ID A0A176VXW1_MARPO Unreviewed; 1017 AA.
AC A0A176VXW1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=AXG93_4368s1130 {ECO:0000313|EMBL:OAE25654.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25654.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE25654.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25654.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE25654.1}.
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DR EMBL; LVLJ01002295; OAE25654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VXW1; -.
DR OrthoDB; 355614at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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; 2.
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:UP000077202}.
FT REGION 407..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 715
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1017 AA; 114888 MW; 5CA5DF2C4919079C CRC64;
MTDTTDDIAE EISFQAYDDD CHLLGNLLND CLMREVGPDF TEKVDRVRLL AQSECNMRLA
GVTDAADYLS TQLEKEVSTM ELEDAVPLAR TFSHYLNLMG IAETHHRYHL LITRTAIRCG
VDNVSNQNLR SVQEVGIVLT AHPTQINRRT IQYKFLRIAH LLERNDRTDL THEDKDLLIE
DLVREITSLW QTDELRRRKP TPVDEARGGL HIVEQSLWKA VPHYLRRVSN ALKKHTGRSL
PLTSTPIKFG SWMGGDRDGN PNVTAKVTRD VSYLARWIAA DLYLREVDGL RFELSMSTCS
DKLAQFAYNI LAHEQQVHDD HHVSWFNQRQ KKHSDHVDIP GHPLPYHIPF GADVPGFTGN
ANDGEADLEM PLLELPLTDG EYRTADIMGY GLIAKATPSL PKAEGLGLQP LKISSPHSST
PTTPKGLAKS GSFKKKSSSE SNLNKSSVDR LLHPSLSGRP DIAPYRIVLG HVREKLVNTR
RRMEMLLEGL TCDFEQDEYY ESTEDLLEPL LLCHESMETT GSEVLADGRI ADLIRRISTF
GMTLMKLDVR QESDKHTETL DAITEYLGMG TYSEWDEERK IRFLTQELRG KRPLVPPSIE
VTPEVQEVLN TFRVAAELGS QSLEAYIISM ASEASDVLAV ELLQKEARLV VAGELGRPCP
GTTLRVVPLF ETVKDLRDAG TVIRKLLGID WYREHLIANH NGHQEVMLGY SDSGKDAGRF
TAAWELYKAQ EDVVKACQEF GIKGSLRVTE QGEMVQAKFG LAQTSVRQLE IYTTAVLLAT
LHPPDPPRSP NWRNVMEHIS EVSCQNYRNI VFHNEQFLQY FHEATPEAEL GNLNIGSRPT
RRKKTGGVQQ LRAIPWIFAW TQTRLTLPAW LGVGAGLDAV IAKGDRDELQ AMYREWPFFQ
STIDLIEMVL AKADIPIAKH YDEVLVSPER QQLGAEIREA FHTTEKCVLE VSGHHKLSEN
NKTLRRLIES RLAYLNPINM LQVEILRRLR QDENNPKLRD ALLITINGIA AGMRNTG
//
