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Reviewed, UniProtKB/Swiss-Prot Q3YRP7 (FABH_EHRCJ)

Last modified November 3, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Ecaj_0574
OrganismEhrlichia canis (strain Jake) [Complete proteome] [HAMAP]
Taxonomic identifier269484 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Subcellular location

Cytoplasm Probable.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3193193-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056357

Regions

Region247 – 2515ACP-binding By similarity

Sites

Active site1131 By similarity
Active site2461 By similarity
Active site2761 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3YRP7-1 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 02AD9694D9FFF08F

FASTA31934,503
        10         20         30         40         50         60 
MKRSLILGIG SYLPKKVVTN DELTLTIETS DEWIVKRTGI KQRHIAEDNE MTSDMATSAA 

        70         80         90        100        110        120 
KLALDNAGID KNEIDLIIVA TTTPDRTFPS CATIVQSKLG CKNAFAFDIQ AVCSGFVYAL 

       130        140        150        160        170        180 
SIADNFIKSG QVRTVLVIGA EIMSRILDWQ DRSTCVLFGD GAGAIVLSSS TEDDSGIIST 

       190        200        210        220        230        240 
NLHSDGTFHD LLYTSGGTAY NGVAGTICMN GTVVFEHAIE KLSASILEIL SQNDLEICDI 

       250        260        270        280        290        300 
DWFVLHQANI RIIELVARRL KIPYEKMIVS IDQHANTSAA SIPLALYYAR SSGKLKKHDV 

       310 
AVLAAIGGGL TWGTCLVRI 

« Hide

References

[1]"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
J. Bacteriol. 188:4015-4023(2006) [PubMed: 16707693] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000107 Genomic DNA. Translation: AAZ68608.1.
RefSeqYP_303206.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3YRP7.

Genome annotation databases

GeneID3617921.
GenomeReviewsGene locus Ecaj_0574 in contig CP000107_GR.
KEGGecn:Ecaj_0574.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3YRP7.
OMAYSRITGT.

Enzyme and pathway databases

BioCycECAN269484:ECAJ_0574-MON.

Family and domain databases

HAMAPMF_01815.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH_EHRCJ
AccessionPrimary (citable) accession number: Q3YRP7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 27, 2005
Last modified: November 3, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents