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A0M6N9 (A0M6N9_GRAFK) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | 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 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:fabH EMBL CAL68284.1
Synonyms:fabH2 HAMAP MF_01815
Ordered Locus Names:GFO_3343
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Gramella

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 site2871 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
A0M6N9 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 25B34FAA3DEBC200

FASTA33236,483
        10         20         30         40         50         60 
MNKITAAITA VGGYVPEDVL TNEMLEKMVD TTDEWIFSRT GIKERRILKD PDKGTSYLAI 

        70         80         90        100        110        120 
QAAKEILRKT DLDPKEIDLI ILGTVSPDMP VAATGVHVAT EIGATNAFSY DLQAACSSFL 

       130        140        150        160        170        180 
YGMSTGAAYI ESGRYKKVLV IGADKMSSII DYTDRTTCII FGDGAGAVLM EPNEEGLGLQ 

       190        200        210        220        230        240 
DEILRCDSIG RNSLKIAAGG SLIPPTKETI EQKLHYVRQD GKTVFKFAVS NMADVSEEIM 

       250        260        270        280        290        300 
KKNNLTNEDV NWLVAHQANK RIIDATANRM NLTDEDKVLM NIQRYGNTTA ATLPLLLSDY 

       310        320        330 
EKKFKKGDNL IFASFGGGFT WGATYLKWAY NS

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU207366 Genomic DNA. Translation: CAL68284.1.
RefSeqYP_863351.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M6N9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0M6N9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4651399.
GenomeReviewsGene locus GFO_3343 in contig CU207366_GR.
KEGGgfo:GFO_3343.
NMPDRfig|411154.5.peg.3154.
PATRIC22075418. VBIGraFor5527_3222.

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 nameA0M6N9_GRAFK
AccessionPrimary (citable) accession number: A0M6N9
Entry history
Integrated into UniProtKB/TrEMBL: December 12, 2006
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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