ID   A0A2V1IXA3_9BACT        Unreviewed;       625 AA.
AC   A0A2V1IXA3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Carboxylase {ECO:0000313|EMBL:PWB07497.1};
GN   ORFNames=C5O25_07270 {ECO:0000313|EMBL:PWB07497.1};
OS   Paramuribaculum intestinale.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC   Paramuribaculum.
OX   NCBI_TaxID=2094151 {ECO:0000313|EMBL:PWB07497.1, ECO:0000313|Proteomes:UP000244925};
RN   [1] {ECO:0000313|Proteomes:UP000244925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100764 {ECO:0000313|Proteomes:UP000244925};
RA   Clavel T., Strowig T.;
RL   Submitted (FEB-2018) 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:PWB07497.1}.
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DR   EMBL; PUBV01000012; PWB07497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1IXA3; -.
DR   Proteomes; UP000244925; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 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   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
FT   DOMAIN          6..292
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          548..624
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   625 AA;  69048 MW;  7D872676CD8E44E8 CRC64;
     MEARKLKIRD LTMRDGQQSL FATRMSQQTI DRLLPLYENA GFYIMEVWGG AVPDSVMRYL
     GESPWDRLRK ASEAMKGKSL LSALSRGRNL FGYVPYPDSV LEGFYKEAIA NGLNVMRIFD
     ALNDIDNVRE SIKMINRLGG IADGAVCYTV DPKSEPAKGG FGSRMRRLFG GQSEPEKIFT
     DEYFVEKALE MEALGAKIIT LKDMAGLVNP LRAASIISKL KSRLKVPVDF HTHCTPGYGL
     ASSVMAMIHG VDILDTNIWW FGGGSAAPAI ELIYVFAQRL GIEVEADMEA VGKIRNELLG
     ARRELAPFDL VKEFPVEFDP LNDTLPAEIS QLFDDAIAAG RAGDEEAMLE ACHAIENYFR
     FPKPNLLVKN AEVPGGMYSN MVAQLKALQS EDVLDDAMAL IPKVRRDAGL VPLVTPTSQI
     VGSQAVFLAL DRKKGNADYT NKSNQFMSLI KGEYGHTPVA VDPEFRRQIT GDAEEHPYDV
     SSYKAPENPE VAELGGMKLA QNDEEYLLLE LLPNVATTFL RNKRQAEYDA QQAAVRQAAA
     AKEAEKEEKI EPITGEVVSG PMPGTVLEVS VKPGDTVKKG QKLLVYESMK MENDVEAEHD
     ATVKRVFVKP GDRFAADAPM IEYQD
//