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A0AKV5 (FABH_LISW6) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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:lwe2219
OrganismListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334) [Complete proteome] [HAMAP]
Taxonomic identifier386043 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length312 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 – 3123123-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056374

Regions

Region238 – 2425ACP-binding By similarity

Sites

Active site1121 By similarity
Active site2371 By similarity
Active site2671 By similarity

Sequences

Sequence LengthMass (Da)Tools
A0AKV5 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 3402F87C2623930B

FASTA31234,029
        10         20         30         40         50         60 
MNAGILGVGK YVPERILTNF DLEKMMETSD EWIRTRTGIE ERRIARDDEY THDLAYEAAK 

        70         80         90        100        110        120 
VAIENAGLTP NDIDLFIVAT VTQEATFPSV ANIIQDRLGA KNAAGMDVEA ACAGFTFGVV 

       130        140        150        160        170        180 
TAAQFIKTGA YKNIVVVGAD KLSKITNWDD RATAVLFGDG AGAIVMGPVS DDHGLLSFDL 

       190        200        210        220        230        240 
GSDGSGGKYL NLDENKKIYM NGREVFRFAV RQMGEASLRV LERAGLEKED LDLLIPHQAN 

       250        260        270        280        290        300 
IRIMEASRER LNLPEEKLMK TVHKYGNTSS SSIALALVDA VEEGRIKDND NVLLVGFGGG 

       310 
LTWGALIIRW GK 

« Hide

References

[1]"Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T. expand/collapse author list , Lampidis R., Kreft J., Goebel W., Chakraborty T.
J. Bacteriol. 188:7405-7415(2006) [PubMed: 16936040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35897 / DSM 20650 / SLCC5334.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM263198 Genomic DNA. Translation: CAK21637.1.
RefSeqYP_850416.1. NC_008555.1.

3D structure databases

ProteinModelPortalA0AKV5.
SMRA0AKV5. Positions 1-311.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0AKV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4465223.
GenomeReviewsGene locus lwe2219 in contig AM263198_GR.
KEGGlwe:lwe2219.
NMPDRfig|386043.6.peg.2158.
PATRIC20331659. VBILisWel39304_2230.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAKEIGAIN.
PhylomeDBA0AKV5.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycLWEL386043:LWE2219-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_LISW6
AccessionPrimary (citable) accession number: A0AKV5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 28, 2006
Last modified: December 14, 2011
This is version 38 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