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Reviewed, UniProtKB/Swiss-Prot Q3JQ65 (FABH_BURP1)

Last modified February 9, 2010. Version 35. 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: BURPS1710b_2907
OrganismBurkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP]
Taxonomic identifier320372 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length329 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: 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 – 3293293-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000070222

Regions

Region257 – 2615ACP-binding By similarity

Sites

Active site1231 By similarity
Active site2561 By similarity
Active site2861 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3JQ65-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: C59750221AD45C3D

FASTA32934,853
        10         20         30         40         50         60 
MAQSTLYSRV LGTGSYLPPD RVTNQELADR LAKDGIETSD EWIVARTGIR ARHFAAPDVT 

        70         80         90        100        110        120 
TSDLALVAAQ RAIEAADVDP QSIDLIIVAT STPDFVFPST ACLLQNKLGI KNGGAAFDVQ 

       130        140        150        160        170        180 
AVCSGFAYAL ATADSFIRTG QHRTALVIGA ETFSRILDFK DRTTCVLFGD GAGAVVLSAS 

       190        200        210        220        230        240 
EEPGILGSAL HADGSYSNIL CTPGNVNRGV IAGSAFLHMD GQAVFKLAVN VLEKVAVEAL 

       250        260        270        280        290        300 
SKAELASEQV DWLIPHQANI RIMTSTCRKL GLPQERMIVT VDEHGNTSAA SIPLALDVAV 

       310        320 
RDGRIKRGQH VLIEGVGGGF TWGASVFRF 

« Hide

References

[1]Woods D.E., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000124 Genomic DNA. Translation: ABA49489.1.
RefSeqYP_334288.1.

3D structure databases

SMRQ3JQ65. Positions 6-329.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3JQ65.

Genome annotation databases

GeneID3690950.
GenomeReviewsGene locus BURPS1710b_2907 in contig CP000124_GR.
KEGGbpm:BURPS1710b_2907.
TIGRBURPS1710b_2907.

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMATSADRGI.

Enzyme and pathway databases

BioCycBPSE320372:BURPS1710B_A3155-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.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH_BURP1
AccessionPrimary (citable) accession number: Q3JQ65
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 8, 2005
Last modified: February 9, 2010
This is version 35 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