ID CAPP1_MAIZE STANDARD; PRT; 970 AA. AC P04711; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 2. DT 16-MAY-2006, entry version 63. 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 OF 39-970. RX MEDLINE=86148496; PubMed=3005978; 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 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 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. 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 MaizeDB; 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 TURN 73 74 FT TURN 77 77 FT HELIX 78 89 FT STRAND 90 90 FT HELIX 92 122 FT HELIX 143 151 FT TURN 152 153 FT STRAND 154 154 FT HELIX 158 166 FT TURN 167 167 FT STRAND 169 175 FT TURN 178 179 FT STRAND 182 182 FT HELIX 184 199 FT TURN 200 201 FT TURN 203 204 FT HELIX 207 226 FT STRAND 227 227 FT STRAND 230 230 FT STRAND 233 233 FT HELIX 237 248 FT TURN 249 255 FT HELIX 256 268 FT TURN 269 271 FT STRAND 274 274 FT TURN 278 279 FT STRAND 282 287 FT TURN 289 291 FT STRAND 292 292 FT TURN 294 295 FT TURN 297 298 FT STRAND 299 299 FT HELIX 301 329 FT HELIX 337 350 FT TURN 356 357 FT STRAND 359 361 FT STRAND 363 363 FT TURN 367 368 FT STRAND 369 369 FT HELIX 370 394 FT STRAND 395 396 FT STRAND 399 400 FT STRAND 402 402 FT TURN 403 404 FT STRAND 405 405 FT STRAND 408 408 FT HELIX 409 425 FT TURN 426 426 FT STRAND 427 427 FT TURN 430 434 FT HELIX 435 446 FT TURN 447 448 FT STRAND 449 456 FT HELIX 459 473 FT TURN 474 474 FT STRAND 475 475 FT STRAND 478 478 FT TURN 479 480 FT STRAND 481 481 FT HELIX 483 495 FT STRAND 498 498 FT TURN 503 504 FT HELIX 509 523 FT STRAND 524 524 FT STRAND 526 526 FT TURN 527 528 FT STRAND 529 534 FT TURN 535 536 FT STRAND 539 539 FT TURN 540 540 FT HELIX 541 552 FT TURN 553 553 FT STRAND 556 557 FT STRAND 561 565 FT STRAND 567 567 FT HELIX 568 572 FT TURN 573 573 FT HELIX 574 582 FT TURN 583 583 FT HELIX 585 591 FT TURN 592 592 FT STRAND 593 601 FT TURN 602 603 FT HELIX 604 607 FT STRAND 608 608 FT HELIX 610 629 FT TURN 630 632 FT STRAND 634 640 FT STRAND 643 644 FT HELIX 645 647 FT TURN 648 648 FT HELIX 652 657 FT TURN 658 658 FT STRAND 659 659 FT TURN 661 662 FT STRAND 663 663 FT TURN 665 666 FT STRAND 667 673 FT HELIX 674 681 FT STRAND 682 683 FT HELIX 684 703 FT STRAND 704 704 FT HELIX 711 732 FT TURN 733 734 FT TURN 736 737 FT HELIX 738 745 FT STRAND 746 746 FT HELIX 749 754 FT STRAND 757 757 FT TURN 770 771 FT STRAND 774 774 FT HELIX 775 783 FT TURN 784 785 FT HELIX 788 791 FT TURN 792 793 FT HELIX 794 804 FT TURN 806 807 FT HELIX 808 818 FT HELIX 820 833 FT TURN 834 835 FT HELIX 838 847 FT TURN 848 848 FT STRAND 849 849 FT STRAND 851 851 FT TURN 852 853 FT HELIX 854 875 FT TURN 876 876 FT STRAND 878 879 FT TURN 880 881 FT STRAND 882 883 FT HELIX 885 913 FT TURN 915 916 FT STRAND 926 926 FT TURN 937 941 FT STRAND 942 944 FT STRAND 946 947 FT TURN 949 950 FT HELIX 951 966 FT TURN 967 967 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 //