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Q1LKL9 (Q1LKL9_RALME) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 48. 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:Rmet_2430
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length350 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

Region278 – 2825ACP-binding By similarity HAMAP MF_01815

Sites

Active site1441 By similarity HAMAP MF_01815
Active site2771 By similarity HAMAP MF_01815
Active site3071 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q1LKL9 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: CCF3F2D6B4D986CC

FASTA35036,942
        10         20         30         40         50         60 
MPAAAGSLRD RAQGDPVSIT IRHDMTKYAK IIGTGSYLPP RRVTNADLAA QLAEKGIETS 

        70         80         90        100        110        120 
DEWIVSRSGI SARYWAEPDV TSSDLAVKAA ERAIEAAGID RQDIDLIIVA TSTPDYVFPS 

       130        140        150        160        170        180 
AACLVQQKLG ITNQCAAFDL QAVCSGFVYA LATADKFIRS GSHKNVLVIG SEVFSRILDF 

       190        200        210        220        230        240 
NDRTTCVLFG DGAGAVVLTA SDEPGILSTA MHSDGSHVGI LCVPGNVSGG AITGNAFLHM 

       250        260        270        280        290        300 
DGQAVFKLAV TVLDKVAREA ITAAEMQADE IDWLIPHQAN IRIMQGTAKK LGLPSERMIA 

       310        320        330        340        350 
TVHEHGNTSA ASIPLALDVA VRDGRIKPGQ TVLMEGVGGG FTWGAVLLRM

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References

[1]"Complete sequence of the chromosome of Ralstonia metallidurans CH34."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000352 Genomic DNA. Translation: ABF09307.1.
RefSeqYP_584576.3. NC_007973.1.

3D structure databases

ProteinModelPortalQ1LKL9.
SMRQ1LKL9. Positions 28-350.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LKL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4039252.
GenomeReviewsGene locus Rmet_2430 in contig CP000352_GR.
KEGGrme:Rmet_2430.
PATRIC20289500. VBIRalMet4734_2832.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMARILNFLA.
PhylomeDBQ1LKL9.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycRMET266264:RMET_2430-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 nameQ1LKL9_RALME
AccessionPrimary (citable) accession number: Q1LKL9
Entry history
Integrated into UniProtKB/TrEMBL: May 30, 2006
Last sequence update: May 30, 2006
Last modified: December 14, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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