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PGK_MYCPN
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   03-AUG-2022, entry version 110.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=MPN_429; ORFNames=MP412;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
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}.
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DR   EMBL; U00089; AAB96060.1; -; Genomic_DNA.
DR   PIR; S73738; S73738.
DR   RefSeq; NP_110117.1; NC_000912.1.
DR   RefSeq; WP_010874785.1; NC_000912.1.
DR   AlphaFoldDB; P78018; -.
DR   SMR; P78018; -.
DR   IntAct; P78018; 2.
DR   STRING; 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   OMA; DMIFDIG; -.
DR   BioCyc; MetaCyc:MON-549; -.
DR   BioCyc; MPNE272634:G1GJ3-693-MON; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000808; 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   Gene3D; 3.40.50.1260; -; 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; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 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
 
 
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