ID D8SHT8_SELML Unreviewed; 1020 AA.
AC D8SHT8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=SELMODRAFT_117085 {ECO:0000313|EMBL:EFJ16055.1};
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:EFJ16055.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001071};
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; GL377620; EFJ16055.1; -; Genomic_DNA.
DR RefSeq; XP_002982810.1; XM_002982764.1.
DR AlphaFoldDB; D8SHT8; -.
DR STRING; 88036.D8SHT8; -.
DR EnsemblPlants; EFJ16055; EFJ16055; SELMODRAFT_117085.
DR Gramene; EFJ16055; EFJ16055; SELMODRAFT_117085.
DR KEGG; smo:SELMODRAFT_117085; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR HOGENOM; CLU_006557_2_0_1; -.
DR InParanoid; D8SHT8; -.
DR OMA; TCEISKM; -.
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:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 2.
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 154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 687
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1020 AA; 114865 MW; 2D730DEB1FCF7FBD CRC64;
MTDATDDIAE EISFQAFDDD CHLLGNLLND CLQREVGPRL MEKVERVRLL AQSVCNMRTV
GVEEAALWLS KQIEKELLNM SVDETVPLAR AFSHHLSLMG IAETHHRVRR NRMASHPSKS
CDDVFKRLIQ SGVSQDDIYN AVSNQEVEIV LTAHPTQINR RTLQYKHHLL ERNDRQDLTH
EEKELLIEDL VREITSLWQT DELRRRRPTP LDEARGGLHI VEQTLWRAVP QYLRRISTAL
KKHTGRPLPL SSTPIKFGSW MGGDRDGNPH VTAKVTRDVC YLARWIAADL YLREVDSLRF
ELSVSNCDEK LAQFAYDIVA KDVTTGRMEG TESCLHPVST PISQLVQIYP HALASSNTTT
ALQSNESSPS AVKAEIMRDS IQHDQESPAS PTRAATILAA AISAGIRKRT GTDSISKSSV
DKLLNPSATG RPDIAPYRVV LGHIREKLVN TRRRMEELLD DLPCDYDPSE FYETPEQLLE
PLMLCHRSME SCEAEVLADG RLTDLIRRVS IFGMTLMKLD LRQEAEKHSE ALDAITKFLD
MGTYSAWDED KKLDFLTKEL KGKRPLVPPT IAVSSEVQEV LNTFRVAAEL GSNSLGAYIV
SMTSEASDVL AVELLQKEAR LVVSGELGKP CPGTSLRVVP LFETVKDLRD AGTIIRRLLS
IPWYRDHLVT NHQGHQEVML GYSDSGKDAG RFTAAWELYK AQEDVVAACK DYGIKLTLFH
GRGGSVGRGG GPMYLAIQSQ PPGSVIGTLR ITEQGEMVQA KFGLPQTALR ELEIYTTAVL
LATLNPPDSP RVSCWRTVME QISDVSRQHY RNVVYENKEF LHYFQEATPE SELGNLNIGS
RPTRRKKSGG IGQLRAIPWI FAWTQSRFVL PAWLGVGKGL EAVISQGYIQ ELQAMYREWP
FFQSTIDLIE MGLAKADIAI AKHYDDWLVN PARQTLGQEL RDEFHKTERC VLEVSGHHRL
AENNKTLRRL IESRLPYLTP LNMLQVEVLR RLRQDQSNQR LRDALLISIN GIAAGMRNTG
//
