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Q6B945 (FABH_GRATL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Grc000008
Encoded onPlastid; Chloroplast
OrganismGracilaria tenuistipitata var. liui (Red alga)
Taxonomic identifier285951 [NCBI]
Taxonomic lineageEukaryotaRhodophytaFlorideophyceaeGracilarialesGracilariaceaeGracilaria

Protein attributes

Sequence length330 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

Plastidchloroplast 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3303303-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_0000110516

Regions

Region256 – 2605ACP-binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q6B945 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 4DF9347E04164614

FASTA33036,075
        10         20         30         40         50         60 
MQGAQIISIG SAVPDLCINN KEISQIVETS DEWIVTRTGI QERRVLTGTN KSVVDLAYSA 

        70         80         90        100        110        120 
AMKALDKIHM DPLEIDLIIL ATSSPNDLFG SASQVQAKIG AARAVAFDLT AACSGFVLAI 

       130        140        150        160        170        180 
VTATQFIQNG SYKNILIIGA DVLSKWIDWS DRKTCILFGD GAGAAIIQAC YEEDNAILGF 

       190        200        210        220        230        240 
QLNTDGKQYK KLSITYKENN YSLNTLKLFQ GQFQYISMNG KEVYKFAVSK VPASIIKCLN 

       250        260        270        280        290        300 
ALHLSIQDVN WLLLHQANKR ILQAVANRLS VDNYKIISNL SKYGNTSAAS IPLALDEAWQ 

       310        320        330 
NNQIAKEDII VISGFGAGLT WGTVVIKWKC 

« Hide

References

[1]"Comparative analysis of the complete plastid genome sequence of the red alga Gracilaria tenuistipitata var. liui provides insights into the evolution of rhodoplasts and their relationship to other plastids."
Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.
J. Mol. Evol. 59:464-477(2004) [PubMed: 15638458] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY673996 Genomic DNA. Translation: AAT79590.1.
RefSeqYP_063515.1. NC_006137.1.

3D structure databases

ProteinModelPortalQ6B945.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2943979.

Phylogenomic databases

ProtClustDBCHL00203.

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.
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_GRATL
AccessionPrimary (citable) accession number: Q6B945
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: September 13, 2004
Last modified: November 16, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families