFPAVAVQV QACLGMTAGF GFDISAACSG 

       130        140        150        160        170        180 
FVYALATATA LMQSGQANKV LVIGSEVFSR LLDWTDRSTC VLFGDGAGAV LLETGAGEGE 

       190        200        210        220        230        240 
GVLSTHLHSD GRTGDILYVD GAAGCPSTSQ HLRMQGREVF RHAVVKLSQA VDEALEANGL 

       250        260        270        280        290        300 
TGQDIQWMVP HQANLRIIEG MAKKLALPAD RVVVTVDRHA NTSAASIPLA LNEAVRDGRV 

       310        320 
RKGDLVLMEA LGGGLTWGSA LIRM 

« Hide

References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000009 Genomic DNA. Translation: AAW59909.1.
RefSeqYP_190565.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FUN7.
SMRQ5FUN7. Positions 6-323.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3249214.
GenomeReviewsGene locus GOX0115 in contig CP000009_GR.
KEGGgox:GOX0115.
NMPDRfig|290633.1.peg.110.
PATRIC32607902. VBIGluOxy81109_0342.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMARILNFLA.
ProtClustDBCLSK935911.

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 nameQ5FUN7_GLUOX
AccessionPrimary (citable) accession number: Q5FUN7
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2005
Last sequence update: March 1, 2005
Last modified: December 14, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)