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F7ZTB7 (F7ZTB7_CLOAT) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 15. 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 EMBL AEI34012.1
ORF Names:SMB_G3610 EMBL AEI34012.1
OrganismClostridium acetobutylicum DSM 1731 EMBL AEI34012.1
Taxonomic identifier991791 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length285 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. HAMAP-Rule MF_01395 SAAS SAAS011762

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01395 SAAS SAAS011762.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Zinc finger37 – 5923C4-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 binding561Zinc By similarity HAMAP-Rule MF_01395
Metal binding591Zinc By similarity HAMAP-Rule MF_01395

Sequences

Sequence LengthMass (Da)Tools
F7ZTB7 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: D157DE90B38C1731

FASTA28531,702
        10         20         30         40         50         60 
MGLFKKRKYI TVSSKNLDEN NDVENQPTIP DGMWIKCSKC GKILYKSDVD DNFKVCPKCN 

        70         80         90        100        110        120 
AHLRMNARER IEFIIDEGTF IEFDKNMMAA NPLEFPNYEA KIKSMQEKTG LKDGVVTGLG 

       130        140        150        160        170        180 
NINGYKTVIA VMDSNFMMGS MGSVVGEKIT RAIEEATERK LPVIIFTTSG GARMQEGMFS 

       190        200        210        220        230        240 
LMQMAKTSAA LAKHNEAGLL YVSVLTDPTT GGVTASFAML GDIILAEPKT LIGFAGRRVI 

       250        260        270        280 
EQTINQKLPS DFQTSEFLFK HGFIDMIVER KELKVTLGNI LRMHS

« Hide

References

[1]"Complete Genome Sequence of Clostridium acetobutylicum DSM 1731, a Solvent-Producing Strain with Multireplicon Genome Architecture."
Bao G., Wang R., Zhu Y., Dong H., Mao S., Zhang Y., Chen Z., Li Y., Ma Y.
J. Bacteriol. 193:5007-5008(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 1731 EMBL AEI34012.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002660 Genomic DNA. Translation: AEI34012.1.
RefSeqYP_004638223.1. NC_015687.1.

3D structure databases

ProteinModelPortalF7ZTB7.
SMRF7ZTB7. Positions 30-284.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEI34012; AEI34012; SMB_G3610.
GeneID10851515.
KEGGcae:SMB_G3610.

Phylogenomic databases

KOK01963.

Enzyme and pathway databases

BioCycCACE991791:GIVN-3693-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 nameF7ZTB7_CLOAT
AccessionPrimary (citable) accession number: F7ZTB7
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: April 3, 2013
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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