ID   PGK_MESH2               Reviewed;         404 AA.
AC   Q7WZ28; Q600G7;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145};
DE            EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145};
GN   Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=mhp488;
OS   Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mesomycoplasma.
OX   NCBI_TaxID=295358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Minion F.C., Wallace J., Lefkowitz E.J., Madsen M.L., Swartzell S.,
RA   Cleary B.J., Mahairas G.G.;
RT   "Genome sequence of Mycoplasma hyopneumoniae.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232;
RX   PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA   Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA   Mahairas G.G.;
RT   "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT   swine mycoplasmosis.";
RL   J. Bacteriol. 186:7123-7133(2004).
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:0000255|HAMAP-Rule:MF_00145};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00145}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00145}.
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DR   EMBL; AY319328; AAP82943.1; -; Genomic_DNA.
DR   EMBL; AE017332; AAV27590.1; -; Genomic_DNA.
DR   RefSeq; WP_011206322.1; NC_006360.1.
DR   AlphaFoldDB; Q7WZ28; -.
DR   SMR; Q7WZ28; -.
DR   KEGG; mhy:mhp488; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_14; -.
DR   PhylomeDB; Q7WZ28; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000006822; Chromosome.
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-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
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:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..404
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145966"
FT   BINDING         26..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         64..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         359..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ   SEQUENCE   404 AA;  44223 MW;  CBE30FDFF43B0D7A CRC64;
     MQPTYKNKKF IDDIDFLNKT VILRVDFNVP IKNGEISSIK RIIASLKTIK KIVNNGGKLV
     ILSHLGRIKS KEDLPKKSLR IVAEKLAEIL GQEIKFIPEN RGPKVENAIS QLEKGEILVL
     ENTRFQDLNN KAESKNDAEL GRYWASLGDV FINDAFGTLH RAHGSNVGIA TYIKESAIGY
     LVKEELDALS KLIFSPQRPF YAIIGGAKIS DKIGIISTLL EKADKVLIGG GMAYTFKKAL
     GYKIGLSIYE DDKLELAASL VKKYPDKLIL ALDAALAPEF ADLEPLYNQE NPLEIPDHLE
     GMDIGPLTIE LFKDHLKDGK TILWNGTLGV AEFKNFARGT KEVAKIIANL KECYSIIGGG
     DSIAAIEAEG LSNSFSHIST GGGASISFIE NGDLIGLGPI QEKD
//