ID A0A7T0M4F7_9ERIC Unreviewed; 513 AA. AC A0A7T0M4F7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 27-MAR-2024, entry version 11. DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {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:QPL15763.1}; OS Camellia pubipetala. OG Plastid; Chloroplast {ECO:0000313|EMBL:QPL15763.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; Ericales; Theaceae; Camellia. OX NCBI_TaxID=147930 {ECO:0000313|EMBL:QPL15763.1}; RN [1] {ECO:0000313|EMBL:QPL15763.1} RP NUCLEOTIDE SEQUENCE. RA Fan Y., Zhao B.; RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QSJ55674.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf {ECO:0000313|EMBL:QSJ55674.1}; RA Tang S., Zheng H.; RL Submitted (JAN-2021) 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=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl- CC CoA + N(6)-biotinyl-L-lysyl-[protein]; 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, biotin carboxylase and 2 subunits each of CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD). CC {ECO:0000256|ARBA:ARBA00011842}. CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin CC carboxyl carrier protein, biotin carboxylase and two subunits each of CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD). CC {ECO:0000256|HAMAP-Rule:MF_01395}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000256|HAMAP- CC Rule:MF_01395}. 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; MW186719; QPL15763.1; -; Genomic_DNA. DR EMBL; MW543444; QSJ55674.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7T0M4F7; -. DR UniPathway; UPA00655; UER00711. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0009570; C:chloroplast stroma; 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_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:QPL15763.1}; 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|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|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01395}; Plastid {ECO:0000313|EMBL:QPL15763.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01395}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}. FT DOMAIN 246..513 FT /note="CoA carboxyltransferase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50980" FT ZN_FING 250..272 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT REGION 43..76 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 54..69 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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" FT BINDING 269 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 272 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" SQ SEQUENCE 513 AA; 58361 MW; F86D215041ACCAFA CRC64; MTIHLLYFHA NRGQENYMEK WRFNSILSKK ELEHRCRLSK SMDSLGPIEN TSESEDPNRN DRDKNIHSWN DSDSSSYSNV DHLFGVKDIQ NFISDDTFLV RDSNGGGYSI YFDIENQIFE INKDRSFLSE LESYFYSYRN SGYLNNGSKS EDPYYDRYMY DTQYSWNNHI NSCIDSYLHS QIRIDTYIVS GSNNYSDSYI YSSVCGESGN SSESESSSIR TSTNGSDLNI RESANDLDVT QKYKHLWVQC ENCYGLNYKK FFKSKMNICE QCGYHLKMNS SDRIELLIDP GTWDPMDEDM VSLDPIEFHS EEEPYKDRID SYQRKTGLTE AVQTGIGQLN GIPVAIGVMD FQFMGGSMGS VVGEKITRLI EHATKKFLPL IIVCASGGAR MQEGSLSLMQ MAKISSALYD YQSNKKLFYI SILTSPTTGG VTASFGMLGD IIIAEPNAYI AFAGKRVIEQ TLNKTVPEGS QAAEYLFQKG LFDLIVPRNP LKSVLSELFQ LHAFFPLNKN SIK //