ID   PGK_MYCPN               Reviewed;         409 AA.
AC   P78018;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 125.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=MPN_429; ORFNames=MP412;
OS   Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasma pneumoniae).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {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; U00089; AAB96060.1; -; Genomic_DNA.
DR   PIR; S73738; S73738.
DR   RefSeq; WP_010874785.1; NC_000912.1.
DR   AlphaFoldDB; P78018; -.
DR   SMR; P78018; -.
DR   IntAct; P78018; 2.
DR   STRING; 272634.MPN_429; -.
DR   PaxDb; 272634-MPN_429; -.
DR   EnsemblBacteria; AAB96060; AAB96060; MPN_429.
DR   KEGG; mpn:MPN_429; -.
DR   PATRIC; fig|272634.6.peg.464; -.
DR   HOGENOM; CLU_025427_0_2_14; -.
DR   OrthoDB; 9808460at2; -.
DR   BioCyc; MetaCyc:MONOMER-549; -.
DR   BioCyc; MPNE272634:G1GJ3-693-MONOMER; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0043531; F:ADP binding; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:TreeGrafter.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:TreeGrafter.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.40.50.1260:FF:000006; Phosphoglycerate kinase; 1.
DR   FunFam; 3.40.50.1260:FF:000031; Phosphoglycerate kinase 1; 1.
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   Reference proteome; Transferase.
FT   CHAIN           1..409
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145971"
FT   BINDING         22..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         365..368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  44212 MW;  6AF230188D398731 CRC64;
     MVDFKTVQAF DFQGKTVVLR ADLNVPMKDG VITDNERILA SLDTIKYLLG HNCKIVLLSH
     LSRVKSLDDK KGKKSLQPVA SALQNLLKNT KVHFCPENTG DKVKVAVNQL PLGEILVLEN
     TRYCDVNEAG EVVKHESKNN AELAQFWASL GDIFVNDAFG TAHRRHASNA GIAKYIKNSC
     IGLLMERELI NLYRLINNPP KPFVVVLGGA KVSDKLQVVN NLFKIADHIL IGGGMVNTFL
     KALGNEVGTS LVEEDLVQTA KQILDSDKDK KIVLGVDQML HASFKDEPGV ECVVAPQWPA
     ELQGFMSLDV GSKTVALFSS YLAKAKTIFW NGPMGVFEFS NYAQGTLAIG KAIAQNQQAF
     SVIGGGDSAA AAKQLQIADQ FSFISTGGGA SLALIGGEEL VGISDIQKK
//