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A1BJA1 (FABH_CHLPD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. 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:Cpha266_2490
OrganismChlorobium phaeobacteroides (strain DSM 266) [Complete proteome] [HAMAP]
Taxonomic identifier290317 [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_1000056340

Regions

Region256 – 2605ACP-binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A1BJA1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 7CA732AA90950317

FASTA32935,624
        10         20         30         40         50         60 
MKAAITATAK YLPQSVLSNH DLEQMLETND EWIRSRTGIG ERRIMNDPSK ATAYMCGEVA 

        70         80         90        100        110        120 
LQLLEARKMK PEEIEVIIVA TMTPDMLFPA TACFVQGIIG ATNAWAFDIN AACSGFLFAL 

       130        140        150        160        170        180 
STASRLIESG AHKKVMVIGG DKMSSVIDYT NRSTAILFGD GAAGVILEPS TNDNYGILDA 

       190        200        210        220        230        240 
RLYSDGASGT SHLLMAAGGS LNPATHETVD KRMHFLHQDG KQVFKSAVTS MADVAAEIMT 

       250        260        270        280        290        300 
RNNLSAEDIS FLVPHQANQR IINATAERMG LDQEKVYSNV ARYGNTTAGT IPICLAELNE 

       310        320 
QEQLKTGSNL VLVSFGAGYT WGGIYIKWQ 

« Hide

References

[1]"Complete sequence of Chlorobium phaeobacteroides DSM 266."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Bryant D.A., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 266.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000492 Genomic DNA. Translation: ABL66478.1.
RefSeqYP_912902.1. NC_008639.1.

3D structure databases

ProteinModelPortalA1BJA1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1BJA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4568543.
GenomeReviewsGene locus Cpha266_2490 in contig CP000492_GR.
KEGGcph:Cpha266_2490.
NMPDRfig|290317.7.peg.2606.
PATRIC21393637. VBIChlPha122104_2976.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMATSHEWIS.
PhylomeDBA1BJA1.
ProtClustDBPRK09352.

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_CHLPD
AccessionPrimary (citable) accession number: A1BJA1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 38 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