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A1TLD7 (FABH_ACIAC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. 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:Aave_1183
OrganismAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length325 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 – 3253253-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_1000070209

Regions

Region253 – 2575ACP-binding By similarity

Sites

Active site1191 By similarity
Active site2521 By similarity
Active site2821 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TLD7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: FBA24B2D0ED9C164

FASTA32534,062
        10         20         30         40         50         60 
MSRYSRITGT GSSLPPRRLT NADLVAELAG RGVETSDQWI VERTGIRARH FAERDVCSSD 

        70         80         90        100        110        120 
LGLEAARQAL DAAGVQPADI DLIIVATSTP DMVFPSTACI LQNKLGANGC PAFDVQAVCS 

       130        140        150        160        170        180 
GFIYALTVAD SMIRSGAARR ALVVGSEVFS RLLDFNDRTT CVLFGDGAGA VVLEASETPG 

       190        200        210        220        230        240 
ILASDLHADG RHVGILCVPG NVYGGQILGD PLLKMDGQAV FKLAVGVLDK AARAVLDKAG 

       250        260        270        280        290        300 
LKESDVDWLI PHQANIRIMQ GTAKKLGLPM DRVVVTVDQH GNTSAASIPL ALDHAVRSGQ 

       310        320 
ARPGQNLLLE GVGGGFTWGA VLLTL 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AAC00-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000512 Genomic DNA. Translation: ABM31775.1.
RefSeqYP_969549.1. NC_008752.1.

3D structure databases

ProteinModelPortalA1TLD7.
SMRA1TLD7. Positions 4-324.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TLD7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4667457.
GenomeReviewsGene locus Aave_1183 in contig CP000512_GR.
KEGGaav:Aave_1183.
NMPDRfig|397945.5.peg.1033.
PATRIC20677406. VBIAciCit38535_1207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMACSSDLGL.
PhylomeDBA1TLD7.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycAAVE397945:AAVE_1183-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_ACIAC
AccessionPrimary (citable) accession number: A1TLD7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 40 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