ID   PGK_NEIMB               Reviewed;         392 AA.
AC   Q9K1R0;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=NMB0010;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAF40489.1; Type=Miscellaneous discrepancy; Note=Probable incorrect perfect sequence repeat which was excised.; Evidence={ECO:0000305};
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DR   EMBL; AE002098; AAF40489.1; ALT_SEQ; Genomic_DNA.
DR   PIR; H81247; H81247.
DR   RefSeq; NP_273076.1; NC_003112.2.
DR   AlphaFoldDB; Q9K1R0; -.
DR   SMR; Q9K1R0; -.
DR   STRING; 122586.NMB0010; -.
DR   PaxDb; Q9K1R0; -.
DR   EnsemblBacteria; AAF40489; AAF40489; NMB0010.
DR   KEGG; nme:NMB0010; -.
DR   PATRIC; fig|122586.8.peg.11; -.
DR   HOGENOM; CLU_025427_0_2_4; -.
DR   OMA; DMIFDIG; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000425; 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   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..392
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145976"
FT   BINDING         21..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         346..349
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        281
FT                   /note="A -> AADAEAVVKDIA (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  40632 MW;  9011CDD6661B04BD CRC64;
     MAFLKLTEQN VQGKTVLIRA DMNVPFKDGK ISDDTRIRAS LASIKYCVDN GASVIVMTHL
     GRPTEGEFHP EDDVAPVAAH LGSLLGKDVK VLNDWRENKP ALNAGDVVML QNVRINKGEK
     KNDLELGKAY ASLCDVFVND AFGTAHRAQA STEAVAQAAP VACAGVLMAG ELDALGKALK
     QPARPMVAIV AGSKVSTKLT ILESLADKVD QLIVGGGIAN TFLLAEGKAI GKSLAEHDLV
     EESKKIMAKM AAKGGSVPLP TDVVVAKAFA ADAEAVVKDI ADVAEDEMIL DIGPKSAAAL
     ADLLKAAGTV VWNGPVGVFE FDQFAGGTKA LAEAIAQSKA FSIAGGGDTL AAIAKFGVTE
     QIGYISTGGG AFLEFLEGKE LPAVAALEKR GA