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Q1WUS4 (Q1WUS4_LACS1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 49. 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 1 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III 1 HAMAP MF_01815
Beta-ketoacyl-ACP synthase III 1 HAMAP MF_01815
Gene names
Name:fabH EMBL ABD99261.1
Synonyms:fabH1 HAMAP MF_01815
Ordered Locus Names:LSL_0451
OrganismLactobacillus salivarius (strain UCC118) [Complete proteome] [HAMAP] EMBL ABD99261.1
Taxonomic identifier362948 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length326 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

Region254 – 2585ACP-binding By similarity HAMAP MF_01815

Sites

Active site1121 By similarity HAMAP MF_01815
Active site2531 By similarity HAMAP MF_01815
Active site2831 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q1WUS4 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: 66CD3A8BF1C02D06

FASTA32636,044
        10         20         30         40         50         60 
MENIEISYTA RYVPPEVIDN QRLTEFMDTS DEWISQRTGI KKRHISLNES TADLAKKVAE 

        70         80         90        100        110        120 
KLLTKSGWNP NSLDLIIVAT MSPNSFTPAT AAIVQGRISA DNAVCFDISA ACSGYIYGLS 

       130        140        150        160        170        180 
IVEAMLRNMN LKRAMLIGSE NLSKLIDWND RSTAVLFGDG AAGALIELKE DTDSKFISSD 

       190        200        210        220        230        240 
LKTIGNEAEF LTAGITDPLE KFPDLDSIRK YTTFKMDGRR VYTFATREVP QSILRAVQKA 

       250        260        270        280        290        300 
NLSLEDIDYF ILHQANSRII RQVAKKLKQD EEKFPINIDS FGNTSAASEP LLLDELIENG 

       310        320 
TVKRGMTLAL SGFGGGLTVG THIIKY

« Hide

References

[1]"Multireplicon genome architecture of Lactobacillus salivarius."
Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P., Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.
Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006) [PubMed: 16617113] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCC118.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000233 Genomic DNA. Translation: ABD99261.1.
RefSeqYP_535344.1. NC_007929.1.

3D structure databases

ProteinModelPortalQ1WUS4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1WUS4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3977616.
GenomeReviewsGene locus LSL_0451 in contig CP000233_GR.
KEGGlsl:LSL_0451.
PATRIC22277799. VBILacSal43464_0527.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMADYFILHQ.
PhylomeDBQ1WUS4.

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 nameQ1WUS4_LACS1
AccessionPrimary (citable) accession number: Q1WUS4
Entry history
Integrated into UniProtKB/TrEMBL: May 2, 2006
Last sequence update: May 2, 2006
Last modified: December 14, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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