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
//