Skip Header

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

B2IBF3 (B2IBF3_BEII9) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 25. 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 1 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III 1 HAMAP MF_01815
Beta-ketoacyl-ACP synthase III 1 HAMAP MF_01815
Gene names
Name:fabH1 HAMAP MF_01815
Ordered Locus Names:Bind_3017
OrganismBeijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) [Complete proteome] [HAMAP]
Taxonomic identifier395963 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Beijerinckiaceae › Beijerinckia

Protein attributes

Sequence length348 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

Region276 – 2805ACP-binding By similarity HAMAP MF_01815

Sites

Active site1341 By similarity HAMAP MF_01815
Active site2751 By similarity HAMAP MF_01815
Active site3051 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
B2IBF3 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 13DB5AD53B724584

FASTA34837,176
        10         20         30         40         50         60 
MGTIIFLLTT GPHDRPERLN SLTTSLILGT GAYAPKKILS NQDLEQMIAT TDQWITERTG 

        70         80         90        100        110        120 
IKTRHIAAEG ETTSDMAVCA AREALALAGT SAEELDMIIV GTISADMPLP SCAVLIQAKL 

       130        140        150        160        170        180 
GARNAFAFDL SAACAGSLYG MSIADQFIRS GKARRVLVIG AELLSRLIDW SDRNTCILFG 

       190        200        210        220        230        240 
DGAGAVVMGP CEDPQRGLLS THLHTDGSTA DLLKIPGGGS LHPQSEEVLA NKWHKVAMNG 

       250        260        270        280        290        300 
REIYKFAAKV LPLALNEALQ ANGLQANDVD HVIAHQANAR IVETVLERVG IPQEKCWLNL 

       310        320        330        340 
DRYGNTSSAS LPISLDEANR AGRLRPGDLI AMMAIGAGMA WGSALLRW

« Hide

References

[1]"Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC 9039."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N. expand/collapse author list , Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9039 / DSM 1715 / NCIB 8712.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001016 Genomic DNA. Translation: ACB96579.1.
RefSeqYP_001834068.1. NC_010581.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2IBF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6198235.
GenomeReviewsGene locus Bind_3017 in contig CP001016_GR.
KEGGbid:Bind_3017.
PATRIC21089057. VBIBeiInd21058_3439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMAFLNLPSK.
ProtClustDBCLSK946392.

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 nameB2IBF3_BEII9
AccessionPrimary (citable) accession number: B2IBF3
Entry history
Integrated into UniProtKB/TrEMBL: June 10, 2008
Last sequence update: June 10, 2008
Last modified: December 14, 2011
This is version 25 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