ID   D1PM75_9FIRM            Unreviewed;       469 AA.
AC   D1PM75;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Conserved carboxylase domain protein {ECO:0000313|EMBL:EFB75660.1};
GN   ORFNames=SUBVAR_05434 {ECO:0000313|EMBL:EFB75660.1};
OS   Subdoligranulum variabile DSM 15176.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75660.1, ECO:0000313|Proteomes:UP000003438};
RN   [1] {ECO:0000313|EMBL:EFB75660.1, ECO:0000313|Proteomes:UP000003438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75660.1,
RC   ECO:0000313|Proteomes:UP000003438};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2009) 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:EFB75660.1}.
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DR   EMBL; ACBY02000023; EFB75660.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1PM75; -.
DR   STRING; 411471.SUBVAR_05434; -.
DR   eggNOG; COG5016; Bacteria.
DR   HOGENOM; CLU_000395_4_2_9; -.
DR   Proteomes; UP000003438; 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:UP000003438}.
FT   DOMAIN          8..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   469 AA;  52445 MW;  9C6C6C0ACAF0AF39 CRC64;
     MTLAKKPIKI TEVVLRDAHQ SLLATRMTMD EMRPILPEMD KIPYFSVECW GGATFDSCIR
     FLDEDPWERL RILRKELPHQ KLQMLFRGQN MLGYRPYADD AVEYFVQKSV ANGIDVIRIF
     DALNDPRNLQ TAIEAANKEG AHVQACISYT LSPVHNNEYF AKYAKTLEEM GANSICIKDM
     AGLLKPYTCY DLVKELKSTV SIPVDIHSHY TAGLASMSIL KGIEAGADIV DTAMSPLALG
     TSHMPTESLV AALQGTDYDT GLDLNQLNVV RAYFAKLREK YIANGQISPK SLGVDANTLL
     YQVPGGMFSN MLKQLKDAGK EDKLDEVLAE IPRVREDAGY PPLVTPTSQI VGTQAVFNVI
     LGERYKMVTK EFKGLVHGDY GKTPAPIKKE FSDFILKGEK PITCRFADTL EPEMDKLKAE
     AAKYAIQEED VLTYAMFPQV APKFFEKRNA RLQGVDALHA DYENKSHPV
//