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 24-JAN-2024, entry version 165.
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.P04711; -.
DR iPTMnet; P04711; -.
DR PaxDb; 4577-GRMZM2G083841_P01; -.
DR MaizeGDB; 30066; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR InParanoid; P04711; -.
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 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:SF5; PHOSPHOENOLPYRUVATE CARBOXYLASE 1; 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 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
//
