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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//