ID   PGK_ZYMMO               Reviewed;         397 AA.
AC   P09404; Q5NR52;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=ZMO0178;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2832389; DOI=10.1128/jb.170.4.1926-1933.1988;
RA   Conway T., Ingram L.O.;
RT   "Phosphoglycerate kinase gene from Zymomonas mobilis: cloning, sequencing,
RT   and localization within the gap operon.";
RL   J. Bacteriol. 170:1926-1933(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX   PubMed=3680173; DOI=10.1128/jb.169.12.5653-5662.1987;
RA   Conway T., Sewell G.W., Ingram L.O.;
RT   "Glyceraldehyde-3-phosphate dehydrogenase gene from Zymomonas mobilis:
RT   cloning, sequencing, and identification of promoter region.";
RL   J. Bacteriol. 169:5653-5662(1987).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; M19376; AAA27699.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV88802.1; -; Genomic_DNA.
DR   EMBL; M18802; AAA27689.1; -; Genomic_DNA.
DR   PIR; A27745; KIZYG.
DR   RefSeq; WP_011240133.1; NZ_CP035711.1.
DR   AlphaFoldDB; P09404; -.
DR   SMR; P09404; -.
DR   STRING; 264203.ZMO0178; -.
DR   GeneID; 79904584; -.
DR   KEGG; zmo:ZMO0178; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_5; -.
DR   SABIO-RK; P09404; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001173; 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   CDD; cd00318; Phosphoglycerate_kinase; 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..397
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146048"
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         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         354..357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  41388 MW;  F4EABD81139C5E20 CRC64;
     MAFRTLDDIG DVKGKRVLVR EDLNVPMDGD RVTDDTRLRA AIPTVNELAE KGAKVLILAH
     FGRPKGQPNP EMSLARIKDA LAGVLGRPVH FINDIKGEAA AKAVDALNPG AVALLENTRF
     YAGEEKNDPA LAAEVAKLGD FYVNDAFSAA HRAHVSTEGL AHKLPAFAGR AMQKELEALE
     AALGKPTHPV AAVVGGAKVS TKLDVLTNLV SKVDHLIIGG GMANTFLAAQ GVDVGKSLCE
     HELKDTVKGI FAAAEKTGCK IHLPSDVVVA KEFKANPPIR TIPVSDVAAD EMILDVGPKA
     VAALTEVLKA SKTLVWNGPL GAFEIEPFDK ATVALAKEAA ALTKAGSLIS VAGGGDTVAA
     LNHAGVAKDF SFVSTAGGAF LEWMEGKELP GVKALEA
//