ID A0A1V0J0R2_9ROSA Unreviewed; 491 AA. AC A0A1V0J0R2; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 20-JUN-2018, entry version 7. DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395}; DE Short=ACCase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395}; DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_01395}; DE EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01395}; GN Name=accD {ECO:0000256|HAMAP-Rule:MF_01395, GN ECO:0000313|EMBL:ARD02310.1}; OS Prunus salicina. OG Plastid {ECO:0000313|EMBL:ARD02310.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Rosales; Rosaceae; Amygdaloideae; OC Amygdaleae; Prunus. OX NCBI_TaxID=88123 {ECO:0000313|EMBL:ARD02310.1}; RN [1] {ECO:0000313|EMBL:ARD02310.1} RP NUCLEOTIDE SEQUENCE. RA Zhang S.-D., Jin J.-J., Chen S.-Y., Chase M.W., Soltis D.E., Li H.-T., RA Yang J.-B., Li D.-Z., Yi T.-S.; RT "Diversification of Rosaceae since the Late Cretaceous based on RT plastid phylogenomics."; RL New Phytol. 0:0-0(2017). CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) CC complex. Biotin carboxylase (BC) catalyzes the carboxylation of CC biotin on its carrier protein (BCCP) and then the CO(2) group is CC transferred by the transcarboxylase to acetyl-CoA to form malonyl- CC CoA. {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- CATALYTIC ACTIVITY: [Biotin carboxyl-carrier protein]-N(6)- CC carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier CC protein]-N(6)-biotinyl-L-lysine + malonyl-CoA. {ECO:0000256|HAMAP- CC Rule:MF_01395}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01395}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01395}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of CC biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) CC and two subunits each of ACCase subunit alpha (AccA) and ACCase CC subunit beta (AccD). {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of CC biotin carboxyl carrier protein, biotin carboxylase and 2 subunits CC each of ACCase subunit alpha and ACCase plastid-coded subunit beta CC (accD). {ECO:0000256|SAAS:SAAS00709959}. CC -!- SUBCELLULAR LOCATION: Plastid {ECO:0000256|SAAS:SAAS00710087}. CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000256|HAMAP- CC Rule:MF_01395}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KY420002; ARD02310.1; -; Genomic_DNA. DR UniPathway; UPA00655; UER00711. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01395; AcetylCoA_CT_beta; 1. DR InterPro; IPR034733; AcCoA_carboxyl. DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR011762; COA_CT_N. DR Pfam; PF01039; Carboxyl_trans; 1. DR PRINTS; PR01070; ACCCTRFRASEB. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR00515; accD; 1. DR PROSITE; PS50980; COA_CT_NTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01395}; KW Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395}; KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01395}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01395}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01395}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01395}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01395}; KW Plastid {ECO:0000313|EMBL:ARD02310.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01395, KW ECO:0000313|EMBL:ARD02310.1}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}. FT DOMAIN 227 491 CoA carboxyltransferase N-terminal. FT {ECO:0000259|PROSITE:PS50980}. FT ZN_FING 231 253 C4-type. {ECO:0000256|HAMAP-Rule: FT MF_01395}. FT METAL 231 231 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 234 234 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 250 250 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 253 253 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. SQ SEQUENCE 491 AA; 55896 MW; 5AFED6CFA905C662 CRC64; MEKRRFHSML FNGELEYRCR LSKSMDSLGP FENTSVSEDP IINDMDKDIL NCNDKSNYSN VDRLVSDRYI RNFISADTFF VRDSNRDSYS IYFDIENKNF EIDNDRSFLS ELKSSFYSYQ TSSYINNAPK SNDTRHDRYV YDTNSHYIWN NHINSCIDSY LRSQICIDSY ILSNSDNYSD SYIYSYICSE SVNSSKSESS SIKTSTDGSD FTISSNNLNV TQKYRHLWIQ CENCYGLNYK KFLKLKMNIC EQCGCHLKMS SFDRIELSID PGTWDPMNED MVSLDPIEFH SEEEPYKNRI DSYQKNTGLT EAVQTGTGQL NGIPVAIGVM DFQFMGGSMG SVVGEKITRL AEYATNQFLP LIIVCASGGA RMQEGSLSLM QMAKISSALY DYQSNKKLFY VSILTSPTTG GVTASFGMLG DIIIAEPNAY IAFAGKRVIE QTLNKTVPED SQVAEYLFHK GLFDPIVPRN PLKGVLGELF RLHAFFPLNQ N //