ID A0A482CGF9_9FLOR Unreviewed; 290 AA. AC A0A482CGF9; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 24-JAN-2024, entry version 13. 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:QBL75584.1}; OS Corallina ferreyrae. OG Plastid {ECO:0000313|EMBL:QBL75584.1}. OC Eukaryota; Rhodophyta; Florideophyceae; Corallinophycidae; Corallinales; OC Corallinaceae; Corallinoideae; Corallina. OX NCBI_TaxID=2547422 {ECO:0000313|EMBL:QBL75584.1}; RN [1] {ECO:0000313|EMBL:QBL75584.1} RP NUCLEOTIDE SEQUENCE. RA Bustamante D.E., Calderon M.S., Hughey J.R.; RT "Conspecificity of the Peruvian Corallina ferreyrae with C. caespitosa RT (Corallinaceae, Rhodophyta) inferred from genomic analysis of the type RT specimen."; RL Mitochondrial DNA Part B Resour 0:0-0(2019). 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 (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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. 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; MK408748; QBL75584.1; -; Genomic_DNA. DR AlphaFoldDB; A0A482CGF9; -. DR UniPathway; UPA00655; UER00711. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0009536; C:plastid; 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 InterPro; IPR041010; Znf-ACC. 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 Pfam; PF17848; zf-ACC; 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}; KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP- KW Rule:MF_01395}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP- KW 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:QBL75584.1}; 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|ARBA:ARBA00022771, ECO:0000256|HAMAP- KW Rule:MF_01395}. FT DOMAIN 34..290 FT /note="CoA carboxyltransferase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50980" FT ZN_FING 38..60 FT /note="C4-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" FT BINDING 60 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01395" SQ SEQUENCE 290 AA; 32410 MW; DAB5B55D94181217 CRC64; MKSKMSLSDW LLVKRNIVAK KNIKKLNLKI PDGLWIKCDK CGLLMYHKTL KKNFKVCPQC VHHFPTSSQD RIQQILEIGS WEPLNSNLSS TDPLGFSDQK LYGKRLEDMK VKTGLNDAVQ TGLGKIGKIS IALGVMDFRF MGGSMGSVVG EKLTRLIEFA TIYKLPIVII CASGGARMQE GMLSLMQMAK VSSALQKHKK SGLLYISILT SPTTGGVTAS FAMLGDLIIA EPNALIAFAG RRVIEQTIRQ DLPNNFQTSE YLFHHGFIDL IVPRTQLKLR LMQILNFYYP //