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}.
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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
//