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Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 6.4.1.2)

 A0A0A8WN57_9DELT        Unreviewed;       270 AA.
A0A0A8WN57;
04-MAR-2015, integrated into UniProtKB/TrEMBL.
04-MAR-2015, sequence version 1.
27-SEP-2017, entry version 20.
RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395};
EC=6.4.1.2 {ECO:0000256|HAMAP-Rule:MF_01395};
Name=accD {ECO:0000256|HAMAP-Rule:MF_01395,
ECO:0000313|EMBL:GAM08449.1};
ORFNames=OR1_00721 {ECO:0000313|EMBL:GAM08449.1};
Geobacter sp. OR-1.
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
Geobacteraceae; Geobacter.
NCBI_TaxID=1266765 {ECO:0000313|EMBL:GAM08449.1, ECO:0000313|Proteomes:UP000030972};
[1] {ECO:0000313|EMBL:GAM08449.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM08449.1,
ECO:0000313|Proteomes:UP000030972};
PubMed=23668621; DOI=10.1021/es400231x;
Ohtsuka T., Yamaguchi N., Makino T., Sakurai K., Kimura K., Kudo K.,
Homma E., Dong DT., Amachi S.;
"Arsenic dissolution from Japanese paddy soil by a dissimilatory
arsenate-reducing bacterium Geobacter sp. OR-1.";
Environ. Sci. Technol. 47:6263-6271(2013).
[2] {ECO:0000313|EMBL:GAM08449.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM08449.1,
ECO:0000313|Proteomes:UP000030972};
Ehara A., Suzuki H., Amachi S.;
"Draft Genome Sequence of Geobacter sp. Strain OR-1, an Arsenate-
Respiring Bacterium Isolated from Japanese Paddy Soil.";
Genome Announc. 3:e01478-14(2015).
-!- 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 CO(2) group is
transferred by the transcarboxylase to acetyl-CoA to form malonyl-
CoA. {ECO:0000256|HAMAP-Rule:MF_01395}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01395}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_01395};
Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01395};
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01395}.
-!- SUBUNIT: 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). {ECO:0000256|HAMAP-Rule:MF_01395,
ECO:0000256|SAAS:SAAS00753290}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395,
ECO:0000256|SAAS:SAAS00710105}.
-!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
Rule:MF_01395}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:GAM08449.1}.
-----------------------------------------------------------------------
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EMBL; BAZF01000002; GAM08449.1; -; Genomic_DNA.
RefSeq; WP_041969965.1; NZ_BAZF01000002.1.
EnsemblBacteria; GAM08449; GAM08449; OR1_00721.
UniPathway; UPA00655; UER00711.
Proteomes; UP000030972; Unassembled WGS sequence.
GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
InterPro; IPR029045; ClpP/crotonase-like_dom.
InterPro; IPR011762; COA_CT_N.
Pfam; PF01039; Carboxyl_trans; 1.
PRINTS; PR01070; ACCCTRFRASEB.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR00515; accD; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01395};
Complete proteome {ECO:0000313|Proteomes:UP000030972};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01395,
ECO:0000256|SAAS:SAAS00709970};
Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
Ligase {ECO:0000256|HAMAP-Rule:MF_01395};
Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01395};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01395};
Reference proteome {ECO:0000313|Proteomes:UP000030972};
Transferase {ECO:0000313|EMBL:GAM08449.1};
Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
DOMAIN 11 270 CoA carboxyltransferase N-terminal.
{ECO:0000259|PROSITE:PS50980}.
ZN_FING 15 37 C4-type. {ECO:0000256|HAMAP-
Rule:MF_01395}.
METAL 15 15 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
METAL 18 18 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
METAL 34 34 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
METAL 37 37 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
SEQUENCE 270 AA; 29497 MW; 1C3502525F353D35 CRC64;
MKKTVKVPEG LWTKCSNCGE VIISKEIENN LNVCPKCSFH FRVSARKRLD ILLDEGSFRE
HDAGMVSVDF LEFKDSKSYQ DRIDVALAKG GSKDAVICGE GKIEGIPVDI SVFDFSFMGG
SMGSVVGEKI TRSIERGVKN HTPVIVVSAS GGARMQESIL SLMQMAKTSA ALARLKAKGL
PFLSILTDPT TGGVTASFAM LGDINIAEPR ALVGFAGPRV IEQTIRQKLP EGFQRAEYLL
DHGMVDIIVE RKDMRRKVAS ILSMLYRPKA


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