PGK2_HORSE
ID PGK2_HORSE Reviewed; 417 AA.
AC Q8MIF7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Phosphoglycerate kinase 2;
DE EC=2.7.2.3;
DE AltName: Full=Phosphoglycerate kinase, testis specific;
GN Name=PGK2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12119100; DOI=10.1016/s0378-1119(02)00673-x;
RA Giese A., Jude R., Kuiper H., Piumi F., Schambony A., Guerin G., Distl O.,
RA Topfer-Petersen E., Leeb T.;
RT "Molecular characterization of the equine AEG1 locus.";
RL Gene 292:65-72(2002).
CC -!- FUNCTION: Essential for sperm motility and male fertility but is not
CC required for the completion of spermatogenesis.
CC {ECO:0000250|UniProtKB:P09041}.
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|UniProtKB:P09041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; AJ315378; CAD43034.1; -; Genomic_DNA.
DR RefSeq; NP_001077063.1; NM_001083594.1.
DR AlphaFoldDB; Q8MIF7; -.
DR SMR; Q8MIF7; -.
DR STRING; 9796.ENSECAP00000039253; -.
DR PeptideAtlas; Q8MIF7; -.
DR PRIDE; Q8MIF7; -.
DR Ensembl; ENSECAT00000003386; ENSECAP00000039253; ENSECAG00000003389.
DR GeneID; 100036552; -.
DR KEGG; ecb:100036552; -.
DR CTD; 5232; -.
DR GeneTree; ENSGT00390000008820; -.
DR InParanoid; Q8MIF7; -.
DR OrthoDB; 838642at2759; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000002281; Chromosome 20.
DR Bgee; ENSECAG00000003389; Expressed in testis and 3 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0035686; C:sperm fibrous sheath; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
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; 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 Acetylation; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT CHAIN 2..417
FT /note="Phosphoglycerate kinase 2"
FT /id="PRO_0000145830"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63..66
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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
SQ SEQUENCE 417 AA; 44879 MW; 5AA58A6CF3685392 CRC64;
MSLSKKLTLD KLDVKGKRII MRVDFNVPMK KNQITNNQRI KASIPSIKYC LDNGARSVVL
MSHLGRPDGV PMPDKYSLEP VAAELKSLLG KDVLFLKDCV GSEVEKACAN PATGSVILLE
NLRFHVEEEG KGQDPSGNKL KAEAGKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGIN
LPQKASGFLM KKELEYFAKA LENPERPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM
AYTFLKVLNN MEIGASLFDE EGAKIVKDIM AKANKNGVRI TFPVDFVTAD KFEENAKVGQ
ATVASGIPAG WMGLDCGPET NKKYAQVMAQ AKLIVWNGPV GVFEWDAFAK GTKALMDEIV
KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKILPG VDALSNL
