ID CAPP_MAIZE STANDARD; PRT; 970 AA. AC P04711; DT 13-AUG-1987 (REL. 05, CREATED) DT 01-OCT-1989 (REL. 12, LAST SEQUENCE UPDATE) DT 01-AUG-1992 (REL. 23, LAST ANNOTATION UPDATE) DE PHOSPHOENOLPYRUVATE CARBOXYLASE (EC 4.1.1.31) (PEPCASE). GN PPC. OS ZEA MAYS (MAIZE). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE; OC CYPERALES; GRAMINEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=B37; TISSUE=LEAF; RA HUDSPETH R.L., GRULA J.W.; RL PLANT MOL. BIOL. 12:579-589(1989). RN [2] RP SEQUENCE OF 39-970 FROM N.A. RM 86148496 RA IZUI K., ISHIJIMA S., YAMAGUCHI Y., KATAGIRI F., MURATA T., RA SHIGESADA K., SUGIYAMA T., KATSUKI H.; RL NUCLEIC ACIDS RES. 14:1615-1628(1986). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. GOLDEN CROSS BANTAM; RM 89276342 RA MATSUOKA M., MINAMI E.; RL EUR. J. BIOCHEM. 181:593-598(1989). RN [4] RP SEQUENCE OF 1-3 FROM N.A. RC STRAIN=H84; TISSUE=LEAF; RM 90186704 RA YANAGISAWA S., IZUI K.; RL J. BIOCHEM. 106:982-987(1989). RN [5] RP SEQUENCE OF 1-82 FROM N.A. RM 88152202 RA YANAGISAWA S., IZUI K., YAMAGUCHI Y., SHIGESADA K., KATSUKI H.; RL FEBS LETT. 229:107-110(1988). RN [6] RP ACTIVE SITE, AND SEQUENCE OF 599-610. RM 91098247 RA JIAO J.-A., PODESTA F.E., CHOLLET R., O'LEARY M.H., ANDREO C.S.; RL BIOCHIM. BIOPHYS. ACTA 1041:291-295(1990). CC -!- FUNCTION: TO FORM OXALOACETATE, A FOUR-CARBON DICARBOXYLIC ACID CC SOURCE FOR THE TRICARBOXYLIC ACID CYCLE. CC -!- CATALYTIC ACTIVITY: ORTHOPHOSPHATE + OXALOACETATE = H(2)O + CC PHOSPHOENOLPYRUVATE + CO(2). CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SUBUNIT: HOMOTETRAMER. 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; ZMPEPC1. DR EMBL; X03613; ZMPEPCR. DR EMBL; X14581; ZMPC21. DR EMBL; X14579; ZMPC324. DR EMBL; X14580; ZMPC91. DR EMBL; X15642; ZMPEP. DR EMBL; X07168; ZMPEPC5A. DR PIR; S04546; QYZM. DR PIR; S00348; S00348. DR PROSITE; PS00393; PEPCASE. KW LYASE; CARBON DIOXIDE FIXATION; ALLOSTERIC ENZYME; KW TRICARBOXYLIC ACID CYCLE. 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; 4823633 CN; 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 //