ID   D8TAC4_SELML            Unreviewed;       955 AA.
AC   D8TAC4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-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=SELMODRAFT_269944 {ECO:0000313|EMBL:EFJ06433.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ06433.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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DR   EMBL; GL377701; EFJ06433.1; -; Genomic_DNA.
DR   RefSeq; XP_002992495.1; XM_002992449.1.
DR   AlphaFoldDB; D8TAC4; -.
DR   SMR; D8TAC4; -.
DR   STRING; 88036.D8TAC4; -.
DR   EnsemblPlants; EFJ06433; EFJ06433; SELMODRAFT_269944.
DR   GeneID; 9629223; -.
DR   Gramene; EFJ06433; EFJ06433; SELMODRAFT_269944.
DR   KEGG; smo:SELMODRAFT_269944; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_2_0_1; -.
DR   InParanoid; D8TAC4; -.
DR   OMA; WAFGEQL; -.
DR   OrthoDB; 355614at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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   Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        594
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   955 AA;  108872 MW;  91728E45085913C6 CRC64;
     MVSIDDRMRL LVPTKVTADD KLIEYDMLLL NHFLSVLKDL HGEEMRELVH RCYELSGQYG
     QAEGCGDPAK LEDLGNLVKS LQPGPAIVIA SSLSHMLNLG NLAEEVQIAH RRRVSEKSGG
     IGDENSALTE SDIEETFRRL MKLGKSPQEI FEALKTQTVD LVLTAHPTQS IRRSLLQKHS
     RIRSCLSELY KDDITPDEKQ ELEEALHREV QAAFRTDEIR RTPPTPQDEM RAGMSYFHET
     IWNCLPKFLR RVDTALKAIG INERLPYNVP LIQFSSWMGG DRDGNPRVTP EVTRDVCLLA
     RLMASSLYFS QIEDLMFELS MWRCNEELRA RVAQLELRTK EDAKHYKEFW KPIPSNEPFR
     VILGDIRDRL YRTRERARQI LATGKSDVNE EEAFSSVEEI LEPLELCYRS LCSTGDKLIA
     DGSLLDFMRQ VSCFGLGLVR LDIRQESDRH TDVMDAITTH LGIGSYRSWT EEERQEWLLA
     ELRGKRPLFG ADLPKTDEIK DVLETFHVIA ELPTDCFGAY IISMATAPSD VLVVELLQRE
     CRVNVPLRVV PLFEKLADLE AAPASLTRLF SIDWYRNRIK GKQEVMIGYS DSGKDAGRFS
     AAWQLYKCQE ELVKVAKQFG VKLTMFHGRG GTVGRGGGPT HLAILSQPRD TIDGSLRVTI
     QGEVIEQSFG EEHLCFRTLQ RFTAATLEHG MHPPTAPKED WRKLMDEMAA IATEAYRSVV
     FKDPQFVHYF RMATPELEYG RMNIGSRPSK RKPSGGIESL RAIPWIFAWT QTRFHLPVWL
     GFGEAFKDVI DGNPQTLKML QAMYREWPFF RVTVDLVEMV FAKGDPRIAE LYDRLLVSPE
     LQDIGKKLRG KYEETRKLLL EVACHSELLE ENPTLKQRLR LREPFITTLN VQQAYTLKKM
     RQIEPDDAPM PRTNANSASA EELVELNTTT EYAPGLEDTI ILTMKGIAAG MQNTG
//