PGK_LACDE
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 03-AUG-2022, entry version 94.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk;
OS Lactobacillus delbrueckii subsp. bulgaricus.
OC Bacteria; Firmicutes; 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_QOVB01000001.1.
DR AlphaFoldDB; O32756; -.
DR SMR; O32756; -.
DR GeneID; 66399600; -.
DR OMA; DMIFDIG; -.
DR BioCyc; MetaCyc:MON-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 CDD; cd00318; Phosphoglycerate_kinase; 1.
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 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
