ID   G7IH71_MEDTR            Unreviewed;       966 AA.
AC   G7IH71;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   Name=11407264 {ECO:0000313|EnsemblPlants:AES66636};
GN   OrderedLocusNames=MTR_2g076670 {ECO:0000313|EMBL:AES66636.1};
GN   ORFNames=MtrunA17_Chr2g0315891 {ECO:0000313|EMBL:RHN74952.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES66636.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES66636.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES66636.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES66636,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES66636.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:AES66636.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES66636,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES66636}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES66636};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:RHN74952.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN74952.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(2018).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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DR   EMBL; CM001218; AES66636.1; -; Genomic_DNA.
DR   EMBL; PSQE01000002; RHN74952.1; -; Genomic_DNA.
DR   RefSeq; XP_003596385.1; XM_003596337.2.
DR   AlphaFoldDB; G7IH71; -.
DR   STRING; 3880.G7IH71; -.
DR   PaxDb; 3880-AES66636; -.
DR   ProMEX; G7IH71; -.
DR   EnsemblPlants; AES66636; AES66636; MTR_2g076670.
DR   GeneID; 11407264; -.
DR   Gramene; AES66636; AES66636; MTR_2g076670.
DR   KEGG; mtr:11407264; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_2_0_1; -.
DR   OMA; KDLWPFG; -.
DR   OrthoDB; 355614at2759; -.
DR   Proteomes; UP000002051; Chromosome 2.
DR   Proteomes; UP000265566; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0048366; P:leaf development; IBA:GO_Central.
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:SF33; PHOSPHOENOLPYRUVATE CARBOXYLASE 3; 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   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RHN74952.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyruvate {ECO:0000313|EMBL:RHN74952.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   966 AA;  110874 MW;  47CCB1ABC2C3AC71 CRC64;
     MANKMEKMAS IDAQLRQLVP AKVSEDDKLI EYDALLLDRF LDILQDLHGE DLKDSVQEVY
     ELSAEYERKH DPKKLEELGN LITSFDAGDS IVVAKSFSHM LNLANLAEEV QIAHRRRNKL
     KKGDFRDESN ATTESDIEET LKKLVFDMKK SPQEVFDALK NQTVDLVLTA HPTQSVRRSL
     LQKHGRVRNC LSQLYAKDIT PDDKQELDEA LQREIQAAFR TDEIKRTPPT PQDEMRAGMS
     YFHETIWKGV PKFLRRVDTA LKNIGINERV PYNAPLIQFS SWMGGDRDGN PRVTPEVTRD
     VCLLARMMAA NLYYSQIEDL MFELSMWRCN DELRVRAEEL HRNSKKDEVA KHYIEFWKKI
     PLNEPYRVVL GEVRDKLYRT RERSRYLLAH GYSEIPEEAT FTNVDEFLEP LELCYRSLCA
     CGDRAIADGS LLDFLRQVST FGLSLVRLDI RQESDRHTDV MDAITKHLEI GSYQEWSEEK
     RQEWLLSELI GKRPLFGPDL PQTDEIRDVL DTFRVIAELP SDNFGAYIIS MATAPSDVLA
     VELLQRECKV RNPLRVVPLF EKLDDLESAP AALARLFSID WYINRIDGKQ EVMIGYSDSG
     KDAGRFSAAW QLYKAQEDLI KVAQKFGVKL TMFHGRGGTV GRGGGPTHLA ILSQPPETIH
     GSLRVTVQGE VIEQSFGEEH LCFRTLQRFT AATLEHGMRP PSSPKPEWRA LMDQMAVIAT
     EEYRSIVFKE PRFVEYFRLA TPEMEYGRMN IGSRPAKRRP SGGIETLRAI PWIFAWTQTR
     FHLPVWLGFG AAFRQVVQKD VKNLHMLQEM YNQWPFFRVT IDLVEMVFAK GDPGIAALND
     RLLVSKDLWP FGEQLRSKYE ETKKLLLQVA AHKEVLEGDP YLKQRLRLRD SYITTLNVFQ
     AYTLKRIRDP NYKVEVRPPI SKESAETSKP ADELVTLNPT SEYAPGLEDT LILTMKGIAA
     GMQNTG
//