ID   Q9SAZ6_MAIZE            Unreviewed;       960 AA.
AC   Q9SAZ6; A0A3L6ELM6;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   Name=Ppc1C {ECO:0000313|EMBL:BAA28170.1};
GN   Synonyms=542479 {ECO:0000313|EnsemblPlants:Zm00001eb238670_P001};
GN   ORFNames=ZEAMMB73_Zm00001d016166 {ECO:0000313|EMBL:AQK70234.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:BAA28170.1};
RN   [1] {ECO:0000313|EMBL:BAA28170.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H84 {ECO:0000313|EMBL:BAA28170.1};
RC   TISSUE=Root {ECO:0000313|EMBL:BAA28170.1};
RA   Dong L., Masuda T., Kawamura T., Hata S., Izui K.;
RT   "Cloning, expression and characterization of a root-form
RT   phosphoenolpyruvate carboxylase from Zea mays: Comparison with the C4-form
RT   enzyme.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:Zm00001eb238670_P001, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb238670_P001,
RC   ECO:0000313|Proteomes:UP000007305};
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA   Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA   Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA   Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA   Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA   Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA   Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA   Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA   Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA   Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA   Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA   Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA   SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA   Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA   Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA   Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA   Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA   Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
RN   [3] {ECO:0000313|EMBL:AQK70234.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK70234.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblPlants:Zm00001eb238670_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb238670_P001};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) 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}.
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DR   EMBL; CM000781; AQK70234.1; -; Genomic_DNA.
DR   EMBL; AB012228; BAA28170.1; -; mRNA.
DR   RefSeq; NP_001105503.1; NM_001112033.1.
DR   AlphaFoldDB; Q9SAZ6; -.
DR   SMR; Q9SAZ6; -.
DR   IntAct; Q9SAZ6; 3.
DR   STRING; 4577.Q9SAZ6; -.
DR   PaxDb; 4577-GRMZM2G069542_P01; -.
DR   EnsemblPlants; Zm00001eb238670_T001; Zm00001eb238670_P001; Zm00001eb238670.
DR   GeneID; 542479; -.
DR   Gramene; Zm00001eb238670_T001; Zm00001eb238670_P001; Zm00001eb238670.
DR   KEGG; zma:542479; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_1_0_1; -.
DR   InParanoid; Q9SAZ6; -.
DR   OMA; PSFEVMP; -.
DR   OrthoDB; 355614at2759; -.
DR   SABIO-RK; Q9SAZ6; -.
DR   Proteomes; UP000007305; Chromosome 5.
DR   ExpressionAtlas; Q9SAZ6; baseline and differential.
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:0015979; P:photosynthesis; 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:SF48; PHOSPHOENOLPYRUVATE CARBOXYLASE; 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   1: Evidence at protein level;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:BAA28170.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9SAZ6};
KW   Pyruvate {ECO:0000313|EMBL:BAA28170.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        596
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   960 AA;  109429 MW;  7B7F156A506F7C2D CRC64;
     MPERHQSIDA QLRLLAPGKV SEDDKLVEYD ALLVDRFLDI LQDLHGPHLR EFVQECYELS
     AEYENDRDEA RLGELGSKLT SLPPGDSIVV ASSFSHMLNL ANLAEEVQIA HRRRIKLKRG
     DFADEASAPT ESDIEETLKR LVSQLGKSRE EVFDALKNQT VDLVFTAHPT QSVRRSLLQK
     HGRIRNCLRQ LYAKDITADD KQELDEALQR EIQAAFRTDE IRRTPPTPQD EMRAGMSYFH
     ETIWKGVPKF LRRIDTALKN IGINERLPYN APLIQFSSWM GGDRDGNPRV TPEVTRDVCL
     LARMMAANLY FSQIEDLMFE LSMWRCSDEL RIRADELHRS SRKAAKHYIE FWKQVPPNEP
     YRVILGDVRD KLYYTRERSR HLLTSGISEI LEEATFTNVE QFLEPLELCY RSLCACGDKP
     IADGSLLDFL RQVSTFGLAL VKLDIRQESD RHTDVLDSIT THLGIGSYAE WSEEKRQDWL
     LSELRGKRPL FGSDLPQTEE TADVLGTFHV LAELPADCFG AYIISMATAP SDVLAVELLQ
     RECHVKHPLR VVPLFEKLAD LEAAPAAVAR LFSIDWYMDR INGKQEVMIG YSDSGKDAGR
     LSAAWQMYKA QEELIKVAKH YGVKLTMFHG RGGTVGRGGG PTHLAILSQP PDTIHGSLRV
     TVQGEVIEHS FGEELLCFRT LQRYTAATLE HGMHPPISPK PEWRALMDEM AVVATKEYRS
     IVFQEPRFVE YFRSATPETE YGRMNIGSRP SKRKPSGGIE SLRAIPWIFA WTQTRFHLPV
     WLGFGAAIKH IMQKDIRNIH ILREMYNEWP FFRVTLDLLE MVFAKGDPGI AAVYDKLLVA
     DDLQSFGEQL RKNYEETKEL LLQVAGHKDV LEGDPYLKQR LRLRESYITT LNVCQAYTLK
     RIRDPSFQVS PQPPLSKEFT DESQPAELVQ LNQQSEYAPG LEDTLILTMK GIAAGMQNTG
//