ID   PGK_FUNMO               Reviewed;         416 AA.
AC   O74233;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-MAY-2023, entry version 86.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=PGK;
OS   Funneliformis mosseae (Endomycorrhizal fungus) (Glomus mosseae).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Funneliformis.
OX   NCBI_TaxID=27381;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BEG 12;
RX   PubMed=9871121; DOI=10.1007/s002940050411;
RA   Harrier L.A., Wright F., Hooker J.E.;
RT   "Isolation of the 3-phosphoglycerate kinase gene of the arbuscular
RT   mycorrhizal fungus Glomus mosseae (Nicol. & Gerd.) Gerdemann & Trappe.";
RL   Curr. Genet. 34:386-392(1998).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AF072893; AAD09406.1; -; mRNA.
DR   EMBL; AF074394; AAC26131.1; -; mRNA.
DR   AlphaFoldDB; O74233; -.
DR   SMR; O74233; -.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..416
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145881"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  44765 MW;  53179DF32EEFEC48 CRC64;
     MSLSNKLSIR DLNVKDKRVL IRVDFNVPLD GTTITNNQRI VAALPTIKYA LEQKAKTVVL
     MSHLGRPDGK KVDKYSLAPV AKEVERLLGK KVTFLEDCVG EGVENYVKNA CDGEVILLEN
     LRFHAEEEGS SKGPDGKKVK ADLEKVKEFR RSLTALGDVY INDAFGTAHR AHSSMVGVEL
     PQKAAGFLVK KELEYFAKAL ESPERPFLAI LGGAKVSDKI QLIDNLIAKV DSLIICGGMA
     FTFKKTLENV KIGNSLFDAD GAKTVGEVME KAKKHDVEVV LPVDYITADK FAKDAQVGYA
     TDQEGIPDGW MGLDCGEKSV ELYKQTIAKA KTILWNGPAG VFEFDNFAKG TKATLDCAVE
     AAQSGKIVII GGGDTATVAA KYGVEDKLSH VSTGGGASLE LLEGKDLPGV SALSSK
//