ID C6ZTA6_LISMN Unreviewed; 223 AA.
AC C6ZTA6;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Acetyl-CoA carboxylase subunit beta {ECO:0000313|EMBL:ACN24728.1};
DE Flags: Fragment;
GN Name=accD {ECO:0000313|EMBL:ACN24728.1};
GN ORFNames=lmo1573 {ECO:0000313|EMBL:ACN24728.1};
OS Listeria monocytogenes.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639 {ECO:0000313|EMBL:ACN24728.1};
RN [1] {ECO:0000313|EMBL:ACN24728.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL_B-33100 {ECO:0000313|EMBL:ACN24728.1}, and NRRL_B-33189
RC {ECO:0000313|EMBL:ACN24746.1};
RA Ward T.J., Ducey T.F., Usgaard T.R., Dunn K.A., Bielawski J.P.;
RT "Multilocus Genotyping Assays for SNP-Based Subtyping of Listeria
RT monocytogenes.";
RL Submitted (AUG-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.
CC {ECO:0000256|ARBA:ARBA00025280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; FJ029253; ACN24728.1; -; Genomic_DNA.
DR EMBL; FJ029262; ACN24746.1; -; Genomic_DNA.
DR AlphaFoldDB; C6ZTA6; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
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 PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF17848; zf-ACC; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 30..223
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT NON_TER 223
FT /evidence="ECO:0000313|EMBL:ACN24728.1"
SQ SEQUENCE 223 AA; 24266 MW; D15E07AD970EAD45 CRC64;
MLGDLFTKPK KRKYATIPSD GTKADVPEGI MTKCPECKKI MYTKELQKNL MVCNYCGFHH
PIGAKARIDM LVDEGSFEEI DASLTTANPL GFEDYMDRIE KDKQKSGLNE AIVTGHATIG
GNPLVIAVMD SRFRMASMGS VVGEKIFRAV EDADKTNKPF VIFTASGGAR MQEGMLSLMQ
MAKTSAAFKR FSNHGGLIIT VMTHPTTGGV SASFASLGDY NFA
//
