ID   C4LLS4_CORK4            Unreviewed;       527 AA.
AC   C4LLS4;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   10-JUN-2026, entry version 64.
DE   SubName: Full=Putative acyl-CoA carboxylase, beta chain {ECO:0000313|EMBL:ACR16842.1};
GN   OrderedLocusNames=ckrop_0043 {ECO:0000313|EMBL:ACR16842.1};
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR16842.1, ECO:0000313|Proteomes:UP000001473};
RN   [1] {ECO:0000313|EMBL:ACR16842.1, ECO:0000313|Proteomes:UP000001473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC   {ECO:0000313|Proteomes:UP000001473};
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00006102}.
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DR   EMBL; CP001620; ACR16842.1; -; Genomic_DNA.
DR   RefSeq; WP_012730730.1; NC_012704.1.
DR   AlphaFoldDB; C4LLS4; -.
DR   STRING; 645127.ckrop_0043; -.
DR   GeneID; 78090417; -.
DR   KEGG; ckp:ckrop_0043; -.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_018822_6_2_11; -.
DR   OrthoDB; 4434131at2; -.
DR   Proteomes; UP000001473; 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:0004658; F:propionyl-CoA carboxylase activity; IEA:TreeGrafter.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 2.
DR   InterPro; IPR051047; AccD/PCCB.
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; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR   PANTHER; PTHR43842:SF2; PROPIONYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001473}.
FT   DOMAIN          10..265
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          271..511
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   527 AA;  56692 MW;  C63C7C09EB5CB2F7 CRC64;
     MSEQPHDPSM PERLGQLEEE RNRIRLGGGQ ARLDKQHDRG KMTARERITK LVDEDTFQET
     GMFAKHRTTH FGMDKADAPA DGVVTGSGAV YGRPVHIASQ DFSVMGGSAG EMQSNKVVAM
     MKASATTGTP FVFINDSGGA RVQEGIDSLS GYGRVFYNNV LLSGLVPQVS IIAGPCAGGA
     AYSPALTDFI IQTRKANMFI TGPKVIESVT GEKVTADELG GADAHMSTAG NIHFVADDDE
     QAILIAQKLL SFLPQNNTEE PPIVDPDEVV EPDDSLRDIV PVDGRKGYDV RDIIRKIVDY
     GDFLEVQAGY AQNLVVGFAR VVGRTVGIVA NQSQVMSGVL DINSSDKGAS FVRFCDSFNI
     PLLTLVDVPG FMPGVAQEHG GIIRHGAKML FAYSAATVPK LTVVLRKSYG GSYLAMCSKD
     LGADRVWAWP TAEIAVMGAD GAVNVVFRKE IKKAQEEGGD EAAAAKKSEL VQLYKDTFST
     PYMAASRGLV DDIIDPADTR REIALALELL TNKRENRPSK KHGLAPN
//