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Reviewed, UniProtKB/Swiss-Prot Q82M29 (FABH2_STRAW)

Last modified November 3, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2
    EC=2.3.1.180
Alternative name(s):
    3-oxoacyl-[acyl-carrier-protein] synthase III protein 2
    Beta-ketoacyl-ACP synthase III 2
      Short name=KAS III 2
Gene names
Name: fabH2
Ordered Locus Names: SAV_1831
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Probable.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.

Sequence similarities

Belongs to the fabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3153153-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 HAMAP MF_01815
PRO_0000110482

Regions

Region242 – 2465ACP-binding By similarity

Sites

Active site1131 By similarity
Active site2411 By similarity
Active site2711 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82M29-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E490D12CBA86583C

FASTA31532,372
        10         20         30         40         50         60 
MNGSRIAAVG HYQPAKVLTN EDLASLVDTS DEWIRSRVGI RTRHFAGPDE PVDELAGHAA 

        70         80         90        100        110        120 
AKALASAGLA PADIDLVLVA TSTAEDRSPN MAARVAARLG IPSPAAMDIN VVCAGFTHAL 

       130        140        150        160        170        180 
ATADHAVRAG AATRALVIGA DKMSAVTDWS DRTTCVLVGD GAGAAVVDAC PEGAEPGIGP 

       190        200        210        220        230        240 
VLWGSVPEMG HAVRIEGTPP RFAQEGQSVY RWATTQLPAI ARRACERAGL TPADLAGVVL 

       250        260        270        280        290        300 
HQANLRIIEP LAAKIGAVNA VVARDVVESG NTSAASIPLA FSKLVERGEI STGDPVLLFG 

       310 
FGGNLSYAGQ VIRCP 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

BA000030 Genomic DNA. Translation: BAC69542.1.
RefSeqNP_823007.1.

3D structure databases

HSSPHSSP built from PDB template 1HNK based on UniProtKB P24249.
ModBaseSearch...

Genome annotation databases

GeneID1210291.
GenomeReviewsGene locus SAV_1831 in contig BA000030_GR.
KEGGsma:SAV_1831.
NMPDRfig|227882.1.peg.1833.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ82M29.
OMAVFRWATT.

Enzyme and pathway databases

BioCycSAVE227882:SAV1831-MON.
BRENDA2.3.1.180. 140873.

Family and domain databases

HAMAPMF_01815.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
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]
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH2_STRAW
AccessionPrimary (citable) accession number: Q82M29
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents