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Database: UniProt
Entry: E8JX80_STRCR
LinkDB: E8JX80_STRCR
Original site: E8JX80_STRCR 
ID   E8JX80_STRCR            Unreviewed;       399 AA.
AC   E8JX80;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
GN   Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145,
GN   ECO:0000313|EMBL:EFX51947.1};
GN   ORFNames=HMPREF9422_1718 {ECO:0000313|EMBL:EFX51947.1};
OS   Streptococcus cristatus ATCC 51100.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=889201 {ECO:0000313|EMBL:EFX51947.1, ECO:0000313|Proteomes:UP000002829};
RN   [1] {ECO:0000313|EMBL:EFX51947.1, ECO:0000313|Proteomes:UP000002829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51100 {ECO:0000313|EMBL:EFX51947.1,
RC   ECO:0000313|Proteomes:UP000002829};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000642, ECO:0000256|HAMAP-
CC         Rule:MF_00145, ECO:0000256|RuleBase:RU000532};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00145}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFX51947.1}.
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DR   EMBL; AEVC01000027; EFX51947.1; -; Genomic_DNA.
DR   RefSeq; WP_005591663.1; NZ_LS483383.1.
DR   AlphaFoldDB; E8JX80; -.
DR   GeneID; 48424140; -.
DR   PATRIC; fig|889201.11.peg.1293; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_9; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000002829; Unassembled WGS sequence.
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; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00145}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00145};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00145};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00145};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00145}.
FT   BINDING         21..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         59..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         328
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         355..358
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   399 AA;  42133 MW;  4070A594D4138212 CRC64;
     MAKLTVKDVD LKGKKVLVRV DFNIPVKDGV ITNDNRITAA LPTIKYILEQ GGRAILFSHL
     GRVKEEADKE GKSLAPVAAD LAAKLGQEVK FIPGVTRGAE LEAAVNALED GQVLLVENTR
     FEDVDGKKES KNDPELGKYW ASLGDGIFVN DAFGTAHRAH ASNVGISANV EKAVAGFLLE
     NEIAYIQEAV ETPERPFVAI LGGSKVSDKI GVIENLLEKA DKVLIGGGMT YTFYKAQGIE
     IGNSLVEEDK LDVAKALLEK ANGKLILPVD SKEANAFADY TEVKDTEGEA VDPGFLGLDI
     GPKSIAKFDE ALTGAKTVVW NGPMGVFENP DFQAGTIGVM DAIVKQPGVK SIIGGGDSAA
     AAINLGRADK FSWISTGGGA SMELLEGKVL PGLAALTEK
//
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