ID   A0A1S2Z6T0_CICAR        Unreviewed;       967 AA.
AC   A0A1S2Z6T0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   Name=LOC101514127 {ECO:0000313|RefSeq:XP_004516076.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004516076.1};
RN   [1] {ECO:0000313|RefSeq:XP_004516076.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004516076.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_004516076.1; XM_004516019.3.
DR   AlphaFoldDB; A0A1S2Z6T0; -.
DR   SMR; A0A1S2Z6T0; -.
DR   STRING; 3827.A0A1S2Z6T0; -.
DR   PaxDb; 3827-XP_004516076-1; -.
DR   GeneID; 101514127; -.
DR   KEGG; cam:101514127; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   OrthoDB; 355614at2759; -.
DR   Proteomes; UP000087171; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
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; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087171}.
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        602
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   967 AA;  110641 MW;  D1705AECB92E30AE CRC64;
     MANRNLEKMA SIDAHLRQLV PAKVSEDDKL IEYDALLLDR FLDILQDLHG EDLKETVQEV
     YELSAEYEGK HDPEKLEELG NLITSLDAGD SIVVAKSFSH MLNLANLAEE VQIAHRRRIK
     LKKGDFADEN NATTESDIEE TLKRLVGDLN KSPQEVFDAL KNQTVDLVLT AHPTQSIRRS
     LLQKHGRIRN CLAHLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTPP TPQDEMRAGM
     SYFHETIWMG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
     DVCLLARMMA ANLYYSQIED LMFELSMWRC NDELRVRAEE LNRSSKKDAV AKHYIEFWKN
     IPPNEPYRVL LGEVRDRLYQ TRERSRHLLA NGYSDIPEEH TFTNVDEFLE PLELCYRSLC
     ACGDRAIADG SLLDFLRQVS TFGLSLVRLD IRQESERHSD VLDAITKHLE IGSYQEWSEE
     KRQQWLLSEL SGKRPLFGPD LPQTEEIRDV LDTFHVIAEL PSDNFGAYII SMATAASDVL
     AVELLQRECH VKHPLRVVPL FEKLADLEAA PAALARLFSI DWYRNRINGK QEVMIGYSDS
     GKDAGRFSAA WQLYKAQEEL IKVAKEYGVK LTMFHGRGGT VGRGGGPTHL AILSQPPETI
     HGSLRVTVQG EVIEQSFGEQ HLCFRTLQRF TAATLEHGMH PPISPKPEWR ALMDQMAVIA
     TEEYRAMVFQ EPRFVEYFRL ATPELEYGRM NIGSRPAKRK PSGGIETLRA IPWIFAWTQT
     RFHLPVWLGF GAAFKQVIDK DIRNLQMLQE MYNQWPFFRV TIDLVEMVFA KGDPGIAALY
     DRLLVSKDLW PFGEQLRTKF EETKKLLLQV AAHKDLLEGD PYLKQRLRLR DSYITTLNVC
     QAYTLKRIRD PNYNVKLRPH ISKESIEISK AADELVTLNP TSEYAPGLED TLILTMKGIA
     AGLQNTG
//