ID E4ZM83_LEPMJ Unreviewed; 416 AA.
AC E4ZM83;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00016471, ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN ORFNames=LEMA_P051380.1 {ECO:0000313|EMBL:CBX92432.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000642,
CC ECO:0000256|RuleBase:RU000532};
CC -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR EMBL; FP929094; CBX92432.1; -; Genomic_DNA.
DR RefSeq; XP_003835797.1; XM_003835749.1.
DR AlphaFoldDB; E4ZM83; -.
DR STRING; 985895.E4ZM83; -.
DR EnsemblFungi; CBX92432; CBX92432; LEMA_P051380.1.
DR GeneID; 13285061; -.
DR eggNOG; KOG1367; Eukaryota.
DR HOGENOM; CLU_025427_0_0_1; -.
DR InParanoid; E4ZM83; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 5477183at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:EnsemblFungi.
DR GO; GO:0006096; P:glycolytic process; IEA:EnsemblFungi.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 416 AA; 44597 MW; 6B864698D7C57F80 CRC64;
MSLSNKLSIA DVDLKGKRVL IRVDFNVPLD GDKITNNQRI VGALPTIKHA IDNGAKAVIL
MSHLGRPDGK PNPKYSLKPV VPELEKLLGK SVTFTGDCVG KKVEETVNSA SNGQVILLEN
LRFHAEEEGS YKDDEGKKQK VDKSKIDEFR KGLTALGDIY INDAFGTAHR AHSSMVGVDL
PQKASGFLVK KELDYFAKAL EEPKRPFLAI LGGAKVSDKI QLIDNLLGKV DSLIICGGMS
FTFKKTLEGV KIGNSLFDEA GSKTVRDLVE KAKKNNVKIV LPVDYITADK FDKDAKTGYA
TDEEGIPDGW MGLDCGEKSI KLYKEAISEA KTILWNGPAG VFEFDAFAKG TKETLDAAVE
AAQSGKIVII GGGDTATVAA KYGVEDKLSH VSTGGGASLE LLEGKDLPGV SALSSK
//
