ID   PGK_LACDE               Reviewed;         403 AA.
AC   O32756;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   13-SEP-2023, entry version 100.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk;
OS   Lactobacillus delbrueckii subsp. bulgaricus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B107;
RX   PubMed=9579064; DOI=10.1099/00221287-144-4-905;
RA   Branny P., Delatorre F., Garel J.R.;
RT   "An operon encoding three glycolytic enzymes in Lactobacillus delbrueckii
RT   subsp. bulgaricus: glyceraldehyde-3-phosphate dehydrogenase,
RT   phosphoglycerate kinase and triosephosphate isomerase.";
RL   Microbiology 144:905-914(1998).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ000339; CAA04015.1; -; Genomic_DNA.
DR   PIR; T09634; T09634.
DR   RefSeq; WP_003618962.1; NZ_RIST01000003.1.
DR   AlphaFoldDB; O32756; -.
DR   SMR; O32756; -.
DR   OMA; DMIFDIG; -.
DR   BioCyc; MetaCyc:MONOMER-13053; -.
DR   UniPathway; UPA00109; UER00185.
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   Transferase.
FT   CHAIN           1..403
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145952"
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         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         359..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   403 AA;  42712 MW;  D90FC78FBB9FE397 CRC64;
     MAKLIVSDVD VKDKKVLVRV DFNVPIKDGV IGDDNRIVAA LPTIKYIIEN GGKAILLSHL
     GRIKSDEDKK SLSLAPVAKR LGELLEKPVT FVPSNEGKEV EDAINNMKDG DVVVLENTRF
     QDIDNDFGKR ESKNDPKLGE YWASLGDVFV NDAFGTAHRS HASNVGIATA MKAAGKPAAA
     GFLLEKEIKF LGNAVANPVH PFVTILGGAK VSDKIGVITN LIPKADHIII GGGMAYTFLK
     AQGHNIGKSL VEDDKVEFAK ELLEKAGDKL VLPIDNVAAT EFNNDAASEV VGQDIPDNEM
     GLDIGPKTIE LFKKTLEGAK TVVWNGPMGV FEMPNFAKGT LEVGRALADL PDATTIVGGG
     DSTAAAKQLG IAPKLTHIST GGGASLEYLE GKELPGIACV SDK
//