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Q5L1U1 (FABH_GEOKA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3

EC=2.3.1.41
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III
Beta-ketoacyl-ACP synthase III
Short name=KAS III
Gene names
Name:fabH
Ordered Locus Names:GK0804
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length310 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

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. HAMAP MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815

Subunit structure

Homodimer By similarity. HAMAP MF_01815

Subcellular location

Cytoplasm Probable HAMAP MF_01815.

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.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3103103-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056362

Regions

Region236 – 2405ACP-binding By similarity

Sites

Active site1121 By similarity
Active site2351 By similarity
Active site2651 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L1U1 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 1C2D026B912C7463

FASTA31033,617
        10         20         30         40         50         60 
MGAGIIGVGR YVPEKVLTNF DLEKMMDTSD EWIRTRTGIE ERRIAADDID TSDMAYFAAK 

        70         80         90        100        110        120 
RALQDAGMEA KDIDLILVAT VTPDRPFPSV ACMLQERLGA VNAAALDISA ACAGFMYGMV 

       130        140        150        160        170        180 
TAAQFIDTGA YKYILVVGAD KLSKITDWTD RNTAVLFGDG AGAVVMGPVS PGRGILSFEL 

       190        200        210        220        230        240 
GADGTGGKHL YKDEYIVMNG REVFKFAVRQ MGESSVRVLE KAGLTKDDVD FLIPHQANIR 

       250        260        270        280        290        300 
IVEAARQRLE LPEEKISTTI RRYGNTSAAS IPISLVEELE AGKIHDDDLI IMVGFGGGLT 

       310 
WGAIALRWGR 

« Hide

References

[1]"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
Nucleic Acids Res. 32:6292-6303(2004) [PubMed: 15576355] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTA426.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000043 Genomic DNA. Translation: BAD75089.1.
RefSeqYP_146657.1. NC_006510.1.

3D structure databases

HSSPHSSP built from PDB template 1ZOW based on UniProtKB Q8NXE2.
ProteinModelPortalQ5L1U1.
SMRQ5L1U1. Positions 1-309.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3183625.
GenomeReviewsGene locus GK0804 in contig BA000043_GR.
KEGGgka:GK0804.
NMPDRfig|235909.3.peg.1497.
PATRIC21962832. VBIGeoKau81518_0887.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMAKEIGAIN.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycGKAU235909:GK0804-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 nameFABH_GEOKA
AccessionPrimary (citable) accession number: Q5L1U1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 1, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families