ID   ACCD_FLAB3              Reviewed;         282 AA.
AC   C6X3B5;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000255|HAMAP-Rule:MF_01395}; OrderedLocusNames=FIC_02495;
OS   Flavobacteriaceae bacterium (strain 3519-10).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=531844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3519-10;
RX   PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA   Raymond J.A., Christner B.C., Schuster S.C.;
RT   "A bacterial ice-binding protein from the Vostok ice core.";
RL   Extremophiles 12:713-717(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_01395};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01395}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
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DR   EMBL; CP001673; ACU08928.1; -; Genomic_DNA.
DR   RefSeq; WP_015807212.1; NC_013062.1.
DR   AlphaFoldDB; C6X3B5; -.
DR   SMR; C6X3B5; -.
DR   STRING; 531844.FIC_02495; -.
DR   EnsemblBacteria; ACU08928; ACU08928; FIC_02495.
DR   KEGG; fba:FIC_02495; -.
DR   eggNOG; COG0777; Bacteria.
DR   HOGENOM; CLU_015486_1_1_10; -.
DR   OMA; PEGLWIK; -.
DR   OrthoDB; 504557at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001512; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
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: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   Pfam; PF01039; Carboxyl_trans; 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; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..282
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta"
FT                   /id="PRO_0000389742"
FT   DOMAIN          26..282
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
SQ   SEQUENCE   282 AA;  31563 MW;  E905D94090E07CE7 CRC64;
     MAFDWFKRKT KNITTSTEDK KDVPKGLWHQ TPTGKIIEHE ELKANNYVSP EDGFHVRIGS
     REFFSILFDD NKFTELDANV ESVDMLGFKD TKAYVDRLKE VKAKTKLTDS IRNAVGRVNG
     EQMVISCMDF AFIGGSLGSV MGEKIRRAVD YCIANRLPYM IICQSGGARM QEATYSLMQL
     AKVQAKLAQL SEEGLLYIAY LCDPTFGGIT ASFAMTADII MAEPGALIGF AGPRVIRETI
     GKDLPEGFQT SEFLQEKGFV DFIVKRTEIK EKVSKTVKLL VH