PEPP_ALLCE
ID PEPP_ALLCE Reviewed; 481 AA.
AC Q93WP4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Phosphoenolpyruvate phosphatase;
DE Short=PEP phosphatase;
DE EC=3.1.3.60;
DE Flags: Precursor;
GN Name=ACPEPP;
OS Allium cepa (Onion).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Allioideae; Allieae; Allium.
OX NCBI_TaxID=4679;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBCELLULAR LOCATION.
RX DOI=10.1016/S0168-9452(01)00480-0;
RA Shinano T., Yonetani R., Ushihara N., Adachi H., Wasaki J., Matsui H.,
RA Osaki M.;
RT "Characteristics of phosphoenolpyruvate phosphatase purified from Allium
RT cepa.";
RL Plant Sci. 161:861-869(2001).
CC -!- FUNCTION: Phosphoenolpyruvate phosphatase that probably operates in the
CC vacuole to release phosphate from phosphoenolpyruvate (PEP) under
CC phosphorus starvation. {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phosphoenolpyruvate = phosphate + pyruvate;
CC Xref=Rhea:RHEA:19997, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=3.1.3.60;
CC Evidence={ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.44 mM for phosphoenolpyruvate {ECO:0000269|Ref.1};
CC KM=3.72 mM for fructose 6-phosphate {ECO:0000269|Ref.1};
CC KM=1.47 mM for glucose 6-phosphate {ECO:0000269|Ref.1};
CC KM=1.60 mM for p-nitrophenylphosphate {ECO:0000269|Ref.1};
CC KM=1.51 mM for ATP {ECO:0000269|Ref.1};
CC KM=2.69 mM for ADP {ECO:0000269|Ref.1};
CC KM=1.36 mM for phytic acid {ECO:0000269|Ref.1};
CC Vmax=240 umol/min/mg enzyme toward phosphoenolpyruvate
CC {ECO:0000269|Ref.1};
CC Vmax=242 umol/min/mg enzyme toward fructose 6-phosphate
CC {ECO:0000269|Ref.1};
CC Vmax=374 umol/min/mg enzyme toward glucose 6-phosphate
CC {ECO:0000269|Ref.1};
CC Vmax=279 umol/min/mg enzyme toward p-nitrophenylphosphate
CC {ECO:0000269|Ref.1};
CC Vmax=349 umol/min/mg enzyme toward ATP {ECO:0000269|Ref.1};
CC Vmax=510 umol/min/mg enzyme toward ADP {ECO:0000269|Ref.1};
CC Vmax=178 umol/min/mg enzyme toward phytic acid {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|Ref.1};
CC -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000305|Ref.1}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. Purple
CC acid phosphatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB052619; BAB60719.1; -; mRNA.
DR AlphaFoldDB; Q93WP4; -.
DR SMR; Q93WP4; -.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050189; F:phosphoenolpyruvate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd00839; MPP_PAPs; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR039331; PPA-like.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR PANTHER; PTHR22953; PTHR22953; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF49363; SSF49363; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Iron; Metal-binding; Protein phosphatase; Signal;
KW Vacuole; Zinc.
FT SIGNAL 1..36
FT CHAIN 37..481
FT /note="Phosphoenolpyruvate phosphatase"
FT /id="PRO_5000049662"
FT ACT_SITE 327
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 354..356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 481 AA; 55970 MW; 6DA72EB851D7C8FD CRC64;
MPIYTSRSCF YLLLFHIILL CSVDKTLCRQ TSSFVRSEFP AVDIPIDSKE FAVPKNQFSP
QQVHITQGDY DGKAVIVSWV TFIDPGKSEV VYGTSPNSYD HSAQGKTTNY TYYDYTSGYI
HHCLLDKLEY DTKYYYKIGK GDAAREFWFH TPPQIHPDAS YTFGIIGDLG QTYNSLSTLE
HYMKSKGQTV LFVGDLSYAD RYSCNNGTRW DSWGRFVERS VAYQPWIWTV GNHEIEYRPD
LGEVFPFRAY LNRYPTPHLA SASSSPLWYS IRRASAHIIV LSSYSPFVKY TPQWLWLSEE
LTRVDREKTP WLIVLMHAPL YNSNEAHYME GESMRVAFES WFVQYKVDLV FAGHVHAYER
SYRISNIVYN ITSGNRYPIP DKSAPVYITV GDGGNQEGLA ERFSESQPDY SAFRESSYGH
STLELRNRTH AFYQWNRNDD GKHIPVDRII FRNQYWASNT RRRRLKKTRP SQAVERLISS
Y
