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Database: UniProt
Entry: A0A151SX88_CAJCA
LinkDB: A0A151SX88_CAJCA
Original site: A0A151SX88_CAJCA 
ID   A0A151SX88_CAJCA        Unreviewed;       967 AA.
AC   A0A151SX88;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=KK1_014855 {ECO:0000313|EMBL:KYP59419.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
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; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP59419.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP59419.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
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; CM003612; KYP59419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151SX88; -.
DR   STRING; 3821.A0A151SX88; -.
DR   OMA; WAFGEQL; -.
DR   OrthoDB; 355614at2759; -.
DR   Proteomes; UP000075243; Chromosome 10.
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:UP000075243}.
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;  110726 MW;  E407F8E77FD8ABCD CRC64;
     MANRNLEKMA SIDAQLRLLV PAKVSEDDKL VEYDALLLDR FLDILQDLHG EDLKETVQEV
     YELSAEYEGK HDPKKLEELG NLITSLDAGD SIVVAKSFSH MLNLANLAEE VQIAHRRRNK
     LKKGDFADEN NATTESDIEE TLKRLVVDLK KSPQEVFDAL KNQTVDLVLT AHPTQSVRRS
     LLQKHGRVRN CLTQLYAKDI TPDDKQELDE ALQREVQAAF RTDEIRRTPP TPQDEMRAGM
     SYFHETIWKG VPTFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
     DVCLLARMMA ANLYYSQIED LMFELSMWRC NDELRVRADE LNRSSKKDAV AKHYIEFWKT
     IPPNEPYRVL LGEVRDRLYQ TRERSRHLLA HGHSDIPEEE TFTNVEEFLE PLELCYRSLC
     ACGDRAIADG SLLDFLRQVS TFGLSLVRLD IRQESDRHTD VLDAITKHLE IGSYQEWSEE
     KRQQWLLSEL SGKRPLFGPD LPQTEEIRDV LDTFHVIAEL PADNFGAYII SMATAPSDVL
     AVELLQRECH VKHPLRVVPL FEKLADLEAA PAALARLFSV DWYRNRINGK QEVMIGYSDS
     GKDAGRFSAA WQLYKAQEEL IKVAKEYGVK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI
     HGSLRVTVQG EVIEQSFGEQ HLCFRTLQRY TAATLEHGMH PPISPKPEWR ALMDEMAVIA
     TEEYRSIVFK EPRFVEYFRL ATPELEYGRM NIGSRPAKRR PSGGIETLRA IPWIFAWTQT
     RFHLPVWLGF GAAFKHVIEK DVRNIHMLQE MYNQWPFFRV TLDLVEMVFA KGDPGIAALY
     DRLLVSKDLW PFAEQLRTKY EETKELLLQV AAHRDLLEGD PYLKQRLRLR DSYITTLNVC
     QAYTLKRIRD PNYNVKLRPH ISKESIEISK PADELITLNP TSEYAPGLED TLILTMKGIA
     AGLQNTG
//
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