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F3Y967 (F3Y967_MELPT) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 13. 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:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP-Rule MF_01395
Short name=ACCase subunit beta HAMAP-Rule MF_01395
Short name=Acetyl-CoA carboxylase carboxyltransferase subunit beta HAMAP-Rule MF_01395
EC=6.4.1.2 HAMAP-Rule MF_01395
Gene names
Name:accD HAMAP-Rule MF_01395
Ordered Locus Names:MPTP_0577 EMBL BAK21045.1
OrganismMelissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443) [Complete proteome] [HAMAP] EMBL BAK21045.1
Taxonomic identifier940190 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Enterococcaceae › Melissococcus ›

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA By similarity. HAMAP-Rule MF_01395

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP-Rule MF_01395

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01395

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP-Rule MF_01395

Subunit structure

Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD) By similarity. SAAS SAAS011762 HAMAP-Rule MF_01395

Subcellular location

Cytoplasm By similarity SAAS SAAS000022 HAMAP-Rule MF_01395.

Sequence similarities

Belongs to the AccD/PCCB family. HAMAP-Rule MF_01395

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Zinc finger37 – 5822C4-type By similarity HAMAP-Rule MF_01395

Sites

Metal binding371Zinc By similarity HAMAP-Rule MF_01395
Metal binding401Zinc By similarity HAMAP-Rule MF_01395
Metal binding551Zinc By similarity HAMAP-Rule MF_01395
Metal binding581Zinc By similarity HAMAP-Rule MF_01395

Sequences

Sequence LengthMass (Da)Tools
F3Y967 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 36F75387E9FED780

FASTA29533,423
        10         20         30         40         50         60 
MALFKKKKYI RINPEHSSKK QESHKKPSVP DNMWAKCPNC KRTLYTKNIG EEKICPHCSY 

        70         80         90        100        110        120 
SFRIGAWERI SLTVDEGSFE EWDNEVITKD PLEFPGYLDK IQKIQEKTDL SEAVLTGTAL 

       130        140        150        160        170        180 
IDEQKIAIGV MDSNFIMGSM GTVVGEKITR LFEKSTKEKL PVILFTASGG ARMQEGIFSL 

       190        200        210        220        230        240 
MQMAKVSSAL QRHNRAGLLY ITVLTDPTTG GVTASFAMDG DIILAEPQSL IGFAGRRVIE 

       250        260        270        280        290 
QTIHQELPED FQKAEFLLKH GFIDRIVPRN QMKQQLSQLI HMHSMKGWLD EKEND

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Melissococcus plutonius ATCC 35311."
Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M., Miyoshi-Akiyama T.
J. Bacteriol. 193:4029-4030(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443.
[2]"Whole genome sequence of Melissococcus plutonius ATCC 35311."
Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D., Akiyama T.
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 35311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP012200 Genomic DNA. Translation: BAK21045.1.
RefSeqYP_004455854.1. NC_015516.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAK21045; BAK21045; MPTP_0577.
GeneID10595403.
KEGGmps:MPTP_0577.
PATRIC54619875. VBIMelPlu182073_0570.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01963.

Enzyme and pathway databases

BioCycMPLU940190:GH20-727-MONOMER.
UniPathwayUPA00655; UER00711.

Family and domain databases

HAMAPMF_01395. AcetylCoA_CT_beta.
InterProIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR011762. COA_CT_N.
[Graphical view]
PfamPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSPR01070. ACCCTRFRASEB.
TIGRFAMsTIGR00515. accD. 1 hit.
PROSITEPS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF3Y967_MELPT
AccessionPrimary (citable) accession number: F3Y967
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 3, 2013
This is version 13 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