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Database: UniProt
Entry: A0A1F3E5Q3_9BACT
LinkDB: A0A1F3E5Q3_9BACT
Original site: A0A1F3E5Q3_9BACT 
ID   A0A1F3E5Q3_9BACT        Unreviewed;       580 AA.
AC   A0A1F3E5Q3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Oxaloacetate decarboxylase {ECO:0000313|EMBL:OFX50348.1};
GN   ORFNames=A2X13_13400 {ECO:0000313|EMBL:OFX50348.1};
OS   Bacteroidetes bacterium GWC2_33_15.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797324 {ECO:0000313|EMBL:OFX50348.1, ECO:0000313|Proteomes:UP000177978};
RN   [1] {ECO:0000313|EMBL:OFX50348.1, ECO:0000313|Proteomes:UP000177978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OFX50348.1}.
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DR   EMBL; MENN01000018; OFX50348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3E5Q3; -.
DR   Proteomes; UP000177978; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 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; PS50991; PYR_CT; 1.
PE   4: Predicted;
FT   DOMAIN          4..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   580 AA;  65538 MW;  A4C32F86E15CF0E0 CRC64;
     MAKEIKFSLV YRDMWQSSGK YVPRVDQLKE IAPVIIDMGC FSRIETNGGA FEQVNLLYGE
     NPNTAVREWT KPFNDAGIQT HMLERALNGI RMYPVPADVR RLMYKVKKAQ GVDIARSFCG
     LNDHRNLELS IKYAKEAGMI SQATLSITHS AIHTVEYYMG VVDKAVEYGT DEICLKDMAG
     VGRPATLGRL VTEIKKKYPH LIVQYHGHSG PGFSVASTLE CARAGADYID VAMEPLSWGM
     VHPDVITIQE MLKDAGFKVP EINMKAYMKA RALTQDFMDD FLGYFIDPKN RYTSSLLVQS
     GLPGGMMGSM MADLKGVHRG VNQMIESQGK KALTEDDLLV KLFDEVIDIW PRLGNPPLVT
     PFSQYVKNIA LINVMQEIQG KGKFEMIDNN SWDMILGKAG KLPGTLDPEI VKLAEKLGKE
     FYTGVPQDAY PDELDKFRKE MIENGWDPGQ DDEELFEFAM HDRQYRDYKS GLAKKRFQEE
     LQKVKGDSKT TPGKPAKKVE AGKKDIVAPY MGKIFYNLNY FIEEKAIELG NMVKKGERIC
     YIESNYTYDE IISEFDGEVD EIFFNHGDNV SKGDIIVRLK
//
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