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
//