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P59813 (FABH_HELHP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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:HH_0681
OrganismHelicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]
Taxonomic identifier235279 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length332 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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3323323-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_0000110433

Regions

Region256 – 2605ACP-binding By similarity

Sites

Active site1161 By similarity
Active site2551 By similarity
Active site2851 By similarity

Sequences

Sequence LengthMass (Da)Tools
P59813 [UniParc].

Last modified August 15, 2003. Version 1.
Checksum: 6C9F97E930998428

FASTA33235,943
        10         20         30         40         50         60 
MGKIYASLKS IASYIPPTCI SNVDFEKTLD TNDEWITKRT GIKTRYFALP SQQTSDLAYE 

        70         80         90        100        110        120 
AGKKAIERAG IEPKDIDAVI VATLSPDYLT MPSTACITSF KLGIENKAAF DISAACSGFV 

       130        140        150        160        170        180 
YLLSLAKSFI ESGTYKQILI IGAEKTSSVL DFSDRSTCVL FGDGAGACVI GSTNDEKAAI 

       190        200        210        220        230        240 
LGVNVSANGR YQDFLCTPRV HATFGATQAQ EKQSFIQMKG NETFKVAVKT LVSEVKEILN 

       250        260        270        280        290        300 
THHINPQDVS FFIPHQANLR IINAVGENLN FTPEQIVVSI QKYGNTSAAS IPMAMNDLYE 

       310        320        330 
EKKLKYGDLM LLDALGGGLT WGSALVHFGG TN 

« Hide

References

[1]"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus."
Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. expand/collapse author list , Shen Z., Weber J., Frosch M., Fox J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed: 12810954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017125 Genomic DNA. Translation: AAP77278.1.
RefSeqNP_860212.1. NC_004917.1.

3D structure databases

ProteinModelPortalP59813.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1493735.
GenomeReviewsGene locus HH_0681 in contig AE017125_GR.
KEGGhhe:HH0681.
NMPDRfig|235279.1.peg.681.
PATRIC20588816. VBIHelHep90276_0682.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMARADETIF.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycHHEP235279:HH_0681-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.
KOK00648.
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_HELHP
AccessionPrimary (citable) accession number: P59813
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: August 15, 2003
Last modified: January 25, 2012
This is version 61 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