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 26-NOV-2014, entry version 122. 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; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogoneae; 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 RT 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., RA Shigesada K., Sugiyama T., Katsuki H.; RT "Cloning and sequence analysis of cDNA encoding active RT phosphoenolpyruvate 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 RT from 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; 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 RT carboxylase involved in C4 photosynthesis. Nucleotide sequence of RT entire open reading frame and evidence for polyadenylation of mRNA at RT 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'- RT 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 RT phosphoenolpyruvate 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) CC it forms oxaloacetate, a four-carbon dicarboxylic acid source for CC the tricarboxylic acid cycle. CC -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O + CC phosphoenolpyruvate + HCO(3)(-). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ENZYME 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 RefSeq; NP_001105418.1; NM_001111948.1. DR UniGene; Zm.2433; -. DR PDB; 1JQO; X-ray; 3.00 A; A/B=1-970. DR PDBsum; 1JQO; -. DR ProteinModelPortal; P04711; -. DR SMR; P04711; 35-970. DR PRIDE; P04711; -. DR GeneID; 542372; -. DR KEGG; zma:542372; -. DR Gramene; P04711; -. DR MaizeGDB; 30066; -. DR HOGENOM; HOG000238648; -. DR KO; K01595; -. DR SABIO-RK; P04711; -. DR UniPathway; UPA00322; -. DR EvolutionaryTrace; P04711; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR HAMAP; MF_00595; PEPcase_type1; 1. DR InterPro; IPR021135; PEP_COase. DR InterPro; IPR018129; PEP_COase_AS. DR InterPro; IPR022805; PEP_COase_bac/pln-type. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. 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. FT CHAIN 1 970 Phosphoenolpyruvate carboxylase 1. FT /FTId=PRO_0000166667. FT ACT_SITE 177 177 {ECO:0000269|PubMed:2268676}. FT ACT_SITE 606 606 {ECO:0000269|PubMed:2268676}. FT ACT_SITE 647 647 {ECO:0000269|PubMed:2268676}. FT MOD_RES 15 15 Phosphoserine. FT {ECO:0000269|PubMed:16668168}. FT CONFLICT 239 239 A -> D (in Ref. 2 and 3). {ECO:0000305}. FT CONFLICT 338 339 EL -> DV (in Ref. 2; CAA27270). FT {ECO:0000305}. FT CONFLICT 482 482 P -> S (in Ref. 2 and 3). {ECO:0000305}. FT CONFLICT 509 509 D -> E (in Ref. 3; CAA33663). FT {ECO:0000305}. FT CONFLICT 557 559 QPL -> PAV (in Ref. 2 and 3). FT {ECO:0000305}. FT CONFLICT 570 570 D -> S (in Ref. 2 and 3). {ECO:0000305}. FT CONFLICT 573 574 SA -> LR (in Ref. 2; CAA27270). FT {ECO:0000305}. FT CONFLICT 687 687 C -> S (in Ref. 2; CAA27270). FT {ECO:0000305}. FT CONFLICT 736 736 A -> P (in Ref. 2; CAA27270). FT {ECO:0000305}. FT CONFLICT 963 963 A -> R (in Ref. 2; CAA27270). FT {ECO:0000305}. FT HELIX 36 53 {ECO:0000244|PDB:1JQO}. FT HELIX 55 72 {ECO:0000244|PDB:1JQO}. FT HELIX 78 89 {ECO:0000244|PDB:1JQO}. FT HELIX 92 122 {ECO:0000244|PDB:1JQO}. FT HELIX 143 151 {ECO:0000244|PDB:1JQO}. FT HELIX 158 166 {ECO:0000244|PDB:1JQO}. FT STRAND 169 175 {ECO:0000244|PDB:1JQO}. FT HELIX 184 199 {ECO:0000244|PDB:1JQO}. FT HELIX 207 226 {ECO:0000244|PDB:1JQO}. FT HELIX 237 248 {ECO:0000244|PDB:1JQO}. FT TURN 249 255 {ECO:0000244|PDB:1JQO}. FT HELIX 256 268 {ECO:0000244|PDB:1JQO}. FT TURN 269 271 {ECO:0000244|PDB:1JQO}. FT STRAND 282 287 {ECO:0000244|PDB:1JQO}. FT TURN 289 291 {ECO:0000244|PDB:1JQO}. FT HELIX 301 329 {ECO:0000244|PDB:1JQO}. FT HELIX 337 350 {ECO:0000244|PDB:1JQO}. FT STRAND 359 361 {ECO:0000244|PDB:1JQO}. FT HELIX 370 394 {ECO:0000244|PDB:1JQO}. FT HELIX 409 425 {ECO:0000244|PDB:1JQO}. FT TURN 430 434 {ECO:0000244|PDB:1JQO}. FT HELIX 435 446 {ECO:0000244|PDB:1JQO}. FT STRAND 449 456 {ECO:0000244|PDB:1JQO}. FT HELIX 459 473 {ECO:0000244|PDB:1JQO}. FT HELIX 483 495 {ECO:0000244|PDB:1JQO}. FT HELIX 509 523 {ECO:0000244|PDB:1JQO}. FT STRAND 529 534 {ECO:0000244|PDB:1JQO}. FT HELIX 541 552 {ECO:0000244|PDB:1JQO}. FT STRAND 561 565 {ECO:0000244|PDB:1JQO}. FT HELIX 568 572 {ECO:0000244|PDB:1JQO}. FT HELIX 574 582 {ECO:0000244|PDB:1JQO}. FT HELIX 585 591 {ECO:0000244|PDB:1JQO}. FT STRAND 593 601 {ECO:0000244|PDB:1JQO}. FT HELIX 604 607 {ECO:0000244|PDB:1JQO}. FT HELIX 610 629 {ECO:0000244|PDB:1JQO}. FT TURN 630 632 {ECO:0000244|PDB:1JQO}. FT STRAND 634 640 {ECO:0000244|PDB:1JQO}. FT HELIX 645 647 {ECO:0000244|PDB:1JQO}. FT HELIX 652 657 {ECO:0000244|PDB:1JQO}. FT STRAND 667 673 {ECO:0000244|PDB:1JQO}. FT HELIX 674 681 {ECO:0000244|PDB:1JQO}. FT HELIX 684 703 {ECO:0000244|PDB:1JQO}. FT HELIX 711 732 {ECO:0000244|PDB:1JQO}. FT HELIX 738 745 {ECO:0000244|PDB:1JQO}. FT HELIX 749 754 {ECO:0000244|PDB:1JQO}. FT HELIX 775 783 {ECO:0000244|PDB:1JQO}. FT HELIX 788 791 {ECO:0000244|PDB:1JQO}. FT HELIX 794 804 {ECO:0000244|PDB:1JQO}. FT HELIX 808 818 {ECO:0000244|PDB:1JQO}. FT HELIX 820 833 {ECO:0000244|PDB:1JQO}. FT HELIX 838 847 {ECO:0000244|PDB:1JQO}. FT HELIX 854 875 {ECO:0000244|PDB:1JQO}. FT HELIX 885 913 {ECO:0000244|PDB:1JQO}. FT TURN 937 941 {ECO:0000244|PDB:1JQO}. FT STRAND 942 944 {ECO:0000244|PDB:1JQO}. FT HELIX 951 966 {ECO:0000244|PDB:1JQO}. 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 //