ID   A0A0K2GYE5_9CORY        Unreviewed;       545 AA.
AC   A0A0K2GYE5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acetyl-CoA carboxylase subunit beta {ECO:0000313|EMBL:ALA66804.1};
GN   ORFNames=CLAC_02620 {ECO:0000313|EMBL:ALA66804.1};
OS   Corynebacterium lactis RW2-5.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1408189 {ECO:0000313|EMBL:ALA66804.1, ECO:0000313|Proteomes:UP000058446};
RN   [1] {ECO:0000313|EMBL:ALA66804.1, ECO:0000313|Proteomes:UP000058446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW2-5 {ECO:0000313|EMBL:ALA66804.1,
RC   ECO:0000313|Proteomes:UP000058446};
RA   Ruckert C., Albersmeier A., Lipski A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium lactis DSM 45799(T), isolated
RT   from raw cow milk.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00006102}.
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DR   EMBL; CP006841; ALA66804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K2GYE5; -.
DR   STRING; 1408189.CLAC_02620; -.
DR   KEGG; clw:CLAC_02620; -.
DR   PATRIC; fig|1408189.4.peg.521; -.
DR   Proteomes; UP000058446; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR045190; MCCB/AccD1-like.
DR   PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR22855:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
FT   DOMAIN          32..288
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          291..537
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  58707 MW;  C9DC2BBD38B2AD48 CRC64;
     MTLATETAQQ NAAQQKTAQQ NSAAPTTNRG KHEQLVSNLK GLLEQAAKGG SDKARARHIS
     RGKLLPRQRI NQLLDPGSPF LEVAPLAAHE MYGGKVPAAG VIAGIGLIHG RRCLVVANDA
     TVSGGTYYPM TVKKHLRAQE IAGQNRLPCI YLVDSGGAML LNQDEVFPDR DHFGRIFYNQ
     ANLSARGIPQ IASVMGSCTA GGAYVPAMSD EAVIVKNQGT IFLAGPPLVK AATGEDVTPE
     DLGGGELHSK TSGVTDHLAV NDADALRRVR DIVATLPKDP EAPWDIAPSI APKRSQTDLY
     DVVPTDSKTP YDVHEVIEII ADGGQYKEFK AEFGKTLVTA FARIHGHPVG IVANNGILFA
     ESAQKGAHFI ELCDQRKIPL VFLQNTTGFM VGREYEAGGI AKHGAKMVNA VATTRVPKFT
     VVIGGAFGAG NYSMCGRAYS PRFLWMWPNA RIAVMGGPQA AMTLSTVRRN QIERSGESWS
     AEEQEQFEAP IREQFERQSD CYYSSARLWD DGVIDPADTR RILGMALDVA SAAPLDDPGF
     GVFRM
//