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Database: UniProt
Entry: C3G3A9_BACTU
LinkDB: C3G3A9_BACTU
Original site: C3G3A9_BACTU 
ID   C3G3A9_BACTU            Unreviewed;       513 AA.
AC   C3G3A9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Propionyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=bthur0009_23010 {ECO:0000313|EMBL:EEM71698.1};
OS   Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM71698.1};
RN   [1] {ECO:0000313|EMBL:EEM71698.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM71698.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEM71698.1}.
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DR   EMBL; ACNG01000065; EEM71698.1; -; Genomic_DNA.
DR   RefSeq; WP_000566963.1; NZ_CM000754.1.
DR   AlphaFoldDB; C3G3A9; -.
DR   HOGENOM; CLU_018822_6_1_9; -.
DR   Proteomes; UP000001380; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
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   4: Predicted;
FT   DOMAIN          1..256
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          262..499
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   513 AA;  56634 MW;  5103B50E977513B0 CRC64;
     MIDQKQQSNT FEERVETIKQ GGAPKYHEQN KAKGKLFVRD RLALLFDNGE YVEDALFANC
     EETGLPADGV ITATGKIHGR TACVMANDST VKAGSWGART VEKILRIQET AEKLRVPLFY
     LVDSAGARIT DQVEMFPGRR GAGRIFYNQV KLSGKVPQVC LLFGPSAAGG AYIPAFCDVV
     MMVEGNASMY LGSPRMAEMV IGEKVTLEEM GGARMHCSIS GCGDVLCKTE EDAITQARQY
     ISYFPNNYLE KTPLVTPQEP KQFDKTLEQI IPENQNAPFN MKDLINRVID EGSFYEVKKL
     FAQELITGLA RIDGKPVGII ANQPRMKGGV LFHDSADKAA KFINLCDAYH IPLLFLADVP
     GFMIGTKVER AGIIRHGAKM ISAMSEATVP KISIVVRKAY GAGLYAMAGP AFEPDCCLAL
     PTASIAVMGP EAAVNAVYAN KIAALPEEER DSFIAEKREE YKKDIDIYHL ASEMVIDGIV
     HPNNLREELK GRFEMYMSKY QVFTDRKHPV YPV
//
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