PGK_TETTH
ID PGK_TETTH Reviewed; 420 AA.
AC P50313;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=PGK;
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=CU329;
RX PubMed=1602492; DOI=10.1007/bf00162995;
RA Vohra G.B., Golding G.B., Tsao N., Pearlman R.E.;
RT "A phylogenetic analysis based on the gene encoding phosphoglycerate
RT kinase.";
RL J. Mol. Evol. 34:383-395(1992).
RN [2]
RP ERRATUM OF PUBMED:1602492.
RX PubMed=1487830;
RA Vohra G.B., Golding G.B., Tsao N., Pearlman R.E.;
RL J. Mol. Evol. 35:466-466(1992).
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 -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; X63529; CAA45092.1; -; mRNA.
DR EMBL; X63528; CAA45091.1; -; Genomic_DNA.
DR AlphaFoldDB; P50313; -.
DR SMR; P50313; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
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 CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
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 2: Evidence at transcript level;
KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..420
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145861"
FT BINDING 25..27
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64..67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 420 AA; 45914 MW; FCCE8F842FEA8016 CRC64;
MLSRKIGIDH ILKHIENKRV LMRVDFNVPL KEGKVKDPTR IQGSVPSIKK ILEQNPKGLV
LMSHLGRPDG NRVEKHSMKP VVPKLEELLG TKVTFLNDCV GKDVEEAVKS SRNGEIILLE
NLRFHPEEEG KYIDAAGNKV KADSKAVKEF RKSLTSLGDL FVNDAFGTAH RAHSSMVGVD
HKIRAAGYLL KRELDYFSKA LESPNRPFLV VLGGAKVKDK IQLIESMLDK VDEMIIGGGM
AFTFLKKIHN IEIGNSLFDE EGYKIVDQLL EKAKAKNVKI HLPVDFLCGD SLEANANTRS
FDLKSGIPAG WIGLDAGPKT MAENAEAVAR ANTIVWNGPQ GRFEVDKFKV GSSDLLKHVA
TRTSQGATSI IGGGDTVNLV QQEKATQKVS HVSTGGGASL ELLEGKVLPG VAYLTDIDQL