ID A0A482CGF9_9FLOR Unreviewed; 290 AA. AC A0A482CGF9; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 18-SEP-2019, entry version 4. 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; OC Corallinales; 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) 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: CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = CC malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]; CC Xref=Rhea:RHEA:54728, Rhea:RHEA-COMP:10505, Rhea:RHEA- CC COMP:10506, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, CC 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; 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 -!- 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 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. 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 Pfam; PF01039; Carboxyl_trans; 1. DR Pfam; PF17848; zf-ACC; 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:QBL75584.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01395, KW ECO:0000313|EMBL:QBL75584.1}; Zinc {ECO:0000256|HAMAP-Rule:MF_01395}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01395}. FT DOMAIN 34 290 CoA carboxyltransferase N-terminal. FT {ECO:0000259|PROSITE:PS50980}. FT ZN_FING 38 60 C4-type. {ECO:0000256|HAMAP-Rule: FT MF_01395}. FT METAL 38 38 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 41 41 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 57 57 Zinc. {ECO:0000256|HAMAP-Rule:MF_01395}. FT METAL 60 60 Zinc. {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 //