ID D8SEV5_SELML Unreviewed; 975 AA.
AC D8SEV5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=SELMODRAFT_115610 {ECO:0000313|EMBL:EFJ16936.1};
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:EFJ16936.1, 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; GL377616; EFJ16936.1; -; Genomic_DNA.
DR RefSeq; XP_002981843.1; XM_002981797.1.
DR AlphaFoldDB; D8SEV5; -.
DR STRING; 88036.D8SEV5; -.
DR EnsemblPlants; EFJ16936; EFJ16936; SELMODRAFT_115610.
DR Gramene; EFJ16936; EFJ16936; SELMODRAFT_115610.
DR KEGG; smo:SELMODRAFT_115610; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR HOGENOM; CLU_006557_2_0_1; -.
DR InParanoid; D8SEV5; -.
DR OMA; FGWTQSR; -.
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 134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 642
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 975 AA; 109872 MW; 3C2EA333645E8160 CRC64;
MTDATDDIAE EISFQAFDDD CHLLGNLLND CLQREVGPRL MEKVERVRLL AQSVCNMRTV
GVEEAALWLS KQIEKELLNM SVDETVPLAR AFSHHLSLMG IAETHHRLIQ SGVSQDDIYN
AVSNQEVEIV LTAHPTQINR RTLQYKHVRI GHLLERNDRQ DLTHEEKELL IEDLVREITS
LWQTDELRRR RPTPLDEARG GLHIVEQTLW RAVPQYLRRI STALKKHTGR PLPLSSTPIK
FGSWMGGDRD GNPHVTAKVT RDVCYLARWI AADLYLREVD SLRFELSVSN CDEKLAQFAY
DIFIRLVQAS SNTTTALQSN ESSPSAVKAE IMRDSIQHDQ ESPASPTRAA TILAAAISAG
IRKRTGTDSI SKSSVDKLLN PSATGRPDIA PYRVVLGHIR EKLVNTRRRM EELLDDLPCD
YDPSEFYETP EQLLEPLMLC HRSMESCEAE VLADGRLTDL IRRVSIFGMT LMKLDLRQEA
EKHSEALDAI TKFLDMGTYS AWDEDKKLDF LTKELKGKRP LVPPTIAVSS EVQEVLNTFR
VAAELGSNSL GAYIVSMTSE ASDVLAVELL QKEARLVVSG ELGKPCPGTS LRVVPLFETV
KDLRDAGTII RRLLSIPWYR DHLVTNHQGH QEVMLGYSDS GKDAGRFTAA WELYKAQEDV
VAACKDYGIK LTLFHGRGGS VGRGGGPMYL AIQSQPPGSV IGTLRITEQG EMVQAKFGLP
QTALRELEIY TTAVLLATLN PPDSPRVSCW RTVMEQISDV SRQHYRNVVY ENKEFLHYFQ
EATPESELGN LNIGSRPTRR KKSGGIGQLR AIPWIFAWTQ SRFVLPAWLG VGKGLEAVIS
QGYIQELQAM YREWPFFQST IDLIEMGLAK ADTAIAKHYD DWLVNPARQT LGQELRDEFH
KTERCVLEVS GHHRLAENNK TLRRLIESRL PYLTPLNMLQ VEVLRRLRQD QGNQRLRDAL
LISINGIAAG MRNTG
//
