ID   ACCD_METS4              Reviewed;         303 AA.
AC   B0UKV1;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=M446_0476;
OS   Methylobacterium sp. (strain 4-46).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4-46;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL   Submitted (FEB-2008) 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: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; CP000943; ACA15040.1; -; Genomic_DNA.
DR   RefSeq; WP_012330457.1; NC_010511.1.
DR   AlphaFoldDB; B0UKV1; -.
DR   SMR; B0UKV1; -.
DR   STRING; 426117.M446_0476; -.
DR   EnsemblBacteria; ACA15040; ACA15040; M446_0476.
DR   KEGG; met:M446_0476; -.
DR   eggNOG; COG0777; Bacteria.
DR   HOGENOM; CLU_015486_1_0_5; -.
DR   OMA; PEGLWIK; -.
DR   OrthoDB; 504557at2; -.
DR   UniPathway; UPA00655; UER00711.
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; Transferase.
FT   CHAIN           1..303
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta"
FT                   /id="PRO_0000389800"
FT   DOMAIN          29..298
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
SQ   SEQUENCE   303 AA;  33392 MW;  6D25E90999AE4C82 CRC64;
     MKVETMNWIT EVVRPRIKTL FKRETPENLW VKCPETGQMV FHKEVEAHDF VIPGSEHHLR
     MSAQQRLKMM FDQGTWLDVP LPEAPVDPLK FRDEKRYVDR LKDARAKTGM ADAFKVGFGR
     VGGLPMTLAV QDFGFMGGSL GMAAGEAFVR GAETALDKRT PYVLFAASGG ARMQEGILSL
     MQMPRTTVAV RRLNRARLPY IVVLTNPTTG GVTASYAMLG DVHLAEPGAL IGFAGPRVIE
     QTIREKLPDG FQRAEYLREH GMIDQVVHRR DLKATVARLC GLLMQAPAAT PAPASAAAQP
     VPA