Skip Header

Contribute Send feedback
Read comments (?) or add your own

A5FM89 (A5FM89_FLAJ1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 36. Feed History...

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

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 2 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III 2 HAMAP MF_01815
Beta-ketoacyl-ACP synthase III 2 HAMAP MF_01815
Gene names
Name:fabH2 HAMAP MF_01815
Ordered Locus Names:Fjoh_0646
OrganismFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae) [Complete proteome] [HAMAP]
Taxonomic identifier376686 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Flavobacterium

Protein attributes

Sequence length332 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 SAAS SAAS013747

Subunit structure

Homodimer By similarity. HAMAP MF_01815 SAAS SAAS013747

Subcellular location

Cytoplasm By similarity HAMAP MF_01815 SAAS SAAS013747.

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. HAMAP MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region257 – 2615ACP-binding By similarity HAMAP MF_01815

Sites

Active site1161 By similarity HAMAP MF_01815
Active site2561 By similarity HAMAP MF_01815
Active site2861 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
A5FM89 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 9EF8608CDDCE6345

FASTA33236,208
        10         20         30         40         50         60 
MNTITAAITA VGGYVPDFVL SNKVLETMVD TNDEWITTRT GIKERRILKD ADKGTSYLAI 

        70         80         90        100        110        120 
QAAQDLIAKA NIDPLEIDMV IMATATPDMM VASTGVYVAT EIGAVNAFAY DLQAACSSFL 

       130        140        150        160        170        180 
YGMSTAAAYV QSGRYKKVLL IGADKMSSIV DYTDRATCII FGDGAGAVLF EPNYEGLGLQ 

       190        200        210        220        230        240 
DEYLRSDGVG RDFLKIPAGG SLIPASEDTV KNRQHNIMQD GKTVFKYAVT NMADASELIL 

       250        260        270        280        290        300 
QRNNLTNQDV DWLVPHQANK RIIDATAGRL ELEESKVLVN IERYGNTTSG TLPLVLSDFE 

       310        320        330 
NQFKKGDNII LAAFGGGFTW GSIYLKWAYD KK

« Hide

References

[1]"Complete sequence of Flavobacterium johnsoniae UW101."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Xie G., McBride M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17061 / DSM 2064 / UW101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000685 Genomic DNA. Translation: ABQ03681.1.
RefSeqYP_001193000.1. NC_009441.1.

3D structure databases

ProteinModelPortalA5FM89.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5FM89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5091391.
GenomeReviewsGene locus Fjoh_0646 in contig CP000685_GR.
KEGGfjo:Fjoh_0646.
PATRIC21895559. VBIFlaJoh53613_0665.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAKEIGAIN.
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 nameA5FM89_FLAJ1
AccessionPrimary (citable) accession number: A5FM89
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info