ID   B9SWL2_RICCO            Unreviewed;       965 AA.
AC   B9SWL2;
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_0551460 {ECO:0000313|EMBL:EEF32001.1};
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   -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC       forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC       tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003774}.
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; EQ974205; EEF32001.1; -; Genomic_DNA.
DR   RefSeq; XP_002530381.1; XM_002530335.2.
DR   AlphaFoldDB; B9SWL2; -.
DR   STRING; 3988.B9SWL2; -.
DR   GeneID; 8287235; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   InParanoid; B9SWL2; -.
DR   OrthoDB; 355614at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0048366; P:leaf development; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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:SF33; PHOSPHOENOLPYRUVATE CARBOXYLASE 3; 1.
DR   Pfam; PF00311; PEPcase; 1.
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   Oxidoreductase {ECO:0000313|EMBL:EEF32001.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyruvate {ECO:0000313|EMBL:EEF32001.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        600
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   965 AA;  110660 MW;  12CF9685C12B6F73 CRC64;
     MQPRNLEKLA SIDAQLRLLV PAKVSEDDKL VEYDALLLDR FLDILQDLHG EDLKETVQEC
     YELSAEYEGK HDPRKLDELG NLLTSLDPGD SIVIAKSFSH MLNLANLAEE VQIAYRRRNK
     LKKGDFADEN SATTESDIEE TFKRLVIDLK KSPEEVFDAL KNQTVDLVLT AHPTQSIRRS
     LLQKHARIRN CLAQLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTAP TPQDEMRAGM
     SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
     DVCLLARMMA ANLYYSQIED LMFELSMWRC SDELRVRADE LHRSSKRDSK HYIEFWKQVP
     PSEPYRVILG DLRDKLYQTR ERSRQMLSHG NSDIPEEATF TNVEQFLEPL ELCYRSLCSC
     GDQPIADGSL LDFLRQVSTF GFSLVRLDIR QESDRHTDVI DTITKHLEIG SYREWSEERR
     QEWLLSELSG KRPLFGPDLQ RTDEVADVLD TFHVIAELPA DSFGAYIISM ATAPSDVLAV
     ELLQRECHVK QPLRVVPLFE KLADLEAAPA ALARLFSIDW YRNRINGKQE VMIGYSDSGK
     DAGRFSAAWQ LYKAQEELIK VAKQFGVKLT MFHGRGGTVG RGGGPTHLAI LSQPPDTIHG
     SLRVTVQGEV IEQSFGEEHL CFRTLQRFTA ATLEHGMHPP VSPKPEWRKL MDEMAVIATE
     EYRSIVFKEP RFVEYFRLAT PELEYGRMNI GSRPSKRKPS GGIESLRAIP WIFAWTQTRF
     HLPVWLGFGA AFKHVIQKDV RNLHMLQEMY NEWPFFRVTI DLVEMVFAKG DPGIAALYDK
     LLVSQDLWSF GERLRTNYEE TKRLLLQIAG HKDLLEGDPY LKQRLRLRDS YITTLNVCQA
     YTLKRIRDPN YNVTLRPHIS KEIMESSKPA DELVKLNPKS DYAPGLEDTL ILTMKGVAAG
     LQNTG
//