PGK_UREPA
ID PGK_UREPA Reviewed; 422 AA.
AC Q9PQL2;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=UU279;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(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}.
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DR EMBL; AF222894; AAF30688.1; -; Genomic_DNA.
DR RefSeq; WP_006688945.1; NC_002162.1.
DR AlphaFoldDB; Q9PQL2; -.
DR SMR; Q9PQL2; -.
DR STRING; 273119.UU279; -.
DR EnsemblBacteria; AAF30688; AAF30688; UU279.
DR GeneID; 29672564; -.
DR KEGG; uur:UU279; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_1_14; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000423; 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-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1260; -; 2.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..422
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000146033"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64..67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 370..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 47383 MW; F3F45A1542A3783C CRC64;
MNSLNKKSIK DLDVNGKTIV LHLDLNVVVD YENKRILNDR KLRASLPTIN YLINHNAKIV
ILSHLGRIKT LADKQSGKYS LEIIVDELRN RVSKNVNRVV FSPLNYGETV VQMVNDLEER
DILILENTRY CDISDEGEYV GLEWDGSEIL GQFWGMLGDI FIDDAYGVAH RQLSSNYQTA
KFAKKSALGF LIVNEINHLD IALEVPKSPY LALIGGNRVA DKIAAIEVLC ERADQVIIGG
GLVYTFLYAQ GYNVGLNLVE RNMIDDCNNI LEKYGKKILI CFDFLCNNDF SDTRPIYRKI
DEGLEGLYGL DIGKRSLKFI KHEIYRSKTI LLNGPFGVIE NIKNYAQGTT EICKSMAKQT
TRGAYTIICD IDTSSHAEYL GLDKYINFIS TGGGASLSYI EEGVLDGLET IDNVPLNVLK
KE
