PGK2_MACFA
ID PGK2_MACFA Reviewed; 417 AA.
AC Q4R3K4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Phosphoglycerate kinase 2;
DE EC=2.7.2.3;
GN Name=PGK2; ORFNames=QtsA-16404;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB179262; BAE02313.1; -; mRNA.
DR RefSeq; NP_001272227.1; NM_001285298.1.
DR AlphaFoldDB; Q4R3K4; -.
DR SMR; Q4R3K4; -.
DR STRING; 9541.XP_005552823.1; -.
DR Ensembl; ENSMFAT00000041199; ENSMFAP00000010531; ENSMFAG00000007944.
DR GeneID; 101866226; -.
DR CTD; 5232; -.
DR VEuPathDB; HostDB:ENSMFAG00000007944; -.
DR eggNOG; KOG1367; Eukaryota.
DR GeneTree; ENSGT00390000008820; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 838642at2759; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000233100; Chromosome 4.
DR Bgee; ENSMFAG00000007944; Expressed in multicellular organism.
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 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 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_0000288667"
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; 44865 MW; F3082B9C8CA3729C CRC64;
MSLSKKLTLD KLDVRGKRVI MRVDFNVPMK KNQITNNQRI KASIPSIKYC LDNGAKAVVL
MSHLGRPDGV PMPDKYSLQP VAAELKSLLG KDVLFLKDCV GAEVENACAN PAPGSVILLE
NLRFHVEEEG KGQDPSGKKI KAEPDKIEGF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
LPHKASGFLM KKELDYFAKA LENPVRPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM
AYTFLKVLNN MEIGASLFDE EGAKIVKDIM TKAQKNGVRI TFPVDFVTAD KFDENAQVGK
ATVASGIPPG WMGLDCGPES NKNHAQVVAQ ARLIVWNGPL GVFEWDAFAK GTKALMDEIV
KATSKGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM
