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Database: UniProt
Entry: A0A2K1YIL3_POPTR
LinkDB: A0A2K1YIL3_POPTR
Original site: A0A2K1YIL3_POPTR 
ID   A0A2K1YIL3_POPTR        Unreviewed;       865 AA.
AC   A0A2K1YIL3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=POPTR_011G110700 {ECO:0000313|EMBL:PNT12854.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT12854.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT12854.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
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; CM009300; PNT12854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1YIL3; -.
DR   OMA; RRDEKHY; -.
DR   Proteomes; UP000006729; Chromosome 11.
DR   ExpressionAtlas; A0A2K1YIL3; baseline and differential.
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:UP000006729}.
FT   ACT_SITE        72
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        500
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   865 AA;  99098 MW;  A8C10E17938F803F CRC64;
     MLNLANLAEE VQIAYRRRNK LKKGDFADEN SATTESDIEE TLRRLVVDLK KSPEEVFDAL
     KNQTVDLVLT AHPTQSVRRS LLQKHARLRN CLAQLYAKDI TPNEKQELDE ALQREIQAAF
     RTDEIRRTPP TPQDEMRAGM SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF
     SSWMGGDRDG NPRVTPEVTR DVCLLARMMA ANLYYSQIED LMFELSMWRC SDELRVRADV
     LHRSSKRDSK HYIEFWKQIP PNEPYRVILG ELRDRLYQTR ERSRQLLSHG ISETPEEATF
     TNVEQFLEPL ELCYRSLCSC GDRPIADGSL LDFLRQVSTF GLSLVRLDIR QESDRHTDVM
     DAITKHLEIG SYREWSEEQR QEWLLSELSG KRPLFGPDLP KTEEIADVLD TFHVIAELPS
     DSFGAYIISM ATAASDVLAV ELLQRECHVK QPLRVVPLFE KLADLEAAPA ALSRLFSIEW
     YRDQINGKQE VMIGYSDSGK DAGRFSAAWQ LYKAQEELIK VAKQYGVKLT MFHGRGGTVG
     RGGGPTHLAI LSQPPDTIHG SLRVTVQGEV IEQSFGEEHL CFRTLQRFAA ATLEHGMHPP
     VSPKPEWRAL MDEMAVVATE EYRSIVFKEP RFVEYFRLAT PELEYGRMNI GSRPSKRKPS
     GGIESLRAIP WIFAWTQTRF HLPVWLGFGA AFKHVIQKDI RNLHMLQEMY NEWPFFRVTI
     DLVEMVFAKG DPGIAALNDK LLVSKELWPF GEKLRANYKE TKSLLLQIAG HKDLLEGDPY
     LKQRLRLRDS YITTLNVCQA YTLKRIRDPN YCVTPRPHLS KEIMESNKPA DELVKLNPTS
     DYAPGMEDTL ILTMKGIAAG MQNTG
//
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