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O67185 (FABH_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:aq_1099
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_01815

Subcellular location

Cytoplasm Probable HAMAP-Rule 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-Rule MF_01815

Sequence similarities

Belongs to the FabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3093093-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP-Rule MF_01815
PRO_0000110392

Regions

Region237 – 2415ACP-binding By similarity

Sites

Active site1111 By similarity
Active site2361 By similarity
Active site2661 By similarity

Secondary structure

............................................................ 309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67185 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: EB97518DB168140D

FASTA30933,825
        10         20         30         40         50         60 
MGTKIIGTGV YLPKNVLTNF DLEKIVDTSD EWITTRTGIK ERRIAKEETI TYMATQAAKE 

        70         80         90        100        110        120 
ALREANLSPE ELDLIILATL TPQKRFPSTA CLVQAQLKAK GVYAFDISAA CSGFIYALDI 

       130        140        150        160        170        180 
ADSFIKSGKA KNVLVIGAEK LSEAVDWEDR STCVLFGDGA GAVVVTRSED KSDILATRMY 

       190        200        210        220        230        240 
AEGSLEELLH ADNCGYIRMK GRELFKVAVR SMEEVCREVL EKAGVKPEEV SLVIPHQANV 

       250        260        270        280        290        300 
RIINALAEKL NIPKEKVFVN IQKYGNTSAA SIPIALHEAI KEGKVKRGDL ILMTAMGGGL 


TWGAVLLRY 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07144.1.
PIRF70394.
RefSeqNP_213748.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBDX-ray2.10A/B1-309[»]
ProteinModelPortalO67185.
SMRO67185. Positions 1-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07144; AAC07144; aq_1099.
GeneID1193819.
KEGGaae:aq_1099.
PATRIC20959474. VBIAquAeo85532_0857.

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHOG000246674.
KOK00648.
OMAIRIMQGT.
OrthoDBEOG6J74XN.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-783-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. SSF53901. 1 hit.
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO67185.

Entry information

Entry nameFABH_AQUAE
AccessionPrimary (citable) accession number: O67185
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways