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Reviewed, UniProtKB/Swiss-Prot Q5P0D6 (FABH_AZOSE)

Last modified November 3, 2009. Version 37. 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: AZOSEA31030
ORF Names: ebA5455
OrganismAzoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length321 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 – 3213213-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000056325

Regions

Region249 – 2535ACP-binding By similarity

Sites

Active site1151 By similarity
Active site2481 By similarity
Active site2781 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P0D6-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 47C637CDFAFD17F2

FASTA32133,695
        10         20         30         40         50         60 
MIYARIAGTG SFLPGEPITN DDLVARGIDT SDQWIIERTG IRSRHLASAE MSSSDLAKTA 

        70         80         90        100        110        120 
SERALDAAGV RPDDIDLIIV ATSTPDCIFP STAALLQSKL GIRNGAAAFD VQAVCSGFVY 

       130        140        150        160        170        180 
GLTIAEKFIR SGSHKRALVV GAEVFSRILD WSDRGTCVLF GDGAGAVVLE AAEAPGILAS 

       190        200        210        220        230        240 
ALHADGSHHP ILCVPGAVAA GQVVGDPFLR MDGQAVFKFA VRVLGDVALE VLDQAGVTVD 

       250        260        270        280        290        300 
SVDWLIPHQA NIRILQATAR RLGVSMDKVI TTVDHHGNTS AASIPLALDL AVRDGRIRPG 

       310        320 
HRFIIEGVGG GFTWGAALLQ F 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR555306 Genomic DNA. Translation: CAI09228.1.
RefSeqYP_160129.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P0D6.

Genome annotation databases

GeneID3180040.
GenomeReviewsGene locus AZOSEA31030 in contig CR555306_GR.
KEGGeba:ebA5455.
NMPDRfig|76114.4.peg.3107.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5P0D6.
OMAFKSAVTS.

Enzyme and pathway databases

BioCycASP76114:EBA5455-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_AZOSE
AccessionPrimary (citable) accession number: Q5P0D6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 4, 2005
Last modified: November 3, 2009
This is version 37 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