ID CAP1_MAIZE STANDARD; PRT; 970 AA. AC P04711; DT 13-AUG-1987 (Rel. 05, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Phosphoenolpyruvate carboxylase 1 (EC 4.1.1.31) (PEPCase 1). GN PEP1 OR 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 SEQUENCE FROM N.A. 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 SEQUENCE OF 39-970 FROM N.A. 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 SEQUENCE FROM N.A. 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 SEQUENCE OF 1-3 FROM N.A. 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 SEQUENCE OF 1-82 FROM N.A. RX MEDLINE=88152202; PubMed=2894322; 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 SEQUENCE OF 599-610. RX MEDLINE=91098247; PubMed=2268676; 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 RT 5'-phosphate."; RL Biochim. Biophys. Acta 1041:291-295(1990). RN [7] RP PHOSPHORYLATION SITE. 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). 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 CC C4 PHOTOSYNTHESIS. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. 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; -. DR EMBL; X03613; CAA27270.1; -. DR EMBL; X14581; CAA32724.1; -. DR EMBL; X14579; CAA32722.1; ALT_INIT. DR EMBL; X14580; CAA32723.1; -. DR EMBL; X15642; CAA33663.1; -. DR EMBL; X07168; CAA30158.1; -. DR PIR; S04546; QYZM. DR PIR; S00348; S00348. DR PDB; 1JQO; 14-JAN-03. DR MaizeDB; 30066; -. DR InterPro; IPR001449; PEPcase. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR PROSITE; PS00393; PEPCASE_2; 1. DR PROSITE; PS00781; PEPCASE_1; 1. KW Lyase; Carbon dioxide fixation; Allosteric enzyme; Multigene family; KW Tricarboxylic acid cycle; Phosphorylation; Photosynthesis; KW 3D-structure. FT MOD_RES 15 15 PHOSPHORYLATION. FT ACT_SITE 177 177 BY SIMILARITY. FT ACT_SITE 606 606 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). SQ SEQUENCE 970 AA; 109296 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 //