PEPM_MYTED
ID PEPM_MYTED Reviewed; 295 AA.
AC P56839;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphoenolpyruvate phosphomutase;
DE Short=PEP mutase;
DE Short=PEP phosphomutase;
DE Short=Phosphoenolpyruvate mutase;
DE EC=5.4.2.9;
OS Mytilus edulis (Blue mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=6550;
RN [1]
RP PROTEIN SEQUENCE OF 2-16 AND 115-129, MUTAGENESIS OF ASP-58; ASP-85;
RP ASP-87; GLU-114 AND ARG-159, AND HOMOTETRAMERIZATION.
RX PubMed=10571990; DOI=10.1021/bi990771j;
RA Jia Y., Lu Z., Huang K., Herzberg O., Dunaway-Mariano D.;
RT "Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived
RT from site-directed mutagenesis studies of active site residues.";
RL Biochemistry 38:14165-14173(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MG(2+) AND AN OXALATE
RP INHIBITOR, AND HOMOTETRAMERIZATION.
RX PubMed=10378273; DOI=10.1016/s0969-2126(99)80070-7;
RA Huang K., Li Z., Jia Y., Dunaway-Mariano D., Herzberg O.;
RT "Helix swapping between two alpha/beta barrels: crystal structure of
RT phosphoenolpyruvate mutase with bound Mg(2+)-oxalate.";
RL Structure 7:539-548(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 6-295 IN COMPLEX WITH
RP SULFOPYRUVATE, AND MUTAGENESIS OF ASP-58; ASN-122 AND HIS-190.
RX PubMed=12162742; DOI=10.1021/bi026024v;
RA Liu S., Lu Z., Jia Y., Dunaway-Mariano D., Herzberg O.;
RT "Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the
RT enzyme/sulfopyruvate complex and kinetic properties of mutants.";
RL Biochemistry 41:10270-10276(2002).
CC -!- FUNCTION: Formation of a carbon-phosphorus bond by converting
CC phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + phosphoenolpyruvate = 3-phosphonopyruvate;
CC Xref=Rhea:RHEA:17013, ChEBI:CHEBI:15378, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:71402; EC=5.4.2.9;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PATHWAY: Phosphorus metabolism; phosphonate biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10378273,
CC ECO:0000269|PubMed:12162742}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000305}.
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DR PDB; 1M1B; X-ray; 2.25 A; A/B=1-295.
DR PDB; 1PYM; X-ray; 1.80 A; A/B=1-295.
DR PDB; 1S2T; X-ray; 2.00 A; A/B=1-295.
DR PDB; 1S2U; X-ray; 2.00 A; A/B=1-295.
DR PDB; 1S2V; X-ray; 2.10 A; A/B/C/D=1-295.
DR PDB; 1S2W; X-ray; 1.69 A; A=1-295.
DR PDBsum; 1M1B; -.
DR PDBsum; 1PYM; -.
DR PDBsum; 1S2T; -.
DR PDBsum; 1S2U; -.
DR PDBsum; 1S2V; -.
DR PDBsum; 1S2W; -.
DR AlphaFoldDB; P56839; -.
DR SMR; P56839; -.
DR PRIDE; P56839; -.
DR BioCyc; MetaCyc:MON-16744; -.
DR BRENDA; 5.4.2.9; 3544.
DR UniPathway; UPA00960; -.
DR EvolutionaryTrace; P56839; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0032923; P:organic phosphonate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR012698; PEnolPyrv_PMutase_core.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR02320; PEP_mutase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Magnesium;
KW Metal-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10571990"
FT CHAIN 2..295
FT /note="Phosphoenolpyruvate phosphomutase"
FT /id="PRO_0000068824"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 58
FT /note="D->A,S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:10571990,
FT ECO:0000269|PubMed:12162742"
FT MUTAGEN 58
FT /note="D->N: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:10571990,
FT ECO:0000269|PubMed:12162742"
FT MUTAGEN 85
FT /note="D->A: Strongly reduces enzyme activity and increases
FT KM."
FT /evidence="ECO:0000269|PubMed:10571990"
FT MUTAGEN 87
FT /note="D->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:10571990"
FT MUTAGEN 114
FT /note="E->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:10571990"
FT MUTAGEN 122
FT /note="N->A,D: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:12162742"
FT MUTAGEN 159
FT /note="R->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:10571990"
FT MUTAGEN 190
FT /note="H->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:12162742"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1S2W"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1PYM"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1PYM"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1PYM"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1S2W"
FT TURN 162..166
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1S2U"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1S2W"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:1S2W"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1S2W"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:1S2W"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:1PYM"
SQ SEQUENCE 295 AA; 32912 MW; A8A7CC4FD6B031F8 CRC64;
MSTKVKKTTQ LKQMLNSKDL EFIMEAHNGL SARIVQEAGF KGIWGSGLSV SAQLGVRDSN
EASWTQVVEV LEFMSDASDV PILLDADTGY GNFNNARRLV RKLEDRGVAG ACLEDKLFPK
TNSLHDGRAQ PLADIEEFAL KIKACKDSQT DPDFCIVARV EAFIAGWGLD EALKRAEAYR
NAGADAILMH SKKADPSDIE AFMKAWNNQG PVVIVPTKYY KTPTDHFRDM GVSMVIWANH
NLRASVSAIQ QTTKQIYDDQ SLVNVEDKIV SVKEIFRLQR DDELVQAEDK YLPKN
