Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q81F42 (FABH2_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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 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:BC_1760
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length327 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-Rule MF_01815

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01815

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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-Rule MF_01815

Sequence similarities

Belongs to the FabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3273273-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 HAMAP-Rule MF_01815
PRO_0000110396

Regions

Region252 – 2565ACP-binding By similarity

Sites

Active site1141 By similarity
Active site2511 By similarity
Active site2811 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81F42 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8C03B6E178732409

FASTA32736,247
        10         20         30         40         50         60 
MHSKSRITAI GTYVPDQILS NNDLEKMVHT NDEWIVQRTG MRERRIASEE EYSSNLAIKA 

        70         80         90        100        110        120 
IENLCTTYKK NLEDVDCIIV ATTTADYVFP SVACQIQQYF NIPHTLAFDL NATCAGFTYG 

       130        140        150        160        170        180 
LHVGNSLITS ESHEKVLVVA TETLSKVTDY TDRTTCILFG DGAGAILLER DENTPSFIAA 

       190        200        210        220        230        240 
HMGTNGDGGI HLYRTNLSTT MNGTPLQTNE KIVQNGREVY KWATRTVPKG IKNLLHTVNM 

       250        260        270        280        290        300 
QVDDIDWFIP HSANLRMIES ICEKSQIPIQ KTLTSVEYMG NTSSVTIPLA LNLAIKEGKL 

       310        320 
NNGDTLLLYG FGGGLTHLGL IVEWNLI 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP08736.1.
RefSeqNP_831535.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ81F42.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC1760.

Proteomic databases

PRIDEQ81F42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP08736; AAP08736; BC_1760.
GeneID1204109.
KEGGbce:BC1760.
PATRIC32599281. VBIBacCer54481_1749.

Phylogenomic databases

eggNOGCOG0332.
KOK00648.
OMADWFVPHS.
OrthoDBEOG6J74XN.

Enzyme and pathway databases

BioCycBCER226900:GJEU-1760-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
HAMAPMF_01815. FabH.
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 1 hit.
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH2_BACCR
AccessionPrimary (citable) accession number: Q81F42
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways