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CAPP1_MAIZE
ID   CAPP1_MAIZE             Reviewed;         970 AA.
AC   P04711;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 1;
DE            Short=PEPC 1;
DE            Short=PEPCase 1;
DE            EC=4.1.1.31;
GN   Name=PEP1; Synonyms=PPC;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. B73; TISSUE=Leaf;
RA   Hudspeth R.L., Grula J.W.;
RT   "Structure and expression of the maize gene encoding the
RT   phosphoenolpyruvate carboxylase isozyme involved in C4 photosynthesis.";
RL   Plant Mol. Biol. 12:579-589(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 39-970.
RX   PubMed=3005978; DOI=10.1093/nar/14.4.1615;
RA   Izui K., Ishijima S., Yamaguchi Y., Katagiri F., Murata T., Shigesada K.,
RA   Sugiyama T., Katsuki H.;
RT   "Cloning and sequence analysis of cDNA encoding active phosphoenolpyruvate
RT   carboxylase of the C4-pathway from maize.";
RL   Nucleic Acids Res. 14:1615-1628(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Golden cross Bantam;
RX   PubMed=2731539; DOI=10.1111/j.1432-1033.1989.tb14765.x;
RA   Matsuoka M., Minami E.;
RT   "Complete structure of the gene for phosphoenolpyruvate carboxylase from
RT   maize.";
RL   Eur. J. Biochem. 181:593-598(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
RC   STRAIN=cv. H84; TISSUE=Leaf;
RX   PubMed=2628434; DOI=10.1093/oxfordjournals.jbchem.a122986;
RA   Yanagisawa S., Izui K.;
RT   "Maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis:
RT   nucleotide sequence analysis of the 5' flanking region of the gene.";
RL   J. Biochem. 106:982-987(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-82.
RX   PubMed=2894322; DOI=10.1016/0014-5793(88)80807-x;
RA   Yanagisawa S., Izui K., Yamaguchi Y., Shigesada K., Katsuki H.;
RT   "Further analysis of cDNA clones for maize phosphoenolpyruvate carboxylase
RT   involved in C4 photosynthesis. Nucleotide sequence of entire open reading
RT   frame and evidence for polyadenylation of mRNA at multiple sites in vivo.";
RL   FEBS Lett. 229:107-110(1988).
RN   [6]
RP   ACTIVE SITE, AND PROTEIN SEQUENCE OF 599-610.
RX   PubMed=2268676; DOI=10.1016/0167-4838(90)90287-p;
RA   Jiao J.-A., Podesta F.E., Chollet R., O'Leary M.H., Andreo C.S.;
RT   "Isolation and sequence of an active-site peptide from maize leaf
RT   phosphoenolpyruvate carboxylase inactivated by pyridoxal 5'-phosphate.";
RL   Biochim. Biophys. Acta 1041:291-295(1990).
RN   [7]
RP   PHOSPHORYLATION AT SER-15.
RX   PubMed=16668168; DOI=10.1104/pp.96.1.297;
RA   Jiao J.-A., Vidal J., Echevarria C., Chollet R.;
RT   "In vivo regulatory phosphorylation site in C4-leaf phosphoenolpyruvate
RT   carboxylase from maize and sorghum.";
RL   Plant Physiol. 96:297-301(1991).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=12467579; DOI=10.1016/s0969-2126(02)00913-9;
RA   Matsumura H., Xie Y., Shirakata S., Inoue T., Yoshinaga T., Ueno Y.,
RA   Izui K., Kai Y.;
RT   "Crystal structures of C4 form maize and quaternary complex of E. coli
RT   phosphoenolpyruvate carboxylases.";
RL   Structure 10:1721-1730(2002).
CC   -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC       forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC       tricarboxylic acid cycle.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: By light-reversible phosphorylation.
CC   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA32722.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X15238; CAA33316.1; -; mRNA.
DR   EMBL; X03613; CAA27270.1; -; mRNA.
DR   EMBL; X14581; CAA32724.1; -; Genomic_DNA.
DR   EMBL; X14579; CAA32722.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X14580; CAA32723.1; -; Genomic_DNA.
DR   EMBL; X15642; CAA33663.1; -; Genomic_DNA.
DR   EMBL; X07168; CAA30158.1; -; mRNA.
DR   PDB; 1JQO; X-ray; 3.00 A; A/B=1-970.
DR   PDB; 5VYJ; X-ray; 3.30 A; A/B/C/D=1-970.
DR   PDB; 6MGI; X-ray; 2.99 A; A/B=1-970.
DR   PDB; 6U2T; X-ray; 2.80 A; A/B/C/D=1-970.
DR   PDB; 6V3O; X-ray; 2.91 A; A/B/C/D/E/F/G/H=1-970.
DR   PDBsum; 1JQO; -.
DR   PDBsum; 5VYJ; -.
DR   PDBsum; 6MGI; -.
DR   PDBsum; 6U2T; -.
DR   PDBsum; 6V3O; -.
DR   AlphaFoldDB; P04711; -.
DR   SMR; P04711; -.
DR   STRING; 4577.GRMZM2G083841_P01; -.
DR   iPTMnet; P04711; -.
DR   PaxDb; P04711; -.
DR   PRIDE; P04711; -.
DR   MaizeGDB; 30066; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   BRENDA; 4.1.1.31; 6752.
DR   SABIO-RK; P04711; -.
DR   UniPathway; UPA00322; -.
DR   EvolutionaryTrace; P04711; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P04711; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:CACAO.
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:0060359; P:response to ammonium ion; TAS:AgBase.
DR   GO; GO:0009735; P:response to cytokinin; TAS:AgBase.
DR   GO; GO:0010167; P:response to nitrate; TAS:AgBase.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Carbon dioxide fixation; Cytoplasm;
KW   Direct protein sequencing; Lyase; Magnesium; Phosphoprotein;
KW   Photosynthesis; Reference proteome.
FT   CHAIN           1..970
FT                   /note="Phosphoenolpyruvate carboxylase 1"
FT                   /id="PRO_0000166667"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000269|PubMed:2268676"
FT   ACT_SITE        606
FT                   /evidence="ECO:0000269|PubMed:2268676"
FT   ACT_SITE        647
FT                   /evidence="ECO:0000269|PubMed:2268676"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16668168"
FT   CONFLICT        239
FT                   /note="A -> D (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338..339
FT                   /note="EL -> DV (in Ref. 2; CAA27270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        482
FT                   /note="P -> S (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="D -> E (in Ref. 3; CAA33663)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        557..559
FT                   /note="QPL -> PAV (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        570
FT                   /note="D -> S (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        573..574
FT                   /note="SA -> LR (in Ref. 2; CAA27270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        687
FT                   /note="C -> S (in Ref. 2; CAA27270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        736
FT                   /note="A -> P (in Ref. 2; CAA27270)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        963
FT                   /note="A -> R (in Ref. 2; CAA27270)"
FT                   /evidence="ECO:0000305"
FT   HELIX           17..23
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           34..53
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           55..73
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           78..89
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           92..118
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           131..135
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           143..152
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           158..166
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           184..200
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           207..225
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           237..244
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           246..250
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           252..268
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            269..271
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          283..287
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            289..291
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           301..329
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           337..345
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            349..353
FT                   /evidence="ECO:0007829|PDB:5VYJ"
FT   STRAND          357..361
FT                   /evidence="ECO:0007829|PDB:6V3O"
FT   HELIX           370..394
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          402..405
FT                   /evidence="ECO:0007829|PDB:6MGI"
FT   HELIX           409..425
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           429..432
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           435..446
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            447..449
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          450..458
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           459..473
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            478..480
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           483..495
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          496..498
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           509..523
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           526..528
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          529..535
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           540..552
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          561..565
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           568..582
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           585..591
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          594..599
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           601..608
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           610..631
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          634..639
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           644..646
FT                   /evidence="ECO:0007829|PDB:6V3O"
FT   HELIX           651..657
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          667..672
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            674..676
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           677..681
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           684..703
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           711..732
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           738..745
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           748..753
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            754..757
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          761..767
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           768..770
FT                   /evidence="ECO:0007829|PDB:6V3O"
FT   HELIX           774..783
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           788..791
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           794..804
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           808..818
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           820..834
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           838..848
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           851..853
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           854..873
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            874..876
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   TURN            880..883
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           885..892
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   HELIX           895..913
FT                   /evidence="ECO:0007829|PDB:6U2T"
FT   STRAND          930..932
FT                   /evidence="ECO:0007829|PDB:6V3O"
FT   HELIX           934..937
FT                   /evidence="ECO:0007829|PDB:6V3O"
FT   TURN            938..941
FT                   /evidence="ECO:0007829|PDB:6V3O"
FT   STRAND          942..944
FT                   /evidence="ECO:0007829|PDB:1JQO"
FT   STRAND          946..948
FT                   /evidence="ECO:0007829|PDB:6V3O"
FT   HELIX           951..966
FT                   /evidence="ECO:0007829|PDB:6U2T"
SQ   SEQUENCE   970 AA;  109297 MW;  95B66F96ABCE22F4 CRC64;
     MASTKAPGPG EKHHSIDAQL RQLVPGKVSE DDKLIEYDAL LVDRFLNILQ DLHGPSLREF
     VQECYEVSAD YEGKGDTTKL GELGAKLTGL APADAILVAS SILHMLNLAN LAEEVQIAHR
     RRNSKLKKGG FADEGSATTE SDIEETLKRL VSEVGKSPEE VFEALKNQTV DLVFTAHPTQ
     SARRSLLQKN ARIRNCLTQL NAKDITDDDK QELDEALQRE IQAAFRTDEI RRAQPTPQAE
     MRYGMSYIHE TVWKGVPKFL RRVDTALKNI GINERLPYNV SLIRFSSWMG GDRDGNPRVT
     PEVTRDVCLL ARMMAANLYI DQIEELMFEL SMWRCNDELR VRAEELHSSS GSKVTKYYIE
     FWKQIPPNEP YRVILGHVRD KLYNTRERAR HLLASGVSEI SAESSFTSIE EFLEPLELCY
     KSLCDCGDKA IADGSLLDLL RQVFTFGLSL VKLDIRQESE RHTDVIDAIT THLGIGSYRE
     WPEDKRQEWL LSELRGKRPL LPPDLPQTDE IADVIGAFHV LAELPPDSFG PYIISMATAP
     SDVLAVELLQ RECGVRQPLP VVPLFERLAD LQSAPASVER LFSVDWYMDR IKGKQQVMVG
     YSDSGKDAGR LSAAWQLYRA QEEMAQVAKR YGVKLTLFHG RGGTVGRGGG PTHLAILSQP
     PDTINGSIRV TVQGEVIEFC FGEEHLCFQT LQRFTAATLE HGMHPPVSPK PEWRKLMDEM
     AVVATEEYRS VVVKEARFVE YFRSATPETE YGRMNIGSRP AKRRPGGGIT TLRAIPWIFS
     WTQTRFHLPV WLGVGAAFKF AIDKDVRNFQ VLKEMYNEWP FFRVTLDLLE MVFAKGDPGI
     AGLYDELLVA EELKPFGKQL RDKYVETQQL LLQIAGHKDI LEGDPFLKQG LVLRNPYITT
     LNVFQAYTLK RIRDPNFKVT PQPPLSKEFA DENKPAGLVK LNPASEYPPG LEDTLILTMK
     GIAAGMQNTG
 
 
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