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A2S9Y2 (FABH_BURM9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. 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=2.3.1.180
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:BMA10229_A2802
OrganismBurkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP]
Taxonomic identifier412022 [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-Rule MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP-Rule MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP-Rule MF_01815

Sequence similarities

Belongs to the FabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3293293-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP-Rule MF_01815
PRO_1000070218

Regions

Region257 – 2615ACP-binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A2S9Y2 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 3098E02DA5714697

FASTA32934,823
        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 EAFSRILDFK 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]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000546 Genomic DNA. Translation: ABN02604.1.
RefSeqYP_001028751.1. NC_008836.1.

3D structure databases

ProteinModelPortalA2S9Y2.
SMRA2S9Y2. Positions 6-329.
ModBaseSearch...

Protein-protein interaction databases

STRING412022.BMA10229_A2802.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN02604; ABN02604; BMA10229_A2802.
GeneID4791886.
KEGGbml:BMA10229_A2802.
PATRIC19136602. VBIBurMal46188_4996.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHOG000246674.
KOK00648.
OMAAHIVEET.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycBMAL412022:GJI8-2802-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
HAMAPMF_01815. FabH.
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
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_BURM9
AccessionPrimary (citable) accession number: A2S9Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 6, 2007
Last modified: May 1, 2013
This is version 49 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