ID   PGK_MYCPU               Reviewed;         771 AA.
AC   Q98QW4;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=MYPU_2460;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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: In the N-terminal section; belongs to the phosphoglycerate
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AL445563; CAC13419.1; -; Genomic_DNA.
DR   PIR; F90542; F90542.
DR   AlphaFoldDB; Q98QW4; -.
DR   SMR; Q98QW4; -.
DR   STRING; 272635.gene:17576834; -.
DR   KEGG; mpu:MYPU_2460; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_362403_0_0_14; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000528; 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; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 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   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF141571; Pentapeptide repeat-like; 1.
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..771
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145972"
FT   REGION          1..406
FT                   /note="Phosphoglycerate kinase"
FT   REGION          407..771
FT                   /note="Unknown"
FT   BINDING         20..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         58..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         361..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   771 AA;  86689 MW;  CFC542BC9071AB98 CRC64;
     MKKLITDLNL NDKKVLIRLD LNVPLKGKKI TSLKRIEESI PTIKYVQERG GKIILLSHLG
     RVKTKEDKEK KSLSIVVEAL ASLLNSPVKF VDQTRGKKLE SAIEKLKPGD VLLIENTRFE
     DLNNNAESNN DPELGKYWAS LGDVFINDAF GTAHRAHASN VGIASNIKES ALGILVQKEV
     NALWKLMEQQ EKPFVAILGG SKVSDKINVL EKIIDKVDRL IIGGAMAYTF LKAQGIGIGD
     SIYEQDKIEF ATEFLKKYNH KIILPIDHAL AKKFKNAKPI FNNENPLEIP QTFIGMDVGP
     KTIELIHKYI KGDTKLGISP AKTIFWNGPM GVTEFEEFQS GSLAVVEAIS QLVGAYSVVG
     GGDSIAIIEK LNAQMLFSHI STGGGASLEF IESKVLPGID AIQNYEQTYE QYDSQVQSQD
     FSQNFDSPLV EETFSQSTSE NFSDFASSTQ EHFATSENQN TLINNYENPG FDSQDMFKTE
     EQNDSTSSFL TSTNPFSSEF SNEFKTSDFQ DLKQTQETET QETLIPHTFE YTTDDLRHTL
     EQYVRETSFQ TRESTFPTEE ASFETLEETS FQTLEESFPT QSFEQVEQTS EKNMEVSTEN
     FENASSQTNS FTVSDIPKTT STFEDLETPE TQNTTLEEVA LETSNFEAQN LETPNLQTSN
     FETSNLETSN FETSNFETST FESFNTGNFS TPSSTFEDLD LQSATFQTND ESERSTQENF
     EPTEVIESDL LAMKTTELEQ EITNNTSRDI LSEDEVAAPH KKRFWFFGRK R
//