ID A0A1V0J0R2_9ROSA Unreviewed; 491 AA. AC A0A1V0J0R2; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 27-NOV-2024, entry version 26. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus. OX NCBI_TaxID=88123 {ECO:0000313|EMBL:ARD02310.1}; RN [1] {ECO:0000313|EMBL:ARD02310.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28186635; DOI=.1111/nph.14461; 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 plastid RT phylogenomics."; RL New Phytol. 214:1355-1367(2017). RN [2] {ECO:0000313|EMBL:QJA13991.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf {ECO:0000313|EMBL:QJA13991.1}; RX PubMed=31666958; RA Xue S., Shi T., Luo W., Ni X., Iqbal S., Ni Z., Huang X., Yao D., Shen Z., RA Gao Z.; RT "Comparative analysis of the complete chloroplast genome among Prunus mume, RT P. armeniaca, and P. salicina."; RL Hortic Res 6:0-89(2019). RN [3] {ECO:0000313|EMBL:QWK45302.1} RP NUCLEOTIDE SEQUENCE. RA Xu Y., Yu J., Li J., Han F., Yuan J.; RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. CC Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its CC carrier protein (BCCP) and then the CO(2) group is transferred by the CC transcarboxylase to acetyl-CoA to form malonyl-CoA. {ECO:0000256|HAMAP- CC Rule:MF_01395}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-carboxybiotinyl-L-lysyl-[protein] + acetyl-CoA = N(6)- CC biotinyl-L-lysyl-[protein] + malonyl-CoA; Xref=Rhea:RHEA:54728, CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01395}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01395}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01395}; CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from CC acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta CC (AccD). {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin CC carboxyl carrier protein, biotin carboxylase and 2 subunits each of CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD). CC {ECO:0000256|ARBA:ARBA00011842}. CC -!- SIMILARITY: Belongs to the AccD/PCCB family. CC {ECO:0000256|ARBA:ARBA00006102, ECO:0000256|HAMAP-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 EMBL; MH700952; QJA13991.1; -; Genomic_DNA. DR EMBL; MW406457; QWK45302.1; -; Genomic_DNA. DR EMBL; MW406461; QWK45642.1; -; Genomic_DNA. DR EMBL; MW406462; QWK45727.1; -; Genomic_DNA. DR EMBL; MW406469; QWK46322.1; -; Genomic_DNA. DR EMBL; MW406472; QWK46577.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1V0J0R2; -. DR UniPathway; UPA00655; UER00711. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. 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_beta. DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR011762; COA_CT_N. DR NCBIfam; TIGR00515; accD; 1. DR PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1. DR PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1. DR Pfam; PF01039; Carboxyl_trans; 1. DR PRINTS; PR01070; ACCCTRFRASEB. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR PROSITE; PS50980; COA_CT_NTER; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01395}; Chloroplast {ECO:0000313|EMBL:QJA13991.1}; 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|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_01395}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_01395}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01395}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01395}; Plastid {ECO:0000313|EMBL:ARD02310.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01395}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01395}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}. FT DOMAIN 227..491 FT /note="CoA carboxyltransferase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50980" FT ZN_FING 231..253 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 250 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 253 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="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 //