ID   A0A0D3EU77_9ORYZ        Unreviewed;       966 AA.
AC   A0A0D3EU77;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
OS   Oryza barthii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART01G31510.2};
RN   [1] {ECO:0000313|EnsemblPlants:OBART01G31510.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART01G31510.2};
RX   DOI=10.1007/s12284-009-9025-z;
RA   Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA   Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA   Knight J., Niazi F., Egholm M., Wing R.A.;
RT   "De novo next generation sequencing of plant genomes.";
RL   Rice 2:35-43(2009).
RN   [2] {ECO:0000313|EnsemblPlants:OBART01G31510.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC       forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC       tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003774}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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   AlphaFoldDB; A0A0D3EU77; -.
DR   STRING; 65489.A0A0D3EU77; -.
DR   PaxDb; 65489-OBART01G31510-2; -.
DR   EnsemblPlants; OBART01G31510.2; OBART01G31510.2; OBART01G31510.
DR   Gramene; OBART01G31510.2; OBART01G31510.2; OBART01G31510.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   Proteomes; UP000026960; Chromosome 1.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF47; PHOSPHOENOLPYRUVATE CARBOXYLASE 2; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960}.
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   966 AA;  109905 MW;  C4392ACC682D9FDA CRC64;
     MARNAADKGT SIDAQLRILA PKKLSEDDKL VEYDALLLDR FLDILQDLHG EDIRETVQEC
     YELAAEYESK VDPKQLDAIG NVLTRLDPGD SIVMTKSFSH MLILANLAEE VQIAYRRRIK
     LKKGDFADEN SATTESNFEE TLKRLVGELK KSPHEVFDAL KNQTIDLVLT AHPTQSVRRS
     LLQKHGRIRS CLTKLYAKDI TPDEKQELDE ALQREIQAAF RTDEIRRAPP TPQDEMRAGM
     SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
     DVCLLARMMA ANLYYAQIED LMFELSMWRC SDELRVKADQ LHRCAKKNTT KHYIEFWKQV
     PPSEPYRVIL SNVRDKLYNT RERARHLLAS GFSEIPDEAT FTDVEQFLEP LELCYRSLCA
     CGDNSIADGS LLDFLRQVST FGLSLVRLDI RQESDRHTDV MDAITQYLGI GSYREWSEEK
     RQEWLLSELN GKRPLFGPDL PQTDEIADVL DTFHVIAELP YDSFGAYVIS MATAPSDVLA
     VELLQRECHV KKPLRVVPLF EKLADLEAAP AALARLFSVD WYRNRIDGKQ EVMIGYSDSG
     KDAGRFSAAW ELYKAQEELI KVAKQFGVKL TMFHGRGGTV GRGGGPTHLA ILSQPPDTIH
     GSLRVTVQGE VIEQSFGEEH LCFRTLQRFT SATLEHGMHP PISPKPEWRA LMDEMAAVAT
     KEYRSIVFQE ARFVEYFRLA TPELEYGRMN IGSRPSKRKP SGGIESLRAI PWIFAWTQTR
     FHLPVWLGFG AAFKHVLQKD IRNLQILQEM YNEWPFFRVT IDLVEMVFAK GDPGIAALYD
     KLLVSEDLWP FGARLRANYE ETKQLLLQVA GHKDLLEGDP YLRQRLRIRD SYITALNVCQ
     ACTLKRIRDP GFHVSPRAHL SKDIMDSGKP AAELVKLNTT SEYGPGLEDT LILTMKGIAA
     GMQNTG
//