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

 H2FDZ6_9ASPA            Unreviewed;       488 AA.
H2FDZ6;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
22-NOV-2017, entry version 33.
RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {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:AEX96879.1};
Hosta ventricosa (blue plantain lily).
Plastid; Chloroplast {ECO:0000313|EMBL:AEX96879.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
Agavoideae; Hosta.
NCBI_TaxID=39527 {ECO:0000313|EMBL:AEX96879.1};
[1] {ECO:0000313|EMBL:AEX96879.1}
NUCLEOTIDE SEQUENCE.
PubMed=22291168; DOI=10.3732/ajb.1100491;
Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
Pires J.C.;
"Quality and quantity of data recovered from massively parallel
sequencing: Examples in Asparagales and Poaceae.";
Am. J. Bot. 99:330-348(2012).
[2] {ECO:0000313|EMBL:APO12231.1}
NUCLEOTIDE SEQUENCE.
PubMed=27793858;
McKain M.R., McNeal J.R., Kellar P.R., Eguiarte L.E., Pires J.C.,
Leebens-Mack J.;
"Timing of rapid diversification and convergent origins of active
pollination within Agavoideae (Asparagaceae).";
Am. J. Bot. 103:1717-1729(2016).
-!- 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, biotin carboxylase and 2 subunits
each of ACCase subunit alpha and ACCase plastid-coded subunit beta
(accD). {ECO:0000256|SAAS:SAAS00709959}.
-!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
biotin carboxyl carrier protein, biotin carboxylase and two
subunits each of ACCase subunit alpha and ACCase plastid-coded
subunit beta (accD). {ECO:0000256|HAMAP-Rule:MF_01395}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000256|HAMAP-Rule:MF_01395}.
-!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP-
Rule:MF_01395}.
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EMBL; JQ277068; AEX96879.1; -; Genomic_DNA.
EMBL; KX931460; APO12231.1; -; Genomic_DNA.
RefSeq; YP_009335173.1; NC_032706.1.
GeneID; 30766934; -.
UniPathway; UPA00655; UER00711.
GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
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_sf.
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};
Chloroplast {ECO:0000313|EMBL:AEX96879.1};
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};
Plastid {ECO:0000313|EMBL:AEX96879.1};
Transferase {ECO:0000313|EMBL:APO12231.1};
Zinc {ECO:0000256|HAMAP-Rule:MF_01395};
Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}.
DOMAIN 222 488 CoA carboxyltransferase N-terminal.
{ECO:0000259|PROSITE:PS50980}.
ZN_FING 226 248 C4-type. {ECO:0000256|HAMAP-
Rule:MF_01395}.
METAL 226 226 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
METAL 229 229 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
METAL 245 245 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
METAL 248 248 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}.
SEQUENCE 488 AA; 55486 MW; 4F0763E388D18715 CRC64;
MKKWWFNSML SKDKEKLEHK RGLSKSIDSL NAVGHTGGSE EPLLNDTEKN IPSWSDNSSY
NSRYSFSNVD YLFDIRDIWS LISDNTFLVR DGNGDSYSVY FDIENQIFEI DNNSFFFSYL
NNRSKSNNHY YYHYMYDTQS SWNNHINSCI DSYLRFEVSI HSYIFGGTDN YSDSYISSFI
CTEGVSGSES RNSSIKTGGN SRDFNIRGRS NDFDINKKYR NLWVQCENCY GLNYKKFFRS
KMNICEQCGY HLKMSSSDRI ELLIDPGTWD PMDEDMVSMD PIEFHSEEEP YRDRIDSYQR
RTGLTEAVQT GIGQLNGIPI AIGVMDFQFM GGSMGSVVGE KITRLIEYAT NRSLPVIIVC
ASGGARMQEG SLSLMQMAKI SSASYNYQSN KKLFYVSILT SPTTGGVTAS FGMLGDVIIA
EPNAYIAFAG KRVIEQTLNK TVPDGSQAAE YSFHKGLFDP IVPRNLLKGV LSELFQLHGF
FPLNKNKK


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