ID   B9SEG3_RICCO            Unreviewed;       986 AA.
AC   B9SEG3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=RCOM_0704240 {ECO:0000313|EMBL:EEF37993.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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DR   EMBL; EQ973936; EEF37993.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9SEG3; -.
DR   STRING; 3988.B9SEG3; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   InParanoid; B9SEG3; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 2.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT   REGION          262..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        653
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   986 AA;  111301 MW;  0E01AE629882A4F0 CRC64;
     MTDTTDDIAE EISFQSFDDD CCPFRYFRTR EEREKGKEKK LVRKARSMTH LSKSCDDIFN
     QLLQSGISAE ELYDTVCKQE VEIVLTAHPT QINRRTLQYK HIRIAHLLDY NDRPDLTHED
     REMLIEDLVR EITSIWQTDE LRRHKPTPVD EARAGLNIVE QSLWKALPHY LRRVSTALKK
     HTGKPLPLTC MPIRFGSWMG GDRDGNPNVT AKVTRDVSLL SRWMAVDLYI REVDSLRFEL
     SMVQCSDRLL KVANDILIEE TSSEDHHESW NQPASRSQTK FPRKSLPTQL PPRADLPACT
     ECNDGESQYP KLELPGTDYM PFNRQEALGS SYSESSSQDI NHGLPKTTGN GSVANSSGSP
     RASFSSAQLV AQRKLFAESK IGRSSFQKLL EPSLPQRPGI APYRIVLGNV KDKLMRTRRR
     LELLLEDLPC EYDQWDYYET TDQLLDPLLL CYESLQSCGA GVLADGRLAD LIRRVATFGM
     VLMKLDLRQE SGRHADTLDA ITKYLEMGTY SEWDEEKKLE FLTRELKGKR PLVPPTIEVA
     PDVKEVLDAF RVAAELGSDS LGAYVISMAS NASDVLAVEL LQKDARLAVS GELGRPCPGG
     TLRVVPLFET VKDLRGAGSV IRKLLSIDWY REHIIKNHNG HQEVMVGYSD SGKDAGRFTA
     AWELYKAQED VVAACNDFGI KVTLFHGRGG SIGRGGGPTY LAIQSQPPGS VMGTLRSTEQ
     GEMVQAKFGL PHTAIRQLEI YTTAVLLATL RPPHPPREEK WRNVMEEISK ISCQNYRSTV
     YENPEFLAYF HEATPQAELG FLNIGSRPTR RKSSTGIGHL RAIPWVFAWT QTRFVLPAWL
     GVGAGLKGAC EKGFTEDLKA MYKEWPFFQS TIDLIEMVLG KADIPIAKHY DEVLVSESRR
     ELGAELRSEL LTTEKYVLVV SGHEKLSQNN RSLRRLIESR LPYLNPMNML QVEVLKRLRR
     DDDNNKLRDA LLITINGIAA GMRNTG
//