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 20-MAR-2007, entry version 70. DE Phosphoenolpyruvate carboxylase 1 (EC 4.1.1.31) (PEPCase 1) (PEPC 1). GN Name=PEP1; Synonyms=PPC; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD 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 MEDLINE=86148496; 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. RC STRAIN=cv. Golden cross Bantam; RX MEDLINE=89276342; PubMed=2731539; 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 MEDLINE=90186704; 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 MEDLINE=88152202; 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 MEDLINE=91098247; 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; 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 MEDLINE=22357225; 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 + CO(2). CC -!- ENZYME REGULATION: By light-reversible phosphorylation. CC -!- PATHWAY: Tricarboxylic acid cycle. This isozyme is involved in C4 CC photosynthesis. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the PEPCase family. 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 UniGene; Zm.2433; -. DR PDB; 1JQO; X-ray; A/B=1-970. DR Gramene; P04711; -. DR MaizeGDB; 30066; -. DR InterPro; IPR001449; PEPcase. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 1. KW 3D-structure; Allosteric enzyme; Carbon dioxide fixation; KW Direct protein sequencing; Lyase; Phosphorylation; Photosynthesis; KW Tricarboxylic acid cycle. FT CHAIN 1 970 Phosphoenolpyruvate carboxylase 1. FT /FTId=PRO_0000166667. FT ACT_SITE 177 177 FT ACT_SITE 606 606 FT ACT_SITE 647 647 FT MOD_RES 15 15 Phosphoserine. FT CONFLICT 239 239 A -> D (in Ref. 2 and 3). FT CONFLICT 338 339 EL -> DV (in Ref. 2). FT CONFLICT 482 482 P -> S (in Ref. 2 and 3). FT CONFLICT 509 509 D -> E (in Ref. 3). FT CONFLICT 557 559 QPL -> PAV (in Ref. 2 and 3). FT CONFLICT 570 570 D -> S (in Ref. 2 and 3). FT CONFLICT 573 574 SA -> LR (in Ref. 2). FT CONFLICT 687 687 C -> S (in Ref. 2). FT CONFLICT 736 736 A -> P (in Ref. 2). FT CONFLICT 963 963 A -> R (in Ref. 2). FT HELIX 36 53 FT HELIX 55 72 FT HELIX 78 89 FT HELIX 92 122 FT HELIX 143 151 FT HELIX 158 166 FT STRAND 169 175 FT HELIX 184 199 FT HELIX 207 226 FT HELIX 237 248 FT TURN 249 255 FT HELIX 256 268 FT TURN 269 271 FT STRAND 282 287 FT TURN 289 291 FT HELIX 301 329 FT HELIX 337 350 FT STRAND 359 361 FT HELIX 370 394 FT HELIX 409 425 FT TURN 430 434 FT HELIX 435 446 FT STRAND 449 456 FT HELIX 459 473 FT HELIX 483 495 FT HELIX 509 523 FT STRAND 529 534 FT HELIX 541 552 FT STRAND 561 565 FT HELIX 568 572 FT HELIX 574 582 FT HELIX 585 591 FT STRAND 593 601 FT HELIX 604 607 FT HELIX 610 629 FT TURN 630 632 FT STRAND 634 640 FT HELIX 645 647 FT HELIX 652 657 FT STRAND 667 673 FT HELIX 674 681 FT HELIX 684 703 FT HELIX 711 732 FT HELIX 738 745 FT HELIX 749 754 FT HELIX 775 783 FT HELIX 788 791 FT HELIX 794 804 FT HELIX 808 818 FT HELIX 820 833 FT HELIX 838 847 FT HELIX 854 875 FT HELIX 885 913 FT TURN 937 941 FT STRAND 942 944 FT HELIX 951 966 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 //