ID   PGK_MYCGE               Reviewed;         411 AA.
AC   P47542; Q49338; Q59521;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=MG300;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50; 199-306 AND 309-409.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
RN   [3]
RP   SEQUENCE REVISION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA   Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA   Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT   "Essential genes of a minimal bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
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.
CC   -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC       global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD12464.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L43967; AAC71522.2; -; Genomic_DNA.
DR   EMBL; U02226; AAA03379.1; -; Genomic_DNA.
DR   EMBL; U02234; AAA03386.1; -; Genomic_DNA.
DR   EMBL; U02178; AAD12464.1; ALT_INIT; Genomic_DNA.
DR   PIR; B64233; B64233.
DR   RefSeq; WP_010869417.1; NC_000908.2.
DR   AlphaFoldDB; P47542; -.
DR   SMR; P47542; -.
DR   STRING; 243273.MG_300; -.
DR   KEGG; mge:MG_300; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_14; -.
DR   InParanoid; P47542; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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   Reference proteome; Transferase.
FT   CHAIN           1..411
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145965"
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         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         366..369
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        199..201
FT                   /note="SPQ -> KPT (in Ref. 2; AAA03379)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   411 AA;  44847 MW;  147781D8A519D1E7 CRC64;
     MLNFKTLQAI DFQNKTVVLR SDFNVPMING VISDSERILA GLDTIKFLVK KNCKIVLLSH
     LSRIKSLEDK LNNKKSLKPV AELLQQLLPT VKVQFSCKNT GAEVKQKVQA LAFGEILLLE
     NTRYCDVNDK GEIVKLESKN DPELAKFWAS LGEIFVNDAF GTAHRKHASN AGIAKYVAKS
     CIGFLMEKEL KNLSYLIQSP QKPFVVVLGG AKVSDKLKVV ENLLKLADNI LIGGGMVNTF
     LKAKGKATAN SLVEKELIDV AKQILDKDTH NKIVLAIDQV MGSEFKDQTG ITLDVSDKIQ
     EQYQSYMSLD VGSKTIALFE SYLKTAKTIF WNGPLGVFEF TNFAKGTSKI GEIIAKNKTA
     FSVIGGGDSA AAVKQMQLSD QFSFISTGGG ASLALIGGEE LVGISDIQKN S
//