ID   A0A1Y3W4N2_9FIRM        Unreviewed;       470 AA.
AC   A0A1Y3W4N2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Oxaloacetate decarboxylase {ECO:0000313|EMBL:OUN68186.1};
GN   ORFNames=B5G11_13920 {ECO:0000313|EMBL:OUN68186.1};
OS   Drancourtella sp. An57.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Drancourtella.
OX   NCBI_TaxID=1965647 {ECO:0000313|EMBL:OUN68186.1, ECO:0000313|Proteomes:UP000196207};
RN   [1] {ECO:0000313|Proteomes:UP000196207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An57 {ECO:0000313|Proteomes:UP000196207};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OUN68186.1}.
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DR   EMBL; NFHY01000019; OUN68186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3W4N2; -.
DR   Proteomes; UP000196207; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000196207}.
FT   DOMAIN          7..267
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   470 AA;  52949 MW;  5D134409C4F9EC1A CRC64;
     MAEKKPIKIT ETILRDAHQS LIATRMTTEQ MMPIVEKLDK VGYHSVECWG GATFDASLRF
     LKEDPWDRLR KFRDGFKNTK LQMLFRGQNI LGYRPYGDDV VEYFVQKSVA NGIDIIRIFD
     CLNDLRNLQT AVRAANKEKA HAQVALSYTI GDAYTLEYWV QKAKEIEEMG ADSICIKDMA
     GLLLPYKATE LVTALKEATN LPIQLHTHYT SGVASMTYLK AVEAGVDVID TAMSPFALGT
     SQPATEVMVE TFKGTPYDTG FDQQLLSEIA DYFRPIRDEA LESGLLNPKN LGVNIKTLLY
     QVPGGMLSNL TSQLKEQGAE DKYYEVLEEV PRVRKDLGEP PLVTPSSQIV GTQAVFNVLM
     GERYKMATKE TKDILKGKYG ATVCPFNEDV KKKCLGDEID DCITCRPADL IPDELETLEN
     EMKQWKQQDE DVLTYALFPQ VAIDFFKYRQ AQQTKVDETI ADTKNGSYPV
//