ID   ACCD_LIBAP              Reviewed;         284 AA.
AC   C6XFZ0;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-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};
GN   OrderedLocusNames=CLIBASIA_03555;
OS   Liberibacter asiaticus (strain psy62).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=537021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62;
RX   PubMed=19589076; DOI=10.1094/mpmi-22-8-1011;
RA   Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L.,
RA   Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y.,
RA   Gottwald T.;
RT   "Complete genome sequence of citrus huanglongbing bacterium, 'Candidatus
RT   Liberibacter asiaticus' obtained through metagenomics.";
RL   Mol. Plant Microbe Interact. 22:1011-1020(2009).
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; CP001677; ACT57293.1; -; Genomic_DNA.
DR   RefSeq; WP_012778722.1; NC_012985.3.
DR   AlphaFoldDB; C6XFZ0; -.
DR   SMR; C6XFZ0; -.
DR   STRING; 537021.CLIBASIA_03555; -.
DR   EnsemblBacteria; ACT57293; ACT57293; CLIBASIA_03555.
DR   GeneID; 66285979; -.
DR   KEGG; las:CLIBASIA_03555; -.
DR   eggNOG; COG0777; Bacteria.
DR   HOGENOM; CLU_015486_1_0_5; -.
DR   OMA; PEGLWIK; -.
DR   OrthoDB; 504557at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000002744; 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..284
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta"
FT                   /id="PRO_0000389780"
FT   DOMAIN          25..284
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
SQ   SEQUENCE   284 AA;  31759 MW;  6C3445319073C1D1 CRC64;
     MNWITNFVRP RINSVFGRRA IPENLWVKCP ETGAMVYHKD LKENQWVISS SDFHMKIPAK
     ERLKFLFDNA KYCLLDQPQV CQDPLKFRDN KKYIDRLKEN RSKTGLIDSI VSAVGNVRDF
     KLVAVVHEFS FIGGSIGIAA GEAIVKSCER AIAEKCPLVM FTASGGARMQ EGILSLMQLP
     RTTIAINMLK DAGLPYIVVL TNPTTGGVTA SYAMLGDIHL AEPGAEIGFA GRRVIEQTVR
     EKLPDGFQRS EYLVEHGMID RIVHRHDIPE VVSSLCKILT KSVQ