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B1LZA0 (B1LZA0_METRJ) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 44. 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 HAMAP-Rule MF_01815
EC=2.3.1.180 HAMAP-Rule MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP-Rule MF_01815
Beta-ketoacyl-ACP synthase III HAMAP-Rule MF_01815
Gene names
Name:fabH HAMAP-Rule MF_01815
Ordered Locus Names:Mrad2831_3968 EMBL ACB25942.1
OrganismMethylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831) [Complete proteome] [HAMAP] EMBL ACB25942.1
Taxonomic identifier426355 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium ›

Protein attributes

Sequence length335 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 SAAS SAAS004655

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815 SAAS SAAS004655

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01815 SAAS SAAS004655

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01815 SAAS SAAS004655.

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. HAMAP-Rule MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region263 – 2675ACP-binding By similarity HAMAP-Rule MF_01815

Sites

Active site1281 By similarity HAMAP-Rule MF_01815
Active site2621 By similarity HAMAP-Rule MF_01815
Active site2921 By similarity HAMAP-Rule MF_01815

Sequences

Sequence LengthMass (Da)Tools
B1LZA0 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: F2251D22DA37780E

FASTA33535,471
        10         20         30         40         50         60 
MATLRTDPGQ HRRVPPLRSV VVGTGSSLPA RVVTNADLAE RVDTSDEWIV QRTGIRQRHL 

        70         80         90        100        110        120 
AGPDETTSVL GTRAARAALD DAGLTADDID LVICATSTPD HTFPATATQI QAALGIHQGA 

       130        140        150        160        170        180 
AFDLQAVCAG FVFAVSTADK FLTTGAARRA LVIGAETFSR IVDWEDRTTC VLFGDGAGAV 

       190        200        210        220        230        240 
VLEAQEGAGD RGVLSASLRS DGRHREKLYV DGGPGSTGTT GHLRMEGRDV FRFAVGQVTD 

       250        260        270        280        290        300 
VIVEAFAQAG ITAEELDWFV PHQANRRIIE ASADKLGVAR DKIVLTVDRH GNTSAASIPL 

       310        320        330 
ALDVARRDGR IRAGDLVMIE AIGGGFSWGA ALIRW

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium radiotolerans JCM 2831."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marx C.J., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27329 / DSM 1819 / JCM 2831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001001 Genomic DNA. Translation: ACB25942.1.
RefSeqYP_001756625.1. NC_010505.1.

3D structure databases

ProteinModelPortalB1LZA0.
ModBaseSearch...

Protein-protein interaction databases

STRING426355.Mrad2831_3968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB25942; ACB25942; Mrad2831_3968.
GeneID6140023.
KEGGmrd:Mrad2831_3968.
PATRIC22576382. VBIMetRad70578_4064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHOG000246674.
KOK00648.
OMAASPDESC.
ProtClustDBCLSK2330945.

Enzyme and pathway databases

BioCycMRAD426355:GJB5-4013-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. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB1LZA0_METRJ
AccessionPrimary (citable) accession number: B1LZA0
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 1, 2013
This is version 44 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