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Q3AQ09 (FABH_CHLCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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=2.3.1.41
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:Cag_1664
OrganismChlorobium chlorochromatii (strain CaD3) [Complete proteome] [HAMAP]
Taxonomic identifier340177 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

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: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: EC

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_1000056339

Regions

Region256 – 2605ACP-binding By similarity

Sites

Active site1131 By similarity
Active site2551 By similarity
Active site2851 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3AQ09 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 35462C0B369355DF

FASTA32935,744
        10         20         30         40         50         60 
MKAAITATAN YLPPDILSNH DLELMLDTND EWIRSRTGIG ERRILKDPTK ATSYMCGEVA 

        70         80         90        100        110        120 
RQLLEKRQLA ATDIELIIVA TITPDMPFPA TACLVQDLIG AKNAWAFDLN AACSGFLYAL 

       130        140        150        160        170        180 
NTAIRFVESG AHKKVMVIGA DKMSSIIDYT DRATAILFGD GAGGVLVEPA ADDSCGVLDV 

       190        200        210        220        230        240 
RLYSDGTNGR ERLLMTGGGS RYPASHETVD KKMHYIYQDG RQVFKAAVTA MADVATEIMQ 

       250        260        270        280        290        300 
RNNLTADDVA YLVPHQANQR IIDAIAERMG VDRAKVVSNV GYYGNTTAGT IPICLAELDA 

       310        320 
NNKLKHGDNL VLVSFGAGYT WGGIYVKWQ 

« Hide

References

[1]"Complete sequence of Chlorobium chlorochromatii CaD3."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CaD3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000108 Genomic DNA. Translation: ABB28916.1.
RefSeqYP_379959.1. NC_007514.1.

3D structure databases

ProteinModelPortalQ3AQ09.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3AQ09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3747258.
GenomeReviewsGene locus Cag_1664 in contig CP000108_GR.
KEGGcch:Cag_1664.
PATRIC21371065. VBIChlChl46571_1728.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAKEIGAIN.
PhylomeDBQ3AQ09.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycCCHL340177:CAG_1664-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_CHLCH
AccessionPrimary (citable) accession number: Q3AQ09
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 45 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