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}; 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 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 //